BPG is committed to discovery and dissemination of knowledge
Cited by in F6Publishing
For: Darling AL, Uversky VN. Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter. Front Genet 2018;9:158. [PMID: 29780404 DOI: 10.3389/fgene.2018.00158] [Cited by in Crossref: 95] [Cited by in F6Publishing: 90] [Article Influence: 23.8] [Reference Citation Analysis]
Number Citing Articles
1 Lee JH, Paull TT. Mitochondria at the crossroads of ATM-mediated stress signaling and regulation of reactive oxygen species. Redox Biol 2020;32:101511. [PMID: 32244177 DOI: 10.1016/j.redox.2020.101511] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 4.5] [Reference Citation Analysis]
2 Garaizar A, Sanchez-Burgos I, Collepardo-Guevara R, Espinosa JR. Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid-Liquid Phase Separation. Molecules 2020;25:E4705. [PMID: 33076213 DOI: 10.3390/molecules25204705] [Cited by in Crossref: 6] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
3 Mergner J, Frejno M, Messerer M, Lang D, Samaras P, Wilhelm M, Mayer KFX, Schwechheimer C, Kuster B. Proteomic and transcriptomic profiling of aerial organ development in Arabidopsis. Sci Data 2020;7:334. [PMID: 33037224 DOI: 10.1038/s41597-020-00678-w] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 1.5] [Reference Citation Analysis]
4 Mamonova T, Friedman PA. Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box. Int J Mol Sci 2021;22:1087. [PMID: 33499384 DOI: 10.3390/ijms22031087] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
5 Seviour T, Wong LL, Lu Y, Mugunthan S, Yang Q, Shankari U d/o Chanda Segaran, Bessarab I, Liebl D, Williams RBH, Law Y, Kjelleberg S. Phase Transitions by an Abundant Protein in the Anammox Extracellular Matrix Mediate Cell-to-Cell Aggregation and Biofilm Formation. mBio 2020;11:e02052-20. [PMID: 32900808 DOI: 10.1128/mBio.02052-20] [Reference Citation Analysis]
6 Li F, Fan C, Marquez-Lago TT, Leier A, Revote J, Jia C, Zhu Y, Smith AI, Webb GI, Liu Q, Wei L, Li J, Song J. PRISMOID: a comprehensive 3D structure database for post-translational modifications and mutations with functional impact. Brief Bioinform 2020;21:1069-79. [PMID: 31161204 DOI: 10.1093/bib/bbz050] [Cited by in Crossref: 11] [Cited by in F6Publishing: 12] [Article Influence: 11.0] [Reference Citation Analysis]
7 Sharma V, Srinivasan A, Nikolajeff F, Kumar S. Biomineralization process in hard tissues: The interaction complexity within protein and inorganic counterparts. Acta Biomater 2021;120:20-37. [PMID: 32413577 DOI: 10.1016/j.actbio.2020.04.049] [Cited by in Crossref: 24] [Cited by in F6Publishing: 20] [Article Influence: 24.0] [Reference Citation Analysis]
8 Abyadeh M, Meyfour A, Gupta V, Zabet Moghaddam M, Fitzhenry MJ, Shahbazian S, Hosseini Salekdeh G, Mirzaei M. Recent Advances of Functional Proteomics in Gastrointestinal Cancers- a Path towards the Identification of Candidate Diagnostic, Prognostic, and Therapeutic Molecular Biomarkers. Int J Mol Sci 2020;21:E8532. [PMID: 33198323 DOI: 10.3390/ijms21228532] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
9 Zhang Q, Xiao K, Paredes JM, Mamonova T, Sneddon WB, Liu H, Wang D, Li S, McGarvey JC, Uehling D, Al-Awar R, Joseph B, Jean-Alphonse F, Orte A, Friedman PA. Parathyroid hormone initiates dynamic NHERF1 phosphorylation cycling and conformational changes that regulate NPT2A-dependent phosphate transport. J Biol Chem 2019;294:4546-71. [PMID: 30696771 DOI: 10.1074/jbc.RA119.007421] [Cited by in Crossref: 11] [Cited by in F6Publishing: 3] [Article Influence: 3.7] [Reference Citation Analysis]
10 Saito A, Shofa M, Ode H, Yumiya M, Hirano J, Okamoto T, Yoshimura SH. How Do Flaviviruses Hijack Host Cell Functions by Phase Separation? Viruses 2021;13:1479. [PMID: 34452345 DOI: 10.3390/v13081479] [Reference Citation Analysis]
