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Dealing with difficult clients via personalized chaperone inhibitors
The importance of molecular chaperones in cancer is well established, yet several chaperone inhibitors have failed in clinical trials due to toxicity. Recent efforts have focused on targeting chaperone function in cancer by either manipulating the “chaperone code” or inhibiting helper cochaperones,...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7948493/ https://www.ncbi.nlm.nih.gov/pubmed/33837724 http://dx.doi.org/10.1016/j.jbc.2020.100211 |
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author | Truman, Andrew W. |
author_facet | Truman, Andrew W. |
author_sort | Truman, Andrew W. |
collection | PubMed |
description | The importance of molecular chaperones in cancer is well established, yet several chaperone inhibitors have failed in clinical trials due to toxicity. Recent efforts have focused on targeting chaperone function in cancer by either manipulating the “chaperone code” or inhibiting helper cochaperones, such as DNAJA1. Tong et al. identify a novel inhibitor that specifically disrupts DNAJA1's interaction with p53, promoting p53 degradation. This finding highlights specific DNAJA1 interactions with the potential for less toxicity compared to traditional chaperone inhibitors. |
format | Online Article Text |
id | pubmed-7948493 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-79484932021-03-19 Dealing with difficult clients via personalized chaperone inhibitors Truman, Andrew W. J Biol Chem Editors' Pick Highlight The importance of molecular chaperones in cancer is well established, yet several chaperone inhibitors have failed in clinical trials due to toxicity. Recent efforts have focused on targeting chaperone function in cancer by either manipulating the “chaperone code” or inhibiting helper cochaperones, such as DNAJA1. Tong et al. identify a novel inhibitor that specifically disrupts DNAJA1's interaction with p53, promoting p53 degradation. This finding highlights specific DNAJA1 interactions with the potential for less toxicity compared to traditional chaperone inhibitors. American Society for Biochemistry and Molecular Biology 2021-01-28 /pmc/articles/PMC7948493/ /pubmed/33837724 http://dx.doi.org/10.1016/j.jbc.2020.100211 Text en https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Editors' Pick Highlight Truman, Andrew W. Dealing with difficult clients via personalized chaperone inhibitors |
title | Dealing with difficult clients via personalized chaperone inhibitors |
title_full | Dealing with difficult clients via personalized chaperone inhibitors |
title_fullStr | Dealing with difficult clients via personalized chaperone inhibitors |
title_full_unstemmed | Dealing with difficult clients via personalized chaperone inhibitors |
title_short | Dealing with difficult clients via personalized chaperone inhibitors |
title_sort | dealing with difficult clients via personalized chaperone inhibitors |
topic | Editors' Pick Highlight |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7948493/ https://www.ncbi.nlm.nih.gov/pubmed/33837724 http://dx.doi.org/10.1016/j.jbc.2020.100211 |
work_keys_str_mv | AT trumanandreww dealingwithdifficultclientsviapersonalizedchaperoneinhibitors |