System-wide identification and prioritization of enzyme substrates by thermal analysis

The global identification of enzyme substrates is still challenging. Here, the authors develop a method based on proteome-wide thermal shift assays to discover enzyme substrates directly from cell lysates, identifying known and novel oxidoreductase, kinase and poly-(ADP-ribose) polymerase substrates...

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Autores principales:	Amir Ata Saei, Christian M. Beusch, Pierre Sabatier, Juan Astorga Wells, Hassan Gharibi, Zhaowei Meng, Alexey Chernobrovkin, Sergey Rodin, Katja Näreoja, Ann-Gerd Thorsell, Tobias Karlberg, Qing Cheng, Susanna L. Lundström, Massimiliano Gaetani, Ákos Végvári, Elias S. J. Arnér, Herwig Schüler, Roman A. Zubarev
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/565c329cae24403687890498fa03809d
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spelling	oai:doaj.org-article:565c329cae24403687890498fa03809d2021-12-02T13:14:48ZSystem-wide identification and prioritization of enzyme substrates by thermal analysis10.1038/s41467-021-21540-62041-1723https://doaj.org/article/565c329cae24403687890498fa03809d2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21540-6https://doaj.org/toc/2041-1723The global identification of enzyme substrates is still challenging. Here, the authors develop a method based on proteome-wide thermal shift assays to discover enzyme substrates directly from cell lysates, identifying known and novel oxidoreductase, kinase and poly-(ADP-ribose) polymerase substrates.Amir Ata SaeiChristian M. BeuschPierre SabatierJuan Astorga WellsHassan GharibiZhaowei MengAlexey ChernobrovkinSergey RodinKatja NäreojaAnn-Gerd ThorsellTobias KarlbergQing ChengSusanna L. LundströmMassimiliano GaetaniÁkos VégváriElias S. J. ArnérHerwig SchülerRoman A. ZubarevNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Amir Ata Saei Christian M. Beusch Pierre Sabatier Juan Astorga Wells Hassan Gharibi Zhaowei Meng Alexey Chernobrovkin Sergey Rodin Katja Näreoja Ann-Gerd Thorsell Tobias Karlberg Qing Cheng Susanna L. Lundström Massimiliano Gaetani Ákos Végvári Elias S. J. Arnér Herwig Schüler Roman A. Zubarev System-wide identification and prioritization of enzyme substrates by thermal analysis
description	The global identification of enzyme substrates is still challenging. Here, the authors develop a method based on proteome-wide thermal shift assays to discover enzyme substrates directly from cell lysates, identifying known and novel oxidoreductase, kinase and poly-(ADP-ribose) polymerase substrates.
format	article
author	Amir Ata Saei Christian M. Beusch Pierre Sabatier Juan Astorga Wells Hassan Gharibi Zhaowei Meng Alexey Chernobrovkin Sergey Rodin Katja Näreoja Ann-Gerd Thorsell Tobias Karlberg Qing Cheng Susanna L. Lundström Massimiliano Gaetani Ákos Végvári Elias S. J. Arnér Herwig Schüler Roman A. Zubarev
author_facet	Amir Ata Saei Christian M. Beusch Pierre Sabatier Juan Astorga Wells Hassan Gharibi Zhaowei Meng Alexey Chernobrovkin Sergey Rodin Katja Näreoja Ann-Gerd Thorsell Tobias Karlberg Qing Cheng Susanna L. Lundström Massimiliano Gaetani Ákos Végvári Elias S. J. Arnér Herwig Schüler Roman A. Zubarev
author_sort	Amir Ata Saei
title	System-wide identification and prioritization of enzyme substrates by thermal analysis
title_short	System-wide identification and prioritization of enzyme substrates by thermal analysis
title_full	System-wide identification and prioritization of enzyme substrates by thermal analysis
title_fullStr	System-wide identification and prioritization of enzyme substrates by thermal analysis
title_full_unstemmed	System-wide identification and prioritization of enzyme substrates by thermal analysis
title_sort	system-wide identification and prioritization of enzyme substrates by thermal analysis
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/565c329cae24403687890498fa03809d
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System-wide identification and prioritization of enzyme substrates by thermal analysis

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