(Q27930200)

GOA release 2020-03-11

author name string

T Weikl

2

0 references

T Scheibel

1

0 references

S Lindquist

5

0 references

R Rimerman

3

0 references

J Buchner

6

0 references

D Smith

Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery

4

0 references

language of work or name

English

0 references

publication date

November 1999

0 references

published in

Molecular Microbiology

1 reference

1 December 2016

34

0 references

page(s)

701-13

0 references

issue

4

0 references

cites work

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046/J.1365-2958.1999.01632.X

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Hsp90 & Co. - a holding for folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Protein folding in vivo: unraveling complex pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Sequences That Regulate the Divergent GAL1-GAL10 Promoter in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The assembly of progesterone receptor-hsp90 complexes using purified proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Hsp90 is required for pheromone signaling in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Reduced levels of hsp90 compromise steroid receptor action in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Steroid receptor interactions with heat shock protein and immunophilin chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The Hsp90 complex--a super-chaperone machine as a novel drug target.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

ATP-binding properties of human Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Getting started with yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Purification of heat shock protein-peptide complexes for use in vaccination against cancers and intracellular pathogens

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone GRP94.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Interaction of the Rous sarcoma virus protein pp60src with the cellular proteins pp50 and pp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Hsp90 Regulates Androgen Receptor Hormone Binding Affinityin Vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Trypanosoma cruzi heat-shock protein 90 can functionally complement yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

Targeted replacement of the mouse apolipoprotein E gene with the common human APOE3 allele enhances diet-induced hypercholesterolemia and atherosclerosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X

In vitro evidence that hsp90 contains two independent chaperone sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01632.X