11 Lapteva YS, Vologzhannikova AA, Sokolov AS, Ismailov RG, Uversky VN, Permyakov SE. In Vitro N-Terminal Acetylation of Bacterially Expressed Parvalbumins by N-Terminal Acetyltransferases from Escherichia coli. Appl Biochem Biotechnol 2021;193:1365-78. [PMID: 32394317 DOI: 10.1007/s12010-020-03324-8] [Reference Citation Analysis]
12 Wei T, Liu H, Chu B, Blasco P, Liu Z, Tian R, Li DX, Li X. Phosphorylation-regulated HMGA1a-P53 interaction unveils the function of HMGA1a acidic tail phosphorylations via synthetic proteins. Cell Chem Biol 2021;28:722-732.e8. [PMID: 33545070 DOI: 10.1016/j.chembiol.2021.01.007] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
13 LeBlanc SJ, Kulkarni P, Weninger KR. Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins. Biomolecules 2018;8:E140. [PMID: 30413085 DOI: 10.3390/biom8040140] [Cited by in Crossref: 27] [Cited by in F6Publishing: 21] [Article Influence: 6.8] [Reference Citation Analysis]
14 Hardivillé S, Banerjee PS, Selen Alpergin ES, Smith DM, Han G, Ma J, Talbot CC Jr, Hu P, Wolfgang MJ, Hart GW. TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation. Mol Cell 2020;77:1143-1152.e7. [PMID: 31866147 DOI: 10.1016/j.molcel.2019.11.022] [Cited by in Crossref: 11] [Cited by in F6Publishing: 9] [Article Influence: 3.7] [Reference Citation Analysis]
15 Cascarina SM, Ross ED. Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes. BMC Genomics 2020;21:23. [PMID: 31914925 DOI: 10.1186/s12864-019-6425-3] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
16 Kämpf K, Izmailov SA, Rabdano SO, Groves AT, Podkorytov IS, Skrynnikov NR. What Drives 15N Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail. Biophys J 2018;115:2348-67. [PMID: 30527335 DOI: 10.1016/j.bpj.2018.11.017] [Cited by in Crossref: 14] [Cited by in F6Publishing: 9] [Article Influence: 3.5] [Reference Citation Analysis]
17 Weisz J, Uversky VN. Zooming into the Dark Side of Human Annexin-S100 Complexes: Dynamic Alliance of Flexible Partners. Int J Mol Sci 2020;21:E5879. [PMID: 32824294 DOI: 10.3390/ijms21165879] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.5] [Reference Citation Analysis]
18 Ukmar-Godec T, Wegmann S, Zweckstetter M. Biomolecular condensation of the microtubule-associated protein tau. Semin Cell Dev Biol 2020;99:202-14. [PMID: 31260737 DOI: 10.1016/j.semcdb.2019.06.007] [Cited by in Crossref: 12] [Cited by in F6Publishing: 6] [Article Influence: 4.0] [Reference Citation Analysis]
19 Laskowska E, Kuczyńska-Wiśnik D. New insight into the mechanisms protecting bacteria during desiccation. Curr Genet 2020;66:313-8. [PMID: 31559453 DOI: 10.1007/s00294-019-01036-z] [Cited by in Crossref: 10] [Cited by in F6Publishing: 9] [Article Influence: 3.3] [Reference Citation Analysis]
20 Koenigsberg AL, Heldwein EE. The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 2018;293:15827-39. [PMID: 30166339 DOI: 10.1074/jbc.RA118.004481] [Cited by in Crossref: 11] [Cited by in F6Publishing: 7] [Article Influence: 2.8] [Reference Citation Analysis]
21 Darling AL, Shorter J. Combating deleterious phase transitions in neurodegenerative disease. Biochim Biophys Acta Mol Cell Res 2021;1868:118984. [PMID: 33549703 DOI: 10.1016/j.bbamcr.2021.118984] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
22 Salem A, Wilson CJ, Rutledge BS, Dilliott A, Farhan S, Choy W, Duennwald ML. Matrin3: Disorder and ALS Pathogenesis. Front Mol Biosci 2022;8:794646. [DOI: 10.3389/fmolb.2021.794646] [Reference Citation Analysis]
23 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]
24 [DOI: 10.1101/523308] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
