Conformational plasticity of a BiP-GRP94 chaperone complex
Conformational plasticity of a BiP-GRP94 chaperone complex
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Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Language
English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Contents
Hsp70/Hsp90-chaperones and their regulatory co-chaperones are critical for maintaining protein homeostasis. GRP94, the sole Hsp90-chaperone in the secretory pathway of mammalian cells, is essential for the maturation of important secretory and transmembrane proteins. Without the requirement of co-chaperones, the Hsp70-protein BiP controls regulator...
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Full title
Conformational plasticity of a BiP-GRP94 chaperone complex
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TN_cdi_proquest_journals_2921298614
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2921298614
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E-ISSN
2692-8205
DOI
10.1101/2024.02.01.578445
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https://www.proquest.com/docview/2921298614?pq-origsite=primo&accountid=13902
