KDAC8 substrate specificity quantified by a biologically relevant, label-free deacetylation assay-Reference-Cited by-同舟云学术

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KDAC8 substrate specificity quantified by a biologically relevant, label-free deacetylation assay

Published:2015-10-07 Issue:12 Volume:24 Page:2020-2032
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Toro Tasha B.¹,Watt Terry J.¹

Affiliation:

1. Department of Chemistry; Xavier University of Louisiana; New Orleans Louisiana 70125

Funder

The Louisiana Cancer Research Consortium

National Institute on Minority Health and Health Disparities RCMI

U. S. Army Research Laboratory and U. S. Army Research Office

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2813/fullpdf

Reference59 articles.

1. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey;Kim;Mol Cell,2006

2. Proteome-wide prediction of acetylation substrates;Basu;Proc Natl Acad Sci USA,2009

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

4. Regulation of cellular metabolism by protein lysine acetylation;Zhao;Science,2010

5. Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns;Lundby;Cell Rep,2012

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1. Retracted: Fruit‐juice concentrate of Asian plum attenuates vascular remodeling associated with hypertension;The FASEB Journal;2024-01-17

2. Endogenous expression of inactive lysine deacetylases reveals deacetylation-dependent cellular mechanisms;PLOS ONE;2023-09-18

3. Continuous Fluorescent Sirtuin Activity Assay Based on Fatty Acylated Lysines;International Journal of Molecular Sciences;2023-04-18

4. Lysine Deacetylase Substrate Selectivity: Distinct Interaction Surfaces Drive Positive and Negative Selection for Residues Following Acetyllysine;Biochemistry;2023-04-12

5. Crystal structures of Schistosoma mansoni histone deacetylase 8 reveal a novel binding site for allosteric inhibitors;Journal of Biological Chemistry;2022-10

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