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

Influence of sequence and lipid type on membrane perturbation by human and rat amyloid β-peptide (1-42).

Archives of biochemistry and biophysics - 15 Jan 2017

Brown Anne M, Bevan David R

Abstract excerpt

The hallmark characteristics of plaque formation and neuronal cell death in Alzheimer's disease (AD) are caused principally by the amyloid β-peptide (Aβ). Aβ sequence and lipid composition are essential variables to consider when elucidating the impact of biological membranes on Aβ structure and the effect of Aβ on membrane integrity. Atomistic molecular dynamics simulations testing two Aβ sequences, human and...

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 Amyloid beta-Protein Precursor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Arginine

Share to Cholesterol

Share to Lipid Bilayers

Share to Lipids

Share to Membrane Microdomains

Share to Molecular Dynamics Simulation

Source

Identifiers

PMID: 27884599
DOI: 10.1016/j.abb.2016.11.006

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

Influence of sequence and lipid type on membrane perturbation by human and rat amyloid β-peptide (1-42).PMID 27884599Read ↗

Impact of the Rat R5G, Y10F, and H13R Mutations on Tetrameric Aβ42 β-Barrel in a Lipid Bilayer Membrane Model.Semantic proximity Read ↗

Impact of A2T and D23N Mutations on Tetrameric Aβ42 Barrel within a Dipalmitoylphosphatidylcholine Lipid Bilayer Membrane by Replica Exchange Molecular Dynamics.Semantic proximity Read ↗

Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.Semantic proximity Read ↗

Membrane-Anchored Aβ Accelerates Amyloid Formation and Exacerbates Amyloid-Associated Toxicity in MiceSemantic proximity Read ↗

Apolipoprotein A-I Mimetic 4F Peptide Generates Amyloid Cytotoxins by Forming Hetero-oligomers with β-amyloidSemantic proximity Read ↗

Stability of Aβ11-40 Trimers with Parallel and Antiparallel β-Sheet Organizations in a Membrane-Mimicking Environment by Replica Exchange Molecular Dynamics Simulation.Semantic proximity Read ↗

Effects of the Arctic (E22-->G) mutation on amyloid beta-protein folding: discrete molecular dynamics study.Semantic proximity Read ↗

Ganglioside enriched phospholipid vesicles induce cooperative Aβ oligomerization and membrane disruptionSemantic proximity Read ↗

Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants.Semantic proximity Read ↗

Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Semantic proximity Read ↗

Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal PathologiesSemantic proximity Read ↗

Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.Semantic proximity Read ↗

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