Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene-Reference-Cited by-同舟云学术

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Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene

Published:2020-09-17 Issue:40 Volume:59 Page:3869-3878
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bi David¹,Yang Jie¹,Hong Jun Young²,Parikh Prashit¹,Hinds Nicole¹,Infanti Joseph¹,Lin Hening²³^ORCID,Weiser Brian P.¹^ORCID

Affiliation:

1. Department of Molecular Biology, Rowan University School of Osteopathic Medicine, Stratford, New Jersey 08084, United States

2. Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States

3. Howard Hughes Medical Institute and Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States

Funder

Osteopathic Heritage Foundation

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00564

Reference41 articles.

1. Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins

2. Efficient Demyristoylase Activity of SIRT2 Revealed by Kinetic and Structural Studies

3. Kinetic and Structural Basis for Acyl-Group Selectivity and NAD+ Dependence in Sirtuin-Catalyzed Deacylation

4. SIRT2 Reverses 4-Oxononanoyl Lysine Modification on Histones

5. Direct Comparison of SIRT2 Inhibitors: Potency, Specificity, Activity‐Dependent Inhibition, and On‐Target Anticancer Activities

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1. A homogeneous time-resolved fluorescence screen to identify SIRT2 deacetylase and defatty-acylase inhibitors;PLOS ONE;2024-06-24

2. Effects of Dimerization on the Deacylase Activities of Human SIRT2;Biochemistry;2023-11-15

3. In silico drug discovery of SIRT2 inhibitors from natural source as anticancer agents;Scientific Reports;2023-02-07

4. Substrate-selective small-molecule modulators of enzymes: Mechanisms and opportunities;Current Opinion in Chemical Biology;2023-02

5. A Conserved Mechanism for Hormesis in Molecular Systems;Dose-Response;2022-07

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