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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Nature Portfolio
2019
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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) |
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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 AT rajatgupta analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation AT lindabaldus analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation AT davidlyon analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation AT takeonarita analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation AT michaellammers analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation AT chunaramchoudhary analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation AT briantweinert analysisofhumanacetylationstoichiometrydefinesmechanisticconstraintsonproteinregulation |
_version_ |
1718386450503827456 |