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

Identification of beta-amyloid-binding sites on transthyretin.

Protein engineering, design & selection : PEDS - 1 Jul 2012

Du Jiali, Cho Patricia Y, Yang Dennis T, Murphy Regina M

Abstract excerpt

Transthyretin (TTR) binds to the Alzheimer-related peptide beta-amyloid (Aβ), and may protect against Aβ-induced neurotoxicity. In this work, the specific domains on TTR involved with binding to Aβ were probed. An array was constructed of peptides derived from overlapping sequences from TTR. Strong binding of Aβ to TIAALLSPYSYS (residues 106-117) was detected, corresponding to strand G on the inner β-sheet of...

Read the complete abstract on PubMed

Topics

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

Share to Protein Structure, Secondary
Share to Alanine
Share to Amyloid beta-Peptides

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Binding Sites

Share to Models, Molecular

Share to Prealbumin

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Source

Open in PubMed Open full text

Identifiers

PMID: 22670059
DOI: 10.1093/protein/gzs026
PMCID: PMC3530273

Genes

TTR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of beta-amyloid-binding sites on transthyretin.PMID 22670059Read ↗

Characterization of the interaction of β-amyloid with transthyretin monomers and tetramers.Semantic proximity Read ↗

Stability of the transthyretin molecule as a key factor in the interaction with a-beta peptide--relevance in Alzheimer's disease.Semantic proximity Read ↗

Amyloidogenic and anti-amyloidogenic properties of recombinant transthyretin variantsSemantic proximity Read ↗

Crystal structures of amyloidogenic segments of human transthyretin.Semantic proximity Read ↗

Transthyretin Mimetics as Anti-β-Amyloid Agents: A Comparison of Peptide and Protein Approaches.Semantic proximity Read ↗

Transthyretin mutagenesis: impact on amyloidogenesis and disease.Semantic proximity Read ↗

Transthyretin: a review from a structural perspective.Semantic proximity Read ↗

The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.Semantic proximity Read ↗

A comparative analysis of 23 structures of the amyloidogenic protein transthyretin.Semantic proximity Read ↗

Review: TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies.Semantic proximity Read ↗

A new isoleucine substitution of Val-20 in transthyretin tetramers selectively impairs dimer-dimer contacts and causes systemic amyloidosis.Semantic proximity Read ↗

Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.Semantic proximity Read ↗

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