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

Quaternary structure, aggregation and cytotoxicity of transthyretin.

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis - 1 Jun 2012

Mizuguchi Mineyuki, Yokoyama Takeshi, Nabeshima Yuko, Kawano Keiichi, Tanaka Ichiro, Niimura Nobuo

Abstract excerpt

Transthyretin (TTR) with a Ser112-to-Ile mutation is known to cause amyloidosis with severe cardiomyopathy. We investigated the quaternary structure, aggregation and cytotoxicity of the S112I variant. This variant exists as a dimer at physiological pH, self-assembles into spherical aggregates and induces cell death in human neuroblastoma IMR-32 cells. In addition, we determined the neutron crystal structure of...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidosis
Share to Cell Death

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

Share to Crystallography, X-Ray

Share to Hydrogen Bonding

Share to Hydrogen-Ion Concentration

Share to Prealbumin

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Source

Identifiers

PMID: 22439750
DOI: 10.3109/13506129.2012.666510

Genes

TTR

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Quaternary structure, aggregation and cytotoxicity of transthyretin.PMID 22439750Read ↗

Dimeric transthyretin variant assembles into spherical neurotoxins.Semantic proximity Read ↗

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

Disruption of the CD Loop by Enzymatic Cleavage Promotes the Formation of Toxic Transthyretin Oligomers through a Common Transthyretin Misfolding Pathway.Semantic proximity Read ↗

The Physical Driving Forces of Conformational Transition for TTR91-96 with Proline Mutations.Semantic proximity Read ↗

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

Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation.Semantic proximity Read ↗

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.Semantic proximity Read ↗

Different disease-causing mutations in transthyretin trigger the same conformational conversion.Semantic proximity Read ↗

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

Comparative MD analysis of the stability of transthyretin providing insight into the fibrillation mechanism.Semantic proximity Read ↗

Conformational Dynamics of an Amyloidogenic Intermediate of Transthyretin: Implications for Structural Remodeling and Amyloid Formation.Semantic proximity Read ↗

Cellular secretion and cytotoxicity of transthyretin mutant proteins underlie late-onset amyloidosis and neurodegeneration.Semantic proximity Read ↗

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