Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1 (Q24337678)

chaperone binding

1 reference

Hch1p YNL281W

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Aha1p YDR214W

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author

Chrisostomos Prodromou

16

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Paul Workman

13

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Giuliano Siligardi

2

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Stefan Millson

Stefan H Millson

7

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Robert C. Stein

Rob Stein

10

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Paul A Clarke

Paul A Clarke

8

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Rainer Cramer

Rainer Cramer

11

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Philippe Meyer

Philippe Meyer

3

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Peter W Piper

Peter W Piper

14

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Mehdi Mollapour

Mehdi Mollapour

12

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author name string

Barry Panaretou

1

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Alison Maloney

4

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Janis K Sullivan

5

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Shradha Singh

6

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Soren Naaby-Hansen

9

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Laurence H Pearl

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

15

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language of work or name

English

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publication date

December 2002

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published in

Molecular Cell

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volume

10

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issue

6

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page(s)

1307-18

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cites work

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In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

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Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone.

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Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE.

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All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae

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Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth

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Cluster analysis and display of genome-wide expression patterns

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SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins

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Genomic expression programs in the response of yeast cells to environmental changes

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New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites

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Cluster analysis of an extensive human breast cancer cell line protein expression map database

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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

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Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

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A model for the mechanism of strand passage by DNA gyrase

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Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties

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The role of ATP in the functional cycle of the DnaK chaperone system

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Stimulation of the weak ATPase activity of human hsp90 by a client protein

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Suppression of c-Src Activity by C-Terminal Src Kinase Involves the c-Src SH2 and SH3 Domains: Analysis with Saccharomyces cerevisiae

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Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation

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

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

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Structure, function, and mechanism of the Hsp90 molecular chaperone

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The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor Receptors

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

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

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

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Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

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p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site

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Chaperones in progesterone receptor complexes

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Nucleotides and two functional states of hsp90

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A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae

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Allosteric control by ATP of non-folded protein binding to GroEL

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Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

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10.1016/S1097-2765(02)00785-2

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12504007

1 reference

Consolidated OpenCitations Corpus – April 2017