Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.

The EMBO journal - 4 Mar 2009

Graf Christian, Stankiewicz Marta, Kramer Günter, Mayer Matthias P

Abstract excerpt

The highly conserved 90 kDa heat shock protein (Hsp90) chaperones use ATP to regulate the stability and activity of many signalling molecules like protein kinases and transcription factors. Studies using crystallography, electron microscopy and small-angle X-ray scattering yielded controversial results for the conformational states that these dimeric multidomain proteins assume while progressing through the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Dyes

Share to HSP90 Heat-Shock Proteins

Share to Mass Spectrometry

Share to Protein Conformation

Share to Recombinant Proteins

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 19165152
DOI: 10.1038/emboj.2008.306
PMCID: PMC2657576

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.PMID 19165152Read ↗

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.Semantic proximity Read ↗

ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.Semantic proximity Read ↗

Evolution of the conformational dynamics of the molecular chaperone Hsp90.Semantic proximity Read ↗

Two closed ATP- and ADP-dependent conformations in yeast Hsp90 chaperone detected by Mn(II) EPR spectroscopic techniques.Semantic proximity Read ↗

Symmetric stimulation of Hsp90 catalyzed ATP hydrolysis through enhanced active site gate dynamics.Semantic proximity Read ↗

Understanding of ATP-lid conformational dynamics in the N-terminal domain of Hsp90 and its mutants by use of a computational biochemistry approach.Semantic proximity Read ↗

Structural and kinetic basis for the regulation and potentiation of Hsp104 function.Semantic proximity Read ↗

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains.Semantic proximity Read ↗

Conformational equilibria in allosteric control of Hsp70 chaperones.Semantic proximity Read ↗

Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.Semantic proximity Read ↗

How a pathogenic mutation impairs Hsp60 functional dynamics from monomeric to fully assembled statesSemantic proximity Read ↗

Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.