Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics-Reference-Cited by-同舟云学术

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Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics

Published:2013-04 Issue: Volume:81 Page:80-90
ISSN:1874-3919
Container-title:Journal of Proteomics
language:en
Short-container-title:Journal of Proteomics

Author:

Abshiru Nebiyu,Ippersiel Kevin,Tang Yong,Yuan Hua,Marmorstein Ronen,Verreault Alain,Thibault Pierre

Funder

Natural Sciences and Engineering Research Council (NSERC)

Canadian Institute for Health Research (CIHR)

Publisher

Elsevier BV

Subject

Biochemistry,Biophysics

Reference41 articles.

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2. Preferentially quantized linker DNA lengths in Saccharomyces cerevisiae;Wang;PLoS Comput Biol,2008

3. Structure of the ‘30 nm’ chromatin fibre: a key role for the linker histone;Robinson;Curr Opin Struct Biol,2006

4. Regulation of chromatin by histone modifications;Bannister;Cell Res,2011

5. The complex language of chromatin regulation during transcription;Berger;Nature,2007

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1. Persistent Acetylation of Histone H3 Lysine 56 Compromises the Activity of DNA Replication Origins;Molecular and Cellular Biology;2023-10-09

2. Adaptive partitioning of a gene locus to the nuclear envelope in Saccharomyces cerevisiae is driven by polymer-polymer phase separation;Nature Communications;2023-02-28

3. Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in Saccharomyces cerevisiae;Genetics;2022-08-17

4. Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in Saccharomyces cerevisiae;2022-06-30

5. Persistent acetylation of histone H3 lysine 56 compromises the activity of DNA replication origins;2022-03-22

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