Identification of Direct Protein Targets of Small Molecules

[Image: see text] Small-molecule target identification is a vital and daunting task for the chemical biology community as well as for researchers interested in applying the power of chemical genetics to impact biology and medicine. To overcome this “target ID” bottleneck, new technologies are being...

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Detalles Bibliográficos
Autores principales: Lomenick, Brett, Olsen, Richard W., Huang, Jing
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2010
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3031183/
https://www.ncbi.nlm.nih.gov/pubmed/21077692
http://dx.doi.org/10.1021/cb100294v
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author Lomenick, Brett
Olsen, Richard W.
Huang, Jing
author_facet Lomenick, Brett
Olsen, Richard W.
Huang, Jing
author_sort Lomenick, Brett
collection PubMed
description [Image: see text] Small-molecule target identification is a vital and daunting task for the chemical biology community as well as for researchers interested in applying the power of chemical genetics to impact biology and medicine. To overcome this “target ID” bottleneck, new technologies are being developed that analyze protein–drug interactions, such as drug affinity responsive target stability (DARTS), which aims to discover the direct binding targets (and off targets) of small molecules on a proteome scale without requiring chemical modification of the compound. Here, we review the DARTS method, discuss why it works, and provide new perspectives for future development in this area.
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spelling pubmed-30311832011-01-31 Identification of Direct Protein Targets of Small Molecules Lomenick, Brett Olsen, Richard W. Huang, Jing ACS Chem Biol [Image: see text] Small-molecule target identification is a vital and daunting task for the chemical biology community as well as for researchers interested in applying the power of chemical genetics to impact biology and medicine. To overcome this “target ID” bottleneck, new technologies are being developed that analyze protein–drug interactions, such as drug affinity responsive target stability (DARTS), which aims to discover the direct binding targets (and off targets) of small molecules on a proteome scale without requiring chemical modification of the compound. Here, we review the DARTS method, discuss why it works, and provide new perspectives for future development in this area. American Chemical Society 2010-11-16 2011-01-21 /pmc/articles/PMC3031183/ /pubmed/21077692 http://dx.doi.org/10.1021/cb100294v Text en Copyright © 2010 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.
spellingShingle Lomenick, Brett
Olsen, Richard W.
Huang, Jing
Identification of Direct Protein Targets of Small Molecules
title Identification of Direct Protein Targets of Small Molecules
title_full Identification of Direct Protein Targets of Small Molecules
title_fullStr Identification of Direct Protein Targets of Small Molecules
title_full_unstemmed Identification of Direct Protein Targets of Small Molecules
title_short Identification of Direct Protein Targets of Small Molecules
title_sort identification of direct protein targets of small molecules
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3031183/
https://www.ncbi.nlm.nih.gov/pubmed/21077692
http://dx.doi.org/10.1021/cb100294v
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AT huangjing identificationofdirectproteintargetsofsmallmolecules

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