Chelatable trace zinc causes low, irreproducible KDAC8 activity-Reference-Cited by-同舟云学术

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Chelatable trace zinc causes low, irreproducible KDAC8 activity

Published:2018-01 Issue: Volume:540-541 Page:9-14
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Toro Tasha B.,Edenfield Samantha A.,Hylton Brandon J.,Watt Terry J.^ORCID

Funder

U. S. Army Research Laboratory

U. S. Army Research Office

the Louisiana Cancer Research Consortium

National Institutes of Health

National Science Foundation

Xavier University of Louisiana Center for Undergraduate Research and Summer Undergraduate Research Program

NIH

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference40 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. U.S.A.,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

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

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

2. Continuous Histone Deacylase Activity Assays;Methods in Molecular Biology;2022-10-19

3. Critical review of non‐histone human substrates of metal‐dependent lysine deacetylases;The FASEB Journal;2020-08-30

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