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Cited by in F6Publishing
For: Matena A, Rehic E, Hönig D, Kamba B, Bayer P. Structure and function of the human parvulins Pin1 and Par14/17. Biol Chem 2018;399:101-25. [PMID: 29040060 DOI: 10.1515/hsz-2017-0137] [Cited by in Crossref: 14] [Cited by in F6Publishing: 15] [Article Influence: 3.5] [Reference Citation Analysis]
Number Citing Articles
1 Zgajnar NR, De Leo SA, Lotufo CM, Erlejman AG, Piwien-Pilipuk G, Galigniana MD. Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52. Biomolecules 2019;9:E52. [PMID: 30717249 DOI: 10.3390/biom9020052] [Cited by in Crossref: 32] [Cited by in F6Publishing: 25] [Article Influence: 10.7] [Reference Citation Analysis]
2 Monti A, Ronca R, Campiani G, Ruvo M, Doti N. Expression, Purification, Structural and Functional Characterization of Recombinant Human Parvulin 17. Mol Biotechnol. [DOI: 10.1007/s12033-022-00493-1] [Reference Citation Analysis]
3 Das E, Prasad S, Roy I. Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation. Int J Biol Macromol 2021;191:40-50. [PMID: 34534579 DOI: 10.1016/j.ijbiomac.2021.09.046] [Reference Citation Analysis]
4 Scheuplein NJ, Bzdyl NM, Kibble EA, Lohr T, Holzgrabe U, Sarkar-Tyson M. Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria. J Med Chem 2020;63:13355-88. [PMID: 32786507 DOI: 10.1021/acs.jmedchem.0c00911] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
5 Saeed U, Kim J, Piracha ZZ, Kwon H, Jung J, Chwae YJ, Park S, Shin HJ, Kim K. Parvulin 14 and Parvulin 17 Bind to HBx and cccDNA and Upregulate Hepatitis B Virus Replication from cccDNA to Virion in an HBx-Dependent Manner. J Virol. 2019;93. [PMID: 30567987 DOI: 10.1128/jvi.01840-18] [Cited by in Crossref: 10] [Cited by in F6Publishing: 15] [Article Influence: 3.3] [Reference Citation Analysis]
6 Goehring A, Michin I, Gerdes T, Schulze N, Blueggel M, Rehic E, Kaschani F, Kaiser M, Bayer P. Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization. Biol Chem 2020;401:955-68. [PMID: 32142471 DOI: 10.1515/hsz-2019-0423] [Reference Citation Analysis]
7 Li J, Mo C, Guo Y, Zhang B, Feng X, Si Q, Wu X, Zhao Z, Gong L, He D, Shao J. Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis. Theranostics 2021;11:3348-58. [PMID: 33537091 DOI: 10.7150/thno.45889] [Reference Citation Analysis]
8 Born A, Soetbeer J, Breitgoff F, Henen MA, Sgourakis N, Polyhach Y, Nichols PJ, Strotz D, Jeschke G, Vögeli B. Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance. J Am Chem Soc 2021;143:16055-67. [PMID: 34579531 DOI: 10.1021/jacs.1c06289] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
9 Inoue MK, Nakatsu Y, Yamamotoya T, Hasei S, Kanamoto M, Naitou M, Matsunaga Y, Sakoda H, Fujishiro M, Ono H, Kushiyama A, Asano T. Pin1 Plays Essential Roles in NASH Development by Modulating Multiple Target Proteins. Cells 2019;8:E1545. [PMID: 31795496 DOI: 10.3390/cells8121545] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 1.3] [Reference Citation Analysis]
10 Oliveira HR, Cant JP, Brito LF, Feitosa FLB, Chud TCS, Fonseca PAS, Jamrozik J, Silva FF, Lourenco DAL, Schenkel FS. Genome-wide association for milk production traits and somatic cell score in different lactation stages of Ayrshire, Holstein, and Jersey dairy cattle. J Dairy Sci 2019;102:8159-74. [PMID: 31301836 DOI: 10.3168/jds.2019-16451] [Cited by in Crossref: 16] [Cited by in F6Publishing: 12] [Article Influence: 5.3] [Reference Citation Analysis]
11 Yaseen A, Audette GF. Structural flexibility in the Helicobacter pylori peptidyl-prolyl cis,trans-isomerase HP0175 is achieved through an extension of the chaperone helices. J Struct Biol 2018;204:261-9. [PMID: 30179659 DOI: 10.1016/j.jsb.2018.08.017] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
12 Born A, Henen MA, Vögeli B. Activity and Affinity of Pin1 Variants. Molecules 2019;25:E36. [PMID: 31861908 DOI: 10.3390/molecules25010036] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.7] [Reference Citation Analysis]
13 Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P. Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei. Biomolecules 2019;9:E93. [PMID: 30866577 DOI: 10.3390/biom9030093] [Reference Citation Analysis]
14 Saeed U, Piracha ZZ, Kwon H, Kim J, Kalsoom F, Chwae YJ, Park S, Shin HJ, Lee HW, Lim JH, Kim K. The HBV Core Protein and Core Particle Both Bind to the PPiase Par14 and Par17 to Enhance Their Stabilities and HBV Replication. Front Microbiol 2021;12:795047. [PMID: 34970249 DOI: 10.3389/fmicb.2021.795047] [Reference Citation Analysis]
15 Chen Y, Wu YR, Yang HY, Li XZ, Jie MM, Hu CJ, Wu YY, Yang SM, Yang YB. Prolyl isomerase Pin1: a promoter of cancer and a target for therapy. Cell Death Dis 2018;9:883. [PMID: 30158600 DOI: 10.1038/s41419-018-0844-y] [Cited by in Crossref: 43] [Cited by in F6Publishing: 43] [Article Influence: 10.8] [Reference Citation Analysis]
16 Stifani S. The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer. Biomolecules 2018;8:E112. [PMID: 30314361 DOI: 10.3390/biom8040112] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 1.3] [Reference Citation Analysis]
17 Singh M, Kaur K, Sharma A, Kaur R, Joshi D, Chatterjee M, Dandapath I, Kaur A, Singh H, Singh P. Genome-wide characterization of peptidyl-prolyl cis-trans isomerases in Penicillium and their regulation by salt stress in a halotolerant P. oxalicum. Sci Rep 2021;11:12292. [PMID: 34112860 DOI: 10.1038/s41598-021-91602-8] [Reference Citation Analysis]
18 Zhang XL, Zhang G, Bai ZH. miR-34a attenuates myocardial fibrosis in diabetic cardiomyopathy mice via targeting Pin-1. Cell Biol Int 2021;45:642-53. [PMID: 33289184 DOI: 10.1002/cbin.11512] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]