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For: Baumeister W, Walz J, Zühl F, Seemüller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 1998;92:367-380. [PMID: 9476896 DOI: 10.1016/s0092-8674(00)80929-0] [Cited by in Crossref: 1103] [Cited by in F6Publishing: 389] [Article Influence: 48.0] [Reference Citation Analysis]
Number Citing Articles
1 Shotland Y, Shifrin A, Ziv T, Teff D, Koby S, Kobiler O, Oppenheim AB. Proteolysis of bacteriophage lambda CII by Escherichia coli FtsH (HflB). J Bacteriol 2000;182:3111-6. [PMID: 10809689 DOI: 10.1128/JB.182.11.3111-3116.2000] [Cited by in Crossref: 45] [Cited by in F6Publishing: 19] [Article Influence: 2.1] [Reference Citation Analysis]
2 Vigneron N, Van den Eynde BJ. Proteasome subtypes and regulators in the processing of antigenic peptides presented by class I molecules of the major histocompatibility complex. Biomolecules 2014;4:994-1025. [PMID: 25412285 DOI: 10.3390/biom4040994] [Cited by in Crossref: 58] [Cited by in F6Publishing: 54] [Article Influence: 8.3] [Reference Citation Analysis]
3 Inomata M, Niida S, Shibata K, Into T. Regulation of Toll-like receptor signaling by NDP52-mediated selective autophagy is normally inactivated by A20. Cell Mol Life Sci 2012;69:963-79. [PMID: 21964925 DOI: 10.1007/s00018-011-0819-y] [Cited by in Crossref: 61] [Cited by in F6Publishing: 61] [Article Influence: 6.1] [Reference Citation Analysis]
4 Hamazaki J, Iemura S, Natsume T, Yashiroda H, Tanaka K, Murata S. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J 2006;25:4524-36. [PMID: 16990800 DOI: 10.1038/sj.emboj.7601338] [Cited by in Crossref: 190] [Cited by in F6Publishing: 176] [Article Influence: 12.7] [Reference Citation Analysis]
5 Fedoce ADG, Ferreira F, Bota RG, Bonet-Costa V, Sun PY, Davies KJA. The role of oxidative stress in anxiety disorder: cause or consequence? Free Radic Res 2018;52:737-50. [PMID: 29742940 DOI: 10.1080/10715762.2018.1475733] [Cited by in Crossref: 45] [Cited by in F6Publishing: 35] [Article Influence: 15.0] [Reference Citation Analysis]
6 Piccinini M, Tazartes O, Mezzatesta C, Ricotti E, Bedino S, Grosso F, Dianzani U, Tovo PA, Mostert M, Musso A, Rinaudo MT. Proteasomes are a target of the anti-tumour drug vinblastine. Biochem J 2001;356:835-41. [PMID: 11389692 DOI: 10.1042/0264-6021:3560835] [Cited by in Crossref: 9] [Cited by in F6Publishing: 11] [Article Influence: 0.5] [Reference Citation Analysis]
7 McCarthy MK, Weinberg JB. The immunoproteasome and viral infection: a complex regulator of inflammation. Front Microbiol 2015;6:21. [PMID: 25688236 DOI: 10.3389/fmicb.2015.00021] [Cited by in Crossref: 79] [Cited by in F6Publishing: 78] [Article Influence: 13.2] [Reference Citation Analysis]
8 Chiu HW, Chang JS, Lin HY, Lee HH, Kuei CH, Lin CH, Huang HM, Lin YF. FBXL7 Upregulation Predicts a Poor Prognosis and Associates with a Possible Mechanism for Paclitaxel Resistance in Ovarian Cancer. J Clin Med 2018;7:E330. [PMID: 30301218 DOI: 10.3390/jcm7100330] [Cited by in Crossref: 5] [Cited by in F6Publishing: 7] [Article Influence: 1.7] [Reference Citation Analysis]
9 Ibrahim Z, Martel A, Moulin M, Kim HS, Härtlein M, Franzetti B, Gabel F. Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase. Sci Rep 2017;7:40948. [PMID: 28102317 DOI: 10.1038/srep40948] [Cited by in Crossref: 20] [Cited by in F6Publishing: 17] [Article Influence: 5.0] [Reference Citation Analysis]
10 Fang Q, Andrews J, Sharma N, Wilk A, Clark J, Slyskova J, Koczor CA, Lans H, Prakash A, Sobol RW. Stability and sub-cellular localization of DNA polymerase β is regulated by interactions with NQO1 and XRCC1 in response to oxidative stress. Nucleic Acids Res 2019;47:6269-86. [PMID: 31287140 DOI: 10.1093/nar/gkz293] [Cited by in Crossref: 7] [Cited by in F6Publishing: 5] [Article Influence: 7.0] [Reference Citation Analysis]
11 Yoshioka M, Nakayama Y, Yoshida M, Ohashi K, Morita N, Kobayashi H, Yamamoto Y. Quality control of photosystem II: FtsH hexamers are localized near photosystem II at grana for the swift repair of damage. J Biol Chem 2010;285:41972-81. [PMID: 20921219 DOI: 10.1074/jbc.M110.117432] [Cited by in Crossref: 31] [Cited by in F6Publishing: 13] [Article Influence: 2.8] [Reference Citation Analysis]
12 Mi-Ichi F, Yoshida H, Hamano S. Entamoeba Encystation: New Targets to Prevent the Transmission of Amebiasis. PLoS Pathog 2016;12:e1005845. [PMID: 27764256 DOI: 10.1371/journal.ppat.1005845] [Cited by in Crossref: 27] [Cited by in F6Publishing: 25] [Article Influence: 5.4] [Reference Citation Analysis]
13 Lasker K, Förster F, Bohn S, Walzthoeni T, Villa E, Unverdorben P, Beck F, Aebersold R, Sali A, Baumeister W. Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci U S A 2012;109:1380-7. [PMID: 22307589 DOI: 10.1073/pnas.1120559109] [Cited by in Crossref: 378] [Cited by in F6Publishing: 343] [Article Influence: 42.0] [Reference Citation Analysis]
14 Raynes R, Pomatto LC, Davies KJ. Degradation of oxidized proteins by the proteasome: Distinguishing between the 20S, 26S, and immunoproteasome proteolytic pathways. Mol Aspects Med 2016;50:41-55. [PMID: 27155164 DOI: 10.1016/j.mam.2016.05.001] [Cited by in Crossref: 115] [Cited by in F6Publishing: 103] [Article Influence: 23.0] [Reference Citation Analysis]
15 Sugiyama M, Kurimoto E, Yagi H, Mori K, Fukunaga T, Hirai M, Zaccai G, Kato K. Kinetic asymmetry of subunit exchange of homooligomeric protein as revealed by deuteration-assisted small-angle neutron scattering. Biophys J 2011;101:2037-42. [PMID: 22004758 DOI: 10.1016/j.bpj.2011.09.004] [Cited by in Crossref: 20] [Cited by in F6Publishing: 18] [Article Influence: 2.2] [Reference Citation Analysis]
16 Mei Z, Wang F, Qi Y, Zhou Z, Hu Q, Li H, Wu J, Shi Y. Molecular determinants of MecA as a degradation tag for the ClpCP protease. J Biol Chem 2009;284:34366-75. [PMID: 19767395 DOI: 10.1074/jbc.M109.053017] [Cited by in Crossref: 22] [Cited by in F6Publishing: 16] [Article Influence: 1.8] [Reference Citation Analysis]
17 Koulich E, Li X, DeMartino GN. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol Biol Cell 2008;19:1072-82. [PMID: 18162577 DOI: 10.1091/mbc.e07-10-1040] [Cited by in Crossref: 161] [Cited by in F6Publishing: 124] [Article Influence: 11.5] [Reference Citation Analysis]
18 Kwon YT, Balogh SA, Davydov IV, Kashina AS, Yoon JK, Xie Y, Gaur A, Hyde L, Denenberg VH, Varshavsky A. Altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway. Mol Cell Biol 2000;20:4135-48. [PMID: 10805755 DOI: 10.1128/MCB.20.11.4135-4148.2000] [Cited by in Crossref: 78] [Cited by in F6Publishing: 40] [Article Influence: 3.7] [Reference Citation Analysis]
19 Touitou R, Richardson J, Bose S, Nakanishi M, Rivett J, Allday MJ. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. EMBO J 2001;20:2367-75. [PMID: 11350925 DOI: 10.1093/emboj/20.10.2367] [Cited by in Crossref: 170] [Cited by in F6Publishing: 170] [Article Influence: 8.5] [Reference Citation Analysis]
20 Rennella E, Huang R, Yu Z, Kay LE. Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMR. Proc Natl Acad Sci U S A 2020;117:5298-309. [PMID: 32094174 DOI: 10.1073/pnas.1920770117] [Cited by in Crossref: 7] [Cited by in F6Publishing: 5] [Article Influence: 7.0] [Reference Citation Analysis]
21 Fiumera AC, Dumont BL, Clark AG. Natural variation in male-induced 'cost-of-mating' and allele-specific association with male reproductive genes in Drosophila melanogaster. Philos Trans R Soc Lond B Biol Sci 2006;361:355-61. [PMID: 16612893 DOI: 10.1098/rstb.2005.1791] [Cited by in Crossref: 24] [Cited by in F6Publishing: 21] [Article Influence: 1.6] [Reference Citation Analysis]
22 Fu X, Tan L, Liu S, Li H, Chen L, Qin J, Wu M, Wang H. A novel diagnostic marker, p28GANK distinguishes hepatocellular carcinoma from potential mimics. J Cancer Res Clin Oncol 2004;130:514-20. [PMID: 15221469 DOI: 10.1007/s00432-004-0562-y] [Cited by in Crossref: 6] [Cited by in F6Publishing: 5] [Article Influence: 0.4] [Reference Citation Analysis]
23 Santoro AM, Cunsolo A, D'Urso A, Sbardella D, Tundo GR, Ciaccio C, Coletta M, Diana D, Fattorusso R, Persico M, Di Dato A, Fattorusso C, Milardi D, Purrello R. Cationic porphyrins are tunable gatekeepers of the 20S proteasome. Chem Sci 2016;7:1286-97. [PMID: 29910886 DOI: 10.1039/c5sc03312h] [Cited by in Crossref: 23] [Cited by in F6Publishing: 6] [Article Influence: 3.8] [Reference Citation Analysis]
24 Bonet-Costa V, Pomatto LC, Davies KJ. The Proteasome and Oxidative Stress in Alzheimer's Disease. Antioxid Redox Signal 2016;25:886-901. [PMID: 27392670 DOI: 10.1089/ars.2016.6802] [Cited by in Crossref: 44] [Cited by in F6Publishing: 41] [Article Influence: 8.8] [Reference Citation Analysis]
25 Esaki M, Johjima-Murata A, Islam MT, Ogura T. Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase. Front Mol Biosci 2018;5:56. [PMID: 29951484 DOI: 10.3389/fmolb.2018.00056] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 2.3] [Reference Citation Analysis]
26 de Jesus AA, Canna SW, Liu Y, Goldbach-Mansky R. Molecular mechanisms in genetically defined autoinflammatory diseases: disorders of amplified danger signaling. Annu Rev Immunol 2015;33:823-74. [PMID: 25706096 DOI: 10.1146/annurev-immunol-032414-112227] [Cited by in Crossref: 173] [Cited by in F6Publishing: 137] [Article Influence: 28.8] [Reference Citation Analysis]
27 Wigley WC, Fabunmi RP, Lee MG, Marino CR, Muallem S, DeMartino GN, Thomas PJ. Dynamic association of proteasomal machinery with the centrosome. J Cell Biol 1999;145:481-90. [PMID: 10225950 DOI: 10.1083/jcb.145.3.481] [Cited by in Crossref: 362] [Cited by in F6Publishing: 354] [Article Influence: 16.5] [Reference Citation Analysis]
28 Li X, Kusmierczyk AR, Wong P, Emili A, Hochstrasser M. beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J 2007;26:2339-49. [PMID: 17431397 DOI: 10.1038/sj.emboj.7601681] [Cited by in Crossref: 109] [Cited by in F6Publishing: 104] [Article Influence: 7.8] [Reference Citation Analysis]
29 Pearce MJ, Arora P, Festa RA, Butler-Wu SM, Gokhale RS, Darwin KH. Identification of substrates of the Mycobacterium tuberculosis proteasome. EMBO J 2006;25:5423-32. [PMID: 17082771 DOI: 10.1038/sj.emboj.7601405] [Cited by in Crossref: 82] [Cited by in F6Publishing: 77] [Article Influence: 5.5] [Reference Citation Analysis]
30 Turnell AS, Grand RJ, Gorbea C, Zhang X, Wang W, Mymryk JS, Gallimore PH. Regulation of the 26S proteasome by adenovirus E1A. EMBO J 2000;19:4759-73. [PMID: 10970867 DOI: 10.1093/emboj/19.17.4759] [Cited by in Crossref: 62] [Cited by in F6Publishing: 62] [Article Influence: 3.0] [Reference Citation Analysis]
31 Tan Y, Jin Y, Wu X, Ren Z. PSMD1 and PSMD2 regulate HepG2 cell proliferation and apoptosis via modulating cellular lipid droplet metabolism. BMC Mol Biol 2019;20:24. [PMID: 31703613 DOI: 10.1186/s12867-019-0141-z] [Cited by in Crossref: 11] [Cited by in F6Publishing: 7] [Article Influence: 5.5] [Reference Citation Analysis]
32 Höti N, Shah P, Hu Y, Yang S, Zhang H. Proteomics analyses of prostate cancer cells reveal cellular pathways associated with androgen resistance. Proteomics 2017;17. [PMID: 28116790 DOI: 10.1002/pmic.201600228] [Cited by in Crossref: 10] [Cited by in F6Publishing: 4] [Article Influence: 2.5] [Reference Citation Analysis]
33 Inobe T, Fishbain S, Prakash S, Matouschek A. Defining the geometry of the two-component proteasome degron. Nat Chem Biol 2011;7:161-7. [PMID: 21278740 DOI: 10.1038/nchembio.521] [Cited by in Crossref: 123] [Cited by in F6Publishing: 111] [Article Influence: 12.3] [Reference Citation Analysis]
34 Maculins T, Fiskin E, Bhogaraju S, Dikic I. Bacteria-host relationship: ubiquitin ligases as weapons of invasion. Cell Res 2016;26:499-510. [PMID: 26964724 DOI: 10.1038/cr.2016.30] [Cited by in Crossref: 67] [Cited by in F6Publishing: 58] [Article Influence: 13.4] [Reference Citation Analysis]
35 Fu H, Girod PA, Doelling JH, van Nocker S, Hochstrasser M, Finley D, Vierstra RD. Structure and functional analysis of the 26S proteasome subunits from plants. Mol Biol Rep 1999;26:137-46. [PMID: 10363660 DOI: 10.1023/a:1006926322501] [Cited by in Crossref: 31] [Cited by in F6Publishing: 13] [Article Influence: 1.4] [Reference Citation Analysis]
36 Rajan V, Mitch WE. Ubiquitin, proteasomes and proteolytic mechanisms activated by kidney disease. Biochim Biophys Acta 2008;1782:795-9. [PMID: 18723090 DOI: 10.1016/j.bbadis.2008.07.007] [Cited by in Crossref: 27] [Cited by in F6Publishing: 22] [Article Influence: 2.1] [Reference Citation Analysis]
37 Princiotta MF, Schubert U, Chen W, Bennink JR, Myung J, Crews CM, Yewdell JW. Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival. Proc Natl Acad Sci U S A 2001;98:513-8. [PMID: 11149939 DOI: 10.1073/pnas.021132398] [Cited by in Crossref: 26] [Cited by in F6Publishing: 36] [Article Influence: 1.3] [Reference Citation Analysis]
38 Li S, Jiang C, Pan J, Wang X, Jin J, Zhao L, Pan W, Liao G, Cai X, Li X, Xiao J, Jiang J, Wang P. Regulation of c-Myc protein stability by proteasome activator REGγ. Cell Death Differ 2015;22:1000-11. [PMID: 25412630 DOI: 10.1038/cdd.2014.188] [Cited by in Crossref: 28] [Cited by in F6Publishing: 24] [Article Influence: 4.0] [Reference Citation Analysis]
39 Velichutina I, Connerly PL, Arendt CS, Li X, Hochstrasser M. Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. EMBO J 2004;23:500-10. [PMID: 14739934 DOI: 10.1038/sj.emboj.7600059] [Cited by in Crossref: 71] [Cited by in F6Publishing: 62] [Article Influence: 4.2] [Reference Citation Analysis]
40 Forouzan D, Ammelburg M, Hobel CF, Ströh LJ, Sessler N, Martin J, Lupas AN. The archaeal proteasome is regulated by a network of AAA ATPases. J Biol Chem 2012;287:39254-62. [PMID: 22992741 DOI: 10.1074/jbc.M112.386458] [Cited by in Crossref: 36] [Cited by in F6Publishing: 21] [Article Influence: 4.0] [Reference Citation Analysis]
41 Minis A, Rodriguez JA, Levin A, Liu K, Govek EE, Hatten ME, Steller H. The proteasome regulator PI31 is required for protein homeostasis, synapse maintenance, and neuronal survival in mice. Proc Natl Acad Sci U S A 2019;116:24639-50. [PMID: 31754024 DOI: 10.1073/pnas.1911921116] [Cited by in Crossref: 8] [Cited by in F6Publishing: 7] [Article Influence: 4.0] [Reference Citation Analysis]
42 Peterson-Kaufman KJ, Carlson CD, Rodríguez-Martínez JA, Ansari AZ. Nucleating the assembly of macromolecular complexes. Chembiochem 2010;11:1955-62. [PMID: 20812316 DOI: 10.1002/cbic.201000255] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 0.6] [Reference Citation Analysis]
43 Höhfeld J, Cyr DM, Patterson C. From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep. 2001;2:885-890. [PMID: 11600451 DOI: 10.1093/embo-reports/kve206] [Cited by in Crossref: 245] [Cited by in F6Publishing: 234] [Article Influence: 12.9] [Reference Citation Analysis]
44 Ozcan S, Kazi A, Marsilio F, Fang B, Guida WC, Koomen J, Lawrence HR, Sebti SM. Oxadiazole-isopropylamides as potent and noncovalent proteasome inhibitors. J Med Chem 2013;56:3783-805. [PMID: 23547706 DOI: 10.1021/jm400221d] [Cited by in Crossref: 22] [Cited by in F6Publishing: 21] [Article Influence: 2.8] [Reference Citation Analysis]
45 Lafarga M, Berciano MT, Pena E, Mayo I, Castaño JG, Bohmann D, Rodrigues JP, Tavanez JP, Carmo-Fonseca M. Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome. Mol Biol Cell 2002;13:2771-82. [PMID: 12181345 DOI: 10.1091/mbc.e02-03-0122] [Cited by in Crossref: 96] [Cited by in F6Publishing: 75] [Article Influence: 5.3] [Reference Citation Analysis]
46 Fourie KR, Wilson HL. Understanding GroEL and DnaK Stress Response Proteins as Antigens for Bacterial Diseases. Vaccines (Basel) 2020;8:E773. [PMID: 33348708 DOI: 10.3390/vaccines8040773] [Cited by in Crossref: 4] [Cited by in F6Publishing: 6] [Article Influence: 4.0] [Reference Citation Analysis]
47 Shi L, Kay LE. Tracing an allosteric pathway regulating the activity of the HslV protease. Proc Natl Acad Sci U S A 2014;111:2140-5. [PMID: 24469799 DOI: 10.1073/pnas.1318476111] [Cited by in Crossref: 57] [Cited by in F6Publishing: 52] [Article Influence: 8.1] [Reference Citation Analysis]
48 Kaczowka SJ, Maupin-Furlow JA. Subunit topology of two 20S proteasomes from Haloferax volcanii. J Bacteriol 2003;185:165-74. [PMID: 12486053 DOI: 10.1128/JB.185.1.165-174.2003] [Cited by in Crossref: 41] [Cited by in F6Publishing: 25] [Article Influence: 2.3] [Reference Citation Analysis]
