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Arresting kinase suppressor of Ras in an inactive state
Ras protein signaling pathways are important in controlling the plight of different types of cancer. Here we discussed the paper entitled “Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling” published in Nature journal on inactivating the kinase suppressor of...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5223383/ https://www.ncbi.nlm.nih.gov/pubmed/28069069 http://dx.doi.org/10.1186/s40880-017-0181-z |
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author | Badshah, Syed Lal Mabkhot, Yahia |
author_facet | Badshah, Syed Lal Mabkhot, Yahia |
author_sort | Badshah, Syed Lal |
collection | PubMed |
description | Ras protein signaling pathways are important in controlling the plight of different types of cancer. Here we discussed the paper entitled “Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling” published in Nature journal on inactivating the kinase suppressor of Ras (KSR) protein using a small molecule as an inhibitor by Dhawan et al. A biphenyl ether analogue of a quinazoline binds in one of the binding pockets of KSR and results in stabilization of its inactive state. In this inactive state, KSR is unable to take part in the cascade of protein association to perform the signalling process. |
format | Online Article Text |
id | pubmed-5223383 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-52233832017-01-11 Arresting kinase suppressor of Ras in an inactive state Badshah, Syed Lal Mabkhot, Yahia Chin J Cancer Editorial Ras protein signaling pathways are important in controlling the plight of different types of cancer. Here we discussed the paper entitled “Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling” published in Nature journal on inactivating the kinase suppressor of Ras (KSR) protein using a small molecule as an inhibitor by Dhawan et al. A biphenyl ether analogue of a quinazoline binds in one of the binding pockets of KSR and results in stabilization of its inactive state. In this inactive state, KSR is unable to take part in the cascade of protein association to perform the signalling process. BioMed Central 2017-01-09 /pmc/articles/PMC5223383/ /pubmed/28069069 http://dx.doi.org/10.1186/s40880-017-0181-z Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Editorial Badshah, Syed Lal Mabkhot, Yahia Arresting kinase suppressor of Ras in an inactive state |
title | Arresting kinase suppressor of Ras in an inactive state |
title_full | Arresting kinase suppressor of Ras in an inactive state |
title_fullStr | Arresting kinase suppressor of Ras in an inactive state |
title_full_unstemmed | Arresting kinase suppressor of Ras in an inactive state |
title_short | Arresting kinase suppressor of Ras in an inactive state |
title_sort | arresting kinase suppressor of ras in an inactive state |
topic | Editorial |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5223383/ https://www.ncbi.nlm.nih.gov/pubmed/28069069 http://dx.doi.org/10.1186/s40880-017-0181-z |
work_keys_str_mv | AT badshahsyedlal arrestingkinasesuppressorofrasinaninactivestate AT mabkhotyahia arrestingkinasesuppressorofrasinaninactivestate |