Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone (Q27740876)

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4 November 2019

title

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

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4 November 2019

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Chrisostomos Prodromou

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4 November 2019

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4 November 2019

S M Roe

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4 November 2019

R O'Brien

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4 November 2019

P W Piper

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4 November 2019

L H Pearl

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4 November 2019

language of work or name

English

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publication date

1 July 1997

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4 November 2019

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4 November 2019

volume

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4 November 2019

issue

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4 November 2019

page(s)

65-75

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

4 November 2019

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

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

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

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Physical interaction of mammalian CDC37 with CDK4

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Peptide binding and release by proteins implicated as catalysts of protein assembly

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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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The 24 kDa N-terminal sub-domain of the DNA gyrase B protein binds coumarin drugs

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

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Identifying the catalytic residue of the ATPase reaction of DNA gyrase

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Assessment of the ATP binding properties of Hsp90.

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Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions

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A study into the effects of protein binding on nucleotide conformation

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83‐Kilodalton heat shock proteins of trypanosomes are potent peptide‐stimulated ATPases

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

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Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94.

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A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein

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SSAP: sequential structure alignment program for protein structure comparison

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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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7 January 2021

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

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7 January 2021

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

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7 January 2021

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

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7 January 2021

Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell

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

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7 January 2021

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

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7 January 2021

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

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Nucleotides and two functional states of hsp90

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LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

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7 January 2021

Hsp90 chaperones protein folding in vitro.

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7 January 2021

Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

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Rapid measurement of binding constants and heats of binding using a new titration calorimeter

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Structural analysis of substrate binding by the molecular chaperone DnaK

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DOI

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Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9230303%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9230303%20AND%20SRC:MED&resulttype=core&format=json