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

Molecular determinants and thermodynamics of the amyloid precursor protein transmembrane domain implicated in Alzheimer's disease.

Journal of molecular biology - 20 May 2011

Wang Hao, Barreyro Laura, Provasi Davide, Djemil Imane, Torres-Arancivia Celia, Filizola Marta, Ubarretxena-Belandia Iban

Abstract excerpt

The deposition of toxic amyloid-β (Aβ) peptide aggregates in the brain is a hallmark of Alzheimer's disease. The intramembrane proteolysis by γ-secretase of the amyloid precursor protein β-carboxy-terminal fragment (APP-βCTF) constitutes the final step in the production of Aβ peptides. Mounting evidence suggests that APP-βCTF is a transmembrane domain (TMD) dimer, and that dimerization might modulate the...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer Disease
Share to Amyloid beta-Protein Precursor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloid Precursor Protein Secretases

Share to Computer Simulation

Share to Protein Conformation

Share to Protein Interaction Domains and Motifs

Share to Protein Multimerization

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 21440556
DOI: 10.1016/j.jmb.2011.03.028
PMCID: PMC3082318

Genes

APP

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

Molecular determinants and thermodynamics of the amyloid precursor protein transmembrane domain implicated in Alzheimer's disease.PMID 21440556Read ↗

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

Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.Semantic proximity Read ↗

Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Semantic proximity Read ↗

Tau local structure shields an amyloid-forming motif and controls aggregation propensitySemantic proximity Read ↗

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

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis.Semantic proximity Read ↗

Tau local structure shields amyloid motif and controls aggregation propensitySemantic proximity Read ↗

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

Polymorphic structures of Alzheimer's β-amyloid globulomers.Semantic proximity Read ↗

A thermodynamic investigation of amyloid precursor protein processing by human γ-secretase.Semantic proximity Read ↗

Dissecting conformational changes in APP's transmembrane domain linked to ε-efficiency in familial Alzheimer's disease.Semantic proximity Read ↗

Dimerization Mechanism of Alzheimer Aβ40 Peptides: The High Content of Intrapeptide-Stabilized Conformations in A2V and A2T Heterozygous Dimers Retards Amyloid Fibril Formation.Semantic proximity Read ↗

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