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Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates.
Disruption of zebrafish somite development by pharmacologic inhibition of Hsp90.
Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase.
Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.
Gambogic acid, a natural product inhibitor of Hsp90.
Evidence that protein phosphatase 5 functions to negatively modulate the maturation of the Hsp90-dependent heme-regulated eIF2alpha kinase.
A systematic protocol for the characterization of Hsp90 modulators.
The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.
Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate.
Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases.
The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart.
Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation.
Cdk2: a genuine protein kinase client of Hsp90 and Cdc37.
Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation.
Hsp90 functions to balance the phosphorylation state of Akt during C2C12 myoblast differentiation.