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

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation.

Proceedings of the National Academy of Sciences of the United States of America - 4 May 2010

Lee Sukyeong, Sielaff Bernhard, Lee Jungsoon, Tsai Francis T F

Abstract excerpt

Hsp104 is a ring-forming AAA+ machine that recognizes both aggregated proteins and prion-fibrils as substrates and, together with the Hsp70 system, remodels substrates in an ATP-dependent manner. Whereas the ability to disaggregate proteins is dependent on the Hsp104 M-domain, the location of the M-domain is controversial and its exact function remains unknown. Here we present cryoEM structures of two Hsp104...

Read the complete abstract on PubMed

Topics

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

Share to beta-Galactosidase
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Heat-Shock Proteins

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20404203
DOI: 10.1073/pnas.1003572107
PMCID: PMC2889573

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation.PMID 20404203Read ↗

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.Semantic proximity Read ↗

Structure and function of the molecular chaperone Hsp104 from yeast.Semantic proximity Read ↗

The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation.Semantic proximity Read ↗

Protein disaggregation mediated by heat-shock protein Hsp104.Semantic proximity Read ↗

Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein.Semantic proximity Read ↗

Disaggregating chaperones: an unfolding story.Semantic proximity Read ↗

Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.Semantic proximity Read ↗

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.Semantic proximity Read ↗

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

Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.Semantic proximity Read ↗

Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Semantic proximity Read ↗

Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation.Semantic proximity Read ↗

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