Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase-Reference-Cited by-同舟云学术

Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase

Published:2017-12 Issue:1 Volume:8 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Abplanalp Jeannette^ORCID,Leutert Mario^ORCID,Frugier Emilie,Nowak Kathrin,Feurer Roxane,Kato Jiro,Kistemaker Hans V. A.,Filippov Dmitri V.,Moss Joel,Caflisch Amedeo,Hottiger Michael O.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-017-02253-1.pdf

Reference60 articles.

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2. Hottiger, M. O. Nuclear ADP-ribosylation and its role in chromatin plasticity, cell differentiation, and epigenetics. Annu. Rev. Biochem. 84, 227–263 (2015).

3. Barkauskaite, E. et al. Structures and mechanisms of enzymes employed in the synthesis and degradation of PARP-dependent protein ADP-ribosylation. Mol. Cell 58, 935–946 (2015).

4. Laing, S. et al. ADP-ribosylation of arginine. Amino Acids 41, 257–269 (2011).

5. Du, J. et al. Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogs and 32P-NAD. Biochemistry 48, 2878–2890 (2009).

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