Edward G. Mimnaugh

TL;DR: It is demonstrated that HSP participation in multimolecular complex formation is required for src-mediated transformation and can provide a target for drug modulation.

TL;DR: It is demonstrated that disruption of Hsp90 function promotes Hif-1α degradation via a novel, oxygen-independent E3 ubiquitin ligase and diminishes HIF-1 α transcriptional activity, thus extending the utility of these drugs as therapeutic anticancer agents.

TL;DR: An amino-terminal domain of hsp90 whose crystal structure has recently been solved and determined to contain a geldanamycin-binding site is studied and it is demonstrated that, in solution, drug binding is exclusive to this domain.

TL;DR: The rapid depletion of mature p185c-erbB-2 caused by geldanamycin and the marked, drug-stimulated decrease in half-life of the newly synthesized protein are both mediated by the proteasome, although only the former phenomenon involves polyubiquitination.

TL;DR: It is shown that the chaperone-binding ubiquitin ligase CHIP efficiently ubiquitinates and down-regulates ErbB2, and a previously unrecognized pathway, amenable to pharmacologic manipulation, that mediates Erb B2 stability is described.