49 Kwon YT, Reiss Y, Fried VA, Hershko A, Yoon JK, Gonda DK, Sangan P, Copeland NG, Jenkins NA, Varshavsky A. The mouse and human genes encoding the recognition component of the N-end rule pathway. Proc Natl Acad Sci U S A 1998;95:7898-903. [PMID: 9653112 DOI: 10.1073/pnas.95.14.7898] [Cited by in Crossref: 122] [Cited by in F6Publishing: 117] [Article Influence: 5.3] [Reference Citation Analysis]
50 Liu K, Jones S, Minis A, Rodriguez J, Molina H, Steller H. PI31 Is an Adaptor Protein for Proteasome Transport in Axons and Required for Synaptic Development. Dev Cell 2019;50:509-524.e10. [PMID: 31327739 DOI: 10.1016/j.devcel.2019.06.009] [Cited by in Crossref: 20] [Cited by in F6Publishing: 14] [Article Influence: 10.0] [Reference Citation Analysis]
51 Kitajima Y, Suzuki N, Nunomiya A, Osana S, Yoshioka K, Tashiro Y, Takahashi R, Ono Y, Aoki M, Nagatomi R. The Ubiquitin-Proteasome System Is Indispensable for the Maintenance of Muscle Stem Cells. Stem Cell Reports. 2018;11:1523-1538. [PMID: 30416048 DOI: 10.1016/j.stemcr.2018.10.009] [Cited by in Crossref: 24] [Cited by in F6Publishing: 25] [Article Influence: 8.0] [Reference Citation Analysis]
52 Tone Y, Toh-E A. Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae. Genes Dev. 2002;16:3142-3157. [PMID: 12502737 DOI: 10.1101/gad.1025602] [Cited by in Crossref: 56] [Cited by in F6Publishing: 58] [Article Influence: 3.1] [Reference Citation Analysis]
53 Dudek SE, Luig C, Pauli EK, Schubert U, Ludwig S. The clinically approved proteasome inhibitor PS-341 efficiently blocks influenza A virus and vesicular stomatitis virus propagation by establishing an antiviral state. J Virol 2010;84:9439-51. [PMID: 20592098 DOI: 10.1128/JVI.00533-10] [Cited by in Crossref: 36] [Cited by in F6Publishing: 19] [Article Influence: 3.3] [Reference Citation Analysis]
54 Gransee HM, Mantilla CB, Sieck GC. Respiratory muscle plasticity. Compr Physiol 2012;2:1441-62. [PMID: 23798306 DOI: 10.1002/cphy.c110050] [Cited by in Crossref: 4] [Cited by in F6Publishing: 12] [Article Influence: 0.5] [Reference Citation Analysis]
55 Shang F, Taylor A. Ubiquitin-proteasome pathway and cellular responses to oxidative stress. Free Radic Biol Med. 2011;51:5-16. [PMID: 21530648 DOI: 10.1016/j.freeradbiomed.2011.03.031] [Cited by in Crossref: 245] [Cited by in F6Publishing: 238] [Article Influence: 24.5] [Reference Citation Analysis]
56 Ah Kioon MD, Pierides M, Pannellini T, Lin G, Nathan CF, Barrat FJ. Noncytotoxic Inhibition of the Immunoproteasome Regulates Human Immune Cells In Vitro and Suppresses Cutaneous Inflammation in the Mouse. J Immunol 2021;206:1631-41. [PMID: 33674446 DOI: 10.4049/jimmunol.2000951] [Reference Citation Analysis]
57 Majetschak M, Zedler S, Romero J, Albright JM, Kraft R, Kovacs EJ, Faist E, Gamelli RL. Circulating proteasomes after burn injury. J Burn Care Res 2010;31:243-50. [PMID: 20182370 DOI: 10.1097/BCR.0b013e3181d0f55d] [Cited by in Crossref: 14] [Cited by in F6Publishing: 6] [Article Influence: 1.3] [Reference Citation Analysis]
58 Lehmann A, Jechow K, Enenkel C. Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep 2008;9:1237-43. [PMID: 18927584 DOI: 10.1038/embor.2008.190] [Cited by in Crossref: 46] [Cited by in F6Publishing: 47] [Article Influence: 3.5] [Reference Citation Analysis]
59 Gao Y, Lecker S, Post MJ, Hietaranta AJ, Li J, Volk R, Li M, Sato K, Saluja AK, Steer ML. Inhibition of ubiquitin-proteasome pathway-mediated I kappa B alpha degradation by a naturally occurring antibacterial peptide. J Clin Invest. 2000;106:439-448. [PMID: 10930447 DOI: 10.1172/jci9826] [Cited by in Crossref: 107] [Cited by in F6Publishing: 40] [Article Influence: 5.1] [Reference Citation Analysis]
60 Totaro KA, Barthelme D, Simpson PT, Jiang X, Lin G, Nathan CF, Sauer RT, Sello JK. Rational Design of Selective and Bioactive Inhibitors of the Mycobacterium tuberculosis Proteasome. ACS Infect Dis 2017;3:176-81. [PMID: 28183185 DOI: 10.1021/acsinfecdis.6b00172] [Cited by in Crossref: 16] [Cited by in F6Publishing: 14] [Article Influence: 3.2] [Reference Citation Analysis]
61 Yanaba K, Asano Y, Tada Y, Sugaya M, Kadono T, Sato S. Proteasome inhibitor bortezomib ameliorates intestinal injury in mice. PLoS One. 2012;7:e34587. [PMID: 22479648 DOI: 10.1371/journal.pone.0034587] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 1.0] [Reference Citation Analysis]
62 Shen Y, Hixson KK, Tolić N, Camp DG, Purvine SO, Moore RJ, Smith RD. Mass spectrometry analysis of proteome-wide proteolytic post-translational degradation of proteins. Anal Chem 2008;80:5819-28. [PMID: 18578501 DOI: 10.1021/ac800077w] [Cited by in Crossref: 12] [Cited by in F6Publishing: 11] [Article Influence: 0.9] [Reference Citation Analysis]
63 Blondel M, Galan JM, Chi Y, Lafourcade C, Longaretti C, Deshaies RJ, Peter M. Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4. EMBO J 2000;19:6085-97. [PMID: 11080155 DOI: 10.1093/emboj/19.22.6085] [Cited by in Crossref: 97] [Cited by in F6Publishing: 94] [Article Influence: 4.9] [Reference Citation Analysis]
64 Trader DJ, Simanski S, Dickson P, Kodadek T. Establishment of a suite of assays that support the discovery of proteasome stimulators. Biochim Biophys Acta Gen Subj 2017;1861:892-9. [PMID: 28065760 DOI: 10.1016/j.bbagen.2017.01.003] [Cited by in Crossref: 25] [Cited by in F6Publishing: 23] [Article Influence: 6.3] [Reference Citation Analysis]
65 Cheng Y. Toward an atomic model of the 26S proteasome. Curr Opin Struct Biol 2009;19:203-8. [PMID: 19286367 DOI: 10.1016/j.sbi.2009.02.004] [Cited by in Crossref: 29] [Cited by in F6Publishing: 28] [Article Influence: 2.4] [Reference Citation Analysis]
66 Kurucz E, Andó I, Sümegi M, Hölzl H, Kapelari B, Baumeister W, Udvardy A. Assembly of the Drosophila 26 S proteasome is accompanied by extensive subunit rearrangements. Biochem J 2002;365:527-36. [PMID: 11945175 DOI: 10.1042/BJ20011520] [Cited by in Crossref: 27] [Cited by in F6Publishing: 21] [Article Influence: 1.4] [Reference Citation Analysis]
67 Sula Karreci E, Fan H, Uehara M, Mihali AB, Singh PK, Kurdi AT, Solhjou Z, Riella LV, Ghobrial I, Laragione T, Routray S, Assaker JP, Wang R, Sukenick G, Shi L, Barrat FJ, Nathan CF, Lin G, Azzi J. Brief treatment with a highly selective immunoproteasome inhibitor promotes long-term cardiac allograft acceptance in mice. Proc Natl Acad Sci U S A 2016;113:E8425-32. [PMID: 27956634 DOI: 10.1073/pnas.1618548114] [Cited by in Crossref: 43] [Cited by in F6Publishing: 41] [Article Influence: 8.6] [Reference Citation Analysis]
68 Xu WW, Han MJ, Chen D, Chen L, Guo Y, Willden A, Liu DQ, Zhang HT. Genome-wide search for the genes accountable for the induced resistance to HIV-1 infection in activated CD4+ T cells: apparent transcriptional signatures, co-expression networks and possible cellular processes. BMC Med Genomics 2013;6:15. [PMID: 23635305 DOI: 10.1186/1755-8794-6-15] [Cited by in Crossref: 14] [Cited by in F6Publishing: 16] [Article Influence: 1.8] [Reference Citation Analysis]
69 Ren QG, Yu Y, Luo X, Jie XM, Pan DJ, Wang W. Characterization of proteasome inhibition on astrocytes cell cycle. J Mol Neurosci 2009;38:57-66. [PMID: 19067250 DOI: 10.1007/s12031-008-9161-8] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 0.4] [Reference Citation Analysis]
70 Nagy I, Banerjee T, Tamura T, Schoofs G, Gils A, Proost P, Tamura N, Baumeister W, De Mot R. Characterization of a novel intracellular endopeptidase of the alpha/beta hydrolase family from Streptomyces coelicolor A3(2). J Bacteriol 2003;185:496-503. [PMID: 12511496 DOI: 10.1128/JB.185.2.496-503.2003] [Cited by in Crossref: 9] [Cited by in F6Publishing: 4] [Article Influence: 0.5] [Reference Citation Analysis]
71 Ko JK, Choi CH, Kim YK, Kwon CH. The proteasome inhibitor MG-132 induces AIF nuclear translocation through down-regulation of ERK and Akt/mTOR pathway. Neurochem Res 2011;36:722-31. [PMID: 21203833 DOI: 10.1007/s11064-010-0387-9] [Cited by in Crossref: 10] [Cited by in F6Publishing: 11] [Article Influence: 1.0] [Reference Citation Analysis]
72 Burri L, Höckendorff J, Boehm U, Klamp T, Dohmen RJ, Lévy F. Identification and characterization of a mammalian protein interacting with 20S proteasome precursors. Proc Natl Acad Sci U S A 2000;97:10348-53. [PMID: 10973495 DOI: 10.1073/pnas.190268597] [Cited by in Crossref: 69] [Cited by in F6Publishing: 66] [Article Influence: 3.3] [Reference Citation Analysis]
73 Neefjes J, Dantuma NP. Fluorescent probes for proteolysis: tools for drug discovery. Nat Rev Drug Discov 2004;3:58-69. [PMID: 14708021 DOI: 10.1038/nrd1282] [Cited by in Crossref: 74] [Cited by in F6Publishing: 66] [Article Influence: 4.4] [Reference Citation Analysis]
74 Kostova Z, Wolf DH. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 2003;22:2309-17. [PMID: 12743025 DOI: 10.1093/emboj/cdg227] [Cited by in Crossref: 321] [Cited by in F6Publishing: 299] [Article Influence: 17.8] [Reference Citation Analysis]
75 Kozai T, Sekiguchi T, Satoh T, Yagi H, Kato K, Uchihashi T. Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy. Sci Rep 2017;7:15373. [PMID: 29133893 DOI: 10.1038/s41598-017-15708-8] [Cited by in Crossref: 10] [Cited by in F6Publishing: 8] [Article Influence: 2.5] [Reference Citation Analysis]
76 Roti Roti EC, Ringelstetter AK, Kropp J, Abbott DH, Salih SM. Bortezomib prevents acute doxorubicin ovarian insult and follicle demise, improving the fertility window and pup birth weight in mice. PLoS One 2014;9:e108174. [PMID: 25251158 DOI: 10.1371/journal.pone.0108174] [Cited by in Crossref: 24] [Cited by in F6Publishing: 20] [Article Influence: 3.4] [Reference Citation Analysis]
77 Inostroza-Nieves Y, Venkatraman P, Zavala-Ruiz Z. Role of Sug1, a 19S proteasome ATPase, in the transcription of MHC I and the atypical MHC II molecules, HLA-DM and HLA-DO. Immunol Lett 2012;147:67-74. [PMID: 22771340 DOI: 10.1016/j.imlet.2012.06.005] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 0.6] [Reference Citation Analysis]
78 Beenukumar RR, Gödderz D, Palanimurugan R, Dohmen RJ. Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome. Microb Cell 2015;2:197-207. [PMID: 28357293 DOI: 10.15698/mic2015.06.206] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 1.3] [Reference Citation Analysis]
79 Gilfoy F, Fayzulin R, Mason PW. West Nile virus genome amplification requires the functional activities of the proteasome. Virology. 2009;385:74-84. [PMID: 19101004 DOI: 10.1016/j.virol.2008.11.034] [Cited by in Crossref: 28] [Cited by in F6Publishing: 27] [Article Influence: 2.2] [Reference Citation Analysis]
80 Lin G, Chidawanyika T, Tsu C, Warrier T, Vaubourgeix J, Blackburn C, Gigstad K, Sintchak M, Dick L, Nathan C. N,C-Capped dipeptides with selectivity for mycobacterial proteasome over human proteasomes: role of S3 and S1 binding pockets. J Am Chem Soc 2013;135:9968-71. [PMID: 23782398 DOI: 10.1021/ja400021x] [Cited by in Crossref: 41] [Cited by in F6Publishing: 35] [Article Influence: 5.1] [Reference Citation Analysis]
81 Archer CT, Kodadek T. The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases. Nucleic Acids Res 2010;38:789-96. [PMID: 19939937 DOI: 10.1093/nar/gkp1066] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 0.7] [Reference Citation Analysis]
82 Cascio P. PA28αβ: the enigmatic magic ring of the proteasome? Biomolecules 2014;4:566-84. [PMID: 24970231 DOI: 10.3390/biom4020566] [Cited by in Crossref: 56] [Cited by in F6Publishing: 50] [Article Influence: 8.0] [Reference Citation Analysis]
83 Holzhütter HG, Kloetzel PM. A kinetic model of vertebrate 20S proteasome accounting for the generation of major proteolytic fragments from oligomeric peptide substrates. Biophys J 2000;79:1196-205. [PMID: 10968984 DOI: 10.1016/S0006-3495(00)76374-0] [Cited by in Crossref: 60] [Cited by in F6Publishing: 23] [Article Influence: 2.9] [Reference Citation Analysis]
84 Lima WR, Holder AA, Garcia CR. Melatonin signaling and its modulation of PfNF-YB transcription factor expression in Plasmodium falciparum. Int J Mol Sci 2013;14:13704-18. [PMID: 23839089 DOI: 10.3390/ijms140713704] [Cited by in Crossref: 12] [Cited by in F6Publishing: 11] [Article Influence: 1.5] [Reference Citation Analysis]
85 Zhang M, Pickart CM, Coffino P. Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J 2003;22:1488-96. [PMID: 12660156 DOI: 10.1093/emboj/cdg158] [Cited by in Crossref: 151] [Cited by in F6Publishing: 142] [Article Influence: 8.4] [Reference Citation Analysis]
86 Graciet E, Hu RG, Piatkov K, Rhee JH, Schwarz EM, Varshavsky A. Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen. Proc Natl Acad Sci U S A 2006;103:3078-83. [PMID: 16492767 DOI: 10.1073/pnas.0511224103] [Cited by in Crossref: 67] [Cited by in F6Publishing: 62] [Article Influence: 4.5] [Reference Citation Analysis]
87 Willems AR, Goh T, Taylor L, Chernushevich I, Shevchenko A, Tyers M. SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis. Philos Trans R Soc Lond B Biol Sci 1999;354:1533-50. [PMID: 10582239 DOI: 10.1098/rstb.1999.0497] [Cited by in Crossref: 99] [Cited by in F6Publishing: 94] [Article Influence: 4.7] [Reference Citation Analysis]
88 Bohn S, Beck F, Sakata E, Walzthoeni T, Beck M, Aebersold R, Förster F, Baumeister W, Nickell S. Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution. Proc Natl Acad Sci U S A 2010;107:20992-7. [PMID: 21098295 DOI: 10.1073/pnas.1015530107] [Cited by in Crossref: 116] [Cited by in F6Publishing: 107] [Article Influence: 10.5] [Reference Citation Analysis]
89 Cappellazzo G, Lanfranco L, Bonfante P. A limiting source of organic nitrogen induces specific transcriptional responses in the extraradical structures of the endomycorrhizal fungus Glomus intraradices. Curr Genet 2007;51:59-70. [PMID: 17061094 DOI: 10.1007/s00294-006-0101-2] [Cited by in Crossref: 16] [Cited by in F6Publishing: 14] [Article Influence: 1.1] [Reference Citation Analysis]
90 Hilbi H, Puro RJ, Zychlinsky A. Tripeptidyl peptidase II promotes maturation of caspase-1 in Shigella flexneri-induced macrophage apoptosis. Infect Immun 2000;68:5502-8. [PMID: 10992446 DOI: 10.1128/IAI.68.10.5502-5508.2000] [Cited by in Crossref: 36] [Cited by in F6Publishing: 12] [Article Influence: 1.7] [Reference Citation Analysis]
91 Simkus C, Makiya M, Jones JM. Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase. Mol Immunol 2009;46:1319-25. [PMID: 19118899 DOI: 10.1016/j.molimm.2008.11.009] [Cited by in Crossref: 21] [Cited by in F6Publishing: 19] [Article Influence: 1.6] [Reference Citation Analysis]
92 Türker F, Cook EK, Margolis SS. The proteasome and its role in the nervous system. Cell Chem Biol 2021;28:903-17. [PMID: 33905676 DOI: 10.1016/j.chembiol.2021.04.003] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
93 Cai ZP, Shen Z, Van Kaer L, Becker LC. Ischemic preconditioning-induced cardioprotection is lost in mice with immunoproteasome subunit low molecular mass polypeptide-2 deficiency. FASEB J 2008;22:4248-57. [PMID: 18728217 DOI: 10.1096/fj.08-105940] [Cited by in Crossref: 42] [Cited by in F6Publishing: 45] [Article Influence: 3.2] [Reference Citation Analysis]
94 Rothman S. How is the balance between protein synthesis and degradation achieved? Theor Biol Med Model 2010;7:25. [PMID: 20573219 DOI: 10.1186/1742-4682-7-25] [Cited by in Crossref: 28] [Cited by in F6Publishing: 28] [Article Influence: 2.5] [Reference Citation Analysis]
95 Valmori D, Gileadi U, Servis C, Dunbar PR, Cerottini JC, Romero P, Cerundolo V, Lévy F. Modulation of proteasomal activity required for the generation of a cytotoxic T lymphocyte-defined peptide derived from the tumor antigen MAGE-3. J Exp Med 1999;189:895-906. [PMID: 10075973 DOI: 10.1084/jem.189.6.895] [Cited by in Crossref: 90] [Cited by in F6Publishing: 86] [Article Influence: 4.1] [Reference Citation Analysis]
96 Kwon YT, Kashina AS, Varshavsky A. Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Mol Cell Biol 1999;19:182-93. [PMID: 9858543 DOI: 10.1128/MCB.19.1.182] [Cited by in Crossref: 89] [Cited by in F6Publishing: 65] [Article Influence: 4.0] [Reference Citation Analysis]
97 Zollner TM, Podda M, Pien C, Elliott PJ, Kaufmann R, Boehncke WH. Proteasome inhibition reduces superantigen-mediated T cell activation and the severity of psoriasis in a SCID-hu model. J Clin Invest 2002;109:671-9. [PMID: 11877475 DOI: 10.1172/JCI12736] [Cited by in F6Publishing: 19] [Reference Citation Analysis]
