The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922

Hsp90 is a dimeric ATPase responsible for the activation or maturation of a specific set of substrate proteins termed ‘clients’. This molecular chaperone acts in the context of a structurally dynamic and highly regulated cycle involving ATP, co-chaperone proteins and clients. Co-chaperone proteins r...

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Detalles Bibliográficos
Autores principales: Armstrong, Heather, Wolmarans, Annemarie, Mercier, Rebecca, Mai, BaoChan, LaPointe, Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498168/
https://www.ncbi.nlm.nih.gov/pubmed/23166640
http://dx.doi.org/10.1371/journal.pone.0049322

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498168/
https://www.ncbi.nlm.nih.gov/pubmed/23166640
http://dx.doi.org/10.1371/journal.pone.0049322

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