Identifying Poly(ADP-ribose)-Binding Proteins with Photoaffinity-Based Proteomics-Reference-Cited by-同舟云学术

Identifying Poly(ADP-ribose)-Binding Proteins with Photoaffinity-Based Proteomics

Published:2021-02-17 Issue:8 Volume:143 Page:3037-3042
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Dasovich Morgan¹²,Beckett Morgan Q.³,Bailey Scott²³,Ong Shao-En⁴^ORCID,Greenberg Marc M.¹^ORCID,Leung Anthony K. L.²⁵⁶^ORCID

Affiliation:

1. Department of Chemistry, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, Maryland 21218, United States

2. Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205, United States

3. Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, United States

4. Department of Pharmacology, University of Washington, Seattle, Washington 98195, United States

5. Department of Molecular Biology and Genetics, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, United States

6. Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, United States

Funder

Johns Hopkins University

National Institute on Aging

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.0c12246

Reference54 articles.

1. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs

2. ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease

3. Progress and outlook in studying the substrate specificities of PARPs and related enzymes

4. Mechanisms governing PARP expression, localization, and activity in cells

5. SnapShot: ADP-Ribosylation Signaling

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