98 Koizumi S, Hamazaki J, Murata S. Transcriptional regulation of the 26S proteasome by Nrf1. Proc Jpn Acad Ser B Phys Biol Sci 2018;94:325-36. [PMID: 30305478 DOI: 10.2183/pjab.94.021] [Cited by in Crossref: 14] [Cited by in F6Publishing: 12] [Article Influence: 4.7] [Reference Citation Analysis]
99 Qin JM, Fu XY, Li SJ, Liu SQ, Zeng JZ, Qiu XH, Wu MC, Wang HY. Gene and protein expressions of p28GANK in rat with liver regeneration. World J Gastroenterol 2003; 9(11): 2523-2527 [PMID: 14606089 DOI: 10.3748/wjg.v9.i11.2523] [Cited by in CrossRef: 10] [Cited by in F6Publishing: 7] [Article Influence: 0.6] [Reference Citation Analysis]
100 Yedidi RS, Wendler P, Enenkel C. AAA-ATPases in Protein Degradation. Front Mol Biosci 2017;4:42. [PMID: 28676851 DOI: 10.3389/fmolb.2017.00042] [Cited by in Crossref: 25] [Cited by in F6Publishing: 22] [Article Influence: 6.3] [Reference Citation Analysis]
101 Kim I, Mi K, Rao H. Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol Biol Cell 2004;15:3357-65. [PMID: 15121879 DOI: 10.1091/mbc.e03-11-0835] [Cited by in Crossref: 120] [Cited by in F6Publishing: 92] [Article Influence: 7.1] [Reference Citation Analysis]
102 Motosugi R, Murata S. Dynamic Regulation of Proteasome Expression. Front Mol Biosci 2019;6:30. [PMID: 31119134 DOI: 10.3389/fmolb.2019.00030] [Cited by in Crossref: 20] [Cited by in F6Publishing: 17] [Article Influence: 10.0] [Reference Citation Analysis]
103 Varshavsky A. The early history of the ubiquitin field. Protein Sci 2006;15:647-54. [PMID: 16501229 DOI: 10.1110/ps.052012306] [Cited by in Crossref: 51] [Cited by in F6Publishing: 47] [Article Influence: 3.4] [Reference Citation Analysis]
104 Min JN, Patterson C. Evaluating age-associated phenotypes in a mouse model of protein dyshomeostasis. Methods 2011;53:187-93. [PMID: 21167942 DOI: 10.1016/j.ymeth.2010.12.012] [Reference Citation Analysis]
105 Jäger S, Strayle J, Heinemeyer W, Wolf DH. Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4. EMBO J 2001;20:4423-31. [PMID: 11500370 DOI: 10.1093/emboj/20.16.4423] [Cited by in Crossref: 35] [Cited by in F6Publishing: 34] [Article Influence: 1.8] [Reference Citation Analysis]
106 Koodathingal P, Jaffe NE, Kraut DA, Prakash S, Fishbain S, Herman C, Matouschek A. ATP-dependent proteases differ substantially in their ability to unfold globular proteins. J Biol Chem 2009;284:18674-84. [PMID: 19383601 DOI: 10.1074/jbc.M900783200] [Cited by in Crossref: 58] [Cited by in F6Publishing: 43] [Article Influence: 4.8] [Reference Citation Analysis]
107 Kanamori H, Takemura G, Maruyama R, Goto K, Tsujimoto A, Ogino A, Li L, Kawamura I, Takeyama T, Kawaguchi T, Nagashima K, Fujiwara T, Fujiwara H, Seishima M, Minatoguchi S. Functional significance and morphological characterization of starvation-induced autophagy in the adult heart. Am J Pathol 2009;174:1705-14. [PMID: 19342365 DOI: 10.2353/ajpath.2009.080875] [Cited by in Crossref: 90] [Cited by in F6Publishing: 84] [Article Influence: 7.5] [Reference Citation Analysis]
108 Cerruti F, Jocollè G, Salio C, Oliva L, Paglietti L, Alessandria B, Mioletti S, Donati G, Numico G, Cenci S, Cascio P. Proteasome stress sensitizes malignant pleural mesothelioma cells to bortezomib-induced apoptosis. Sci Rep 2017;7:17626. [PMID: 29247244 DOI: 10.1038/s41598-017-17977-9] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis]
109 Verdoes M, Florea BI, Hillaert U, Willems LI, van der Linden WA, Sae-Heng M, Filippov DV, Kisselev AF, van der Marel GA, Overkleeft HS. Azido-BODIPY acid reveals quantitative Staudinger-Bertozzi ligation in two-step activity-based proteasome profiling. Chembiochem 2008;9:1735-8. [PMID: 18600815 DOI: 10.1002/cbic.200800231] [Cited by in Crossref: 43] [Cited by in F6Publishing: 41] [Article Influence: 3.3] [Reference Citation Analysis]
110 Wehmer M, Rudack T, Beck F, Aufderheide A, Pfeifer G, Plitzko JM, Förster F, Schulten K, Baumeister W, Sakata E. Structural insights into the functional cycle of the ATPase module of the 26S proteasome. Proc Natl Acad Sci U S A 2017;114:1305-10. [PMID: 28115689 DOI: 10.1073/pnas.1621129114] [Cited by in Crossref: 105] [Cited by in F6Publishing: 87] [Article Influence: 26.3] [Reference Citation Analysis]
111 Lichter DI, Danaee H, Pickard MD, Tayber O, Sintchak M, Shi H, Richardson PG, Cavenagh J, Bladé J, Façon T, Niesvizky R, Alsina M, Dalton W, Sonneveld P, Lonial S, van de Velde H, Ricci D, Esseltine DL, Trepicchio WL, Mulligan G, Anderson KC. Sequence analysis of β-subunit genes of the 20S proteasome in patients with relapsed multiple myeloma treated with bortezomib or dexamethasone. Blood 2012;120:4513-6. [PMID: 23018640 DOI: 10.1182/blood-2012-05-426924] [Cited by in Crossref: 49] [Cited by in F6Publishing: 43] [Article Influence: 5.4] [Reference Citation Analysis]
112 Hwang LY, Lieu PT, Peterson PA, Yang Y. Functional regulation of immunoproteasomes and transporter associated with antigen processing. Immunol Res 2001;24:245-72. [PMID: 11817324 DOI: 10.1385/IR:24:3:245] [Cited by in Crossref: 11] [Cited by in F6Publishing: 3] [Article Influence: 0.6] [Reference Citation Analysis]
113 Driscoll JJ, Pelluru D, Lefkimmiatis K, Fulciniti M, Prabhala RH, Greipp PR, Barlogie B, Tai YT, Anderson KC, Shaughnessy JD Jr, Annunziata CM, Munshi NC. The sumoylation pathway is dysregulated in multiple myeloma and is associated with adverse patient outcome. Blood 2010;115:2827-34. [PMID: 19965618 DOI: 10.1182/blood-2009-03-211045] [Cited by in Crossref: 77] [Cited by in F6Publishing: 72] [Article Influence: 6.4] [Reference Citation Analysis]
114 Pickering AM, Davies KJ. Degradation of damaged proteins: the main function of the 20S proteasome. Prog Mol Biol Transl Sci 2012;109:227-48. [PMID: 22727423 DOI: 10.1016/B978-0-12-397863-9.00006-7] [Cited by in Crossref: 104] [Cited by in F6Publishing: 68] [Article Influence: 13.0] [Reference Citation Analysis]
115 Liu CW, Li X, Thompson D, Wooding K, Chang TL, Tang Z, Yu H, Thomas PJ, DeMartino GN. ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome. Mol Cell 2006;24:39-50. [PMID: 17018291 DOI: 10.1016/j.molcel.2006.08.025] [Cited by in Crossref: 135] [Cited by in F6Publishing: 124] [Article Influence: 9.0] [Reference Citation Analysis]
116 Zhang X, Min KW, Wimalasena J, Baek SJ. Cyclin D1 degradation and p21 induction contribute to growth inhibition of colorectal cancer cells induced by epigallocatechin-3-gallate. J Cancer Res Clin Oncol 2012;138:2051-60. [PMID: 22814742 DOI: 10.1007/s00432-012-1276-1] [Cited by in Crossref: 29] [Cited by in F6Publishing: 24] [Article Influence: 3.2] [Reference Citation Analysis]
117 Medalia N, Beer A, Zwickl P, Mihalache O, Beck M, Medalia O, Navon A. Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase. J Biol Chem 2009;284:22952-60. [PMID: 19363223 DOI: 10.1074/jbc.M809643200] [Cited by in Crossref: 12] [Cited by in F6Publishing: 10] [Article Influence: 1.0] [Reference Citation Analysis]
118 Vale RD. AAA proteins. Lords of the ring. J Cell Biol 2000;150:F13-9. [PMID: 10893253 DOI: 10.1083/jcb.150.1.f13] [Cited by in Crossref: 394] [Cited by in F6Publishing: 153] [Article Influence: 18.8] [Reference Citation Analysis]
119 Haugen AC, Kelley R, Collins JB, Tucker CJ, Deng C, Afshari CA, Brown JM, Ideker T, Van Houten B. Integrating phenotypic and expression profiles to map arsenic-response networks. Genome Biol 2004;5:R95. [PMID: 15575969 DOI: 10.1186/gb-2004-5-12-r95] [Cited by in Crossref: 133] [Cited by in F6Publishing: 126] [Article Influence: 7.8] [Reference Citation Analysis]
120 Baumeister W. A voyage to the inner space of cells. Protein Sci 2005;14:257-69. [PMID: 15608126 DOI: 10.1110/ps.041148605] [Cited by in Crossref: 27] [Cited by in F6Publishing: 23] [Article Influence: 1.7] [Reference Citation Analysis]
121 Ohigashi I, Takahama Y. Thymoproteasome optimizes positive selection of CD8+ T cells without contribution of negative selection. Adv Immunol 2021;149:1-23. [PMID: 33993918 DOI: 10.1016/bs.ai.2021.03.001] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
122 Prasad R, Atul, Kolla VK, Legac J, Singhal N, Navale R, Rosenthal PJ, Sijwali PS. Blocking Plasmodium falciparum development via dual inhibition of hemoglobin degradation and the ubiquitin proteasome system by MG132. PLoS One 2013;8:e73530. [PMID: 24023882 DOI: 10.1371/journal.pone.0073530] [Cited by in Crossref: 40] [Cited by in F6Publishing: 35] [Article Influence: 5.0] [Reference Citation Analysis]
123 Tasaki T, Mulder LC, Iwamatsu A, Lee MJ, Davydov IV, Varshavsky A, Muesing M, Kwon YT. A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons. Mol Cell Biol 2005;25:7120-36. [PMID: 16055722 DOI: 10.1128/MCB.25.16.7120-7136.2005] [Cited by in Crossref: 221] [Cited by in F6Publishing: 149] [Article Influence: 13.8] [Reference Citation Analysis]
124 Seo HD, Choi Y, Kim M, Kang K, Urano T, Lee D. The 19S proteasome is directly involved in the regulation of heterochromatin spreading in fission yeast. J Biol Chem 2017;292:17144-55. [PMID: 28784663 DOI: 10.1074/jbc.M117.790824] [Cited by in Crossref: 12] [Cited by in F6Publishing: 10] [Article Influence: 3.0] [Reference Citation Analysis]
125 Burns KE, Darwin KH. Pupylation versus ubiquitylation: tagging for proteasome-dependent degradation. Cell Microbiol 2010;12:424-31. [PMID: 20109157 DOI: 10.1111/j.1462-5822.2010.01447.x] [Cited by in Crossref: 32] [Cited by in F6Publishing: 28] [Article Influence: 2.9] [Reference Citation Analysis]
126 Garcin D, Marq JB, Iseni F, Martin S, Kolakofsky D. A short peptide at the amino terminus of the Sendai virus C protein acts as an independent element that induces STAT1 instability. J Virol 2004;78:8799-811. [PMID: 15280488 DOI: 10.1128/JVI.78.16.8799-8811.2004] [Cited by in Crossref: 24] [Cited by in F6Publishing: 16] [Article Influence: 1.4] [Reference Citation Analysis]
127 Tubío-Santamaría N, Ebstein F, Heidel FH, Krüger E. Immunoproteasome Function in Normal and Malignant Hematopoiesis. Cells 2021;10:1577. [PMID: 34206607 DOI: 10.3390/cells10071577] [Cited by in F6Publishing: 2] [Reference Citation Analysis]
128 Suppahia A, Itagi P, Burris A, Kim FMG, Vontz A, Kante A, Kim S, Im W, Deeds EJ, Roelofs J. Cooperativity in Proteasome Core Particle Maturation. iScience 2020;23:101090. [PMID: 32380419 DOI: 10.1016/j.isci.2020.101090] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
129 Götze S, Saborowski R, Martínez-Cruz O, Muhlia-Almazán A, Sánchez-Paz A. Proteasome properties of hemocytes differ between the whiteleg shrimp Penaeus vannamei and the brown shrimp Crangon crangon (Crustacea, Decapoda). Cell Stress Chaperones 2017;22:879-91. [PMID: 28646424 DOI: 10.1007/s12192-017-0819-4] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 1.3] [Reference Citation Analysis]
130 Maganti N, Moody TD, Truax AD, Thakkar M, Spring AM, Germann MW, Greer SF. Nonproteolytic roles of 19S ATPases in transcription of CIITApIV genes. PLoS One 2014;9:e91200. [PMID: 24625964 DOI: 10.1371/journal.pone.0091200] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 1.0] [Reference Citation Analysis]
131 Vlachostergios PJ, Patrikidou A, Daliani DD, Papandreou CN. The ubiquitin-proteasome system in cancer, a major player in DNA repair. Part 2: transcriptional regulation. J Cell Mol Med 2009;13:3019-31. [PMID: 19522844 DOI: 10.1111/j.1582-4934.2009.00825.x] [Cited by in Crossref: 11] [Cited by in F6Publishing: 13] [Article Influence: 0.9] [Reference Citation Analysis]
132 Sharon M, Regev-Rudzki N. Cell communication and protein degradation: All in one parasitic package. J Extracell Vesicles 2021;10:e12116. [PMID: 34257846 DOI: 10.1002/jev2.12116] [Reference Citation Analysis]
133 Calderon-Villalobos LI, Tan X, Zheng N, Estelle M. Auxin perception--structural insights. Cold Spring Harb Perspect Biol 2010;2:a005546. [PMID: 20504967 DOI: 10.1101/cshperspect.a005546] [Cited by in Crossref: 110] [Cited by in F6Publishing: 104] [Article Influence: 10.0] [Reference Citation Analysis]
134 Gorospe M, Egan JM, Zbar B, Lerman M, Geil L, Kuzmin I, Holbrook NJ. Protective function of von Hippel-Lindau protein against impaired protein processing in renal carcinoma cells. Mol Cell Biol 1999;19:1289-300. [PMID: 9891063 DOI: 10.1128/MCB.19.2.1289] [Cited by in Crossref: 51] [Cited by in F6Publishing: 15] [Article Influence: 2.3] [Reference Citation Analysis]
135 McCormack PL. Carfilzomib: in relapsed, or relapsed and refractory, multiple myeloma. Drugs 2012;72:2023-32. [PMID: 22994535 DOI: 10.2165/11209010-000000000-00000] [Cited by in Crossref: 15] [Cited by in F6Publishing: 13] [Article Influence: 1.9] [Reference Citation Analysis]
136 Perusina Lanfranca M, Mostafa HH, Davido DJ. Two overlapping regions within the N-terminal half of the herpes simplex virus 1 E3 ubiquitin ligase ICP0 facilitate the degradation and dissociation of PML and dissociation of Sp100 from ND10. J Virol. 2013;87:13287-13296. [PMID: 24089549 DOI: 10.1128/jvi.02304-13] [Cited by in Crossref: 11] [Cited by in F6Publishing: 9] [Article Influence: 1.4] [Reference Citation Analysis]
137 Classen M, Breuer S, Baumeister W, Guckenberger R, Witt S. Force spectroscopy of substrate molecules en route to the proteasome's active sites. Biophys J 2011;100:489-97. [PMID: 21244845 DOI: 10.1016/j.bpj.2010.12.3689] [Cited by in Crossref: 4] [Cited by in F6Publishing: 1] [Article Influence: 0.4] [Reference Citation Analysis]
138 Akopian T, Kandror O, Raju RM, Unnikrishnan M, Rubin EJ, Goldberg AL. The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring. EMBO J 2012;31:1529-41. [PMID: 22286948 DOI: 10.1038/emboj.2012.5] [Cited by in Crossref: 78] [Cited by in F6Publishing: 67] [Article Influence: 8.7] [Reference Citation Analysis]
139 Chen D, Frezza M, Schmitt S, Kanwar J, Dou QP. Bortezomib as the first proteasome inhibitor anticancer drug: current status and future perspectives. Curr Cancer Drug Targets 2011;11:239-53. [PMID: 21247388 DOI: 10.2174/156800911794519752] [Cited by in Crossref: 457] [Cited by in F6Publishing: 422] [Article Influence: 45.7] [Reference Citation Analysis]
140 Xing Y, Jameson SC, Hogquist KA. Thymoproteasome subunit-β5T generates peptide-MHC complexes specialized for positive selection. Proc Natl Acad Sci U S A 2013;110:6979-84. [PMID: 23569244 DOI: 10.1073/pnas.1222244110] [Cited by in Crossref: 59] [Cited by in F6Publishing: 64] [Article Influence: 7.4] [Reference Citation Analysis]
141 Pfleger CM, Lee E, Kirschner MW. Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex. Genes Dev 2001;15:2396-407. [PMID: 11562349 DOI: 10.1101/gad.918201] [Cited by in Crossref: 165] [Cited by in F6Publishing: 176] [Article Influence: 8.3] [Reference Citation Analysis]
142 Nagy I, Tamura T, Vanderleyden J, Baumeister W, De Mot R. The 20S proteasome of Streptomyces coelicolor. J Bacteriol 1998;180:5448-53. [PMID: 9765579 DOI: 10.1128/JB.180.20.5448-5453.1998] [Cited by in Crossref: 58] [Cited by in F6Publishing: 25] [Article Influence: 2.5] [Reference Citation Analysis]
143 Mayer TU, Braun T, Jentsch S. Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J 1998;17:3251-7. [PMID: 9628862 DOI: 10.1093/emboj/17.12.3251] [Cited by in Crossref: 159] [Cited by in F6Publishing: 152] [Article Influence: 6.9] [Reference Citation Analysis]
144 Rotanova TV, Botos I, Melnikov EE, Rasulova F, Gustchina A, Maurizi MR, Wlodawer A. Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains. Protein Sci 2006;15:1815-28. [PMID: 16877706 DOI: 10.1110/ps.052069306] [Cited by in Crossref: 60] [Cited by in F6Publishing: 54] [Article Influence: 4.0] [Reference Citation Analysis]
145 Milisav I, Poljsak B, Suput D. Adaptive response, evidence of cross-resistance and its potential clinical use. Int J Mol Sci. 2012;13:10771-10806. [PMID: 23109822 DOI: 10.3390/ijms130910771] [Cited by in Crossref: 53] [Cited by in F6Publishing: 49] [Article Influence: 5.9] [Reference Citation Analysis]
146 Yu J, Hu S, Ma K, Sun L, Hu H, Zou F, Guo Q, Lei Z, Zhou D, Sun Y, Zhang D, Ma L, Shen B, Zhu C. Ribosomal protein S29 regulates metabolic insecticide resistance through binding and degradation of CYP6N3. PLoS One 2014;9:e94611. [PMID: 24728095 DOI: 10.1371/journal.pone.0094611] [Cited by in Crossref: 11] [Cited by in F6Publishing: 12] [Article Influence: 1.6] [Reference Citation Analysis]
