(Q24313523)

peptidyl-prolyl isomerase F

1 reference

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

Hsp90 chaperones protein folding in vitro.

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Chaperones get in touch: the Hip-Hop connection

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Protein Folding In Vivo: Unraveling Complex Pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Steroid receptor interactions with heat shock protein and immunophilin chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

The TPR snap helix: a novel protein repeat motif from mitosis to transcription

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Characterization of functional domains of the eukaryotic co-chaperone Hip

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Mechanism of Dimer Formation of the 90‐kDa Heat‐Shock Protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

Mutational analysis of the hsp70-interacting protein Hip

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

7 January 2021

In vitro evidence that hsp90 contains two independent chaperone sites

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1074/JBC.273.29.18007

7 January 2021