The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
A family of macrodomain proteins reverses cellular mono-ADP-ribosylation
Open accessAbstract
ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD+ to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid substrates, often in response to DNA damage or other stresses. Poly-ADPr-glycohydrolase readily reverses poly-ADP-ribosylation induced by the DNA-damage sensor PARP1 and other enzymes, but it does not remove the most proximal ADPr linked to the target amino acid. Searches for enzymes capable of fully reversing cellular mono-ADP-ribosylation back to the unmodified state have proved elusive, which leaves a gap in the understanding of this modification. Here, we identify a family of macrodomain enzymes present in viruses, yeast and animals that reverse cellular ADP-ribosylation by acting on mono-ADP-ribosylated substrates. Our discoveries establish the complete reversibility of PARP-catalyzed cellular ADP-ribosylation as a regulatory modification.
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Cited by
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
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“Moreover, as mentioned in the previous section, the ADP-ribose hydrolases also exhibit distinct subcellular localizations (Niere et al. 2012; Jankevicius et al. 2013; Sharifi et al. 2013).”
BackgroundInfluentialCoordination of DNA single strand break repair
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Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation
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Phosphoproteomic approach to characterize protein mono- and poly(ADP-ribosyl)ation sites from cells
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Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
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Metadata
- Authors
- Jankevicius, G., Hassler, M., Golia, B., Rybin, V., Zacharias, M., Timinszky, G., & Ladurner, A. G.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2013-03-10
- Volume
- 20
- Issue
- 4
- Pages
- 508-514
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W1982285205
- Cited by
- 328
- References
- 6
- FWCI
- 14.54
- Type
- journal article
- Language
- en
- Open access
- bronze
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