147 Hsu HC, Singh PK, Fan H, Wang R, Sukenick G, Nathan C, Lin G, Li H. Structural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome. Biochemistry 2017;56:324-33. [PMID: 27976853 DOI: 10.1021/acs.biochem.6b01107] [Cited by in Crossref: 13] [Cited by in F6Publishing: 13] [Article Influence: 2.6] [Reference Citation Analysis]
148 Rockel B, Peters J, Müller SA, Seyit G, Ringler P, Hegerl R, Glaeser RM, Baumeister W. Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II. Proc Natl Acad Sci U S A 2005;102:10135-40. [PMID: 16006508 DOI: 10.1073/pnas.0504569102] [Cited by in Crossref: 28] [Cited by in F6Publishing: 19] [Article Influence: 1.8] [Reference Citation Analysis]
149 Matondo M, Marcellin M, Chaoui K, Bousquet-Dubouch MP, Gonzalez-de-Peredo A, Monsarrat B, Burlet-Schiltz O. Determination of differentially regulated proteins upon proteasome inhibition in AML cell lines by the combination of large-scale and targeted quantitative proteomics. Proteomics 2017;17. [PMID: 27709814 DOI: 10.1002/pmic.201600089] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 1.6] [Reference Citation Analysis]
150 Funakoshi M, Sasaki T, Nishimoto T, Kobayashi H. Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 2002;99:745-50. [PMID: 11805328 DOI: 10.1073/pnas.012585199] [Cited by in Crossref: 171] [Cited by in F6Publishing: 175] [Article Influence: 9.0] [Reference Citation Analysis]
151 Baker TA, Bach HH 4th, Gamelli RL, Love RB, Majetschak M. Proteasomes in lungs from organ donors and patients with end-stage pulmonary diseases. Physiol Res 2014;63:311-9. [PMID: 24564596 DOI: 10.33549/physiolres.932607] [Cited by in Crossref: 7] [Cited by in F6Publishing: 14] [Article Influence: 1.0] [Reference Citation Analysis]
152 Bousquet-Dubouch MP, Baudelet E, Guérin F, Matondo M, Uttenweiler-Joseph S, Burlet-Schiltz O, Monsarrat B. Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins. Mol Cell Proteomics 2009;8:1150-64. [PMID: 19193609 DOI: 10.1074/mcp.M800193-MCP200] [Cited by in Crossref: 53] [Cited by in F6Publishing: 30] [Article Influence: 4.4] [Reference Citation Analysis]
153 Enders GA. Mechanism of antigen presentation after hypertonic loading of soluble antigens. Immunology 2002;106:511-6. [PMID: 12153514 DOI: 10.1046/j.1365-2567.2002.01476.x] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.2] [Reference Citation Analysis]
154 Blackburn C, Gigstad KM, Hales P, Garcia K, Jones M, Bruzzese FJ, Barrett C, Liu JX, Soucy TA, Sappal DS, Bump N, Olhava EJ, Fleming P, Dick LR, Tsu C, Sintchak MD, Blank JL. Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S beta5-subunit. Biochem J 2010;430:461-76. [PMID: 20632995 DOI: 10.1042/BJ20100383] [Cited by in Crossref: 111] [Cited by in F6Publishing: 48] [Article Influence: 10.1] [Reference Citation Analysis]
155 Lim HS, Cai D, Archer CT, Kodadek T. Periodate-triggered cross-linking reveals Sug2/Rpt4 as the molecular target of a peptoid inhibitor of the 19S proteasome regulatory particle. J Am Chem Soc 2007;129:12936-7. [PMID: 17929816 DOI: 10.1021/ja075469+] [Cited by in Crossref: 34] [Cited by in F6Publishing: 31] [Article Influence: 2.4] [Reference Citation Analysis]
156 Liu J, Zhang H, Xiao Z, Wang F, Wang X, Wang Y. Combined 3D-QSAR, molecular docking and molecular dynamics study on derivatives of peptide epoxyketone and tyropeptin-boronic acid as inhibitors against the β5 subunit of human 20S proteasome. Int J Mol Sci 2011;12:1807-35. [PMID: 21673924 DOI: 10.3390/ijms12031807] [Cited by in Crossref: 24] [Cited by in F6Publishing: 17] [Article Influence: 2.4] [Reference Citation Analysis]
157 Hsia EY, Gui Y, Zheng X. Regulation of Hedgehog signaling by ubiquitination. Front Biol (Beijing) 2015;10:203-20. [PMID: 26366162 DOI: 10.1007/s11515-015-1343-5] [Cited by in Crossref: 18] [Cited by in F6Publishing: 17] [Article Influence: 3.0] [Reference Citation Analysis]
158 Wilson HL, Aldrich HC, Maupin-Furlow J. Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis. J Bacteriol 1999;181:5814-24. [PMID: 10482525 DOI: 10.1128/JB.181.18.5814-5824.1999] [Cited by in Crossref: 41] [Cited by in F6Publishing: 28] [Article Influence: 1.9] [Reference Citation Analysis]
159 Biddie SC, Hager GL. Glucocorticoid receptor dynamics and gene regulation. Stress 2009;12:193-205. [PMID: 19051126 DOI: 10.1080/10253890802506409] [Cited by in Crossref: 45] [Cited by in F6Publishing: 42] [Article Influence: 3.8] [Reference Citation Analysis]
160 Pathare GR, Nagy I, Śledź P, Anderson DJ, Zhou HJ, Pardon E, Steyaert J, Förster F, Bracher A, Baumeister W. Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proc Natl Acad Sci U S A 2014;111:2984-9. [PMID: 24516147 DOI: 10.1073/pnas.1400546111] [Cited by in Crossref: 93] [Cited by in F6Publishing: 85] [Article Influence: 13.3] [Reference Citation Analysis]
161 Peng Z, Staub JM, Serino G, Kwok SF, Kurepa J, Bruce BD, Vierstra RD, Wei N, Deng XW. The cellular level of PR500, a protein complex related to the 19S regulatory particle of the proteasome, is regulated in response to stresses in plants. Mol Biol Cell 2001;12:383-92. [PMID: 11179422 DOI: 10.1091/mbc.12.2.383] [Cited by in Crossref: 38] [Cited by in F6Publishing: 42] [Article Influence: 1.9] [Reference Citation Analysis]
162 Tyers M, Rottapel R. VHL: a very hip ligase. Proc Natl Acad Sci U S A 1999;96:12230-2. [PMID: 10535903 DOI: 10.1073/pnas.96.22.12230] [Cited by in Crossref: 36] [Cited by in F6Publishing: 34] [Article Influence: 1.6] [Reference Citation Analysis]
163 Zhang F, Hu M, Tian G, Zhang P, Finley D, Jeffrey PD, Shi Y. Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol Cell 2009;34:473-84. [PMID: 19481527 DOI: 10.1016/j.molcel.2009.04.021] [Cited by in Crossref: 139] [Cited by in F6Publishing: 126] [Article Influence: 11.6] [Reference Citation Analysis]
164 Bailly E, Reed SI. Functional characterization of rpn3 uncovers a distinct 19S proteasomal subunit requirement for ubiquitin-dependent proteolysis of cell cycle regulatory proteins in budding yeast. Mol Cell Biol 1999;19:6872-90. [PMID: 10490625 DOI: 10.1128/MCB.19.10.6872] [Cited by in Crossref: 31] [Cited by in F6Publishing: 15] [Article Influence: 1.5] [Reference Citation Analysis]
165 Niu XF, Liu BQ, Du ZX, Gao YY, Li C, Li N, Guan Y, Wang HQ. Resveratrol protects leukemic cells against cytotoxicity induced by proteasome inhibitors via induction of FOXO1 and p27Kip1. BMC Cancer 2011;11:99. [PMID: 21418583 DOI: 10.1186/1471-2407-11-99] [Cited by in Crossref: 14] [Cited by in F6Publishing: 14] [Article Influence: 1.4] [Reference Citation Analysis]
166 England JL, Pande VS. Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework. Biochem Cell Biol 2010;88:359-69. [PMID: 20453936 DOI: 10.1139/o09-187] [Cited by in Crossref: 9] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis]
167 Arlt A, Minkenberg J, Kruse ML, Grohmann F, Fölsch UR, Schäfer H. Immediate early gene-X1 interferes with 26 S proteasome activity by attenuating expression of the 19 S proteasomal components S5a/Rpn10 and S1/Rpn2. Biochem J 2007;402:367-75. [PMID: 17107344 DOI: 10.1042/BJ20061072] [Cited by in Crossref: 13] [Cited by in F6Publishing: 6] [Article Influence: 0.9] [Reference Citation Analysis]
168 Zheng L, Chen Y, Lee WH. Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins. Mol Cell Biol 1999;19:5417-28. [PMID: 10409732 DOI: 10.1128/MCB.19.8.5417] [Cited by in Crossref: 45] [Cited by in F6Publishing: 20] [Article Influence: 2.0] [Reference Citation Analysis]
169 Bai M, Zhao X, Sahara K, Ohte Y, Hirano Y, Kaneko T, Yashiroda H, Murata S. In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals. Biomolecules 2019;9:E213. [PMID: 31159305 DOI: 10.3390/biom9060213] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.5] [Reference Citation Analysis]
170 Kondo H, Matsumura T, Kaneko M, Inoue K, Kosako H, Ikawa M, Takahama Y, Ohigashi I. PITHD1 is a proteasome-interacting protein essential for male fertilization. J Biol Chem 2020;295:1658-72. [PMID: 31915251 DOI: 10.1074/jbc.RA119.011144] [Cited by in Crossref: 2] [Article Influence: 2.0] [Reference Citation Analysis]
171 Lee KY, Chen TT, Chiang LL, Chuang HC, Feng PH, Liu WT, Chen KY, Ho SC. Proteasome activity related with the daily physical activity of COPD patients. Int J Chron Obstruct Pulmon Dis 2017;12:1519-25. [PMID: 28579770 DOI: 10.2147/COPD.S132276] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
172 Park S, Rodermel SR. Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis. Proc Natl Acad Sci U S A 2004;101:12765-70. [PMID: 15304652 DOI: 10.1073/pnas.0402764101] [Cited by in Crossref: 82] [Cited by in F6Publishing: 79] [Article Influence: 4.8] [Reference Citation Analysis]
173 Kumoi K, Satoh T, Murata K, Hiromoto T, Mizushima T, Kamiya Y, Noda M, Uchiyama S, Yagi H, Kato K. An archaeal homolog of proteasome assembly factor functions as a proteasome activator. PLoS One 2013;8:e60294. [PMID: 23555947 DOI: 10.1371/journal.pone.0060294] [Cited by in Crossref: 18] [Cited by in F6Publishing: 17] [Article Influence: 2.3] [Reference Citation Analysis]
174 Lin G, Li D, Chidawanyika T, Nathan C, Li H. Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis proteasome. Arch Biochem Biophys 2010;501:214-20. [PMID: 20558127 DOI: 10.1016/j.abb.2010.06.009] [Cited by in Crossref: 43] [Cited by in F6Publishing: 36] [Article Influence: 3.9] [Reference Citation Analysis]
175 McBride Z, Chen D, Lee Y, Aryal UK, Xie J, Szymanski DB. A Label-free Mass Spectrometry Method to Predict Endogenous Protein Complex Composition. Mol Cell Proteomics 2019;18:1588-606. [PMID: 31186290 DOI: 10.1074/mcp.RA119.001400] [Cited by in Crossref: 20] [Cited by in F6Publishing: 9] [Article Influence: 10.0] [Reference Citation Analysis]
176 Xu J, Kawahata I, Izumi H, Fukunaga K. T-Type Ca2+ Enhancer SAK3 Activates CaMKII and Proteasome Activities in Lewy Body Dementia Mice Model. Int J Mol Sci 2021;22:6185. [PMID: 34201181 DOI: 10.3390/ijms22126185] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
177 Sharon M, Taverner T, Ambroggio XI, Deshaies RJ, Robinson CV. Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol 2006;4:e267. [PMID: 16869714 DOI: 10.1371/journal.pbio.0040267] [Cited by in Crossref: 158] [Cited by in F6Publishing: 143] [Article Influence: 10.5] [Reference Citation Analysis]
178 Dahlqvist J, Klar J, Tiwari N, Schuster J, Törmä H, Badhai J, Pujol R, van Steensel MA, Brinkhuizen T, Gijezen L, Chaves A, Tadini G, Vahlquist A, Dahl N. A single-nucleotide deletion in the POMP 5' UTR causes a transcriptional switch and altered epidermal proteasome distribution in KLICK genodermatosis. Am J Hum Genet 2010;86:596-603. [PMID: 20226437 DOI: 10.1016/j.ajhg.2010.02.018] [Cited by in Crossref: 51] [Cited by in F6Publishing: 42] [Article Influence: 4.6] [Reference Citation Analysis]
179 Sbardella D, Tundo GR, Sciandra F, Bozzi M, Gioia M, Ciaccio C, Tarantino U, Brancaccio A, Coletta M, Marini S. Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution. PLoS One 2015;10:e0132455. [PMID: 26186340 DOI: 10.1371/journal.pone.0132455] [Cited by in Crossref: 17] [Cited by in F6Publishing: 17] [Article Influence: 2.8] [Reference Citation Analysis]
180 Liu B, Archer CT, Burdine L, Gillette TG, Kodadek T. Label transfer chemistry for the characterization of protein-protein interactions. J Am Chem Soc 2007;129:12348-9. [PMID: 17894490 DOI: 10.1021/ja072904r] [Cited by in Crossref: 44] [Cited by in F6Publishing: 40] [Article Influence: 3.1] [Reference Citation Analysis]
181 Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 2008;322:1104-7. [PMID: 18832610 DOI: 10.1126/science.1163885] [Cited by in Crossref: 268] [Cited by in F6Publishing: 265] [Article Influence: 20.6] [Reference Citation Analysis]
182 Franzetti B, Schoehn G, Hernandez JF, Jaquinod M, Ruigrok RW, Zaccai G. Tetrahedral aminopeptidase: a novel large protease complex from archaea. EMBO J 2002;21:2132-8. [PMID: 11980710 DOI: 10.1093/emboj/21.9.2132] [Cited by in Crossref: 62] [Cited by in F6Publishing: 53] [Article Influence: 3.3] [Reference Citation Analysis]
183 Santos RLA, Bai L, Singh PK, Murakami N, Fan H, Zhan W, Zhu Y, Jiang X, Zhang K, Assker JP, Nathan CF, Li H, Azzi J, Lin G. Structure of human immunoproteasome with a reversible and noncompetitive inhibitor that selectively inhibits activated lymphocytes. Nat Commun 2017;8:1692. [PMID: 29167449 DOI: 10.1038/s41467-017-01760-5] [Cited by in Crossref: 32] [Cited by in F6Publishing: 28] [Article Influence: 8.0] [Reference Citation Analysis]
184 Reuter CJ, Maupin-Furlow JA. Analysis of proteasome-dependent proteolysis in Haloferax volcanii cells, using short-lived green fluorescent proteins. Appl Environ Microbiol 2004;70:7530-8. [PMID: 15574956 DOI: 10.1128/AEM.70.12.7530-7538.2004] [Cited by in Crossref: 60] [Cited by in F6Publishing: 28] [Article Influence: 3.8] [Reference Citation Analysis]
185 Dudek EJ, Lampi KJ, Lampi JA, Shang F, King J, Wang Y, Taylor A. Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation. Invest Ophthalmol Vis Sci 2010;51:4164-73. [PMID: 20592226 DOI: 10.1167/iovs.09-4087] [Cited by in Crossref: 16] [Cited by in F6Publishing: 18] [Article Influence: 1.5] [Reference Citation Analysis]
186 Chymkowitch P, Le May N, Charneau P, Compe E, Egly JM. The phosphorylation of the androgen receptor by TFIIH directs the ubiquitin/proteasome process. EMBO J 2011;30:468-79. [PMID: 21157430 DOI: 10.1038/emboj.2010.337] [Cited by in Crossref: 81] [Cited by in F6Publishing: 80] [Article Influence: 7.4] [Reference Citation Analysis]
187 Liou GG, Jane WN, Cohen SN, Lin NS, Lin-Chao S. RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. Proc Natl Acad Sci U S A 2001;98:63-8. [PMID: 11134527 DOI: 10.1073/pnas.011535498] [Cited by in Crossref: 29] [Cited by in F6Publishing: 72] [Article Influence: 1.5] [Reference Citation Analysis]
188 Bach HH 4th, Laporte HM, Wong YM, Gamelli RL, Majetschak M. Proteasome inhibition prolongs survival during lethal hemorrhagic shock in rats. J Trauma Acute Care Surg 2013;74:499-507. [PMID: 23354244 DOI: 10.1097/TA.0b013e31827d5db2] [Cited by in Crossref: 7] [Cited by in F6Publishing: 3] [Article Influence: 0.9] [Reference Citation Analysis]
189 Driscoll JJ, Dechowdhury R. Therapeutically targeting the SUMOylation, Ubiquitination and Proteasome pathways as a novel anticancer strategy. Target Oncol 2010;5:281-9. [PMID: 21125340 DOI: 10.1007/s11523-010-0165-2] [Cited by in Crossref: 23] [Cited by in F6Publishing: 19] [Article Influence: 2.1] [Reference Citation Analysis]
190 Kim YC, Wu SY, Lim HS, Chiang CM, Kodadek T. Non-proteolytic regulation of p53-mediated transcription through destabilization of the activator.promoter complex by the proteasomal ATPases. J Biol Chem 2009;284:34522-30. [PMID: 19846554 DOI: 10.1074/jbc.M109.017277] [Cited by in Crossref: 8] [Cited by in F6Publishing: 5] [Article Influence: 0.7] [Reference Citation Analysis]
191 Lee MY, Jeon JW, Sievers C, Allen CT. Antigen processing and presentation in cancer immunotherapy. J Immunother Cancer 2020;8:e001111. [PMID: 32859742 DOI: 10.1136/jitc-2020-001111] [Cited by in Crossref: 7] [Cited by in F6Publishing: 8] [Article Influence: 7.0] [Reference Citation Analysis]
192 Carew JS, Medina EC, Esquivel JA, Mahalingam D, Swords R, Kelly K, Zhang H, Huang P, Mita AC, Mita MM. Autophagy inhibition enhances vorinostat-induced apoptosis via ubiquitinated protein accumulation. J Cell Mol Med. 2010;14:2448-2459. [PMID: 19583815 DOI: 10.1111/j.1582-4934.2009.00832.x] [Cited by in Crossref: 140] [Cited by in F6Publishing: 144] [Article Influence: 14.0] [Reference Citation Analysis]
193 Goldberg AL. Development of proteasome inhibitors as research tools and cancer drugs. J Cell Biol 2012;199:583-8. [PMID: 23148232 DOI: 10.1083/jcb.201210077] [Cited by in Crossref: 174] [Cited by in F6Publishing: 160] [Article Influence: 21.8] [Reference Citation Analysis]
194 Reid BG, Fenton WA, Horwich AL, Weber-Ban EU. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc Natl Acad Sci U S A 2001;98:3768-72. [PMID: 11259663 DOI: 10.1073/pnas.071043698] [Cited by in Crossref: 115] [Cited by in F6Publishing: 109] [Article Influence: 5.8] [Reference Citation Analysis]
195 Chen JJ, Lin F, Qin ZH. The roles of the proteasome pathway in signal transduction and neurodegenerative diseases. Neurosci Bull 2008;24:183-94. [PMID: 18500392 DOI: 10.1007/s12264-008-0183-6] [Cited by in Crossref: 23] [Cited by in F6Publishing: 24] [Article Influence: 1.8] [Reference Citation Analysis]
