Molecular Tools for the Study of ADP‐Ribosylation: A Unified and Versatile Method to Synthesise Native Mono‐ADP‐Ribosylated Peptides
Author:
Affiliation:
1. Leiden Institute of Chemistry Leiden University Department of Bioorganic Synthesis Einsteinweg 55 2333CC Leiden The Netherlands
2. Sir William Dunn School of Pathology University of Oxford South Parks Road Oxford OX1 3RE United Kingdom
Funder
Wellcome Trust
Biotechnology and Biological Sciences Research Council
Publisher
Wiley
Subject
General Chemistry,Catalysis,Organic Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.202100337
Reference52 articles.
1. ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites.
2. ADP-ribosylation of histone H2B. Identification of glutamic acid residue 2 as the modification site.
3. Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
4. Two Different Types of Bonds Linking Single ADP-Ribose Residues Covalently to Proteins. Quantification in Eukaryotic Cells
5. Serine is a new target residue for endogenous ADP-ribosylation on histones
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