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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

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