196 Song C, Wang Q, Song C, Rogers TJ. Valosin-containing protein (VCP/p97) is capable of unfolding polyubiquitinated proteins through its ATPase domains. Biochem Biophys Res Commun 2015;463:453-7. [PMID: 26043696 DOI: 10.1016/j.bbrc.2015.05.111] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 1.5] [Reference Citation Analysis]
197 Regelmann J, Schüle T, Josupeit FS, Horak J, Rose M, Entian KD, Thumm M, Wolf DH. Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell. 2003;14:1652-1663. [PMID: 12686616 DOI: 10.1091/mbc.E02-08-0456] [Cited by in Crossref: 106] [Cited by in F6Publishing: 83] [Article Influence: 5.9] [Reference Citation Analysis]
198 Shirozu R, Yashiroda H, Murata S. Proteasome Impairment Induces Recovery of Mitochondrial Membrane Potential and an Alternative Pathway of Mitochondrial Fusion. Mol Cell Biol 2016;36:347-62. [PMID: 26552703 DOI: 10.1128/MCB.00920-15] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.3] [Reference Citation Analysis]
199 Sakuma K, Yamaguchi A. Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass. J Cachexia Sarcopenia Muscle 2012;3:77-94. [PMID: 22476916 DOI: 10.1007/s13539-011-0052-4] [Cited by in Crossref: 76] [Cited by in F6Publishing: 77] [Article Influence: 8.4] [Reference Citation Analysis]
200 Lazarov VK, Fraering PC, Ye W, Wolfe MS, Selkoe DJ, Li H. Electron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores. Proc Natl Acad Sci U S A 2006;103:6889-94. [PMID: 16636269 DOI: 10.1073/pnas.0602321103] [Cited by in Crossref: 129] [Cited by in F6Publishing: 124] [Article Influence: 8.6] [Reference Citation Analysis]
201 Nickell S, Beck F, Scheres SH, Korinek A, Förster F, Lasker K, Mihalache O, Sun N, Nagy I, Sali A, Plitzko JM, Carazo JM, Mann M, Baumeister W. Insights into the molecular architecture of the 26S proteasome. Proc Natl Acad Sci U S A 2009;106:11943-7. [PMID: 19581588 DOI: 10.1073/pnas.0905081106] [Cited by in Crossref: 108] [Cited by in F6Publishing: 103] [Article Influence: 9.0] [Reference Citation Analysis]
202 Yang S, Li YP. RGS10-null mutation impairs osteoclast differentiation resulting from the loss of [Ca2+]i oscillation regulation. Genes Dev. 2007;21:1803-1816. [PMID: 17626792 DOI: 10.1101/gad.1544107] [Cited by in Crossref: 98] [Cited by in F6Publishing: 98] [Article Influence: 7.0] [Reference Citation Analysis]
203 Archer CT, Delahodde A, Gonzalez F, Johnston SA, Kodadek T. Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo. J Biol Chem 2008;283:12614-23. [PMID: 18326036 DOI: 10.1074/jbc.M801050200] [Cited by in Crossref: 26] [Cited by in F6Publishing: 17] [Article Influence: 2.0] [Reference Citation Analysis]
204 Lin G, Tsu C, Dick L, Zhou XK, Nathan C. Distinct specificities of Mycobacterium tuberculosis and mammalian proteasomes for N-acetyl tripeptide substrates. J Biol Chem 2008;283:34423-31. [PMID: 18829465 DOI: 10.1074/jbc.M805324200] [Cited by in Crossref: 44] [Cited by in F6Publishing: 31] [Article Influence: 3.4] [Reference Citation Analysis]
205 Singh PK, Fan H, Jiang X, Shi L, Nathan CF, Lin G. Immunoproteasome β5i-Selective Dipeptidomimetic Inhibitors. ChemMedChem 2016;11:2127-31. [PMID: 27561172 DOI: 10.1002/cmdc.201600384] [Cited by in Crossref: 21] [Cited by in F6Publishing: 20] [Article Influence: 4.2] [Reference Citation Analysis]
206 Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 1998;17:7151-60. [PMID: 9857172 DOI: 10.1093/emboj/17.24.7151] [Cited by in Crossref: 943] [Cited by in F6Publishing: 920] [Article Influence: 42.9] [Reference Citation Analysis]
207 Ekici OD, Paetzel M, Dalbey RE. Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration. Protein Sci 2008;17:2023-37. [PMID: 18824507 DOI: 10.1110/ps.035436.108] [Cited by in Crossref: 197] [Cited by in F6Publishing: 163] [Article Influence: 15.2] [Reference Citation Analysis]
208 Cho SK, Chung HS, Ryu MY, Park MJ, Lee MM, Bahk YY, Kim J, Pai HS, Kim WT. Heterologous expression and molecular and cellular characterization of CaPUB1 encoding a hot pepper U-Box E3 ubiquitin ligase homolog. Plant Physiol 2006;142:1664-82. [PMID: 17041029 DOI: 10.1104/pp.106.087965] [Cited by in Crossref: 75] [Cited by in F6Publishing: 69] [Article Influence: 5.0] [Reference Citation Analysis]
209 Takagi K, Kim S, Yukii H, Ueno M, Morishita R, Endo Y, Kato K, Tanaka K, Saeki Y, Mizushima T. Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26 S proteasome, by proteasome-dedicated chaperone Hsm3p. J Biol Chem 2012;287:12172-82. [PMID: 22334676 DOI: 10.1074/jbc.M112.345876] [Cited by in Crossref: 27] [Cited by in F6Publishing: 15] [Article Influence: 3.0] [Reference Citation Analysis]
210 Koues OI, Dudley RK, Truax AD, Gerhardt D, Bhat KP, McNeal S, Greer SF. Regulation of acetylation at the major histocompatibility complex class II proximal promoter by the 19S proteasomal ATPase Sug1. Mol Cell Biol 2008;28:5837-50. [PMID: 18662994 DOI: 10.1128/MCB.00535-08] [Cited by in Crossref: 32] [Cited by in F6Publishing: 20] [Article Influence: 2.5] [Reference Citation Analysis]
211 Hirano Y, Kaneko T, Okamoto K, Bai M, Yashiroda H, Furuyama K, Kato K, Tanaka K, Murata S. Dissecting beta-ring assembly pathway of the mammalian 20S proteasome. EMBO J 2008;27:2204-13. [PMID: 18650933 DOI: 10.1038/emboj.2008.148] [Cited by in Crossref: 102] [Cited by in F6Publishing: 98] [Article Influence: 7.8] [Reference Citation Analysis]
212 Wilson HL, Ou MS, Aldrich HC, Maupin-Furlow J. Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome. J Bacteriol 2000;182:1680-92. [PMID: 10692374 DOI: 10.1128/JB.182.6.1680-1692.2000] [Cited by in Crossref: 59] [Cited by in F6Publishing: 23] [Article Influence: 2.8] [Reference Citation Analysis]
213 Jansen FH, Krijgsveld J, van Rijswijk A, van den Bemd GJ, van den Berg MS, van Weerden WM, Willemsen R, Dekker LJ, Luider TM, Jenster G. Exosomal secretion of cytoplasmic prostate cancer xenograft-derived proteins. Mol Cell Proteomics 2009;8:1192-205. [PMID: 19204029 DOI: 10.1074/mcp.M800443-MCP200] [Cited by in Crossref: 75] [Cited by in F6Publishing: 50] [Article Influence: 6.3] [Reference Citation Analysis]
214 Carlson EJ, Pitonzo D, Skach WR. p97 functions as an auxiliary factor to facilitate TM domain extraction during CFTR ER-associated degradation. EMBO J 2006;25:4557-66. [PMID: 16977321 DOI: 10.1038/sj.emboj.7601307] [Cited by in Crossref: 50] [Cited by in F6Publishing: 47] [Article Influence: 3.3] [Reference Citation Analysis]
215 Cha SS, An YJ, Lee CR, Lee HS, Kim YG, Kim SJ, Kwon KK, De Donatis GM, Lee JH, Maurizi MR, Kang SG. Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. EMBO J 2010;29:3520-30. [PMID: 20834233 DOI: 10.1038/emboj.2010.226] [Cited by in Crossref: 67] [Cited by in F6Publishing: 62] [Article Influence: 6.1] [Reference Citation Analysis]
216 Fan H, Angelo NG, Warren JD, Nathan CF, Lin G. Oxathiazolones Selectively Inhibit the Human Immunoproteasome over the Constitutive Proteasome. ACS Med Chem Lett 2014;5:405-10. [PMID: 24900849 DOI: 10.1021/ml400531d] [Cited by in Crossref: 32] [Cited by in F6Publishing: 31] [Article Influence: 4.6] [Reference Citation Analysis]
217 Wang G, Fan W, Ou M, Wang X, Qin H, Feng F, Du Y, Ni J, Tang J, Song R, Wang G. Dek40 Encodes a PBAC4 Protein Required for 20S Proteasome Biogenesis and Seed Development. Plant Physiol 2019;180:2120-32. [PMID: 31189659 DOI: 10.1104/pp.18.01419] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.5] [Reference Citation Analysis]
218 Ando R, Noda K, Tomaru U, Kamoshita M, Ozawa Y, Notomi S, Hisatomi T, Noda M, Kanda A, Ishibashi T, Kasahara M, Ishida S. Decreased proteasomal activity causes photoreceptor degeneration in mice. Invest Ophthalmol Vis Sci 2014;55:4682-90. [PMID: 24994871 DOI: 10.1167/iovs.13-13272] [Cited by in Crossref: 12] [Cited by in F6Publishing: 11] [Article Influence: 1.7] [Reference Citation Analysis]
219 Johnson SL, Blount JR, Libohova K, Ranxhi B, Paulson HL, Tsou WL, Todi SV. Differential toxicity of ataxin-3 isoforms in Drosophila models of Spinocerebellar Ataxia Type 3. Neurobiol Dis 2019;132:104535. [PMID: 31310802 DOI: 10.1016/j.nbd.2019.104535] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 3.5] [Reference Citation Analysis]
220 Kim YC, DeMartino GN. C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome. J Biol Chem 2011;286:26652-66. [PMID: 21628461 DOI: 10.1074/jbc.M111.246793] [Cited by in Crossref: 29] [Cited by in F6Publishing: 24] [Article Influence: 2.9] [Reference Citation Analysis]
221 Gillette TG, Huang W, Russell SJ, Reed SH, Johnston SA, Friedberg EC. The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes Dev. 2001;15:1528-1539. [PMID: 11410533 DOI: 10.1101/gad.869601] [Cited by in Crossref: 76] [Cited by in F6Publishing: 74] [Article Influence: 3.8] [Reference Citation Analysis]
222 Frankenberg RJ, Hsu TS, Yakota H, Kim R, Clark DS. Chemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasome. Protein Sci 2001;10:1887-96. [PMID: 11514679 DOI: 10.1110/ps.ps.05801] [Cited by in Crossref: 5] [Cited by in F6Publishing: 6] [Article Influence: 0.3] [Reference Citation Analysis]
223 Li JY, Chai BX, Zhang W, Liu YQ, Ammori JB, Mulholland MW. Ankyrin repeat and SOCS box containing protein 4 (Asb-4) interacts with GPS1 (CSN1) and inhibits c-Jun NH2-terminal kinase activity. Cell Signal 2007;19:1185-92. [PMID: 17276034 DOI: 10.1016/j.cellsig.2006.12.010] [Cited by in Crossref: 24] [Cited by in F6Publishing: 23] [Article Influence: 1.7] [Reference Citation Analysis]
224 Azuma Y, Bader DLV, Hilvert D. Substrate Sorting by a Supercharged Nanoreactor. J Am Chem Soc 2018;140:860-3. [PMID: 29278496 DOI: 10.1021/jacs.7b11210] [Cited by in Crossref: 26] [Cited by in F6Publishing: 21] [Article Influence: 8.7] [Reference Citation Analysis]
225 Chhangani D, Jana NR, Mishra A. Misfolded proteins recognition strategies of E3 ubiquitin ligases and neurodegenerative diseases. Mol Neurobiol 2013;47:302-12. [PMID: 23001884 DOI: 10.1007/s12035-012-8351-0] [Cited by in Crossref: 24] [Cited by in F6Publishing: 21] [Article Influence: 2.7] [Reference Citation Analysis]
226 Wong E, Cuervo AM. Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb Perspect Biol 2010;2:a006734. [PMID: 21068151 DOI: 10.1101/cshperspect.a006734] [Cited by in Crossref: 192] [Cited by in F6Publishing: 192] [Article Influence: 17.5] [Reference Citation Analysis]
227 Ustrell V, Hoffman L, Pratt G, Rechsteiner M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J 2002;21:3516-25. [PMID: 12093752 DOI: 10.1093/emboj/cdf333] [Cited by in Crossref: 225] [Cited by in F6Publishing: 211] [Article Influence: 11.8] [Reference Citation Analysis]
228 Mueller O, Anlasik T, Wiedemann J, Thomassen J, Wohlschlaeger J, Hagel V, Keyvani K, Schwieger I, Dahlmann B, Sure U, Sixt SU. Circulating extracellular proteasome in the cerebrospinal fluid: a study on concentration and proteolytic activity. J Mol Neurosci 2012;46:509-15. [PMID: 21881828 DOI: 10.1007/s12031-011-9631-2] [Cited by in Crossref: 24] [Cited by in F6Publishing: 20] [Article Influence: 2.4] [Reference Citation Analysis]
229 Tsvetkov P, Myers N, Eliav R, Adamovich Y, Hagai T, Adler J, Navon A, Shaul Y. NADH binds and stabilizes the 26S proteasomes independent of ATP. J Biol Chem 2014;289:11272-81. [PMID: 24596095 DOI: 10.1074/jbc.M113.537175] [Cited by in Crossref: 28] [Cited by in F6Publishing: 15] [Article Influence: 4.0] [Reference Citation Analysis]
230 Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A, Weber-Ban E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol 2009;16:647-51. [PMID: 19448618 DOI: 10.1038/nsmb.1597] [Cited by in Crossref: 144] [Cited by in F6Publishing: 139] [Article Influence: 12.0] [Reference Citation Analysis]
231 Lin G, Li D, de Carvalho LP, Deng H, Tao H, Vogt G, Wu K, Schneider J, Chidawanyika T, Warren JD, Li H, Nathan C. Inhibitors selective for mycobacterial versus human proteasomes. Nature 2009;461:621-6. [PMID: 19759536 DOI: 10.1038/nature08357] [Cited by in Crossref: 166] [Cited by in F6Publishing: 147] [Article Influence: 13.8] [Reference Citation Analysis]
232 Kim S, Saeki Y, Fukunaga K, Suzuki A, Takagi K, Yamane T, Tanaka K, Mizushima T, Kato K. Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome. J Biol Chem 2010;285:15159-66. [PMID: 20236927 DOI: 10.1074/jbc.M110.104042] [Cited by in Crossref: 17] [Cited by in F6Publishing: 7] [Article Influence: 1.5] [Reference Citation Analysis]
233 Navon A, Ciechanover A. The 26 S proteasome: from basic mechanisms to drug targeting. J Biol Chem 2009;284:33713-8. [PMID: 19812037 DOI: 10.1074/jbc.R109.018481] [Cited by in Crossref: 135] [Cited by in F6Publishing: 73] [Article Influence: 11.3] [Reference Citation Analysis]
234 Groll M, Heinemeyer W, Jäger S, Ullrich T, Bochtler M, Wolf DH, Huber R. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc Natl Acad Sci U S A 1999;96:10976-83. [PMID: 10500111 DOI: 10.1073/pnas.96.20.10976] [Cited by in Crossref: 205] [Cited by in F6Publishing: 191] [Article Influence: 9.3] [Reference Citation Analysis]
235 Tetzlaff MT, Yu W, Li M, Zhang P, Finegold M, Mahon K, Harper JW, Schwartz RJ, Elledge SJ. Defective cardiovascular development and elevated cyclin E and Notch proteins in mice lacking the Fbw7 F-box protein. Proc Natl Acad Sci U S A 2004;101:3338-45. [PMID: 14766969 DOI: 10.1073/pnas.0307875101] [Cited by in Crossref: 176] [Cited by in F6Publishing: 180] [Article Influence: 10.4] [Reference Citation Analysis]
236 Zwickl P, Voges D, Baumeister W. The proteasome: a macromolecular assembly designed for controlled proteolysis. Philos Trans R Soc Lond B Biol Sci 1999;354:1501-11. [PMID: 10582236 DOI: 10.1098/rstb.1999.0494] [Cited by in Crossref: 78] [Cited by in F6Publishing: 71] [Article Influence: 3.7] [Reference Citation Analysis]
237 Kumar B, Kim YC, DeMartino GN. The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation. J Biol Chem 2010;285:39523-35. [PMID: 20937828 DOI: 10.1074/jbc.M110.153627] [Cited by in Crossref: 27] [Cited by in F6Publishing: 19] [Article Influence: 2.5] [Reference Citation Analysis]
238 Li ME, Lauritzen HPMM, O'Neill BT, Wang CH, Cai W, Brandao BB, Sakaguchi M, Tao R, Hirshman MF, Softic S, Kahn CR. Role of p110a subunit of PI3-kinase in skeletal muscle mitochondrial homeostasis and metabolism. Nat Commun 2019;10:3412. [PMID: 31363081 DOI: 10.1038/s41467-019-11265-y] [Cited by in Crossref: 9] [Cited by in F6Publishing: 12] [Article Influence: 4.5] [Reference Citation Analysis]
239 Ferdous A, O'Neal M, Nalley K, Sikder D, Kodadek T, Johnston SA. Phosphorylation of the Gal4 DNA-binding domain is essential for activator mono-ubiquitylation and efficient promoter occupancy. Mol Biosyst 2008;4:1116-25. [PMID: 18931787 DOI: 10.1039/b809291e] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 0.5] [Reference Citation Analysis]
240 Osna NA. Hepatitis C virus and ethanol alter antigen presentation in liver cells. World J Gastroenterol 2009; 15(10): 1201-1208 [PMID: 19291820 DOI: 10.3748/wjg.15.1201] [Cited by in CrossRef: 14] [Cited by in F6Publishing: 19] [Article Influence: 1.2] [Reference Citation Analysis]
241 Kang MS, Kim SR, Kwack P, Lim BK, Ahn SW, Rho YM, Seong IS, Park SC, Eom SH, Cheong GW, Chung CH. Molecular architecture of the ATP-dependent CodWX protease having an N-terminal serine active site. EMBO J 2003;22:2893-902. [PMID: 12805205 DOI: 10.1093/emboj/cdg289] [Cited by in Crossref: 16] [Cited by in F6Publishing: 11] [Article Influence: 0.9] [Reference Citation Analysis]
242 Glickman MH, Rubin DM, Fu H, Larsen CN, Coux O, Wefes I, Pfeifer G, Cjeka Z, Vierstra R, Baumeister W, Fried V, Finley D. Functional analysis of the proteasome regulatory particle. Mol Biol Rep 1999;26:21-8. [PMID: 10363642 DOI: 10.1023/a:1006928316738] [Cited by in Crossref: 84] [Cited by in F6Publishing: 25] [Article Influence: 3.8] [Reference Citation Analysis]
243 Sasaki K, Hamazaki J, Koike M, Hirano Y, Komatsu M, Uchiyama Y, Tanaka K, Murata S. PAC1 gene knockout reveals an essential role of chaperone-mediated 20S proteasome biogenesis and latent 20S proteasomes in cellular homeostasis. Mol Cell Biol 2010;30:3864-74. [PMID: 20498273 DOI: 10.1128/MCB.00216-10] [Cited by in Crossref: 27] [Cited by in F6Publishing: 15] [Article Influence: 2.5] [Reference Citation Analysis]
244 Papa FR, Amerik AY, Hochstrasser M. Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Mol Biol Cell 1999;10:741-56. [PMID: 10069815 DOI: 10.1091/mbc.10.3.741] [Cited by in Crossref: 96] [Cited by in F6Publishing: 93] [Article Influence: 4.4] [Reference Citation Analysis]
