Role of heat shock protein 90 in bradykinin-stimulated endothelial nitric oxide release (Q28211247)

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V J Venema

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M Blackstone

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R C Venema

Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins

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language of work or name

English

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publication date

September 2000

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165-70

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cites work

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Dynamic activation of endothelial nitric oxide synthase by Hsp90.

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Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation

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Chaperones in cell cycle regulation and mitogenic signal transduction: a review

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Biological actions and properties of endothelium-derived nitric oxide formed and released from artery and vein

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Tyrosine kinase inhibitors modulate agonist-induced vasodilation in the hamster cheek pouch

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Direct Interaction of Endothelial Nitric-oxide Synthase and Caveolin-1 Inhibits Synthase Activity

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Role of tyrosine kinase in dilator responses of rat basilar artery in vivo

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Nitric oxide: an endogenous modulator of leukocyte adhesion

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Endothelial nitric oxide synthase interactions with G-protein-coupled receptors

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Nitric oxide production contributes to the angiogenic properties of vascular endothelial growth factor in human endothelial cells

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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

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The anti-aggregating properties of vascular endothelium: interactions between prostacyclin and nitric oxide

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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase

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Bradykinin-stimulated protein tyrosine phosphorylation promotes endothelial nitric oxide synthase translocation to the cytoskeleton

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Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

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