Critical review of non‐histone human substrates of metal‐dependent lysine deacetylases-Reference-Cited by-同舟云学术

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Critical review of non‐histone human substrates of metal‐dependent lysine deacetylases

Published:2020-08-30 Issue:10 Volume:34 Page:13140-13155
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Toro Tasha B.¹,Watt Terry J.¹

Affiliation:

1. Department of Chemistry Xavier University of Louisiana New Orleans LA USA

Funder

National Natural Science Foundation of China

National Institutes of Health

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.202001301RR

Reference120 articles.

1. Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

2. Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

3. Regulation of Cellular Metabolism by Protein Lysine Acetylation

4. Acetylation site specificities of lysine deacetylase inhibitors in human cells

5. Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics

Cited by 12 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. Acetylation and Phosphorylation in the Regulation of Hypoxia-Inducible Factor Activities: Additional Options to Modulate Adaptations to Changes in Oxygen Levels;Life;2023-12-21

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

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

4. Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation;Biology;2023-04-06

5. Human sirtuin 2 inhibitors, their mechanisms and binding modes;Future Medicinal Chemistry;2023-02

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