Hsp70 Forms Antiparallel Dimers Stabilized by Post-translational Modifications to Position Clients for Transfer to Hsp90

Protein folding in cells is regulated by networks of chaperones, including the heat shock protein 70 (Hsp70) system, which consists of the Hsp40 cochaperone and a nucleotide exchange factor. Hsp40 mediates complex formation between Hsp70 and client proteins prior to interaction with Hsp90. We used m...

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Foilsithe in:Cell Rep
Main Authors: Morgner, Nina, Schmidt, Carla, Beilsten-Edmands, Victoria, Ebong, Ima-obong, Patel, Nisha A., Clerico, Eugenia M., Kirschke, Elaine, Daturpalli, Soumya, Jackson, Sophie E., Agard, David, Robinson, Carol V.
Formáid: Artigo
Teanga:Inglês
Foilsithe: Cell Press 2015
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Article
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC4431665/
https://ncbi.nlm.nih.gov/pubmed/25921532
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.celrep.2015.03.063
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