Inactivating mutation in histone deacetylase 3 stabilizes its active conformation-Reference-Cited by-同舟云学术

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Inactivating mutation in histone deacetylase 3 stabilizes its active conformation

Published:2013-08-19 Issue:10 Volume:22 Page:1306-1312
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Arrar Mehrnoosh¹,de Oliveira Cesar Augusto F.¹²,Andrew McCammon J.¹²

Affiliation:

1. Department of Chemistry and Biochemistry; University of California San Diego; La Jolla California 92093-0365

2. Howard Hughes Medical Institute; University of California San Diego; La Jolla California 92093-0365

Funder

NSF Graduate Research Fellowship (Molecular Biophysics Training)

National Science Foundation

NBCR, CTBP, and Howard Hughes Medical Institute

National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2317/fullpdf

Reference24 articles.

1. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer;Minucci;Nat Rev Cancer,2006

2. Histone deacetylases (HDACs): characterization of the classical HDAC family;Ruijter;Biochem J,2003

3. HDAC family: what are the cancer relevant targets?;Witt;Cancer Lett,2009

4. The Biology of HDAC in Cancer: The Nuclear and Epigenetic Components

5. Development of histone deacetylase inhibitors as therapeutics for neurological disease;Gottesfeld;Future Neurol,2009

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