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

Protein ADP-ribosylation has emerged as a key post translational modification that regulates several stress responses. Here the authors characterize ARH3 as a major serine-specific mono–ADP-ribosylhydrolase and use a proteomics approach to identify the cellular targets of ARH3.

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Bibliographic Details
Main Authors:	Jeannette Abplanalp, Mario Leutert, Emilie Frugier, Kathrin Nowak, Roxane Feurer, Jiro Kato, Hans V. A. Kistemaker, Dmitri V. Filippov, Joel Moss, Amedeo Caflisch, Michael O. Hottiger
Format:	article
Language:	EN
Published:	Nature Portfolio 2017
Subjects:	Science Q
Online Access:	https://doaj.org/article/6b5383d3e22d404d94e3d6189a490adf
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spelling	oai:doaj.org-article:6b5383d3e22d404d94e3d6189a490adf2021-12-02T14:40:23ZProteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase10.1038/s41467-017-02253-12041-1723https://doaj.org/article/6b5383d3e22d404d94e3d6189a490adf2017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02253-1https://doaj.org/toc/2041-1723Protein ADP-ribosylation has emerged as a key post translational modification that regulates several stress responses. Here the authors characterize ARH3 as a major serine-specific mono–ADP-ribosylhydrolase and use a proteomics approach to identify the cellular targets of ARH3.Jeannette AbplanalpMario LeutertEmilie FrugierKathrin NowakRoxane FeurerJiro KatoHans V. A. KistemakerDmitri V. FilippovJoel MossAmedeo CaflischMichael O. HottigerNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jeannette Abplanalp Mario Leutert Emilie Frugier Kathrin Nowak Roxane Feurer Jiro Kato Hans V. A. Kistemaker Dmitri V. Filippov Joel Moss Amedeo Caflisch Michael O. Hottiger Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
description	Protein ADP-ribosylation has emerged as a key post translational modification that regulates several stress responses. Here the authors characterize ARH3 as a major serine-specific mono–ADP-ribosylhydrolase and use a proteomics approach to identify the cellular targets of ARH3.
format	article
author	Jeannette Abplanalp Mario Leutert Emilie Frugier Kathrin Nowak Roxane Feurer Jiro Kato Hans V. A. Kistemaker Dmitri V. Filippov Joel Moss Amedeo Caflisch Michael O. Hottiger
author_facet	Jeannette Abplanalp Mario Leutert Emilie Frugier Kathrin Nowak Roxane Feurer Jiro Kato Hans V. A. Kistemaker Dmitri V. Filippov Joel Moss Amedeo Caflisch Michael O. Hottiger
author_sort	Jeannette Abplanalp
title	Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
title_short	Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
title_full	Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
title_fullStr	Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
title_full_unstemmed	Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
title_sort	proteomic analyses identify arh3 as a serine mono-adp-ribosylhydrolase
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6b5383d3e22d404d94e3d6189a490adf
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Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase

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