Pages that link to "Q77953958"

The following pages link to Heat-induced oligomerization of the molecular chaperone Hsp90. Inhibition by ATP and geldanamycin and activation by transition metal oxyanions (Q77953958):

Displaying 14 items.

• The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor (Q24563873) (← links)
• The Hexameric Structures of Human Heat Shock Protein 90 (Q27340111) (← links)
• Identification of gp96 as a novel target for treatment of autoimmune disease in mice (Q28473392) (← links)
• Biochemical and biophysical characterization of the Mg2+-induced 90-kDa heat shock protein oligomers. (Q30494365) (← links)
• Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90 (Q34487157) (← links)
• Temperature sensitive influenza A virus genome replication results from low thermal stability of polymerase-cRNA complexes (Q35037734) (← links)
• Structural changes in alpha-synuclein affect its chaperone-like activity in vitro (Q36281848) (← links)
• Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle (Q42605486) (← links)
• Expression of the Tribolium castaneum (Coleoptera: Tenebrionidae) hsp83 gene and its relation to oogenesis during ovarian maturation (Q48691689) (← links)
• Lipophosphoglycan 3 From Leishmania infantum chagasi Binds Heparin With Micromolar Affinity. (Q52641665) (← links)
• Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity (Q53441134) (← links)
• Adapting to stress - chaperome networks in cancer. (Q54425017) (← links)
• Chaperome heterogeneity and its implications for cancer study and treatment (Q58582458) (← links)
• Cyclic lipopeptide antibiotics bind to the N-terminal domain of the prokaryotic Hsp90 to inhibit the chaperone activity (Q83141781) (← links)