25 Rodriguez G, Orris B, Majumdar A, Bhat S, Stivers JT. Macromolecular crowding induces compaction and DNA binding in the disordered N-terminal domain of hUNG2. DNA Repair (Amst) 2020;86:102764. [PMID: 31855846 DOI: 10.1016/j.dnarep.2019.102764] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.3] [Reference Citation Analysis]
26 Bjarnason S, Ruidiaz SF, McIvor J, Mercadante D, Heidarsson PO. Protein intrinsic disorder on a dynamic nucleosomal landscape. Prog Mol Biol Transl Sci 2021;183:295-354. [PMID: 34656332 DOI: 10.1016/bs.pmbts.2021.06.006] [Reference Citation Analysis]
27 Abdelkarim H, Banerjee A, Grudzien P, Leschinsky N, Abushaer M, Gaponenko V. The Hypervariable Region of K-Ras4B Governs Molecular Recognition and Function. Int J Mol Sci 2019;20:E5718. [PMID: 31739603 DOI: 10.3390/ijms20225718] [Cited by in Crossref: 6] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
28 Alghamdi M, Al Ghamdi KA, Khan RH, Uversky VN, Redwan EM. An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes. Cell Mol Life Sci 2019;76:4635-62. [DOI: 10.1007/s00018-019-03237-8] [Cited by in Crossref: 15] [Cited by in F6Publishing: 14] [Article Influence: 5.0] [Reference Citation Analysis]
29 Kale S, Goncearenco A, Markov Y, Landsman D, Panchenko AR. Molecular recognition of nucleosomes by binding partners. Curr Opin Struct Biol 2019;56:164-70. [PMID: 30991239 DOI: 10.1016/j.sbi.2019.03.010] [Cited by in Crossref: 15] [Cited by in F6Publishing: 11] [Article Influence: 5.0] [Reference Citation Analysis]
30 Eckfeld C, Häußler D, Schoeps B, Hermann CD, Krüger A. Functional disparities within the TIMP family in cancer: hints from molecular divergence. Cancer Metastasis Rev 2019;38:469-81. [PMID: 31529339 DOI: 10.1007/s10555-019-09812-6] [Cited by in Crossref: 8] [Cited by in F6Publishing: 9] [Article Influence: 4.0] [Reference Citation Analysis]
31 Winter DL, Iranmanesh H, Clark DS, Glover DJ. Design of Tunable Protein Interfaces Controlled by Post-Translational Modifications. ACS Synth Biol 2020;9:2132-43. [PMID: 32702241 DOI: 10.1021/acssynbio.0c00208] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
32 Peng Q, Wang L, Qin Z, Wang J, Zheng X, Wei L, Zhang X, Zhang X, Liu C, Li Z, Wu Y, Li G, Yan Q, Ma J. Phase Separation of Epstein-Barr Virus EBNA2 and Its Coactivator EBNALP Controls Gene Expression. J Virol 2020;94:e01771-19. [PMID: 31941785 DOI: 10.1128/JVI.01771-19] [Cited by in Crossref: 18] [Cited by in F6Publishing: 14] [Article Influence: 9.0] [Reference Citation Analysis]
33 Selenko P. Quo Vadis Biomolecular NMR Spectroscopy? Int J Mol Sci 2019;20:E1278. [PMID: 30875725 DOI: 10.3390/ijms20061278] [Cited by in Crossref: 6] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
34 Lambert M, Claeyssen C, Bastide B, Cieniewski-Bernard C. O-GlcNAcylation as a regulator of the functional and structural properties of the sarcomere in skeletal muscle: An update review. Acta Physiol (Oxf) 2020;228:e13301. [PMID: 31108020 DOI: 10.1111/apha.13301] [Cited by in Crossref: 7] [Cited by in F6Publishing: 3] [Article Influence: 3.5] [Reference Citation Analysis]
35 Bitard-Feildel T, Lamiable A, Mornon JP, Callebaut I. Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences. Proteomics 2018;18:e1800054. [PMID: 30299594 DOI: 10.1002/pmic.201800054] [Cited by in Crossref: 10] [Cited by in F6Publishing: 9] [Article Influence: 2.5] [Reference Citation Analysis]
36 Uversky VN, Albar AH, Khan RH, Redwan EM. Multifunctionality and intrinsic disorder of royal jelly proteome. Proteomics 2021;21:e2000237. [PMID: 33463023 DOI: 10.1002/pmic.202000237] [Reference Citation Analysis]
37 Choi UB, Sanabria H, Smirnova T, Bowen ME, Weninger KR. Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins. Biomolecules. 2019;9:114. [PMID: 30909517 DOI: 10.3390/biom9030114] [Cited by in Crossref: 18] [Cited by in F6Publishing: 14] [Article Influence: 6.0] [Reference Citation Analysis]
