Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity

Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target.

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Autores principales:	Robbert Q. Kim, Paul P. Geurink, Monique P. C. Mulder, Alexander Fish, Reggy Ekkebus, Farid El Oualid, Willem J. van Dijk, Duco van Dalen, Huib Ovaa, Hugo van Ingen, Titia K. Sixma
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/822bd4cb8eb04f3199afc82488ed53d3
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spelling	oai:doaj.org-article:822bd4cb8eb04f3199afc82488ed53d32021-12-02T17:32:56ZKinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity10.1038/s41467-018-08231-52041-1723https://doaj.org/article/822bd4cb8eb04f3199afc82488ed53d32019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-08231-5https://doaj.org/toc/2041-1723Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target.Robbert Q. KimPaul P. GeurinkMonique P. C. MulderAlexander FishReggy EkkebusFarid El OualidWillem J. van DijkDuco van DalenHuib OvaaHugo van IngenTitia K. SixmaNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Robbert Q. Kim Paul P. Geurink Monique P. C. Mulder Alexander Fish Reggy Ekkebus Farid El Oualid Willem J. van Dijk Duco van Dalen Huib Ovaa Hugo van Ingen Titia K. Sixma Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
description	Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target.
format	article
author	Robbert Q. Kim Paul P. Geurink Monique P. C. Mulder Alexander Fish Reggy Ekkebus Farid El Oualid Willem J. van Dijk Duco van Dalen Huib Ovaa Hugo van Ingen Titia K. Sixma
author_facet	Robbert Q. Kim Paul P. Geurink Monique P. C. Mulder Alexander Fish Reggy Ekkebus Farid El Oualid Willem J. van Dijk Duco van Dalen Huib Ovaa Hugo van Ingen Titia K. Sixma
author_sort	Robbert Q. Kim
title	Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
title_short	Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
title_full	Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
title_fullStr	Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
title_full_unstemmed	Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
title_sort	kinetic analysis of multistep usp7 mechanism shows critical role for target protein in activity
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/822bd4cb8eb04f3199afc82488ed53d3
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Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity

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