245 Hamazaki J, Murata S. ER-Resident Transcription Factor Nrf1 Regulates Proteasome Expression and Beyond. Int J Mol Sci 2020;21:E3683. [PMID: 32456207 DOI: 10.3390/ijms21103683] [Cited by in Crossref: 10] [Cited by in F6Publishing: 7] [Article Influence: 10.0] [Reference Citation Analysis]
246 Loch S, Tampé R. Viral evasion of the MHC class I antigen-processing machinery. Pflugers Arch 2005;451:409-17. [PMID: 16086162 DOI: 10.1007/s00424-005-1420-8] [Cited by in Crossref: 26] [Cited by in F6Publishing: 27] [Article Influence: 1.6] [Reference Citation Analysis]
247 Thompson D, Hakala K, DeMartino GN. Subcomplexes of PA700, the 19 S regulator of the 26 S proteasome, reveal relative roles of AAA subunits in 26 S proteasome assembly and activation and ATPase activity. J Biol Chem 2009;284:24891-903. [PMID: 19589775 DOI: 10.1074/jbc.M109.023218] [Cited by in Crossref: 48] [Cited by in F6Publishing: 35] [Article Influence: 4.0] [Reference Citation Analysis]
248 Horwich AL, Weber-Ban EU, Finley D. Chaperone rings in protein folding and degradation. Proc Natl Acad Sci U S A 1999;96:11033-40. [PMID: 10500119 DOI: 10.1073/pnas.96.20.11033] [Cited by in Crossref: 139] [Cited by in F6Publishing: 131] [Article Influence: 6.3] [Reference Citation Analysis]
249 Khor B, Bredemeyer AL, Huang CY, Turnbull IR, Evans R, Maggi LB Jr, White JM, Walker LM, Carnes K, Hess RA, Sleckman BP. Proteasome activator PA200 is required for normal spermatogenesis. Mol Cell Biol 2006;26:2999-3007. [PMID: 16581775 DOI: 10.1128/MCB.26.8.2999-3007.2006] [Cited by in Crossref: 97] [Cited by in F6Publishing: 63] [Article Influence: 6.5] [Reference Citation Analysis]
250 Solcia E, Sommi P, Necchi V, Vitali A, Manca R, Ricci V. Particle-rich cytoplasmic structure (PaCS): identification, natural history, role in cell biology and pathology. Biomolecules 2014;4:848-61. [PMID: 25247343 DOI: 10.3390/biom4030848] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 1.0] [Reference Citation Analysis]
251 Yao Y, Toth CR, Huang L, Wong ML, Dias P, Burlingame AL, Coffino P, Wang CC. alpha5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings. Biochem J 1999;344 Pt 2:349-58. [PMID: 10567215 DOI: 10.1042/0264-6021:3440349] [Cited by in Crossref: 10] [Cited by in F6Publishing: 18] [Article Influence: 0.5] [Reference Citation Analysis]
252 Eisele MR, Reed RG, Rudack T, Schweitzer A, Beck F, Nagy I, Pfeifer G, Plitzko JM, Baumeister W, Tomko RJ Jr, Sakata E. Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating. Cell Rep 2018;24:1301-1315.e5. [PMID: 30067984 DOI: 10.1016/j.celrep.2018.07.004] [Cited by in Crossref: 56] [Cited by in F6Publishing: 47] [Article Influence: 28.0] [Reference Citation Analysis]
253 Lim HS, Archer CT, Kodadek T. Identification of a peptoid inhibitor of the proteasome 19S regulatory particle. J Am Chem Soc 2007;129:7750-1. [PMID: 17536803 DOI: 10.1021/ja072027p] [Cited by in Crossref: 85] [Cited by in F6Publishing: 77] [Article Influence: 6.1] [Reference Citation Analysis]
254 Jung HJ, Chen Z, Wang M, Fayad L, Romaguera J, Kwak LW, McCarty N. Calcium blockers decrease the bortezomib resistance in mantle cell lymphoma via manipulation of tissue transglutaminase activities. Blood 2012;119:2568-78. [PMID: 22294726 DOI: 10.1182/blood-2011-09-377598] [Cited by in Crossref: 15] [Cited by in F6Publishing: 15] [Article Influence: 1.7] [Reference Citation Analysis]
255 Ishii K, Noda M, Yagi H, Thammaporn R, Seetaha S, Satoh T, Kato K, Uchiyama S. Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6. Sci Rep 2015;5:18167. [PMID: 26657688 DOI: 10.1038/srep18167] [Cited by in Crossref: 23] [Cited by in F6Publishing: 23] [Article Influence: 3.8] [Reference Citation Analysis]
256 Bieniossek C, Schalch T, Bumann M, Meister M, Meier R, Baumann U. The molecular architecture of the metalloprotease FtsH. Proc Natl Acad Sci U S A 2006;103:3066-71. [PMID: 16484367 DOI: 10.1073/pnas.0600031103] [Cited by in Crossref: 124] [Cited by in F6Publishing: 111] [Article Influence: 8.3] [Reference Citation Analysis]
257 Inobe T, Matouschek A. Protein targeting to ATP-dependent proteases. Curr Opin Struct Biol 2008;18:43-51. [PMID: 18276129 DOI: 10.1016/j.sbi.2007.12.014] [Cited by in Crossref: 35] [Cited by in F6Publishing: 32] [Article Influence: 2.7] [Reference Citation Analysis]
258 Mihalovits LM, Ferenczy GG, Keserű GM. Mechanistic and thermodynamic characterization of oxathiazolones as potent and selective covalent immunoproteasome inhibitors. Comput Struct Biotechnol J 2021;19:4486-96. [PMID: 34471494 DOI: 10.1016/j.csbj.2021.08.008] [Reference Citation Analysis]
259 Franzetti B, Schoehn G, Garcia D, Ruigrok RW, Zaccai G. Characterization of the proteasome from the extremely halophilic archaeon Haloarcula marismortui. Archaea 2002;1:53-61. [PMID: 15803659 DOI: 10.1155/2002/601719] [Cited by in Crossref: 15] [Cited by in F6Publishing: 12] [Article Influence: 0.9] [Reference Citation Analysis]
260 Hamazaki J, Sasaki K, Kawahara H, Hisanaga S, Tanaka K, Murata S. Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse development. Mol Cell Biol 2007;27:6629-38. [PMID: 17646385 DOI: 10.1128/MCB.00509-07] [Cited by in Crossref: 72] [Cited by in F6Publishing: 41] [Article Influence: 5.1] [Reference Citation Analysis]
261 Imai J, Maruya M, Yashiroda H, Yahara I, Tanaka K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J 2003;22:3557-67. [PMID: 12853471 DOI: 10.1093/emboj/cdg349] [Cited by in Crossref: 168] [Cited by in F6Publishing: 155] [Article Influence: 9.3] [Reference Citation Analysis]
262 Lee J, Udugamasooriya DG, Lim HS, Kodadek T. Potent and selective photo-inactivation of proteins with peptoid-ruthenium conjugates. Nat Chem Biol 2010;6:258-60. [PMID: 20228793 DOI: 10.1038/nchembio.333] [Cited by in Crossref: 70] [Cited by in F6Publishing: 56] [Article Influence: 6.4] [Reference Citation Analysis]
263 Nguyen H, Gitig DM, Koff A. Cell-free degradation of p27(kip1), a G1 cyclin-dependent kinase inhibitor, is dependent on CDK2 activity and the proteasome. Mol Cell Biol 1999;19:1190-201. [PMID: 9891053 DOI: 10.1128/MCB.19.2.1190] [Cited by in Crossref: 110] [Cited by in F6Publishing: 40] [Article Influence: 5.0] [Reference Citation Analysis]
264 Archer CT, Burdine L, Liu B, Ferdous A, Johnston SA, Kodadek T. Physical and functional interactions of monoubiquitylated transactivators with the proteasome. J Biol Chem 2008;283:21789-98. [PMID: 18515799 DOI: 10.1074/jbc.M803075200] [Cited by in Crossref: 33] [Cited by in F6Publishing: 23] [Article Influence: 2.5] [Reference Citation Analysis]
265 Benharouga M, Haardt M, Kartner N, Lukacs GL. COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments. J Cell Biol 2001;153:957-70. [PMID: 11381082 DOI: 10.1083/jcb.153.5.957] [Cited by in Crossref: 71] [Cited by in F6Publishing: 71] [Article Influence: 3.6] [Reference Citation Analysis]
266 Graham SH, Liu H. Life and death in the trash heap: The ubiquitin proteasome pathway and UCHL1 in brain aging, neurodegenerative disease and cerebral Ischemia. Ageing Res Rev 2017;34:30-8. [PMID: 27702698 DOI: 10.1016/j.arr.2016.09.011] [Cited by in Crossref: 42] [Cited by in F6Publishing: 39] [Article Influence: 8.4] [Reference Citation Analysis]
267 Necchi V, Sommi P, Ricci V, Solcia E. In vivo accumulation of Helicobacter pylori products, NOD1, ubiquitinated proteins and proteasome in a novel cytoplasmic structure. PLoS One. 2010;5:e9716. [PMID: 20300534 DOI: 10.1371/journal.pone.0009716] [Cited by in Crossref: 31] [Cited by in F6Publishing: 34] [Article Influence: 2.8] [Reference Citation Analysis]
268 Fu XY, Wang HY, Tan L, Liu SQ, Cao HF, Wu MC. Overexpression of p28/gankyrin in human hepatocellular carcinoma and its clinical significance. World J Gastroenterol 2002; 8(4): 638-643 [PMID: 12174370 DOI: 10.3748/wjg.v8.i4.638] [Cited by in CrossRef: 62] [Cited by in F6Publishing: 57] [Article Influence: 3.3] [Reference Citation Analysis]
269 Lin L, DeMartino GN, Greene WC. Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50-p105 heterodimers and is required for effective p50 production. EMBO J 2000;19:4712-22. [PMID: 10970863 DOI: 10.1093/emboj/19.17.4712] [Cited by in Crossref: 81] [Cited by in F6Publishing: 74] [Article Influence: 3.9] [Reference Citation Analysis]
270 Feng P, Scott CW, Cho NH, Nakamura H, Chung YH, Monteiro MJ, Jung JU. Kaposi's sarcoma-associated herpesvirus K7 protein targets a ubiquitin-like/ubiquitin-associated domain-containing protein to promote protein degradation. Mol Cell Biol 2004;24:3938-48. [PMID: 15082787 DOI: 10.1128/MCB.24.9.3938-3948.2004] [Cited by in Crossref: 42] [Cited by in F6Publishing: 28] [Article Influence: 2.5] [Reference Citation Analysis]
271 Osaka F, Saeki M, Katayama S, Aida N, Toh-E A, Kominami K, Toda T, Suzuki T, Chiba T, Tanaka K, Kato S. Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast. EMBO J 2000;19:3475-84. [PMID: 10880460 DOI: 10.1093/emboj/19.13.3475] [Cited by in Crossref: 151] [Cited by in F6Publishing: 162] [Article Influence: 7.2] [Reference Citation Analysis]
272 Li X, Demartino GN. Variably modulated gating of the 26S proteasome by ATP and polyubiquitin. Biochem J 2009;421:397-404. [PMID: 19435460 DOI: 10.1042/BJ20090528] [Cited by in Crossref: 38] [Cited by in F6Publishing: 26] [Article Influence: 3.2] [Reference Citation Analysis]
273 Tsalikis J, Abdel-Nour M, Farahvash A, Sorbara MT, Poon S, Philpott DJ, Girardin SE. Isoginkgetin, a Natural Biflavonoid Proteasome Inhibitor, Sensitizes Cancer Cells to Apoptosis via Disruption of Lysosomal Homeostasis and Impaired Protein Clearance. Mol Cell Biol 2019;39:e00489-18. [PMID: 30910794 DOI: 10.1128/MCB.00489-18] [Cited by in Crossref: 7] [Cited by in F6Publishing: 3] [Article Influence: 3.5] [Reference Citation Analysis]
274 Jayarapu K, Griffin TA. Differential intra-proteasome interactions involving standard and immunosubunits. Biochem Biophys Res Commun 2007;358:867-72. [PMID: 17506986 DOI: 10.1016/j.bbrc.2007.05.011] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.1] [Reference Citation Analysis]
275 Neves MA, Yeager M, Abagyan R. Unusual arginine formations in protein function and assembly: rings, strings, and stacks. J Phys Chem B 2012;116:7006-13. [PMID: 22497303 DOI: 10.1021/jp3009699] [Cited by in Crossref: 57] [Cited by in F6Publishing: 50] [Article Influence: 6.3] [Reference Citation Analysis]
276 Snyder H, Wolozin B. Pathological proteins in Parkinson's disease: focus on the proteasome. J Mol Neurosci 2004;24:425-42. [PMID: 15655264 DOI: 10.1385/JMN:24:3:425] [Cited by in Crossref: 44] [Cited by in F6Publishing: 14] [Article Influence: 2.8] [Reference Citation Analysis]
277 Jansen AH, Reits EA, Hol EM. The ubiquitin proteasome system in glia and its role in neurodegenerative diseases. Front Mol Neurosci 2014;7:73. [PMID: 25152710 DOI: 10.3389/fnmol.2014.00073] [Cited by in Crossref: 66] [Cited by in F6Publishing: 60] [Article Influence: 9.4] [Reference Citation Analysis]
278 Na X, Duan HO, Messing EM, Schoen SR, Ryan CK, di Sant'Agnese PA, Golemis EA, Wu G. Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel-Lindau protein. EMBO J 2003;22:4249-59. [PMID: 12912922 DOI: 10.1093/emboj/cdg410] [Cited by in Crossref: 61] [Cited by in F6Publishing: 63] [Article Influence: 3.4] [Reference Citation Analysis]
279 Singh Gautam AK, Balakrishnan S, Venkatraman P. Direct ubiquitin independent recognition and degradation of a folded protein by the eukaryotic proteasomes-origin of intrinsic degradation signals. PLoS One 2012;7:e34864. [PMID: 22506054 DOI: 10.1371/journal.pone.0034864] [Cited by in Crossref: 14] [Cited by in F6Publishing: 12] [Article Influence: 1.6] [Reference Citation Analysis]
280 Azim MK, Noor S. Characterization of protomer interfaces in HslV protease; the bacterial homologue of 20S proteasome. Protein J 2007;26:213-9. [PMID: 17522969 DOI: 10.1007/s10930-006-9048-x] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 0.2] [Reference Citation Analysis]
281 Simkus C, Bhattacharyya A, Zhou M, Veenstra TD, Jones JM. Correlation between recombinase activating gene 1 ubiquitin ligase activity and V(D)J recombination. Immunology 2009;128:206-17. [PMID: 19740377 DOI: 10.1111/j.1365-2567.2009.03101.x] [Cited by in Crossref: 16] [Cited by in F6Publishing: 13] [Article Influence: 1.3] [Reference Citation Analysis]
282 Kleijnen MF, Alarcon RM, Howley PM. The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. Mol Biol Cell 2003;14:3868-75. [PMID: 12972570 DOI: 10.1091/mbc.e02-11-0766] [Cited by in Crossref: 78] [Cited by in F6Publishing: 59] [Article Influence: 4.3] [Reference Citation Analysis]
283 Murat P, Tellam J. Effects of messenger RNA structure and other translational control mechanisms on major histocompatibility complex-I mediated antigen presentation. Wiley Interdiscip Rev RNA 2015;6:157-71. [PMID: 25264139 DOI: 10.1002/wrna.1262] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 0.7] [Reference Citation Analysis]
284 Simsek E, Mehta A, Zhou T, Dwek RA, Block T. Hepatitis B virus large and middle glycoproteins are degraded by a proteasome pathway in glucosidase-inhibited cells but not in cells with functional glucosidase enzyme. J Virol. 2005;79:12914-12920. [PMID: 16188993 DOI: 10.1128/jvi.79.20.12914-12920.2005] [Cited by in Crossref: 19] [Cited by in F6Publishing: 12] [Article Influence: 1.2] [Reference Citation Analysis]
285 García-Echeverría C. Peptide and Peptide-Like Modulators of 20S Proteasome Enzymatic Activity in Cancer Cells. Int J Pept Res Ther 2006;12:49-64. [PMID: 19617921 DOI: 10.1007/s10989-005-9001-4] [Cited by in Crossref: 10] [Cited by in F6Publishing: 7] [Article Influence: 0.7] [Reference Citation Analysis]
286 Kwegyir-Afful AK, Ramalingam S, Purushottamachar P, Ramamurthy VP, Njar VC. Galeterone and VNPT55 induce proteasomal degradation of AR/AR-V7, induce significant apoptosis via cytochrome c release and suppress growth of castration resistant prostate cancer xenografts in vivo. Oncotarget 2015;6:27440-60. [PMID: 26196320 DOI: 10.18632/oncotarget.4578] [Cited by in Crossref: 62] [Cited by in F6Publishing: 64] [Article Influence: 12.4] [Reference Citation Analysis]
287 Hamazaki J, Hirayama S, Murata S. Redundant Roles of Rpn10 and Rpn13 in Recognition of Ubiquitinated Proteins and Cellular Homeostasis. PLoS Genet 2015;11:e1005401. [PMID: 26222436 DOI: 10.1371/journal.pgen.1005401] [Cited by in Crossref: 53] [Cited by in F6Publishing: 49] [Article Influence: 8.8] [Reference Citation Analysis]
288 Mayer WE, Uinuk-Ool T, Tichy H, Gartland LA, Klein J, Cooper MD. Isolation and characterization of lymphocyte-like cells from a lamprey. Proc Natl Acad Sci U S A 2002;99:14350-5. [PMID: 12388781 DOI: 10.1073/pnas.212527499] [Cited by in Crossref: 110] [Cited by in F6Publishing: 93] [Article Influence: 5.8] [Reference Citation Analysis]
289 Tanaka K. The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci 2009;85:12-36. [PMID: 19145068 DOI: 10.2183/pjab.85.12] [Cited by in Crossref: 362] [Cited by in F6Publishing: 322] [Article Influence: 30.2] [Reference Citation Analysis]
290 Rechsteiner M, Realini C, Ustrell V. The proteasome activator 11 S REG (PA28) and class I antigen presentation. Biochem J. 2000;345 Pt1:1-15. [PMID: 10600633 DOI: 10.1042/0264-6021:3450001] [Cited by in Crossref: 85] [Cited by in F6Publishing: 59] [Article Influence: 4.0] [Reference Citation Analysis]
291 Albright JM, Romero J, Saini V, Sixt SU, Bird MD, Kovacs EJ, Gamelli RL, Peters J, Majetschak M. Proteasomes in human bronchoalveolar lavage fluid after burn and inhalation injury. J Burn Care Res 2009;30:948-56. [PMID: 19826256 DOI: 10.1097/BCR.0b013e3181c07f37] [Cited by in Crossref: 3] [Cited by in F6Publishing: 7] [Article Influence: 0.3] [Reference Citation Analysis]
292 Zhan W, Singh PK, Ban Y, Qing X, Ah Kioon MD, Fan H, Zhao Q, Wang R, Sukenick G, Salmon J, Warren JD, Ma X, Barrat FJ, Nathan CF, Lin G. Structure-Activity Relationships of Noncovalent Immunoproteasome β5i-Selective Dipeptides. J Med Chem 2020;63:13103-23. [PMID: 33095579 DOI: 10.1021/acs.jmedchem.0c01520] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 4.0] [Reference Citation Analysis]
