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

Lipid-induced conformational transition of amyloid beta peptide fragments.

Journal of molecular neuroscience : MN - 1 Jul 2010

Sureshbabu Nagarajan, Kirubagaran R, Thangarajah H, Malar E J Padma, Jayakumar R

Abstract excerpt

Conformational transition of soluble monomeric amyloid beta-peptide (Abeta) into oligomeric and protofibrillar aggregates plays a key role in the pathogenesis of Alzheimer's disease (AD). One of the central questions surrounding the molecular pathophysiology of AD is how the soluble Abeta is converted into its aggregated toxic form. A more detailed understanding of the conformational transitions involved in the...

Read the complete abstract on PubMed

Topics

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

Share to Protein Folding
Share to Amyloid beta-Peptides
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Lipids

Share to Peptide Fragments

Share to Plaque, Amyloid

Share to Protein Structure, Secondary

Share to Static Electricity

Source

Identifiers

PMID: 20480256
DOI: 10.1007/s12031-010-9380-7

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

Lipid-induced conformational transition of amyloid beta peptide fragments.PMID 20480256Read ↗

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

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

Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant.Semantic proximity Read ↗

The effect of Alzheimer's Aβ aggregation state on the permeation of biomimetic lipid vesicles.Semantic proximity Read ↗

Conformational Characterization of Native and L17A/F19A-Substituted Dutch-Type β-Amyloid Peptides.Semantic proximity Read ↗

Environment- and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein.Semantic proximity Read ↗

Self-assembly pathways of E22Δ-type amyloid β peptide mutants generated from non-aggregative O-acyl isopeptide precursors.Semantic proximity Read ↗

Effects of Familial Alzheimer's Disease Mutations on the Assembly of a β-Hairpin Peptide Derived from Aβ16-36.Semantic proximity Read ↗

Molecular Insights into Human Hereditary Apolipoprotein A-I Amyloidosis Caused by the Glu34Lys Mutation.Semantic proximity Read ↗

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

Effects of Familial Alzheimer’s Disease Mutations on the Folding Free Energy and Dipole-Dipole Interactions of the Amyloid <i>β</i> -PeptideSemantic proximity Read ↗

Probing APP Cleavage and Amyloid-β Assembly via Synthetic MUC-Type O-Glycosylated APP Glycopeptides.Semantic proximity Read ↗

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