Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

ADP-ribosylation is a reversible post-translational protein modification involved in many cellular processes. Here the authors describe a sensitive approach for the analysis of ADP-ribosylation sites under physiologic conditions and identify lysine residues as in vivotargets of ADP-ribosylation.

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Autores principales:	Rita Martello, Mario Leutert, Stephanie Jungmichel, Vera Bilan, Sara C. Larsen, Clifford Young, Michael O. Hottiger, Michael L. Nielsen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b0ff57e8f5184691918e14e931684d52
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spelling	oai:doaj.org-article:b0ff57e8f5184691918e14e931684d522021-12-02T17:32:52ZProteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue10.1038/ncomms129172041-1723https://doaj.org/article/b0ff57e8f5184691918e14e931684d522016-09-01T00:00:00Zhttps://doi.org/10.1038/ncomms12917https://doaj.org/toc/2041-1723ADP-ribosylation is a reversible post-translational protein modification involved in many cellular processes. Here the authors describe a sensitive approach for the analysis of ADP-ribosylation sites under physiologic conditions and identify lysine residues as in vivotargets of ADP-ribosylation.Rita MartelloMario LeutertStephanie JungmichelVera BilanSara C. LarsenClifford YoungMichael O. HottigerMichael L. NielsenNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rita Martello Mario Leutert Stephanie Jungmichel Vera Bilan Sara C. Larsen Clifford Young Michael O. Hottiger Michael L. Nielsen Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
description	ADP-ribosylation is a reversible post-translational protein modification involved in many cellular processes. Here the authors describe a sensitive approach for the analysis of ADP-ribosylation sites under physiologic conditions and identify lysine residues as in vivotargets of ADP-ribosylation.
format	article
author	Rita Martello Mario Leutert Stephanie Jungmichel Vera Bilan Sara C. Larsen Clifford Young Michael O. Hottiger Michael L. Nielsen
author_facet	Rita Martello Mario Leutert Stephanie Jungmichel Vera Bilan Sara C. Larsen Clifford Young Michael O. Hottiger Michael L. Nielsen
author_sort	Rita Martello
title	Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
title_short	Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
title_full	Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
title_fullStr	Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
title_full_unstemmed	Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
title_sort	proteome-wide identification of the endogenous adp-ribosylome of mammalian cells and tissue
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/b0ff57e8f5184691918e14e931684d52
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Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

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