Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomics-Reference-Cited by-同舟云学术

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Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomics

Published:2014-09-11 Issue:9 Volume:282 Page:1774-1785
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Kloet Susan L.¹,Baymaz H. Irem¹,Makowski Matthew¹,Groenewold Vincent²,Jansen Pascal W. T. C.¹,Berendsen Madeleine¹,Niazi Hassin¹,Kops Geert J.²³,Vermeulen Michiel¹²³

Affiliation:

1. Department of Molecular Biology; Faculty of Science; Radboud Institute for Molecular Life Sciences; Radboud University Nijmegen; the Netherlands

2. Department of Molecular Cancer Research; UMC Utrecht; the Netherlands

3. Cancer GenomiCs Netherlands; the Netherlands

Funder

European Union

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.12972/fullpdf

Reference39 articles.

1. The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities;Zhang;Cell,1998

2. A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase;Wade;Curr Biol,1998

3. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex;Tong;Nature,1998

4. CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex;Spruijt;Mol BioSyst,2010

5. The NuRD architecture;Allen;Cell Mol Life Sci,2013

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