Structural Basis of Sirtuin 6-Catalyzed Nucleosome Deacetylation-Reference-Cited by-同舟云学术

Structural Basis of Sirtuin 6-Catalyzed Nucleosome Deacetylation

Published:2023-03-17 Issue:12 Volume:145 Page:6811-6822
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Wang Zhipeng A.¹²^ORCID,Markert Jonathan W.³^ORCID,Whedon Samuel D.¹²^ORCID,Yapa Abeywardana Maheeshi¹²,Lee Kwangwoon¹²,Jiang Hanjie¹²,Suarez Carolay¹²,Lin Hening⁴^ORCID,Farnung Lucas³,Cole Philip A.¹²^ORCID

Affiliation:

1. Division of Genetics, Department of Medicine, Brigham and Women’s Hospital, Boston, Massachusetts 02115, United States

2. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, United States

3. Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts 02115, United States

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

Funder

Division of Chemistry

Damon Runyon Cancer Research Foundation

American Heart Association

Harvard Medical School

Health Resources in Action

American Cancer Society

National Institute of General Medical Sciences

Dana-Farber/Harvard Cancer Center

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.2c13512

Reference60 articles.

1. Protein Lysine Acetylation by p300/CBP

2. Distinct biochemical properties of the class I histone deacetylase complexes

3. Sirtuins in Epigenetic Regulation

4. Chemical Screen Identifies Diverse and Novel Histone Deacetylase Inhibitors as Repressors of NUT Function: Implications for NUT Carcinoma Pathogenesis and Treatment

5. A SIRT2-Selective Inhibitor Promotes c-Myc Oncoprotein Degradation and Exhibits Broad Anticancer Activity

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