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dc.contributor.author
Martello, Rita
dc.contributor.author
Leutert, Mario
dc.contributor.author
Jungmichel, Stephanie
dc.contributor.author
Bilan, Vera
dc.contributor.author
Larsen, Sara C.
dc.contributor.author
Young, Clifford
dc.contributor.author
Hottiger, Michael O.
dc.contributor.author
Nielsen, Michael L.
dc.date.accessioned
2018-02-21T12:21:10Z
dc.date.available
2018-01-18T13:05:32Z
dc.date.available
2018-02-21T10:57:30Z
dc.date.available
2018-01-18T14:08:16Z
dc.date.available
2018-01-30T15:45:58Z
dc.date.available
2018-02-21T12:21:10Z
dc.date.issued
2016
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/ncomms12917
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/242742
dc.identifier.doi
10.3929/ethz-b-000242742
dc.description.abstract
Although protein ADP-ribosylation is involved in diverse biological processes, it has remained a challenge to identify ADP-ribose acceptor sites. Here, we present an experimental workflow for sensitive and unbiased analysis of endogenous ADP-ribosylation sites, capable of detecting more than 900 modification sites in mammalian cells and mouse liver. In cells, we demonstrate that Lys residues, besides Glu, Asp and Arg residues, are the dominant in vivo targets of ADP-ribosylation during oxidative stress. In normal liver tissue, we find Arg residues to be the predominant modification site. The cellular distribution and biological processes that involve ADP-ribosylated proteins are different in cultured cells and liver tissue, in the latter of which the majority of sites were found to be in cytosolic and mitochondrial protein networks primarily associated with metabolism. Collectively, we describe a robust methodology for the assessment of the role of ADP-ribosylation and ADP-ribosyltransferases in physiological and pathological states.
en_US
dc.language.iso
en
en_US
dc.publisher
Springer Nature
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Mass spectrometry
en_US
dc.subject
PolyADP-ribosylation
en_US
dc.title
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2016-09-30
ethz.journal.title
Nature Communications
ethz.journal.volume
7
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
12917
en_US
ethz.size
13 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00003 - Schulleitung und Dienste::00022 - Bereich VP Forschung & Wirtschaftsbez. / Domain VP Research & Corporate Relations::02207 - Functional Genomics Center Zürich / Functional Genomics Center Zürich
en_US
ethz.date.deposited
2018-01-18T14:08:16Z
ethz.source
FORM
ethz.source
BATCH
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2018-02-21T12:21:21Z
ethz.rosetta.lastUpdated
2019-02-02T15:36:47Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
dc.identifier.olduri
http://hdl.handle.net/20.500.11850/230800
dc.identifier.olduri
http://hdl.handle.net/20.500.11850/230922
ethz.COinS
ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.atitle=Proteome-wide%20identification%20of%20the%20endogenous%20ADP-ribosylome%20of%20mammalian%20cells%20and%20tissue&rft.jtitle=Nature%20Communications&rft.date=2016&rft.volume=7&rft.spage=12917&rft.issn=2041-1723&rft.au=Martello,%20Rita&Leutert,%20Mario&Jungmichel,%20Stephanie&Bilan,%20Vera&Larsen,%20Sara%20C.&rft.genre=article&
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