Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation

Many human proteins are regulated by lysine acetylation, but the degree of acetylation at individual sites is poorly characterized. Here, the authors measure acetylation stoichiometry in the HeLa cell proteome, providing a resource to assess mechanistic constraints on acetylation-mediated protein re...

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Autores principales: Bogi Karbech Hansen, Rajat Gupta, Linda Baldus, David Lyon, Takeo Narita, Michael Lammers, Chunaram Choudhary, Brian T. Weinert
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/f689076cde19400e8edea6f60e39f647
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spelling oai:doaj.org-article:f689076cde19400e8edea6f60e39f6472021-12-02T15:35:57ZAnalysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation10.1038/s41467-019-09024-02041-1723https://doaj.org/article/f689076cde19400e8edea6f60e39f6472019-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09024-0https://doaj.org/toc/2041-1723Many human proteins are regulated by lysine acetylation, but the degree of acetylation at individual sites is poorly characterized. Here, the authors measure acetylation stoichiometry in the HeLa cell proteome, providing a resource to assess mechanistic constraints on acetylation-mediated protein regulation.Bogi Karbech HansenRajat GuptaLinda BaldusDavid LyonTakeo NaritaMichael LammersChunaram ChoudharyBrian T. WeinertNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Bogi Karbech Hansen
Rajat Gupta
Linda Baldus
David Lyon
Takeo Narita
Michael Lammers
Chunaram Choudhary
Brian T. Weinert
Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
description Many human proteins are regulated by lysine acetylation, but the degree of acetylation at individual sites is poorly characterized. Here, the authors measure acetylation stoichiometry in the HeLa cell proteome, providing a resource to assess mechanistic constraints on acetylation-mediated protein regulation.
format article
author Bogi Karbech Hansen
Rajat Gupta
Linda Baldus
David Lyon
Takeo Narita
Michael Lammers
Chunaram Choudhary
Brian T. Weinert
author_facet Bogi Karbech Hansen
Rajat Gupta
Linda Baldus
David Lyon
Takeo Narita
Michael Lammers
Chunaram Choudhary
Brian T. Weinert
author_sort Bogi Karbech Hansen
title Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
title_short Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
title_full Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
title_fullStr Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
title_full_unstemmed Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
title_sort analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/f689076cde19400e8edea6f60e39f647
work_keys_str_mv AT bogikarbechhansen analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation
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