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PDS5A and PDS5B in Cohesin Function and Human Disease
Precocious dissociation of sisters 5 (PDS5) is an associate protein of cohesin that is conserved from yeast to humans. It acts as a regulator of the cohesin complex and plays important roles in various cellular processes, such as sister chromatid cohesion, DNA damage repair, gene transcription, and...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8198109/ https://www.ncbi.nlm.nih.gov/pubmed/34070827 http://dx.doi.org/10.3390/ijms22115868 |
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author | Zhang, Nenggang Coutinho, Luiza E. Pati, Debananda |
author_facet | Zhang, Nenggang Coutinho, Luiza E. Pati, Debananda |
author_sort | Zhang, Nenggang |
collection | PubMed |
description | Precocious dissociation of sisters 5 (PDS5) is an associate protein of cohesin that is conserved from yeast to humans. It acts as a regulator of the cohesin complex and plays important roles in various cellular processes, such as sister chromatid cohesion, DNA damage repair, gene transcription, and DNA replication. Vertebrates have two paralogs of PDS5, PDS5A and PDS5B, which have redundant and unique roles in regulating cohesin functions. Herein, we discuss the molecular characteristics and functions of PDS5, as well as the effects of its mutations in the development of diseases and their relevance for novel therapeutic strategies. |
format | Online Article Text |
id | pubmed-8198109 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-81981092021-06-14 PDS5A and PDS5B in Cohesin Function and Human Disease Zhang, Nenggang Coutinho, Luiza E. Pati, Debananda Int J Mol Sci Review Precocious dissociation of sisters 5 (PDS5) is an associate protein of cohesin that is conserved from yeast to humans. It acts as a regulator of the cohesin complex and plays important roles in various cellular processes, such as sister chromatid cohesion, DNA damage repair, gene transcription, and DNA replication. Vertebrates have two paralogs of PDS5, PDS5A and PDS5B, which have redundant and unique roles in regulating cohesin functions. Herein, we discuss the molecular characteristics and functions of PDS5, as well as the effects of its mutations in the development of diseases and their relevance for novel therapeutic strategies. MDPI 2021-05-30 /pmc/articles/PMC8198109/ /pubmed/34070827 http://dx.doi.org/10.3390/ijms22115868 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Zhang, Nenggang Coutinho, Luiza E. Pati, Debananda PDS5A and PDS5B in Cohesin Function and Human Disease |
title | PDS5A and PDS5B in Cohesin Function and Human Disease |
title_full | PDS5A and PDS5B in Cohesin Function and Human Disease |
title_fullStr | PDS5A and PDS5B in Cohesin Function and Human Disease |
title_full_unstemmed | PDS5A and PDS5B in Cohesin Function and Human Disease |
title_short | PDS5A and PDS5B in Cohesin Function and Human Disease |
title_sort | pds5a and pds5b in cohesin function and human disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8198109/ https://www.ncbi.nlm.nih.gov/pubmed/34070827 http://dx.doi.org/10.3390/ijms22115868 |
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