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Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1
Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as repressor of heat shockExpand
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Circulating activated platelets exacerbate atherosclerosis in mice deficient in apolipoprotein E
We studied whether circulating activated platelets and platelet–leukocyte aggregates cause the development of atherosclerotic lesions in apolipoprotein-E–deficient (Apoe−/−) mice. CirculatingExpand
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The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Hsp90 is required for the normal activity of steroid receptors, and in steroid receptor complexes it is typically bound to one of the immunophilin‐related co‐chaperones: the peptidylprolyl isomerasesExpand
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Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery*
  • S. Chen, D. Smith
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 25 December 1998
Hop, an abundant and conserved protein of unresolved function, binds concomitantly with heat shock protein 70 (Hsp70) and Hsp90, participates with heat shock proteins at an intermediate stage ofExpand
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Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes
The ability to bind immunosuppressive drugs such as cyclosporin and FK506 defines the immunophilin family of proteins, and the FK506-binding proteins form the FKBP subfamily of immunophilins. SomeExpand
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Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells
P-selectin (CD62, GMP-140, PADGEM), a Ca(2+)-dependent lectin on activated platelets and endothelium, functions as a receptor for myeloid cells by interacting with sialylated, fucosylatedExpand
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Galectin-1, -2, and -3 Exhibit Differential Recognition of Sialylated Glycans and Blood Group Antigens*
Human galectins have functionally divergent roles, although most of the members of the galectin family bind weakly to the simple disaccharide lactose (Galβ1-4Glc). To assess the specificity ofExpand
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Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes.
  • D. Smith
  • Biology, Medicine
  • Molecular endocrinology
  • 1 November 1993
A cell-free system was used to examine heat shock protein 90 (hsp90)-progesterone receptor (PR) binding at near physiological conditions. Four major findings are presented: 1) hsp90 is required toExpand
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Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
As with many other viruses, the initial cell attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans.Expand
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Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent.
The assembly of progesterone receptor (PR) heterocomplexes in vitro involves at least eight components of the molecular chaperone machinery, and as earlier reports have shown, these proteins exhibitExpand
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