Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions

Mapping protein-ligand interactions is fundamental to advance the understanding of cellular processes and to develop drug discovery strategies. Here, the authors present a photo-activated probe that allows highly efficient labelling and identification of protein binding sites using mass spectrometry...

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Autores principales:	Lucio Manzi, Andrew S. Barrow, Daniel Scott, Robert Layfield, Timothy G. Wright, John E. Moses, Neil J. Oldham
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e5438de36b074b1c86bc4b655e92a87c
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spelling	oai:doaj.org-article:e5438de36b074b1c86bc4b655e92a87c2021-12-02T17:33:09ZCarbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions10.1038/ncomms132882041-1723https://doaj.org/article/e5438de36b074b1c86bc4b655e92a87c2016-11-01T00:00:00Zhttps://doi.org/10.1038/ncomms13288https://doaj.org/toc/2041-1723Mapping protein-ligand interactions is fundamental to advance the understanding of cellular processes and to develop drug discovery strategies. Here, the authors present a photo-activated probe that allows highly efficient labelling and identification of protein binding sites using mass spectrometry.Lucio ManziAndrew S. BarrowDaniel ScottRobert LayfieldTimothy G. WrightJohn E. MosesNeil J. OldhamNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lucio Manzi Andrew S. Barrow Daniel Scott Robert Layfield Timothy G. Wright John E. Moses Neil J. Oldham Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
description	Mapping protein-ligand interactions is fundamental to advance the understanding of cellular processes and to develop drug discovery strategies. Here, the authors present a photo-activated probe that allows highly efficient labelling and identification of protein binding sites using mass spectrometry.
format	article
author	Lucio Manzi Andrew S. Barrow Daniel Scott Robert Layfield Timothy G. Wright John E. Moses Neil J. Oldham
author_facet	Lucio Manzi Andrew S. Barrow Daniel Scott Robert Layfield Timothy G. Wright John E. Moses Neil J. Oldham
author_sort	Lucio Manzi
title	Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
title_short	Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
title_full	Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
title_fullStr	Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
title_full_unstemmed	Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
title_sort	carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/e5438de36b074b1c86bc4b655e92a87c
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Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions

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