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Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane
Sulforaphane is a small molecule isothiocyanate which exhibits anticancer potential, yet its biological targets remain poorly understood. Here we employ a competition-based chemical proteomics strategy to profile sulforaphane's targets and identify over 500 targets along with their relative aff...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6034444/ https://www.ncbi.nlm.nih.gov/pubmed/28439590 http://dx.doi.org/10.1039/c6cc08797c |
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author | Clulow, James A. Storck, Elisabeth M. Lanyon-Hogg, Thomas Kalesh, Karunakaran A. Jones, Lyn H. Tate, Edward W. |
author_facet | Clulow, James A. Storck, Elisabeth M. Lanyon-Hogg, Thomas Kalesh, Karunakaran A. Jones, Lyn H. Tate, Edward W. |
author_sort | Clulow, James A. |
collection | PubMed |
description | Sulforaphane is a small molecule isothiocyanate which exhibits anticancer potential, yet its biological targets remain poorly understood. Here we employ a competition-based chemical proteomics strategy to profile sulforaphane's targets and identify over 500 targets along with their relative affinities. These targets provide a new set of mediators for sulforaphane's bioactivity, and aid understanding of its complex mode of action. |
format | Online Article Text |
id | pubmed-6034444 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-60344442018-07-26 Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane Clulow, James A. Storck, Elisabeth M. Lanyon-Hogg, Thomas Kalesh, Karunakaran A. Jones, Lyn H. Tate, Edward W. Chem Commun (Camb) Chemistry Sulforaphane is a small molecule isothiocyanate which exhibits anticancer potential, yet its biological targets remain poorly understood. Here we employ a competition-based chemical proteomics strategy to profile sulforaphane's targets and identify over 500 targets along with their relative affinities. These targets provide a new set of mediators for sulforaphane's bioactivity, and aid understanding of its complex mode of action. Royal Society of Chemistry 2017-05-07 2017-04-25 /pmc/articles/PMC6034444/ /pubmed/28439590 http://dx.doi.org/10.1039/c6cc08797c Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0) |
spellingShingle | Chemistry Clulow, James A. Storck, Elisabeth M. Lanyon-Hogg, Thomas Kalesh, Karunakaran A. Jones, Lyn H. Tate, Edward W. Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane |
title | Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane
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title_full | Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane
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title_fullStr | Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane
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title_full_unstemmed | Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane
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title_short | Competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane
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title_sort | competition-based, quantitative chemical proteomics in breast cancer cells identifies new target profiles for sulforaphane |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6034444/ https://www.ncbi.nlm.nih.gov/pubmed/28439590 http://dx.doi.org/10.1039/c6cc08797c |
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