38 Meyer K, Selbach M. Peptide-based Interaction Proteomics. Mol Cell Proteomics 2020;19:1070-5. [PMID: 32345597 DOI: 10.1074/mcp.R120.002034] [Cited by in Crossref: 9] [Cited by in F6Publishing: 3] [Article Influence: 4.5] [Reference Citation Analysis]
39 Schiavina M, Murrali MG, Pontoriero L, Sainati V, Kümmerle R, Bermel W, Pierattelli R, Felli IC. Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action. Biophys J 2019;117:46-55. [PMID: 31176511 DOI: 10.1016/j.bpj.2019.05.017] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 3.0] [Reference Citation Analysis]
40 Carnesecchi J, Sigismondo G, Domsch K, Baader CEP, Rafiee MR, Krijgsveld J, Lohmann I. Multi-level and lineage-specific interactomes of the Hox transcription factor Ubx contribute to its functional specificity. Nat Commun 2020;11:1388. [PMID: 32170121 DOI: 10.1038/s41467-020-15223-x] [Cited by in Crossref: 8] [Cited by in F6Publishing: 6] [Article Influence: 4.0] [Reference Citation Analysis]
41 Shamilov R, Staid MJ, Aneskievich BJ. In Silico and In Vitro Considerations of Keratinocyte Nuclear Receptor Protein Structural Order for Improving Experimental Analysis. Methods Mol Biol 2020;2109:93-111. [PMID: 31124000 DOI: 10.1007/7651_2019_240] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
42 Cornish J, Chamberlain SG, Owen D, Mott HR. Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling? Biochem Soc Trans 2020;48:2669-89. [PMID: 33155649 DOI: 10.1042/BST20200467] [Cited by in Crossref: 4] [Cited by in F6Publishing: 1] [Article Influence: 4.0] [Reference Citation Analysis]
43 Yamazaki H, Kosako H, Yoshimura SH. Quantitative proteomics indicate a strong correlation of mitotic phospho-/dephosphorylation with non-structured regions of substrates. Biochim Biophys Acta Proteins Proteom 2020;1868:140295. [PMID: 31676455 DOI: 10.1016/j.bbapap.2019.140295] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.3] [Reference Citation Analysis]
44 Kowalski A. A survey of human histone H1 subtypes interaction networks: Implications for histones H1 functioning. Proteins 2021;89:792-810. [PMID: 33550666 DOI: 10.1002/prot.26059] [Reference Citation Analysis]
45 Christoffer C, Kihara D. IDP-LZerD: Software for Modeling Disordered Protein Interactions. Methods Mol Biol 2020;2165:231-44. [PMID: 32621228 DOI: 10.1007/978-1-0716-0708-4_13] [Reference Citation Analysis]
46 Gingerich MA, Liu X, Chai B, Pearson GL, Vincent MP, Stromer T, Zhu J, Sidarala V, Renberg A, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. An intrinsically disordered protein region encoded by the human disease gene CLEC16A regulates mitophagy. Autophagy 2022. [PMID: 35604110 DOI: 10.1080/15548627.2022.2080383] [Reference Citation Analysis]
47 Balli OI, Uversky VN, Durdagi S, Coskuner-Weber O. Challenges and limitations in the studies of glycoproteins: A computational chemist's perspective. Proteins 2021. [PMID: 34549826 DOI: 10.1002/prot.26242] [Reference Citation Analysis]
48 Chong S, Mir M. Towards Decoding the Sequence-Based Grammar Governing the Functions of Intrinsically Disordered Protein Regions. J Mol Biol 2021;433:166724. [PMID: 33248138 DOI: 10.1016/j.jmb.2020.11.023] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
49 Alquezar C, Arya S, Kao AW. Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation. Front Neurol 2020;11:595532. [PMID: 33488497 DOI: 10.3389/fneur.2020.595532] [Cited by in Crossref: 8] [Cited by in F6Publishing: 15] [Article Influence: 8.0] [Reference Citation Analysis]
50 Yamazaki H, Takagi M, Kosako H, Hirano T, Yoshimura SH. Cell cycle-specific phase separation regulated by protein charge blockiness. Nat Cell Biol 2022. [PMID: 35513709 DOI: 10.1038/s41556-022-00903-1] [Reference Citation Analysis]
