Titlebook: The Networking of Chaperones by Co-chaperones; Gregory L. Blatch Book 2007 Springer-Verlag New York 2007 Blatch.Chaperones.Networking.biol

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Hop: An Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathwtion of nascent polypeptides. Hsp70/Hsp90 organizing protein (Hop), a co-chaperone of the two major molecular chaperones, heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90), facilitates their interaction by acting as an adaptor between the two chaperones, so that substrate is efficientl

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Do Hsp40s Act as Chaperones or Co-Chaperones?,ative regions of proteins at different stages of their life cycles.. Hsp40 proteins not only act as co-chaperones to facilitate complex formation between Hsp70 and client proteins, but it has also been proposed that Hsp40s use an intrinsic chaperone activity to bind and deliver the nonnative substra

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UNC-45: A Chaperone for Myosin and a Co-Chaperone for Hsp90, various important actin- and myosin-dependent cellular processes that include myofibril organization and muscle functions, cell differentiation, embryonic development, cytokinesis and endocytosis. Mutations in the genes that code for UCS domain proteins cause serious defects in these actomyosin-bas

舞蹈編排

The Roles of GroES as a Co-Chaperone for GroEL,ns form the only essential chaperone machine in . Both proteins have seven-fold symmetry. GroES acts by binding to one end of the GroEL complex in the presence of nucleotide. In doing this, it has several roles. It displaces bound substrate protein from GroEL into the folding cavity within the GroEL

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From Creator to Terminator: Co-Chaperones That Link Molecular Chaperones to the Ubiquitin/Proteasom from the functional characterization of certain co-chaperones. In the light of these novel findings long held views regarding the interplay of chaperones and proteases in protein quality control need to be reconsidered. A further elucidation of chaperone-assisted degradation will be essential to un