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Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis
Pin1 belongs to the peptidyl-prolyl cis-trans isomerases (PPIases) superfamily and catalyzes the cis-trans conversion of proline in target substrates to modulate diverse cellular functions including cell cycle progression, cell motility, and apoptosis. Dysregulation of Pin1 has wide-ranging influenc...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Ivyspring International Publisher
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7847688/ https://www.ncbi.nlm.nih.gov/pubmed/33537091 http://dx.doi.org/10.7150/thno.45889 |
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author | Li, Jingyi Mo, Chunfen Guo, Yifan Zhang, Bowen Feng, Xiao Si, Qiuyue Wu, Xiaobo Zhao, Zhe Gong, Lixin He, Dan Shao, Jichun |
author_facet | Li, Jingyi Mo, Chunfen Guo, Yifan Zhang, Bowen Feng, Xiao Si, Qiuyue Wu, Xiaobo Zhao, Zhe Gong, Lixin He, Dan Shao, Jichun |
author_sort | Li, Jingyi |
collection | PubMed |
description | Pin1 belongs to the peptidyl-prolyl cis-trans isomerases (PPIases) superfamily and catalyzes the cis-trans conversion of proline in target substrates to modulate diverse cellular functions including cell cycle progression, cell motility, and apoptosis. Dysregulation of Pin1 has wide-ranging influences on the fate of cells; therefore, it is closely related to the occurrence and development of various diseases. This review summarizes the current knowledge of Pin1 in disease pathogenesis. |
format | Online Article Text |
id | pubmed-7847688 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-78476882021-02-02 Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis Li, Jingyi Mo, Chunfen Guo, Yifan Zhang, Bowen Feng, Xiao Si, Qiuyue Wu, Xiaobo Zhao, Zhe Gong, Lixin He, Dan Shao, Jichun Theranostics Review Pin1 belongs to the peptidyl-prolyl cis-trans isomerases (PPIases) superfamily and catalyzes the cis-trans conversion of proline in target substrates to modulate diverse cellular functions including cell cycle progression, cell motility, and apoptosis. Dysregulation of Pin1 has wide-ranging influences on the fate of cells; therefore, it is closely related to the occurrence and development of various diseases. This review summarizes the current knowledge of Pin1 in disease pathogenesis. Ivyspring International Publisher 2021-01-19 /pmc/articles/PMC7847688/ /pubmed/33537091 http://dx.doi.org/10.7150/thno.45889 Text en © The author(s) This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/). See http://ivyspring.com/terms for full terms and conditions. |
spellingShingle | Review Li, Jingyi Mo, Chunfen Guo, Yifan Zhang, Bowen Feng, Xiao Si, Qiuyue Wu, Xiaobo Zhao, Zhe Gong, Lixin He, Dan Shao, Jichun Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis |
title | Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis |
title_full | Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis |
title_fullStr | Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis |
title_full_unstemmed | Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis |
title_short | Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis |
title_sort | roles of peptidyl-prolyl isomerase pin1 in disease pathogenesis |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7847688/ https://www.ncbi.nlm.nih.gov/pubmed/33537091 http://dx.doi.org/10.7150/thno.45889 |
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