Proteome-wide small molecule and metabolite interaction mapping

Thermal stabilization of proteins upon ligand binding provides an efficient means to assess binding of small molecules to proteins. We show here that in combination with quantitative mass spectrometry the approach allows for the systematic survey of protein engagement by cellular metabolites and dru...

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Detalles Bibliográficos
Autores principales: Huber, Kilian V. M., Olek, Karin M., Müller, André C., Soon Heng Tan, Chris, Bennett, Keiryn L., Colinge, Jacques, Superti-Furga, Giulio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4629415/
https://www.ncbi.nlm.nih.gov/pubmed/26389571
http://dx.doi.org/10.1038/nmeth.3590
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author Huber, Kilian V. M.
Olek, Karin M.
Müller, André C.
Soon Heng Tan, Chris
Bennett, Keiryn L.
Colinge, Jacques
Superti-Furga, Giulio
author_facet Huber, Kilian V. M.
Olek, Karin M.
Müller, André C.
Soon Heng Tan, Chris
Bennett, Keiryn L.
Colinge, Jacques
Superti-Furga, Giulio
author_sort Huber, Kilian V. M.
collection PubMed
description Thermal stabilization of proteins upon ligand binding provides an efficient means to assess binding of small molecules to proteins. We show here that in combination with quantitative mass spectrometry the approach allows for the systematic survey of protein engagement by cellular metabolites and drugs. The profiling of methotrexate, (S)-crizotinib and 2′3′-cGAMP in intact cells identified the respective cognate targets including the transmembrane receptor STING involved in innate immune signalling.
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spelling pubmed-46294152016-05-01 Proteome-wide small molecule and metabolite interaction mapping Huber, Kilian V. M. Olek, Karin M. Müller, André C. Soon Heng Tan, Chris Bennett, Keiryn L. Colinge, Jacques Superti-Furga, Giulio Nat Methods Article Thermal stabilization of proteins upon ligand binding provides an efficient means to assess binding of small molecules to proteins. We show here that in combination with quantitative mass spectrometry the approach allows for the systematic survey of protein engagement by cellular metabolites and drugs. The profiling of methotrexate, (S)-crizotinib and 2′3′-cGAMP in intact cells identified the respective cognate targets including the transmembrane receptor STING involved in innate immune signalling. 2015-09-21 2015-11 /pmc/articles/PMC4629415/ /pubmed/26389571 http://dx.doi.org/10.1038/nmeth.3590 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Huber, Kilian V. M.
Olek, Karin M.
Müller, André C.
Soon Heng Tan, Chris
Bennett, Keiryn L.
Colinge, Jacques
Superti-Furga, Giulio
Proteome-wide small molecule and metabolite interaction mapping
title Proteome-wide small molecule and metabolite interaction mapping
title_full Proteome-wide small molecule and metabolite interaction mapping
title_fullStr Proteome-wide small molecule and metabolite interaction mapping
title_full_unstemmed Proteome-wide small molecule and metabolite interaction mapping
title_short Proteome-wide small molecule and metabolite interaction mapping
title_sort proteome-wide small molecule and metabolite interaction mapping
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4629415/
https://www.ncbi.nlm.nih.gov/pubmed/26389571
http://dx.doi.org/10.1038/nmeth.3590
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