Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells-Reference-Cited by-同舟云学术

Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells

Published:2014-06-24 Issue:8 Volume:13 Page:3510-3522
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Daniels Casey M.¹,Ong Shao-En²,Leung Anthony K. L.¹

Affiliation:

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

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

Funder

U.S. Department of Defense

National Institute on Drug Abuse

National Cancer Institute

Company of Biologists

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/pr401032q

Reference49 articles.

1. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

2. Toward a unified nomenclature for mammalian ADP-ribosyltransferases

3. Identification of the ADP-Ribosylation Sites in the PARP-1 Automodification Domain: Analysis and Implications

4. Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease

5. Mapping PARP-1 Auto-ADP-ribosylation Sites by Liquid Chromatography–Tandem Mass Spectrometry

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