51 Rumjanek FD. Osmolyte Induced Tumorigenesis and Metastasis: Interactions With Intrinsically Disordered Proteins. Front Oncol 2018;8:353. [PMID: 30234016 DOI: 10.3389/fonc.2018.00353] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis]
52 Singh A, Kumar A, Uversky V, Giri R. Understanding the interactability of chikungunya virus proteins via molecular recognition feature analysis. RSC Adv 2018;8:27293-303. [DOI: 10.1039/c8ra04760j] [Cited by in Crossref: 17] [Article Influence: 4.3] [Reference Citation Analysis]
53 Trushina NI, Bakota L, Mulkidjanian AY, Brandt R. The Evolution of Tau Phosphorylation and Interactions. Front Aging Neurosci 2019;11:256. [PMID: 31619983 DOI: 10.3389/fnagi.2019.00256] [Cited by in Crossref: 18] [Cited by in F6Publishing: 16] [Article Influence: 6.0] [Reference Citation Analysis]
54 Esgleas M, Falk S, Forné I, Thiry M, Najas S, Zhang S, Mas-Sanchez A, Geerlof A, Niessing D, Wang Z, Imhof A, Götz M. Trnp1 organizes diverse nuclear membrane-less compartments in neural stem cells. EMBO J 2020;39:e103373. [PMID: 32627867 DOI: 10.15252/embj.2019103373] [Cited by in Crossref: 5] [Cited by in F6Publishing: 6] [Article Influence: 2.5] [Reference Citation Analysis]
55 Aggarwal S, Banerjee SK, Talukdar NC, Yadav AK. Post-translational Modification Crosstalk and Hotspots in Sirtuin Interactors Implicated in Cardiovascular Diseases. Front Genet 2020;11:356. [PMID: 32425973 DOI: 10.3389/fgene.2020.00356] [Cited by in Crossref: 7] [Cited by in F6Publishing: 5] [Article Influence: 3.5] [Reference Citation Analysis]
56 Nicholas TR, Meng J, Greulich BM, Morris TS, Hollenhorst PC. --A high-throughput screen identifies inhibitors of the interaction between the oncogenic transcription factor ERG and the cofactor EWS. PLoS One 2020;15:e0238999. [PMID: 32915889 DOI: 10.1371/journal.pone.0238999] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
57 Zhu W, Jiang X, Sun H, Li Y, Shi W, Zheng M, Liu D, Ma A, Feng X. Global Lysine Acetylation and 2-Hydroxyisobutyrylation Profiling Reveals the Metabolism Conversion Mechanism in Giardia lamblia. Mol Cell Proteomics 2021;20:100043. [PMID: 33376196 DOI: 10.1074/mcp.RA120.002353] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
58 Tsytlonok M, Hemmen K, Hamilton G, Kolimi N, Felekyan S, Seidel CAM, Tompa P, Sanabria H. Specific Conformational Dynamics and Expansion Underpin a Multi-Step Mechanism for Specific Binding of p27 with Cdk2/Cyclin A. J Mol Biol 2020;432:2998-3017. [PMID: 32088186 DOI: 10.1016/j.jmb.2020.02.010] [Cited by in Crossref: 8] [Cited by in F6Publishing: 7] [Article Influence: 4.0] [Reference Citation Analysis]
59 Delorme-Axford E, Popelka H, Klionsky DJ. TEX264 is a major receptor for mammalian reticulophagy. Autophagy 2019;15:1677-81. [PMID: 31362563 DOI: 10.1080/15548627.2019.1646540] [Cited by in Crossref: 9] [Cited by in F6Publishing: 8] [Article Influence: 3.0] [Reference Citation Analysis]
60 Pritišanac I, Vernon RM, Moses AM, Forman Kay JD. Entropy and Information within Intrinsically Disordered Protein Regions. Entropy (Basel) 2019;21:E662. [PMID: 33267376 DOI: 10.3390/e21070662] [Cited by in Crossref: 22] [Cited by in F6Publishing: 8] [Article Influence: 7.3] [Reference Citation Analysis]
61 Wong ETC, So V, Guron M, Kuechler ER, Malhis N, Bui JM, Gsponer J. Protein-Protein Interactions Mediated by Intrinsically Disordered Protein Regions Are Enriched in Missense Mutations. Biomolecules 2020;10:E1097. [PMID: 32722039 DOI: 10.3390/biom10081097] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 2.5] [Reference Citation Analysis]
62 Mignon J, Mottet D, Verrillo G, Matagne A, Perpète EA, Michaux C. Revealing Intrinsic Disorder and Aggregation Properties of the DPF3a Zinc Finger Protein. ACS Omega 2021;6:18793-801. [PMID: 34337219 DOI: 10.1021/acsomega.1c01948] [Reference Citation Analysis]
