Kinetics and thermodynamics of metal-binding to histone deacetylase 8-Reference-Cited by-同舟云学术

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Kinetics and thermodynamics of metal-binding to histone deacetylase 8

Published:2015-01-13 Issue:3 Volume:24 Page:354-365
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Kim Byungchul¹,Pithadia Amit S.²,Fierke Carol A.¹²³

Affiliation:

1. Chemical Biology Program; University of Michigan; Ann Arbor Michigan 48109-2216

2. Department of Chemistry; University of Michigan; Ann Arbor Michigan 48109-1055

3. Department of Biological Chemistry; University of Michigan Medical School; Ann Arbor Michigan 48109-0600

Funder

National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2623/fullpdf

Reference67 articles.

1. The language of covalent histone modifications;Strahl;Nature,2000

2. Lysine acetylation targets protein complexes and co-regulates major cellular functions;Choudhary;Science,2009

3. HDAC8 substrates: histones and beyond;Wolfson;Biopolymers,2013

4. Functional significance of histone deacetylase diversity;Khochbin;Curr Opin Genet Dev,2001

5. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis;Gregoretti;J Mol Biol,2004

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4. How Theoretical Evaluations Can Generate Guidelines for Designing/Engineering Metalloproteins with Desired Metal Affinity and Selectivity;Molecules;2022-12-28

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