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Probing conformational dynamics to understand kinase inhibition
Why do some inhibitors select the on-state in ERK2, a kinase that is involved in many signaling pathways in cells, whereas others bind to more than one conformation?
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10584368/ https://www.ncbi.nlm.nih.gov/pubmed/37850630 http://dx.doi.org/10.7554/eLife.92753 |
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author | Outhwaite, Ian R Seeliger, Markus A |
author_facet | Outhwaite, Ian R Seeliger, Markus A |
author_sort | Outhwaite, Ian R |
collection | PubMed |
description | Why do some inhibitors select the on-state in ERK2, a kinase that is involved in many signaling pathways in cells, whereas others bind to more than one conformation? |
format | Online Article Text |
id | pubmed-10584368 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-105843682023-10-19 Probing conformational dynamics to understand kinase inhibition Outhwaite, Ian R Seeliger, Markus A eLife Biochemistry and Chemical Biology Why do some inhibitors select the on-state in ERK2, a kinase that is involved in many signaling pathways in cells, whereas others bind to more than one conformation? eLife Sciences Publications, Ltd 2023-10-18 /pmc/articles/PMC10584368/ /pubmed/37850630 http://dx.doi.org/10.7554/eLife.92753 Text en © 2023, Outhwaite and Seeliger https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Biochemistry and Chemical Biology Outhwaite, Ian R Seeliger, Markus A Probing conformational dynamics to understand kinase inhibition |
title | Probing conformational dynamics to understand kinase inhibition |
title_full | Probing conformational dynamics to understand kinase inhibition |
title_fullStr | Probing conformational dynamics to understand kinase inhibition |
title_full_unstemmed | Probing conformational dynamics to understand kinase inhibition |
title_short | Probing conformational dynamics to understand kinase inhibition |
title_sort | probing conformational dynamics to understand kinase inhibition |
topic | Biochemistry and Chemical Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10584368/ https://www.ncbi.nlm.nih.gov/pubmed/37850630 http://dx.doi.org/10.7554/eLife.92753 |
work_keys_str_mv | AT outhwaiteianr probingconformationaldynamicstounderstandkinaseinhibition AT seeligermarkusa probingconformationaldynamicstounderstandkinaseinhibition |