293 Majetschak M, Perez M, Sorell LT, Lam J, Maldonado ME, Hoffman RW. Circulating 20S proteasome levels in patients with mixed connective tissue disease and systemic lupus erythematosus. Clin Vaccine Immunol 2008;15:1489-93. [PMID: 18667633 DOI: 10.1128/CVI.00187-08] [Cited by in Crossref: 24] [Cited by in F6Publishing: 13] [Article Influence: 1.8] [Reference Citation Analysis]
294 Ferrington DA, Gregerson DS. Immunoproteasomes: structure, function, and antigen presentation. Prog Mol Biol Transl Sci 2012;109:75-112. [PMID: 22727420 DOI: 10.1016/B978-0-12-397863-9.00003-1] [Cited by in Crossref: 201] [Cited by in F6Publishing: 140] [Article Influence: 25.1] [Reference Citation Analysis]
295 Jomaa A, Damjanovic D, Leong V, Ghirlando R, Iwanczyk J, Ortega J. The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity. J Bacteriol 2007;189:706-16. [PMID: 17122339 DOI: 10.1128/JB.01334-06] [Cited by in Crossref: 39] [Cited by in F6Publishing: 22] [Article Influence: 2.6] [Reference Citation Analysis]
296 Matia-González AM, Laing EE, Gerber AP. Conserved mRNA-binding proteomes in eukaryotic organisms. Nat Struct Mol Biol 2015;22:1027-33. [PMID: 26595419 DOI: 10.1038/nsmb.3128] [Cited by in Crossref: 101] [Cited by in F6Publishing: 87] [Article Influence: 16.8] [Reference Citation Analysis]
297 Lasker K, Topf M, Sali A, Wolfson HJ. Inferential optimization for simultaneous fitting of multiple components into a CryoEM map of their assembly. J Mol Biol 2009;388:180-94. [PMID: 19233204 DOI: 10.1016/j.jmb.2009.02.031] [Cited by in Crossref: 99] [Cited by in F6Publishing: 88] [Article Influence: 8.3] [Reference Citation Analysis]
298 Grünenfelder B, Tawfilis S, Gehrig S, ØSterås M, Eglin D, Jenal U. Identification of the protease and the turnover signal responsible for cell cycle-dependent degradation of the Caulobacter FliF motor protein. J Bacteriol 2004;186:4960-71. [PMID: 15262933 DOI: 10.1128/JB.186.15.4960-4971.2004] [Cited by in Crossref: 22] [Cited by in F6Publishing: 16] [Article Influence: 1.3] [Reference Citation Analysis]
299 Butenko Y, Lin A, Naveh L, Kupervaser M, Levin Y, Reich Z, Adam Z. Differential Roles of the Thylakoid Lumenal Deg Protease Homologs in Chloroplast Proteostasis. Plant Physiol 2018;178:1065-80. [PMID: 30237207 DOI: 10.1104/pp.18.00912] [Cited by in Crossref: 8] [Cited by in F6Publishing: 10] [Article Influence: 2.7] [Reference Citation Analysis]
300 Al-Shami A, Jhaver KG, Vogel P, Wilkins C, Humphries J, Davis JJ, Xu N, Potter DG, Gerhardt B, Mullinax R, Shirley CR, Anderson SJ, Oravecz T. Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development. PLoS One 2010;5:e13654. [PMID: 21048919 DOI: 10.1371/journal.pone.0013654] [Cited by in Crossref: 63] [Cited by in F6Publishing: 62] [Article Influence: 5.7] [Reference Citation Analysis]
301 Bai M, Zhao X, Sahara K, Ohte Y, Hirano Y, Kaneko T, Yashiroda H, Murata S. Assembly mechanisms of specialized core particles of the proteasome. Biomolecules 2014;4:662-77. [PMID: 25033340 DOI: 10.3390/biom4030662] [Cited by in Crossref: 9] [Cited by in F6Publishing: 11] [Article Influence: 1.3] [Reference Citation Analysis]
302 Berges C, Haberstock H, Fuchs D, Miltz M, Sadeghi M, Opelz G, Daniel V, Naujokat C. Proteasome inhibition suppresses essential immune functions of human CD4+ T cells. Immunology. 2008;124:234-246. [PMID: 18217957 DOI: 10.1111/j.1365-2567.2007.02761.x] [Cited by in Crossref: 84] [Cited by in F6Publishing: 86] [Article Influence: 6.5] [Reference Citation Analysis]
303 Gillette TG, Kumar B, Thompson D, Slaughter CA, DeMartino GN. Differential roles of the COOH termini of AAA subunits of PA700 (19 S regulator) in asymmetric assembly and activation of the 26 S proteasome. J Biol Chem 2008;283:31813-22. [PMID: 18796432 DOI: 10.1074/jbc.M805935200] [Cited by in Crossref: 116] [Cited by in F6Publishing: 83] [Article Influence: 8.9] [Reference Citation Analysis]
304 Krycer JR, Pang CN, Wilkins MR. High throughput protein-protein interaction data: clues for the architecture of protein complexes. Proteome Sci 2008;6:32. [PMID: 19032795 DOI: 10.1186/1477-5956-6-32] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.1] [Reference Citation Analysis]
305 Fu X, Liu R, Sanchez I, Silva-Sanchez C, Hepowit NL, Cao S, Chen S, Maupin-Furlow J. Ubiquitin-Like Proteasome System Represents a Eukaryotic-Like Pathway for Targeted Proteolysis in Archaea. mBio 2016;7:e00379-16. [PMID: 27190215 DOI: 10.1128/mBio.00379-16] [Cited by in Crossref: 10] [Cited by in F6Publishing: 15] [Article Influence: 2.0] [Reference Citation Analysis]
306 Gu ZC, Wu E, Sailer C, Jando J, Styles E, Eisenkolb I, Kuschel M, Bitschar K, Wang X, Huang L, Vissa A, Yip CM, Yedidi RS, Friesen H, Enenkel C. Ubiquitin orchestrates proteasome dynamics between proliferation and quiescence in yeast. Mol Biol Cell 2017;28:2479-91. [PMID: 28768827 DOI: 10.1091/mbc.E17-03-0162] [Cited by in Crossref: 20] [Cited by in F6Publishing: 18] [Article Influence: 5.0] [Reference Citation Analysis]
307 Hutschenreiter S, Tinazli A, Model K, Tampé R. Two-substrate association with the 20S proteasome at single-molecule level. EMBO J 2004;23:2488-97. [PMID: 15175655 DOI: 10.1038/sj.emboj.7600262] [Cited by in Crossref: 46] [Cited by in F6Publishing: 44] [Article Influence: 2.7] [Reference Citation Analysis]
308 Gillette TG, Gonzalez F, Delahodde A, Johnston SA, Kodadek T. Physical and functional association of RNA polymerase II and the proteasome. Proc Natl Acad Sci U S A 2004;101:5904-9. [PMID: 15069196 DOI: 10.1073/pnas.0305411101] [Cited by in Crossref: 123] [Cited by in F6Publishing: 116] [Article Influence: 7.2] [Reference Citation Analysis]
309 Roperch JP, Lethrone F, Prieur S, Piouffre L, Israeli D, Tuynder M, Nemani M, Pasturaud P, Gendron MC, Dausset J, Oren M, Amson RB, Telerman A. SIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: identification of common effectors with p53 and p21(Waf1). Proc Natl Acad Sci U S A 1999;96:8070-3. [PMID: 10393949 DOI: 10.1073/pnas.96.14.8070] [Cited by in Crossref: 86] [Cited by in F6Publishing: 85] [Article Influence: 3.9] [Reference Citation Analysis]
310 Cho SK, Ryu MY, Song C, Kwak JM, Kim WT. Arabidopsis PUB22 and PUB23 are homologous U-Box E3 ubiquitin ligases that play combinatory roles in response to drought stress. Plant Cell 2008;20:1899-914. [PMID: 18664614 DOI: 10.1105/tpc.108.060699] [Cited by in Crossref: 151] [Cited by in F6Publishing: 134] [Article Influence: 11.6] [Reference Citation Analysis]
311 Takeuchi J, Fujimuro M, Yokosawa H, Tanaka K, Toh-e A. Rpn9 is required for efficient assembly of the yeast 26S proteasome. Mol Cell Biol 1999;19:6575-84. [PMID: 10490597 DOI: 10.1128/MCB.19.10.6575] [Cited by in Crossref: 51] [Cited by in F6Publishing: 24] [Article Influence: 2.4] [Reference Citation Analysis]
312 Feng S, Ma L, Wang X, Xie D, Dinesh-Kumar SP, Wei N, Deng XW. The COP9 signalosome interacts physically with SCF COI1 and modulates jasmonate responses. Plant Cell 2003;15:1083-94. [PMID: 12724535 DOI: 10.1105/tpc.010207] [Cited by in Crossref: 147] [Cited by in F6Publishing: 136] [Article Influence: 8.2] [Reference Citation Analysis]
313 Yang ZQ, Kwok BH, Lin S, Koldobskiy MA, Crews CM, Danishefsky SJ. Simplified synthetic TMC-95A/B analogues retain the potency of proteasome inhibitory activity. Chembiochem 2003;4:508-13. [PMID: 12794861 DOI: 10.1002/cbic.200300560] [Cited by in Crossref: 23] [Cited by in F6Publishing: 19] [Article Influence: 1.4] [Reference Citation Analysis]
314 Rajan VR, Mitch WE. Muscle wasting in chronic kidney disease: the role of the ubiquitin proteasome system and its clinical impact. Pediatr Nephrol 2008;23:527-35. [PMID: 17987322 DOI: 10.1007/s00467-007-0594-z] [Cited by in Crossref: 48] [Cited by in F6Publishing: 39] [Article Influence: 3.4] [Reference Citation Analysis]
315 Lucchiari-Hartz M, Lindo V, Hitziger N, Gaedicke S, Saveanu L, van Endert PM, Greer F, Eichmann K, Niedermann G. Differential proteasomal processing of hydrophobic and hydrophilic protein regions: contribution to cytotoxic T lymphocyte epitope clustering in HIV-1-Nef. Proc Natl Acad Sci U S A 2003;100:7755-60. [PMID: 12810958 DOI: 10.1073/pnas.1232228100] [Cited by in Crossref: 30] [Cited by in F6Publishing: 30] [Article Influence: 1.7] [Reference Citation Analysis]
316 Song YM, Song SO, Jung YK, Kang ES, Cha BS, Lee HC, Lee BW. Dimethyl sulfoxide reduces hepatocellular lipid accumulation through autophagy induction. Autophagy 2012;8:1085-97. [PMID: 22722716 DOI: 10.4161/auto.20260] [Cited by in Crossref: 36] [Cited by in F6Publishing: 36] [Article Influence: 4.0] [Reference Citation Analysis]
317 Cui Z, Scruggs SB, Gilda JE, Ping P, Gomes AV. Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond. J Mol Cell Cardiol 2014;71:32-42. [PMID: 24140722 DOI: 10.1016/j.yjmcc.2013.10.008] [Cited by in Crossref: 54] [Cited by in F6Publishing: 57] [Article Influence: 6.8] [Reference Citation Analysis]
318 Wang EW, Kessler BM, Borodovsky A, Cravatt BF, Bogyo M, Ploegh HL, Glas R. Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity. Proc Natl Acad Sci U S A 2000;97:9990-5. [PMID: 10954757 DOI: 10.1073/pnas.180328897] [Cited by in Crossref: 86] [Cited by in F6Publishing: 80] [Article Influence: 4.1] [Reference Citation Analysis]
319 Tanahashi N, Kawahara H, Murakami Y, Tanaka K. The proteasome-dependent proteolytic system. Mol Biol Rep 1999;26:3-9. [PMID: 10363639 DOI: 10.1023/a:1006909522731] [Cited by in Crossref: 32] [Cited by in F6Publishing: 14] [Article Influence: 1.5] [Reference Citation Analysis]
320 Humbard MA, Stevens SM Jr, Maupin-Furlow JA. Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii. J Bacteriol 2006;188:7521-30. [PMID: 16950923 DOI: 10.1128/JB.00943-06] [Cited by in Crossref: 23] [Cited by in F6Publishing: 17] [Article Influence: 1.5] [Reference Citation Analysis]
321 Hirsch C, Blom D, Ploegh HL. A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J 2003;22:1036-46. [PMID: 12606569 DOI: 10.1093/emboj/cdg107] [Cited by in Crossref: 162] [Cited by in F6Publishing: 154] [Article Influence: 9.0] [Reference Citation Analysis]
322 Gautier-Bert K, Murol B, Jarrousse AS, Ballut L, Badaoui S, Petit F, Schmid HP. Substrate affinity and substrate specificity of proteasomes with RNase activity. Mol Biol Rep 2003;30:1-7. [PMID: 12688529 DOI: 10.1023/a:1022261925117] [Cited by in Crossref: 19] [Cited by in F6Publishing: 10] [Article Influence: 1.1] [Reference Citation Analysis]
323 Alghamdi A, Vallortigara J, Howlett DR, Broadstock M, Hortobágyi T, Ballard C, Thomas AJ, O'Brien JT, Aarsland D, Attems J, Francis PT, Whitfield DR. Reduction of RPT6/S8 (a Proteasome Component) and Proteasome Activity in the Cortex is Associated with Cognitive Impairment in Lewy Body Dementia. J Alzheimers Dis 2017;57:373-86. [PMID: 28269775 DOI: 10.3233/JAD-160946] [Cited by in Crossref: 12] [Cited by in F6Publishing: 7] [Article Influence: 4.0] [Reference Citation Analysis]
324 Humbard MA, Maupin-Furlow JA. Prokaryotic proteasomes: nanocompartments of degradation. J Mol Microbiol Biotechnol 2013;23:321-34. [PMID: 23920495 DOI: 10.1159/000351348] [Cited by in Crossref: 18] [Cited by in F6Publishing: 16] [Article Influence: 2.3] [Reference Citation Analysis]
325 Trader DJ, Simanski S, Kodadek T. A reversible and highly selective inhibitor of the proteasomal ubiquitin receptor rpn13 is toxic to multiple myeloma cells. J Am Chem Soc 2015;137:6312-9. [PMID: 25914958 DOI: 10.1021/jacs.5b02069] [Cited by in Crossref: 55] [Cited by in F6Publishing: 50] [Article Influence: 9.2] [Reference Citation Analysis]
326 Brancolini C, Iuliano L. Proteotoxic Stress and Cell Death in Cancer Cells. Cancers (Basel) 2020;12:E2385. [PMID: 32842524 DOI: 10.3390/cancers12092385] [Cited by in Crossref: 6] [Cited by in F6Publishing: 5] [Article Influence: 6.0] [Reference Citation Analysis]
327 Liu J, Qiu L, Xia J, Chen S, Yu X, Zhou Y. ZGDHu-1 for cancer therapy. Oncol Lett 2017;14:6334-40. [PMID: 29344112 DOI: 10.3892/ol.2017.7096] [Reference Citation Analysis]
328 Morrow ME, Kim MI, Ronau JA, Sheedlo MJ, White RR, Chaney J, Paul LN, Lill MA, Artavanis-Tsakonas K, Das C. Stabilization of an unusual salt bridge in ubiquitin by the extra C-terminal domain of the proteasome-associated deubiquitinase UCH37 as a mechanism of its exo specificity. Biochemistry 2013;52:3564-78. [PMID: 23617878 DOI: 10.1021/bi4003106] [Cited by in Crossref: 17] [Cited by in F6Publishing: 16] [Article Influence: 2.1] [Reference Citation Analysis]
329 Zhou G, Kowalczyk D, Humbard MA, Rohatgi S, Maupin-Furlow JA. Proteasomal components required for cell growth and stress responses in the haloarchaeon Haloferax volcanii. J Bacteriol 2008;190:8096-105. [PMID: 18931121 DOI: 10.1128/JB.01180-08] [Cited by in Crossref: 45] [Cited by in F6Publishing: 40] [Article Influence: 3.5] [Reference Citation Analysis]
330 Hansen TH, Bouvier M. MHC class I antigen presentation: learning from viral evasion strategies. Nat Rev Immunol 2009;9:503-13. [PMID: 19498380 DOI: 10.1038/nri2575] [Cited by in Crossref: 258] [Cited by in F6Publishing: 242] [Article Influence: 21.5] [Reference Citation Analysis]
331 Wei BL, Denton PW, O'Neill E, Luo T, Foster JL, Garcia JV. Inhibition of lysosome and proteasome function enhances human immunodeficiency virus type 1 infection. J Virol. 2005;79:5705-5712. [PMID: 15827185 DOI: 10.1128/jvi.79.9.5705-5712.2005] [Cited by in Crossref: 78] [Cited by in F6Publishing: 71] [Article Influence: 4.9] [Reference Citation Analysis]
332 Shrestha RK, Ronau JA, Davies CW, Guenette RG, Strieter ER, Paul LN, Das C. Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and product. Biochemistry 2014;53:3199-217. [PMID: 24787148 DOI: 10.1021/bi5003162] [Cited by in Crossref: 39] [Cited by in F6Publishing: 36] [Article Influence: 5.6] [Reference Citation Analysis]
333 Shin SW, Shimizu N, Tokoro M, Nishikawa S, Hatanaka Y, Anzai M, Hamazaki J, Kishigami S, Saeki K, Hosoi Y, Iritani A, Murata S, Matsumoto K. Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition. Biol Open 2013;2:170-82. [PMID: 23429752 DOI: 10.1242/bio.20123020] [Cited by in Crossref: 22] [Cited by in F6Publishing: 19] [Article Influence: 2.4] [Reference Citation Analysis]
334 Nishiyama A, Tachibana K, Igarashi Y, Yasuda H, Tanahashi N, Tanaka K, Ohsumi K, Kishimoto T. A nonproteolytic function of the proteasome is required for the dissociation of Cdc2 and cyclin B at the end of M phase. Genes Dev 2000;14:2344-57. [PMID: 10995390 DOI: 10.1101/gad.823200] [Cited by in Crossref: 54] [Cited by in F6Publishing: 50] [Article Influence: 2.6] [Reference Citation Analysis]
335 Ebstein F, Kloetzel PM, Krüger E, Seifert U. Emerging roles of immunoproteasomes beyond MHC class I antigen processing. Cell Mol Life Sci 2012;69:2543-58. [PMID: 22382925 DOI: 10.1007/s00018-012-0938-0] [Cited by in Crossref: 82] [Cited by in F6Publishing: 77] [Article Influence: 9.1] [Reference Citation Analysis]
336 Li X, Thompson D, Kumar B, DeMartino GN. Molecular and cellular roles of PI31 (PSMF1) protein in regulation of proteasome function. J Biol Chem 2014;289:17392-405. [PMID: 24770418 DOI: 10.1074/jbc.M114.561183] [Cited by in Crossref: 44] [Cited by in F6Publishing: 22] [Article Influence: 6.3] [Reference Citation Analysis]
337 Porciero S, Receveur-Bréchot V, Mori K, Franzetti B, Roussel A. Expression, purification, crystallization and preliminary crystallographic analysis of a deblocking aminopeptidase from Pyrococcus horikoshii. Acta Crystallogr Sect F Struct Biol Cryst Commun 2005;61:239-42. [PMID: 16511005 DOI: 10.1107/S1744309105001910] [Cited by in Crossref: 6] [Cited by in F6Publishing: 2] [Article Influence: 0.4] [Reference Citation Analysis]
338 Xie Y, Varshavsky A. Physical association of ubiquitin ligases and the 26S proteasome. Proc Natl Acad Sci U S A 2000;97:2497-502. [PMID: 10688918 DOI: 10.1073/pnas.060025497] [Cited by in Crossref: 137] [Cited by in F6Publishing: 131] [Article Influence: 6.5] [Reference Citation Analysis]
339 Lai CH, Lee CN, Bai KJ, Yang YL, Chuang KJ, Wu SM, Chuang HC. Protein oxidation and degradation caused by particulate matter. Sci Rep 2016;6:33727. [PMID: 27644844 DOI: 10.1038/srep33727] [Cited by in Crossref: 22] [Cited by in F6Publishing: 17] [Article Influence: 4.4] [Reference Citation Analysis]
340 Pasten C, Ortiz-Pineda PA, García-Arrarás JE. Ubiquitin-proteasome system components are upregulated during intestinal regeneration. Genesis 2012;50:350-65. [PMID: 21913312 DOI: 10.1002/dvg.20803] [Cited by in Crossref: 12] [Cited by in F6Publishing: 10] [Article Influence: 1.3] [Reference Citation Analysis]
