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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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Detalles Bibliográficos
Autor principal: Truman, Andrew W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
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.
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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.
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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
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