About: A family of macrodomain proteins reverses cellular mono-ADP-ribosylation

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About: A family of macrodomain proteins reverses cellular mono-ADP-ribosylation Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A family of macrodomain proteins reverses cellular mono-ADP-ribosylation
Creator	Jankevicius, Gytis Golia, Barbara Hassler, Markus Ladurner, Andreas Rybin, Vladimir Timinszky, Gyula Zacharias, Martin
Source	PMC
abstract	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. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nsmb.2523) contains supplementary material, which is available to authorized users.
has issue date	2013-03-10(xsd:dateTime)
bibo:doi	10.1038/nsmb.2523
bibo:pmid	23474712
has license	no-cc
sha1sum (hex)	e2d3c5ac7ab80bcdea7727d7a9c193c1965411a4
schema:url	https://doi.org/10.1038/nsmb.2523
resource representing a document's title	A family of macrodomain proteins reverses cellular mono-ADP-ribosylation
has PubMed Central identifier	PMC7097781
has PubMed identifier	23474712
schema:publication	Nat Struct Mol Biol
resource representing a document's body	covid:e2d3c5ac7ab80bcdea7727d7a9c193c1965411a4#body_text
is schema:about of	named entity 'FAMILY' named entity 'TARGET' named entity 'SENSOR' named entity 'STATE' named entity 'HERE' named entity 'REMOVE' named entity 'EITHER' named entity 'INDUCED' named entity 'LEAVES' named entity 'ESTABLISH' named entity 'REVERSE' named entity 'ENZYMES' named entity 'ADP' named entity 'MODIFICATION' named entity 'transfer' named entity 'linked' named entity 'MONO' covid:arg/e2d3c5ac7ab80bcdea7727d7a9c193c1965411a4 named entity 'PARP' named entity 'DOES NOT' named entity 'USE' named entity 'ADP-RIBOSYLATION' named entity 'REVERSES' named entity 'PARP1' named entity 'CELLULAR' named entity 'DNA-DAMAGE' named entity 'YEAST' named entity 'UNDERSTANDING' named entity 'IDENTIFY' named entity 'TO TRANSFER' named entity 'FAMILY' named entity 'RIBOSE' named entity 'AMINO ACID' named entity 'FULLY' named entity 'DISTINCT' named entity 'REVERSES' named entity 'REVERSIBILITY' named entity 'COMPLETE' named entity 'RESPONSE TO' named entity 'STRESSES' named entity 'OUR' named entity 'REGULATORY' named entity 'VIRUSES' named entity 'ADP-RIBOSYLATED' named entity 'POLY-ADPR' named entity 'CELLULAR' named entity 'PROXIMAL' named entity 'PROTEINS' named entity 'ADP-RIBOSYLATION' named entity 'PRESENT' named entity 'BUT' named entity 'HAVE' named entity 'SINGLE' named entity 'VARIETY' named entity 'MULTIPLE' named entity 'POLY-ADP-RIBOSYLATION' named entity 'MONO' named entity 'ANIMALS' named entity 'GAP' named entity 'CAPABLE' named entity 'NAD' named entity 'DNA DAMAGE' named entity 'substrates' named entity 'ADP-ribose' named entity 'cellular' named entity 'cellular' named entity 'ADP-ribosylation' named entity 'ADPr' named entity 'cellular' named entity 'yeast' named entity 'viruses' named entity 'Our' named entity 'response to DNA damage' named entity 'poly-ADP-ribosylation' named entity 'ADP-ribose'

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