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An acetylation site in the middle domain of Hsp90 regulates chaperone function.
Heat-shock protein 90 (Hsp90) chaperones a key subset of signaling proteins and is necessary for malignant transformation. Hsp90 is subject to an array of posttranslational modifications that affectExpand
The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties*
The hsp90 family of molecular chaperones was expanded recently due to the cloning of TRAP1 and hsp75 by yeast two-hybrid screens. Careful analysis of the human TRAP1 and hsp75 sequences revealed thatExpand
Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified Chaperones*
Checkpoint kinase 1 (Chk1), a serine/threonine kinase that regulates DNA damage checkpoints, is destabilized when heat shock protein 90 (Hsp90) is inhibited, suggesting that Chk1 is an Hsp90 client.Expand
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies.
Multiple molecular chaperones, including Hsp90 and p23, interact with members of the intracellular receptor (IR) family. To investigate p23 function, we compared the effects of three p23 proteins onExpand
Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer.
The heat shock protein 90 (Hsp90) has a critical role in malignant transformation. Whereas its ability to maintain the functional conformations of mutant and aberrant oncoproteins is established, aExpand
GCUNC-45 Is a Novel Regulator for the Progesterone Receptor/hsp90 Chaperoning Pathway
ABSTRACT The hsp90 chaperoning pathway is a multiprotein system that is required for the production or activation of many cell regulatory proteins, including the progesterone receptor (PR). We reportExpand
Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones.
The Hsp90 family of proteins in mammalian cells consists of Hsp90 alpha and beta, Grp94, and Trap-1 (Hsp75). Radicicol, an antifungal antibiotic that inhibits various signal transduction proteinsExpand
Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone*
p23 is a co-chaperone for the heat shock protein, hsp90. This protein binds hsp90 and participates in the folding of a number of cell regulatory proteins, but its activities are still unclear. WeExpand
A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion
Heat shock protein 90 (Hsp90) is a molecular chaperone that maintains function of numerous intracellular signaling nodes utilized by cancer cells for proliferation and survival. Hsp90 is alsoExpand
p23, a simple protein with complex activities
Abstract p23 is a small but important cochaperone for the Hsp90 chaperoning pathway. It appears to facilitate the adenosine triphosphate–driven cycle of Hsp90 binding to client proteins. It enters atExpand
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