Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes

Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, and expand the repertoire of known deubiquit...

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Autores principales:	David S. Hewings, Johanna Heideker, Taylur P. Ma, Andrew P. AhYoung, Farid El Oualid, Alessia Amore, Gregory T. Costakes, Daniel Kirchhofer, Bradley Brasher, Thomas Pillow, Nataliya Popovych, Till Maurer, Carsten Schwerdtfeger, William F. Forrest, Kebing Yu, John Flygare, Matthew Bogyo, Ingrid E. Wertz
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a36fd9ead45149f0b851c7d214b80597
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spelling	oai:doaj.org-article:a36fd9ead45149f0b851c7d214b805972021-12-02T17:32:32ZReactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes10.1038/s41467-018-03511-62041-1723https://doaj.org/article/a36fd9ead45149f0b851c7d214b805972018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03511-6https://doaj.org/toc/2041-1723Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, and expand the repertoire of known deubiquitinases.David S. HewingsJohanna HeidekerTaylur P. MaAndrew P. AhYoungFarid El OualidAlessia AmoreGregory T. CostakesDaniel KirchhoferBradley BrasherThomas PillowNataliya PopovychTill MaurerCarsten SchwerdtfegerWilliam F. ForrestKebing YuJohn FlygareMatthew BogyoIngrid E. WertzNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q David S. Hewings Johanna Heideker Taylur P. Ma Andrew P. AhYoung Farid El Oualid Alessia Amore Gregory T. Costakes Daniel Kirchhofer Bradley Brasher Thomas Pillow Nataliya Popovych Till Maurer Carsten Schwerdtfeger William F. Forrest Kebing Yu John Flygare Matthew Bogyo Ingrid E. Wertz Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
description	Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, and expand the repertoire of known deubiquitinases.
format	article
author	David S. Hewings Johanna Heideker Taylur P. Ma Andrew P. AhYoung Farid El Oualid Alessia Amore Gregory T. Costakes Daniel Kirchhofer Bradley Brasher Thomas Pillow Nataliya Popovych Till Maurer Carsten Schwerdtfeger William F. Forrest Kebing Yu John Flygare Matthew Bogyo Ingrid E. Wertz
author_facet	David S. Hewings Johanna Heideker Taylur P. Ma Andrew P. AhYoung Farid El Oualid Alessia Amore Gregory T. Costakes Daniel Kirchhofer Bradley Brasher Thomas Pillow Nataliya Popovych Till Maurer Carsten Schwerdtfeger William F. Forrest Kebing Yu John Flygare Matthew Bogyo Ingrid E. Wertz
author_sort	David S. Hewings
title	Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
title_short	Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
title_full	Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
title_fullStr	Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
title_full_unstemmed	Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
title_sort	reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/a36fd9ead45149f0b851c7d214b80597
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Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes

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