63 Dagliyan O, Hahn KM. Controlling protein conformation with light. Curr Opin Struct Biol 2019;57:17-22. [PMID: 30849716 DOI: 10.1016/j.sbi.2019.01.012] [Cited by in Crossref: 12] [Cited by in F6Publishing: 8] [Article Influence: 4.0] [Reference Citation Analysis]
64 Parico GCG, Partch CL. The tail of cryptochromes: an intrinsically disordered cog within the mammalian circadian clock. Cell Commun Signal 2020;18:182. [PMID: 33198762 DOI: 10.1186/s12964-020-00665-z] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.5] [Reference Citation Analysis]
65 Ameri M, Nezafat N, Eskandari S. The potential of intrinsically disordered regions in vaccine development. Expert Rev Vaccines 2021;:1-3. [PMID: 34693831 DOI: 10.1080/14760584.2022.1997600] [Reference Citation Analysis]
66 Dyrda K, Orzołek A, Ner-Kluza J, Wysocki P. Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm. Animals (Basel) 2021;11:3487. [PMID: 34944263 DOI: 10.3390/ani11123487] [Reference Citation Analysis]
67 Zhang L, Gardner ML, Jayasinghe L, Jordan M, Aldana J, Burns N, Freitas MA, Guo P. Detection of single peptide with only one amino acid modification via electronic fingerprinting using reengineered durable channel of Phi29 DNA packaging motor. Biomaterials 2021;276:121022. [PMID: 34298441 DOI: 10.1016/j.biomaterials.2021.121022] [Reference Citation Analysis]
68 Roychowdhury T, Chattopadhyay S. Chemical Decorations of "MARs" Residents in Orchestrating Eukaryotic Gene Regulation. Front Cell Dev Biol 2020;8:602994. [PMID: 33409278 DOI: 10.3389/fcell.2020.602994] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
69 Nassiri Toosi Z, Su X, Austin R, Choudhury S, Li W, Pang YT, Gumbart JC, Torres MP. Combinatorial phosphorylation modulates the structure and function of the G protein γ subunit in yeast. Sci Signal 2021;14:eabd2464. [PMID: 34158397 DOI: 10.1126/scisignal.abd2464] [Reference Citation Analysis]
70 Yang J, Gao M, Xiong J, Su Z, Huang Y. Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding. Protein Sci 2019;28:1952-65. [PMID: 31441158 DOI: 10.1002/pro.3718] [Cited by in Crossref: 24] [Cited by in F6Publishing: 21] [Article Influence: 8.0] [Reference Citation Analysis]
71 Ramberger E, Suarez-Artiles L, Perez-Hernandez D, Haji M, Popp O, Reimer U, Leutz A, Dittmar G, Mertins P. A universal peptide matrix interactomics approach to disclose motif dependent protein binding. Mol Cell Proteomics 2021;:100135. [PMID: 34391889 DOI: 10.1016/j.mcpro.2021.100135] [Reference Citation Analysis]
72 Fatafta H, Samantray S, Sayyed-Ahmad A, Coskuner-Weber O, Strodel B. Molecular simulations of IDPs: From ensemble generation to IDP interactions leading to disorder-to-order transitions. Prog Mol Biol Transl Sci 2021;183:135-85. [PMID: 34656328 DOI: 10.1016/bs.pmbts.2021.06.003] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
73 Avelar GST, Gonçalves LO, Guimarães FG, Guimarães PAS, do Nascimento Rocha LG, Carvalho MGR, de Melo Resende D, Ruiz JC. Diversity and genome mapping assessment of disordered and functional domains in trypanosomatids. J Proteomics 2020;227:103919. [PMID: 32721629 DOI: 10.1016/j.jprot.2020.103919] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
74 Jin F, Gräter F. How multisite phosphorylation impacts the conformations of intrinsically disordered proteins. PLoS Comput Biol 2021;17:e1008939. [PMID: 33945530 DOI: 10.1371/journal.pcbi.1008939] [Reference Citation Analysis]
75 Lawrence DW, Willard PA, Cochran AM, Matchett EC, Kornbluth J. Natural Killer Lytic-Associated Molecule (NKLAM): An E3 Ubiquitin Ligase With an Integral Role in Innate Immunity. Front Physiol 2020;11:573372. [PMID: 33192571 DOI: 10.3389/fphys.2020.573372] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
