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

Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.

Biophysical journal - 21 Apr 2010

Brorsson Ann-Christin, Bolognesi Benedetta, Tartaglia Gian Gaetano, Shammas Sarah L, Favrin Giorgio, Watson Ian, Lomas David A, Chiti Fabrizio, Vendruscolo Michele, Dobson Christopher M, Crowther Damian C, Luheshi Leila M

Abstract excerpt

The extent to which proteins aggregate into distinct structures ranging from prefibrillar oligomers to amyloid fibrils is key to the pathogenesis of many age-related degenerative diseases. We describe here for the Alzheimer's disease-related amyloid beta peptide (Abeta) an investigation of the se...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Peptides
Share to Benzothiazoles

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drosophila melanogaster

Share to Longevity

Share to Mutant Proteins

Share to Neurotoxins

Share to Protein Structure, Quaternary

Share to Thiazoles

Source

Open in PubMed Open full text

Identifiers

PMID: 20409489
DOI: 10.1016/j.bpj.2009.12.4320
PMCID: PMC2856165

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20409489-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.PMID 20409489Read ↗

Systematic In Vivo Analysis of the Intrinsic Determinants of Amyloid β PathogenicitySemantic proximity Read ↗

The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseasesSemantic proximity Read ↗

The Single Toxin Origin of Alzheimer’s Disease and Other Neurodegenerative Disorders Enables Targeted Approach to Treatment and PreventionSemantic proximity Read ↗

Modeling the Aggregation Propensity and Toxicity of Amyloid-β Variants.Semantic proximity Read ↗

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by SequestrationSemantic proximity Read ↗

Structural Determinant of β-Amyloid Formation: From Transmembrane Protein Dimerization to β-Amyloid AggregatesSemantic proximity Read ↗

Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide.Semantic proximity Read ↗

Unraveling the aggregation dynamics of amyloidogenesis: A data-driven mathematical modeling approachSemantic proximity Read ↗

Design of non-aggregating variants of Aβ peptide.Semantic proximity Read ↗

Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models.Semantic proximity Read ↗

Factors influencing compact-extended structure equilibrium in oligomers of aβ1-40 peptide--an ion mobility mass spectrometry study.Semantic proximity Read ↗

Sequestration of the Aβ Peptide Prevents Toxicity and Promotes Degradation In VivoSemantic proximity Read ↗

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