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

Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.

Proceedings of the National Academy of Sciences of the United States of America - 22 Aug 2017

Wälti Marielle A, Schmidt Thomas, Murray Dylan T, Wang Huaibin, Hinshaw Jenny E, Clore G Marius

Abstract excerpt

We have studied the interaction of the prototypical chaperonin GroEL with the prion domain of the Het-s protein using solution and solid-state NMR, electron and atomic force microscopies, and EPR. While GroEL accelerates Het-s protofibril formation by several orders of magnitude, the rate of appearance of fibrils is reduced. GroEL remains bound to Het-s throughout the aggregation process and densely decorates the...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Chaperonin 10

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chaperonin 60

Share to Electron Spin Resonance Spectroscopy

Share to Magnetic Resonance Spectroscopy

Share to Microscopy, Atomic Force

Share to Microscopy, Electron

Share to Prion Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 28784759
DOI: 10.1073/pnas.1711645114
PMCID: PMC5576843

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.PMID 28784759Read ↗

The mechanism of prion inhibition by HET-S.Semantic proximity Read ↗

Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.Semantic proximity Read ↗

The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.Semantic proximity Read ↗

Correlation of structural elements and infectivity of the HET-s prion.Semantic proximity Read ↗

The bacterial chaperonin GroEL requires GroES to reduce aggregation and cell death in a COS-7 cell model of Huntington's disease.Semantic proximity Read ↗

The mechanism of toxicity in HET-S/HET-s prion incompatibility.Semantic proximity Read ↗

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Semantic proximity Read ↗

From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.Semantic proximity Read ↗

The GroEL/GroES cis cavity as a passive anti-aggregation device.Semantic proximity Read ↗

Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Semantic proximity Read ↗

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.Semantic proximity Read ↗

Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.Semantic proximity Read ↗

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