76 Yan J, Cheng J, Kurgan L, Uversky VN. Structural and functional analysis of "non-smelly" proteins. Cell Mol Life Sci 2020;77:2423-40. [PMID: 31486849 DOI: 10.1007/s00018-019-03292-1] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
77 Pinet L, Assrir N, van Heijenoort C. Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs. Biomolecules 2021;11:1690. [PMID: 34827688 DOI: 10.3390/biom11111690] [Reference Citation Analysis]
78 Qiao Y, Luo Y, Long N, Xing Y, Tu J. Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules. Micromachines (Basel) 2021;12:492. [PMID: 33925350 DOI: 10.3390/mi12050492] [Cited by in Crossref: 2] [Article Influence: 2.0] [Reference Citation Analysis]
79 Ginnard SM, Winkler AE, Mellado Fritz C, Bluhm T, Kemmer R, Gilliam M, Butkevich N, Abdrabbo S, Bricker K, Feiler J, Miller I, Zoerman J, El-Mohri Z, Khuansanguan P, Basch M, Petzold T, Kostoff M, Konopka S, Kociba B, Gillis T, Heyl DL, Trievel RC, Albaugh BN. Molecular investigation of the tandem Tudor domain and plant homeodomain histone binding domains of the epigenetic regulator UHRF2. Proteins 2021. [PMID: 34766381 DOI: 10.1002/prot.26278] [Reference Citation Analysis]
80 Bandyopadhyay A, Basu S. Criticality in the conformational phase transition among self-similar groups in intrinsically disordered proteins: Probed by salt-bridge dynamics. Biochim Biophys Acta Proteins Proteom 2020;1868:140474. [PMID: 32579908 DOI: 10.1016/j.bbapap.2020.140474] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
81 Wang X, Li C, Li F, Sharma VS, Song J, Webb GI. SIMLIN: a bioinformatics tool for prediction of S-sulphenylation in the human proteome based on multi-stage ensemble-learning models. BMC Bioinformatics 2019;20:602. [PMID: 31752668 DOI: 10.1186/s12859-019-3178-6] [Cited by in Crossref: 4] [Cited by in F6Publishing: 6] [Article Influence: 1.3] [Reference Citation Analysis]
82 Christoffer CW, Kihara D. Modeling protein-protein interactions with intrinsically disordered proteins. Intrinsically Disordered Proteins. Elsevier; 2019. pp. 189-206. [DOI: 10.1016/b978-0-12-816348-1.00006-5] [Cited by in Crossref: 2] [Article Influence: 0.7] [Reference Citation Analysis]
83 Redwan EM, Alkarim SA, El-Hanafy AA, Saad YM, Almehdar HA, Uversky VN. Disorder in milk proteins: adipophilin and TIP47, important constituents of the milk fat globule membrane. J Biomol Struct Dyn 2020;38:1214-29. [PMID: 30896308 DOI: 10.1080/07391102.2019.1592027] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.3] [Reference Citation Analysis]
84 Sluchanko NN, Bustos DM. Intrinsic disorder associated with 14-3-3 proteins and their partners. Prog Mol Biol Transl Sci 2019;166:19-61. [PMID: 31521232 DOI: 10.1016/bs.pmbts.2019.03.007] [Cited by in Crossref: 19] [Cited by in F6Publishing: 17] [Article Influence: 6.3] [Reference Citation Analysis]
85 Battle S, Gogonea V, Willard B, Wang Z, Fu X, Huang Y, Graham LM, Cameron SJ, DiDonato JA, Crabb JW, Hazen SL. The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta. J Biol Chem 2022;:101832. [PMID: 35304099 DOI: 10.1016/j.jbc.2022.101832] [Reference Citation Analysis]
86 Ortega-Alarcon D, Claveria-Gimeno R, Vega S, Jorge-Torres OC, Esteller M, Abian O, Velazquez-Campoy A. Stabilization Effect of Intrinsically Disordered Regions on Multidomain Proteins: The Case of the Methyl-CpG Protein 2, MeCP2. Biomolecules 2021;11:1216. [PMID: 34439881 DOI: 10.3390/biom11081216] [Reference Citation Analysis]
87 Zarco-Zavala M, Mendoza-Hoffmann F, García-Trejo JJ. Unidirectional regulation of the F1FO-ATP synthase nanomotor by the ζ pawl-ratchet inhibitor protein of Paracoccus denitrificans and related α-proteobacteria. Biochim Biophys Acta Bioenerg 2018;1859:762-74. [PMID: 29886048 DOI: 10.1016/j.bbabio.2018.06.005] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 1.3] [Reference Citation Analysis]
