Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90 (Q24313523)

peptidyl-prolyl isomerase F

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Translocase of outer mitochondrial membrane 34

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Cell division cycle 37, HSP90 cochaperone

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FKBP prolyl isomerase 4

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FKBP prolyl isomerase 5

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heat shock protein binding

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Journal of Biological Chemistry

3

F U Hartl

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author name string

J C Young

series ordinal

1

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W M Obermann

series ordinal

2

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language of work or name

English

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publication date

17 July 1998

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published in

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volume

273

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issue

29

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page(s)

18007-10

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cites work

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Chaperones get in touch: the Hip-Hop connection

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Protein folding in vivo: unraveling complex pathways

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The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain

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Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

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Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein

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

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

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Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.

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Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins

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The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

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In vitro evidence that hsp90 contains two independent chaperone sites

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A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains

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Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding

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Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independent

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