Comparison of the Deacylase and Deacetylase Activity of Zinc-Dependent HDACs-Reference-Cited by-同舟云学术

Comparison of the Deacylase and Deacetylase Activity of Zinc-Dependent HDACs

Published:2017-05-04 Issue:6 Volume:12 Page:1644-1655
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

McClure Jesse J.¹^ORCID,Inks Elizabeth S.¹,Zhang Cheng²^ORCID,Peterson Yuri K.¹,Li Jiaying¹,Chundru Kalyan¹,Lee Bradley¹³,Buchanan Ashley³,Miao Shiqin⁴,Chou C. James¹

Affiliation:

1. Medical University of South Carolina, College of Pharmacy, Charleston, South Carolina, United States

2. China Agricultural University, Department of Applied Chemistry, Beijing, China

3. College of Charleston, Charleston, South Carolina, United States

4. College of Pharmaceutical Sciences, Zhejiang University, Hangzhou, Zhejiang, China

Funder

National Cancer Institute

National Institute of General Medical Sciences

South Carolina Clinical and Translational Research Institute

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.7b00321

Reference53 articles.

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3. Functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK

4. N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage

5. N ε -Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function

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