88 Liew YJM, Lee YK, Khalid N, Rahman NA, Tan BC. Cell-Free Expression of a Plant Membrane Protein BrPT2 From Boesenbergia Rotunda. Mol Biotechnol 2021;63:316-26. [PMID: 33565047 DOI: 10.1007/s12033-021-00304-z] [Reference Citation Analysis]
89 Mills A, Gago F. On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits. Int J Mol Sci 2021;22:6973. [PMID: 34203525 DOI: 10.3390/ijms22136973] [Reference Citation Analysis]
90 Jones CL, Tepe JJ. Proteasome Activation to Combat Proteotoxicity. Molecules 2019;24:E2841. [PMID: 31387243 DOI: 10.3390/molecules24152841] [Cited by in Crossref: 11] [Cited by in F6Publishing: 10] [Article Influence: 3.7] [Reference Citation Analysis]
91 Trumbore CN. Shear-induced amyloid formation of IDPs in the brain. Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part A. Elsevier; 2019. pp. 225-309. [DOI: 10.1016/bs.pmbts.2019.05.008] [Cited by in Crossref: 5] [Cited by in F6Publishing: 3] [Article Influence: 1.7] [Reference Citation Analysis]
92 Soranno A. Physical basis of the disorder-order transition. Archives of Biochemistry and Biophysics 2020;685:108305. [DOI: 10.1016/j.abb.2020.108305] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
93 Goretzki B, Guhl C, Tebbe F, Harder JM, Hellmich UA. Unstructural Biology of TRP Ion Channels: The Role of Intrinsically Disordered Regions in Channel Function and Regulation. J Mol Biol 2021;433:166931. [PMID: 33741410 DOI: 10.1016/j.jmb.2021.166931] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
94 Reinoso TR, Landim-Vieira M, Shi Y, Johnston JR, Chase PB, Parvatiyar MS, Landstrom AP, Pinto JR, Tadros HJ. A comprehensive guide to genetic variants and post-translational modifications of cardiac troponin C. J Muscle Res Cell Motil 2021;42:323-42. [PMID: 33179204 DOI: 10.1007/s10974-020-09592-5] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 1.5] [Reference Citation Analysis]
95 Lesovoy DM, Georgoulia PS, Diercks T, Matečko-Burmann I, Burmann BM, Bocharov EV, Bermel W, Orekhov VY. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*. Angew Chem Int Ed Engl 2021;60:23540-4. [PMID: 34143912 DOI: 10.1002/anie.202102758] [Reference Citation Analysis]
96 Darling AL, Zaslavsky BY, Uversky VN. Intrinsic Disorder-Based Emergence in Cellular Biology: Physiological and Pathological Liquid-Liquid Phase Transitions in Cells. Polymers (Basel) 2019;11:E990. [PMID: 31167414 DOI: 10.3390/polym11060990] [Cited by in Crossref: 23] [Cited by in F6Publishing: 21] [Article Influence: 7.7] [Reference Citation Analysis]
97 Deiana A, Forcelloni S, Porrello A, Giansanti A. Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell. PLoS One 2019;14:e0217889. [PMID: 31425549 DOI: 10.1371/journal.pone.0217889] [Cited by in Crossref: 31] [Cited by in F6Publishing: 25] [Article Influence: 10.3] [Reference Citation Analysis]
98 Hassan SS, Lundstrom K, Serrano-Aroca Á, Adadi P, Aljabali AAA, Redwan EM, Lal A, Kandimalla R, El-Aziz TMA, Pal Choudhury P, Azad GK, Sherchan SP, Chauhan G, Tambuwala M, Takayama K, Barh D, Palu G, Basu P, Uversky VN. Emergence of unique SARS-CoV-2 ORF10 variants and their impact on protein structure and function. Int J Biol Macromol 2022;194:128-43. [PMID: 34863825 DOI: 10.1016/j.ijbiomac.2021.11.151] [Reference Citation Analysis]
99 Choukate K, Gupta A, Basu B, Virk K, Ganguli M, Chaudhuri B. Higher order assembling of the mycobacterial polar growth factor DivIVA/Wag31. J Struct Biol 2020;209:107429. [PMID: 31778770 DOI: 10.1016/j.jsb.2019.107429] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
100 Popelka H, Uversky VN. Theater in the Self-Cleaning Cell: Intrinsically Disordered Proteins or Protein Regions Acting with Membranes in Autophagy. Membranes 2022;12:457. [DOI: 10.3390/membranes12050457] [Reference Citation Analysis]