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Matts, Robert
One or more keywords matched the following items that are connected to
Matts, Robert
Item Type
Name
Concept
Protein Folding
Academic Article
Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates.
Academic Article
Differential inhibition of Hsc70 activities by two Hsc70-binding peptides.
Academic Article
Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.
Academic Article
Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2.
Academic Article
High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase.
Academic Article
The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.
Academic Article
Hsp90-mediated folding of the lymphoid cell kinase p56lck.
Academic Article
Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase.
Academic Article
Luciferase renaturation assays of chaperones and chaperone antagonists.
Academic Article
The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart.
Academic Article
Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.
Academic Article
Derrubone, an inhibitor of the Hsp90 protein folding machinery.
Academic Article
ATP-dependent chaperoning activity of reticulocyte lysate.
Academic Article
Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation.
Academic Article
p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.
Grant
Identification of Natural Product Inhibitors of Hsp90 as Chemotherapeutic Agents
Search Criteria
Protein Folding