Epichaperomics reveals dysfunctional chaperone protein networks

Molecular chaperones establish essential protein-protein interaction networks. Modified versions of these assemblies are generally enriched in certain maladies. A study published in Nature Communications used epichaperomics to identify unique changes occurring in chaperone-formed protein networks du...

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Autores principales: Woodford, Mark R., Bourboulia, Dimitra, Mollapour, Mehdi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Comment
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10444821/
https://www.ncbi.nlm.nih.gov/pubmed/37607923
http://dx.doi.org/10.1038/s41467-023-40713-z
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author Woodford, Mark R.
Bourboulia, Dimitra
Mollapour, Mehdi
author_facet Woodford, Mark R.
Bourboulia, Dimitra
Mollapour, Mehdi
author_sort Woodford, Mark R.
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description Molecular chaperones establish essential protein-protein interaction networks. Modified versions of these assemblies are generally enriched in certain maladies. A study published in Nature Communications used epichaperomics to identify unique changes occurring in chaperone-formed protein networks during mitosis in cancer cells.
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spelling pubmed-104448212023-08-24 Epichaperomics reveals dysfunctional chaperone protein networks Woodford, Mark R. Bourboulia, Dimitra Mollapour, Mehdi Nat Commun Comment Molecular chaperones establish essential protein-protein interaction networks. Modified versions of these assemblies are generally enriched in certain maladies. A study published in Nature Communications used epichaperomics to identify unique changes occurring in chaperone-formed protein networks during mitosis in cancer cells. Nature Publishing Group UK 2023-08-22 /pmc/articles/PMC10444821/ /pubmed/37607923 http://dx.doi.org/10.1038/s41467-023-40713-z Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Comment
Woodford, Mark R.
Bourboulia, Dimitra
Mollapour, Mehdi
Epichaperomics reveals dysfunctional chaperone protein networks
title Epichaperomics reveals dysfunctional chaperone protein networks
title_full Epichaperomics reveals dysfunctional chaperone protein networks
title_fullStr Epichaperomics reveals dysfunctional chaperone protein networks
title_full_unstemmed Epichaperomics reveals dysfunctional chaperone protein networks
title_short Epichaperomics reveals dysfunctional chaperone protein networks
title_sort epichaperomics reveals dysfunctional chaperone protein networks
topic Comment
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10444821/
https://www.ncbi.nlm.nih.gov/pubmed/37607923
http://dx.doi.org/10.1038/s41467-023-40713-z
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