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- W2004635577 abstract "Gp96 (GRP94) is a dimeric glycoprotein and is the endoplasmic reticulum representative of the hsp90 family of molecular chaperones. In addition to the protein substrates it chaperones, gp96 binds weakly to both peptides and ATP, and has been shown to self-assemble into discrete oligomers upon heat shock at 50 °C, although physiological roles for these phenomena have not been well established. Our studies indicate that gp96 homooligomerizes irreversibly in vitro at temperatures as low as 42 °C and could involve pre-dissociation of dimers to monomers. Oligomerization is inhibited significantly by ATP; hydrolysis is not required, since ADP, ATP-γ-S, and NECA inhibit self-assembly equally well. Peptide ligands do not competitively inhibit gp96 self-assembly and, in fact, bind to all oligomeric species, including the dimer. Together, these findings suggest that (1) heat-enhanced chaperone activity does not reside in oligomers per se, and (2) the regions of gp96 involved in peptide binding and oligomerization are distinct." @default.
- W2004635577 created "2016-06-24" @default.
- W2004635577 creator A5000972250 @default.
- W2004635577 creator A5045555505 @default.
- W2004635577 date "2004-10-01" @default.
- W2004635577 modified "2023-10-18" @default.
- W2004635577 title "Heat-induced oligomerization of gp96 occurs via a site distinct from substrate binding and is regulated by ATP" @default.
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- W2004635577 doi "https://doi.org/10.1016/j.bbrc.2004.08.215" @default.
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