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

A multistage pathway for human prion protein aggregation in vitro: from multimeric seeds to β-oligomers and nonfibrillar structures.

Journal of the American Chemical Society - 8 Jun 2011

Cho Kang R, Huang Yu, Yu Shuiliang, Yin Shaoman, Plomp Marco, Qiu S Roger, Lakshminarayanan Rajamani, Moradian-Oldak Janet, Sy Man-Sun, De Yoreo James J

Abstract excerpt

Aberrant protein aggregation causes numerous neurological diseases including Creutzfeldt-Jakob disease (CJD), but the aggregation mechanisms remain poorly understood. Here, we report AFM results on the formation pathways of β-oligomers and nonfibrillar aggregates from wild-type full-length recombinant human prion protein (WT) and an insertion mutant (10OR) with five additional octapeptide repeats linked to...

Read the complete abstract on PubMed

Topics

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

Share to AFM gene
Share to Microscopy, Atomic Force

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Biological

Share to Mutation

Share to Oligopeptides

Share to Particle Size

Share to Prions

Source

Open in PubMed Open full text

Identifiers

PMID: 21534611
DOI: 10.1021/ja1117446
PMCID: PMC4505822

Genes

AFM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A multistage pathway for human prion protein aggregation in vitro: from multimeric seeds to β-oligomers and nonfibrillar structures.PMID 21534611Read ↗

Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitroSemantic proximity Read ↗

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.Semantic proximity Read ↗

Mechanistic Models of Protein Aggregation Across Length-Scales and Time-Scales: From the Test Tube to Neurodegenerative DiseaseSemantic proximity Read ↗

Early stages for Parkinson's development: alpha-synuclein misfolding and aggregation.Semantic proximity Read ↗

Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriersSemantic proximity Read ↗

Self-assembly of protein fibrils into suprafibrillar aggregates: bridging the nano- and mesoscale.Semantic proximity Read ↗

Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generationSemantic proximity Read ↗

Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EMSemantic proximity Read ↗

The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregatesSemantic proximity Read ↗

In vitro generation of highly infectious recombinant prions adopting structural architectures of bona fide prionsSemantic proximity Read ↗

Amyloid structure and assembly: insights from scanning transmission electron microscopy.Semantic proximity Read ↗

Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and KineticsSemantic proximity Read ↗

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