341 Enenkel C. Nuclear transport of yeast proteasomes. Biomolecules 2014;4:940-55. [PMID: 25333764 DOI: 10.3390/biom4040940] [Cited by in Crossref: 14] [Cited by in F6Publishing: 12] [Article Influence: 2.0] [Reference Citation Analysis]
342 Vlachostergios PJ, Patrikidou A, Daliani DD, Papandreou CN. The ubiquitin-proteasome system in cancer, a major player in DNA repair. Part 1: post-translational regulation. J Cell Mol Med 2009;13:3006-18. [PMID: 19522845 DOI: 10.1111/j.1582-4934.2009.00824.x] [Cited by in Crossref: 17] [Cited by in F6Publishing: 18] [Article Influence: 1.4] [Reference Citation Analysis]
343 Cecarini V, Bonfili L, Cuccioloni M, Mozzicafreddo M, Angeletti M, Keller JN, Eleuteri AM. The fine-tuning of proteolytic pathways in Alzheimer's disease. Cell Mol Life Sci 2016;73:3433-51. [PMID: 27120560 DOI: 10.1007/s00018-016-2238-6] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 1.8] [Reference Citation Analysis]
344 Palombella VJ, Conner EM, Fuseler JW, Destree A, Davis JM, Laroux FS, Wolf RE, Huang J, Brand S, Elliott PJ. Role of the proteasome and NF-kappaB in streptococcal cell wall-induced polyarthritis. Proc Natl Acad Sci USA. 1998;95:15671-15676. [PMID: 9861028 DOI: 10.1073/pnas.95.26.15671] [Cited by in Crossref: 205] [Cited by in F6Publishing: 192] [Article Influence: 9.3] [Reference Citation Analysis]
345 Hauser F, Ceciliato PHO, Lin YC, Guo D, Gregerson JD, Abbasi N, Youhanna D, Park J, Dubeaux G, Shani E, Poomchongkho N, Schroeder JI. A seed resource for screening functionally redundant genes and isolation of new mutants impaired in CO2 and ABA responses. J Exp Bot 2019;70:641-51. [PMID: 30346611 DOI: 10.1093/jxb/ery363] [Cited by in Crossref: 3] [Cited by in F6Publishing: 5] [Article Influence: 3.0] [Reference Citation Analysis]
346 Niu C, Mei J, Pan Q, Fu X. Nigral degeneration with inclusion body formation and behavioral changes in rats after proteasomal inhibition. Stereotact Funct Neurosurg 2009;87:69-81. [PMID: 19223692 DOI: 10.1159/000202972] [Cited by in Crossref: 30] [Cited by in F6Publishing: 26] [Article Influence: 2.5] [Reference Citation Analysis]
347 Maupin-Furlow J. Proteasomes and protein conjugation across domains of life. Nat Rev Microbiol 2011;10:100-11. [PMID: 22183254 DOI: 10.1038/nrmicro2696] [Cited by in Crossref: 72] [Cited by in F6Publishing: 62] [Article Influence: 7.2] [Reference Citation Analysis]
348 Sieck GC, Ferreira LF, Reid MB, Mantilla CB. Mechanical properties of respiratory muscles. Compr Physiol 2013;3:1553-67. [PMID: 24265238 DOI: 10.1002/cphy.c130003] [Cited by in Crossref: 27] [Cited by in F6Publishing: 32] [Article Influence: 3.9] [Reference Citation Analysis]
349 Lima JF, Malavazi I, von Zeska Kress Fagundes MR, Savoldi M, Goldman MH, Schwier E, Braus GH, Goldman GH. The csnD/csnE signalosome genes are involved in the Aspergillus nidulans DNA damage response. Genetics 2005;171:1003-15. [PMID: 16079239 DOI: 10.1534/genetics.105.041376] [Cited by in Crossref: 17] [Cited by in F6Publishing: 15] [Article Influence: 1.1] [Reference Citation Analysis]
350 Kurimoto E, Satoh T, Ito Y, Ishihara E, Okamoto K, Yagi-Utsumi M, Tanaka K, Kato K. Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation. Protein Sci 2017;26:1080-5. [PMID: 28263418 DOI: 10.1002/pro.3153] [Cited by in Crossref: 8] [Cited by in F6Publishing: 6] [Article Influence: 2.0] [Reference Citation Analysis]
351 Li J, Gao X, Ortega J, Nazif T, Joss L, Bogyo M, Steven AC, Rechsteiner M. Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta. EMBO J 2001;20:3359-69. [PMID: 11432824 DOI: 10.1093/emboj/20.13.3359] [Cited by in Crossref: 46] [Cited by in F6Publishing: 45] [Article Influence: 2.3] [Reference Citation Analysis]
352 Lee YR, Na BK, Moon EK, Song SM, Joo SY, Kong HH, Goo YK, Chung DI, Hong Y. Essential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellanii. PLoS One 2015;10:e0129884. [PMID: 26075721 DOI: 10.1371/journal.pone.0129884] [Cited by in Crossref: 12] [Cited by in F6Publishing: 14] [Article Influence: 2.0] [Reference Citation Analysis]
353 Rubin DM, Glickman MH, Larsen CN, Dhruvakumar S, Finley D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J 1998;17:4909-19. [PMID: 9724628 DOI: 10.1093/emboj/17.17.4909] [Cited by in Crossref: 233] [Cited by in F6Publishing: 215] [Article Influence: 10.1] [Reference Citation Analysis]
354 Quecine MC, Leite TF, Bini AP, Regiani T, Franceschini LM, Budzinski IG, Marques FG, Labate MT, Guidetti-Gonzalez S, Moon DH, Labate CA. Label-Free Quantitative Proteomic Analysis of Puccinia psidii Uredospores Reveals Differences of Fungal Populations Infecting Eucalyptus and Guava. PLoS One 2016;11:e0145343. [PMID: 26731728 DOI: 10.1371/journal.pone.0145343] [Cited by in Crossref: 12] [Cited by in F6Publishing: 8] [Article Influence: 2.4] [Reference Citation Analysis]
355 Creekmore BC, Chang YW, Lee EB. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors. J Neuropathol Exp Neurol 2021;80:494-513. [PMID: 33860329 DOI: 10.1093/jnen/nlab029] [Reference Citation Analysis]
356 Kang MS, Lim BK, Seong IS, Seol JH, Tanahashi N, Tanaka K, Chung CH. The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine protease. EMBO J 2001;20:734-42. [PMID: 11179218 DOI: 10.1093/emboj/20.4.734] [Cited by in Crossref: 28] [Cited by in F6Publishing: 26] [Article Influence: 1.4] [Reference Citation Analysis]
357 Powell SR, Divald A. The ubiquitin-proteasome system in myocardial ischaemia and preconditioning. Cardiovasc Res 2010;85:303-11. [PMID: 19793765 DOI: 10.1093/cvr/cvp321] [Cited by in Crossref: 34] [Cited by in F6Publishing: 29] [Article Influence: 2.8] [Reference Citation Analysis]
358 Ma X, Loo JA, Wysocki VH. Surface induced dissociation yields substructure of Methanosarcina thermophila 20S proteasome complexes. Int J Mass Spectrom 2015;377:201-4. [PMID: 26005366 DOI: 10.1016/j.ijms.2014.09.011] [Cited by in Crossref: 10] [Cited by in F6Publishing: 10] [Article Influence: 1.7] [Reference Citation Analysis]
359 Lippai M, Lőw P. The role of the selective adaptor p62 and ubiquitin-like proteins in autophagy. Biomed Res Int 2014;2014:832704. [PMID: 25013806 DOI: 10.1155/2014/832704] [Cited by in Crossref: 175] [Cited by in F6Publishing: 187] [Article Influence: 25.0] [Reference Citation Analysis]
360 Maynard CJ, Böttcher C, Ortega Z, Smith R, Florea BI, Díaz-Hernández M, Brundin P, Overkleeft HS, Li JY, Lucas JJ, Dantuma NP. Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment. Proc Natl Acad Sci U S A 2009;106:13986-91. [PMID: 19666572 DOI: 10.1073/pnas.0906463106] [Cited by in Crossref: 64] [Cited by in F6Publishing: 62] [Article Influence: 5.3] [Reference Citation Analysis]
361 Cho-Park PF, Steller H. Proteasome regulation by ADP-ribosylation. Cell 2013;153:614-27. [PMID: 23622245 DOI: 10.1016/j.cell.2013.03.040] [Cited by in Crossref: 95] [Cited by in F6Publishing: 86] [Article Influence: 11.9] [Reference Citation Analysis]
362 Rayavarapu S, Coley W, Van der Meulen JH, Cakir E, Tappeta K, Kinder TB, Dillingham BC, Brown KJ, Hathout Y, Nagaraju K. Activation of the ubiquitin proteasome pathway in a mouse model of inflammatory myopathy: a potential therapeutic target. Arthritis Rheum 2013;65:3248-58. [PMID: 24022788 DOI: 10.1002/art.38180] [Cited by in Crossref: 19] [Cited by in F6Publishing: 14] [Article Influence: 2.7] [Reference Citation Analysis]
363 Dutoit R, Van Gompel T, Brandt N, Van Elder D, Van Dyck J, Sobott F, Droogmans L. How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 of Thermotoga maritima. J Biol Chem 2019;294:17777-89. [PMID: 31611236 DOI: 10.1074/jbc.RA119.009281] [Cited by in Crossref: 4] [Cited by in F6Publishing: 1] [Article Influence: 2.0] [Reference Citation Analysis]
364 Komatsu M, Waguri S, Ueno T, Iwata J, Murata S, Tanida I, Ezaki J, Mizushima N, Ohsumi Y, Uchiyama Y, Kominami E, Tanaka K, Chiba T. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J Cell Biol. 2005;169:425-434. [PMID: 15866887 DOI: 10.1083/jcb.200412022] [Cited by in Crossref: 1616] [Cited by in F6Publishing: 1574] [Article Influence: 101.0] [Reference Citation Analysis]
365 Florea BI, Verdoes M, Li N, van der Linden WA, Geurink PP, van den Elst H, Hofmann T, de Ru A, van Veelen PA, Tanaka K, Sasaki K, Murata S, den Dulk H, Brouwer J, Ossendorp FA, Kisselev AF, Overkleeft HS. Activity-based profiling reveals reactivity of the murine thymoproteasome-specific subunit beta5t. Chem Biol 2010;17:795-801. [PMID: 20797608 DOI: 10.1016/j.chembiol.2010.05.027] [Cited by in Crossref: 65] [Cited by in F6Publishing: 61] [Article Influence: 6.5] [Reference Citation Analysis]
366 Ramaswamy V, Williams JS, Robinson KM, Sopko RL, Schultz MC. Global control of histone modification by the anaphase-promoting complex. Mol Cell Biol 2003;23:9136-49. [PMID: 14645525 DOI: 10.1128/MCB.23.24.9136-9149.2003] [Cited by in Crossref: 25] [Cited by in F6Publishing: 17] [Article Influence: 1.5] [Reference Citation Analysis]
367 Makino DL, Halbach F, Conti E. The RNA exosome and proteasome: common principles of degradation control. Nat Rev Mol Cell Biol 2013;14:654-60. [PMID: 23989960 DOI: 10.1038/nrm3657] [Cited by in Crossref: 60] [Cited by in F6Publishing: 52] [Article Influence: 7.5] [Reference Citation Analysis]
368 Kitajima Y, Suzuki N, Yoshioka K, Izumi R, Tateyama M, Tashiro Y, Takahashi R, Aoki M, Ono Y. Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy. Front Cell Dev Biol 2020;8:859. [PMID: 32984340 DOI: 10.3389/fcell.2020.00859] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
369 Dekel E, Yaffe D, Rosenhek-Goldian I, Ben-Nissan G, Ofir-Birin Y, Morandi MI, Ziv T, Sisquella X, Pimentel MA, Nebl T, Kapp E, Ohana Daniel Y, Karam PA, Alfandari D, Rotkopf R, Malihi S, Temin TB, Mullick D, Revach OY, Rudik A, Gov NS, Azuri I, Porat Z, Bergamaschi G, Sorkin R, Wuite GJL, Avinoam O, Carvalho TG, Cohen SR, Sharon M, Regev-Rudzki N. 20S proteasomes secreted by the malaria parasite promote its growth. Nat Commun 2021;12:1172. [PMID: 33608523 DOI: 10.1038/s41467-021-21344-8] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 7.0] [Reference Citation Analysis]
370 Bose S, Brooks P, Mason GG, Rivett AJ. gamma-Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation. Biochem J 2001;353:291-7. [PMID: 11139393 DOI: 10.1042/0264-6021:3530291] [Cited by in Crossref: 19] [Cited by in F6Publishing: 32] [Article Influence: 1.0] [Reference Citation Analysis]
371 Rockel B, Peters J, Kühlmorgen B, Glaeser RM, Baumeister W. A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy. EMBO J 2002;21:5979-84. [PMID: 12426370 DOI: 10.1093/emboj/cdf601] [Cited by in Crossref: 31] [Cited by in F6Publishing: 25] [Article Influence: 1.7] [Reference Citation Analysis]
372 Wickner S, Maurizi MR. Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon. Proc Natl Acad Sci U S A 1999;96:8318-20. [PMID: 10411867 DOI: 10.1073/pnas.96.15.8318] [Cited by in Crossref: 24] [Cited by in F6Publishing: 23] [Article Influence: 1.1] [Reference Citation Analysis]
373 Festa RA, Pearce MJ, Darwin KH. Characterization of the proteasome accessory factor (paf) operon in Mycobacterium tuberculosis. J Bacteriol 2007;189:3044-50. [PMID: 17277063 DOI: 10.1128/JB.01597-06] [Cited by in Crossref: 41] [Cited by in F6Publishing: 28] [Article Influence: 2.9] [Reference Citation Analysis]
374 Schmitt SM, Frezza M, Dou QP. New applications of old metal-binding drugs in the treatment of human cancer. Front Biosci (Schol Ed) 2012;4:375-91. [PMID: 22202066 DOI: 10.2741/274] [Cited by in Crossref: 3] [Cited by in F6Publishing: 12] [Article Influence: 0.3] [Reference Citation Analysis]
375 Bhattacharyya S, Yu H, Mim C, Matouschek A. Regulated protein turnover: snapshots of the proteasome in action. Nat Rev Mol Cell Biol 2014;15:122-33. [PMID: 24452470 DOI: 10.1038/nrm3741] [Cited by in Crossref: 166] [Cited by in F6Publishing: 152] [Article Influence: 23.7] [Reference Citation Analysis]
376 Kinyamu HK, Archer TK. Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription. Mol Cell Biol 2007;27:4891-904. [PMID: 17438138 DOI: 10.1128/MCB.02162-06] [Cited by in Crossref: 33] [Cited by in F6Publishing: 22] [Article Influence: 2.4] [Reference Citation Analysis]
377 Issaenko OA, Bitterman PB, Polunovsky VA, Dahlberg PS. Cap-dependent mRNA translation and the ubiquitin-proteasome system cooperate to promote ERBB2-dependent esophageal cancer phenotype. Cancer Gene Ther 2012;19:609-18. [PMID: 22767218 DOI: 10.1038/cgt.2012.39] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 1.0] [Reference Citation Analysis]
378 Ferdous A, Sikder D, Gillette T, Nalley K, Kodadek T, Johnston SA. The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters. Genes Dev 2007;21:112-23. [PMID: 17167105 DOI: 10.1101/gad.1493207] [Cited by in Crossref: 51] [Cited by in F6Publishing: 52] [Article Influence: 3.4] [Reference Citation Analysis]
379 Song H, Xiong H, Che J, Xi QS, Huang L, Xiong HH, Zhang P. Gel-based chemical cross-linking analysis of 20S proteasome subunit-subunit interactions in breast cancer. J Huazhong Univ Sci Technolog Med Sci 2016;36:564-70. [PMID: 27465334 DOI: 10.1007/s11596-016-1626-3] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 0.6] [Reference Citation Analysis]
380 Satoh T, Yagi-Utsumi M, Okamoto K, Kurimoto E, Tanaka K, Kato K. Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer. Int J Mol Sci 2019;20:E2231. [PMID: 31067643 DOI: 10.3390/ijms20092231] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 3.5] [Reference Citation Analysis]
381 Dogra C, Changotra H, Wedhas N, Qin X, Wergedal JE, Kumar A. TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J 2007;21:1857-69. [PMID: 17314137 DOI: 10.1096/fj.06-7537com] [Cited by in Crossref: 165] [Cited by in F6Publishing: 157] [Article Influence: 11.8] [Reference Citation Analysis]
382 Kim YC, Li X, Thompson D, DeMartino GN. ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome. J Biol Chem 2013;288:3334-45. [PMID: 23212908 DOI: 10.1074/jbc.M112.424788] [Cited by in Crossref: 27] [Cited by in F6Publishing: 24] [Article Influence: 3.0] [Reference Citation Analysis]
383 He XW, Feng T, Yin QL, Jian YW, Liu T. NOB1 is essential for the survival of RKO colorectal cancer cells. World J Gastroenterol 2015; 21(3): 868-877 [PMID: 25624720 DOI: 10.3748/wjg.v21.i3.868] [Cited by in CrossRef: 14] [Cited by in F6Publishing: 11] [Article Influence: 2.3] [Reference Citation Analysis]
384 Wang S, Xia W, Qiu M, Wang X, Jiang F, Yin R, Xu L. Atlas on substrate recognition subunits of CRL2 E3 ligases. Oncotarget 2016;7:46707-16. [PMID: 27107416 DOI: 10.18632/oncotarget.8732] [Cited by in Crossref: 11] [Cited by in F6Publishing: 13] [Article Influence: 3.7] [Reference Citation Analysis]
385 Koonin EV, Wolf YI, Aravind L. Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach. Genome Res 2001;11:240-52. [PMID: 11157787 DOI: 10.1101/gr.162001] [Cited by in Crossref: 171] [Cited by in F6Publishing: 185] [Article Influence: 8.6] [Reference Citation Analysis]
386 Yousef AA, Suliman GA, Mabrouk MM. The value of correlation of serum 20S proteasome concentration and percentage of lymphocytic apoptosis in critically ill patients: a prospective observational study. Crit Care 2010;14:R215. [PMID: 21108816 DOI: 10.1186/cc9340] [Cited by in Crossref: 8] [Cited by in F6Publishing: 7] [Article Influence: 0.7] [Reference Citation Analysis]
387 Meller R. The role of the ubiquitin proteasome system in ischemia and ischemic tolerance. Neuroscientist 2009;15:243-60. [PMID: 19181875 DOI: 10.1177/1073858408327809] [Cited by in Crossref: 34] [Cited by in F6Publishing: 32] [Article Influence: 2.8] [Reference Citation Analysis]
388 Murakami Y, Matsufuji S, Hayashi SI, Tanahashi N, Tanaka K. ATP-Dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation. Mol Cell Biol 1999;19:7216-27. [PMID: 10490656 DOI: 10.1128/MCB.19.10.7216] [Cited by in Crossref: 28] [Cited by in F6Publishing: 9] [Article Influence: 1.3] [Reference Citation Analysis]
389 Solcia E, Necchi V, Sommi P, Ricci V. Proteasome-Rich PaCS as an Oncofetal UPS Structure Handling Cytosolic Polyubiquitinated Proteins. In Vivo Occurrence, in Vitro Induction, and Biological Role. Int J Mol Sci 2018;19:E2767. [PMID: 30223470 DOI: 10.3390/ijms19092767] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.3] [Reference Citation Analysis]