Cargando…
Liberating cohesin from cohesion
Cohesin was identified through its major role in holding sister chromatids together. We are learning through analysis of cohesin and other members of the protein family (SMC [structural maintenance of chromosomes]) and their regulators that these ring complexes contribute to chromosome organization...
Autor principal: | |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749159/ https://www.ncbi.nlm.nih.gov/pubmed/29237741 http://dx.doi.org/10.1101/gad.309732.117 |
_version_ | 1783289540747722752 |
---|---|
author | Bloom, Kerry |
author_facet | Bloom, Kerry |
author_sort | Bloom, Kerry |
collection | PubMed |
description | Cohesin was identified through its major role in holding sister chromatids together. We are learning through analysis of cohesin and other members of the protein family (SMC [structural maintenance of chromosomes]) and their regulators that these ring complexes contribute to chromosome organization and dynamics throughout the cell cycle. We need to consider not only how ring complexes are regulated but how they interact with their fluctuating chromatin substrate. |
format | Online Article Text |
id | pubmed-5749159 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-57491592018-05-01 Liberating cohesin from cohesion Bloom, Kerry Genes Dev Outlook Cohesin was identified through its major role in holding sister chromatids together. We are learning through analysis of cohesin and other members of the protein family (SMC [structural maintenance of chromosomes]) and their regulators that these ring complexes contribute to chromosome organization and dynamics throughout the cell cycle. We need to consider not only how ring complexes are regulated but how they interact with their fluctuating chromatin substrate. Cold Spring Harbor Laboratory Press 2017-11-01 /pmc/articles/PMC5749159/ /pubmed/29237741 http://dx.doi.org/10.1101/gad.309732.117 Text en © 2017 Bloom; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Outlook Bloom, Kerry Liberating cohesin from cohesion |
title | Liberating cohesin from cohesion |
title_full | Liberating cohesin from cohesion |
title_fullStr | Liberating cohesin from cohesion |
title_full_unstemmed | Liberating cohesin from cohesion |
title_short | Liberating cohesin from cohesion |
title_sort | liberating cohesin from cohesion |
topic | Outlook |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749159/ https://www.ncbi.nlm.nih.gov/pubmed/29237741 http://dx.doi.org/10.1101/gad.309732.117 |
work_keys_str_mv | AT bloomkerry liberatingcohesinfromcohesion |