(Q33632917)

28 July 2017

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title

Hsp90 & Co. - a holding for folding (English)

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28 July 2017

J Buchner

1

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28 July 2017

1 April 1999

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28 July 2017

6

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Trends in Biochemical Sciences

inferred from page(s)

published in

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28 July 2017

24

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28 July 2017

136-141

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28 July 2017

4

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hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures

28 July 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Trypanosoma cruzi heat-shock protein 90 can functionally complement yeast

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Reduced levels of hsp90 compromise steroid receptor action in vivo

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Heat-shock protein hsp90 governs the activity of pp60v-src kinase

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Ancient heat shock gene is dispensable

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Steroid receptor interactions with heat shock protein and immunophilin chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Regulation of protein function through expression of chimaeric proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Dynamic activation of endothelial nitric oxide synthase by Hsp90.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor-hsp90 Heterocomplex Assembly

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Chaperones get in touch: the Hip-Hop connection

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Chaperone function of Hsp90-associated proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Cdc37 is a molecular chaperone with specific functions in signal transduction

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Hsp90 chaperones protein folding in vitro.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

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/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Interaction between casein kinase II and the 90-kDa stress protein, HSP90

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Assessment of the ATP binding properties of Hsp90.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

ATP-binding properties of human Hsp90.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

In vitro evidence that hsp90 contains two independent chaperone sites

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

The charged region of Hsp90 modulates the function of the N-terminal domain

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

Hsp90 as a capacitor for morphological evolution

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901373-0

7 January 2021

10.1016/S0968-0004(99)01373-0

Identifiers

DOI

1 reference

28 July 2017

1 reference

PubMed ID

10322418