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

Cooperative stabilization of transthyretin by clusterin and diflunisal.

Biochemistry - 20 Jan 2015

Greene Michael J, Klimtchuk Elena S, Seldin David C, Berk John L, Connors Lawreen H

Abstract excerpt

The circulating protein transthyretin (TTR) can unfold, oligomerize, and form highly structured amyloid fibrils that are deposited in tissues, causing organ damage and disease. This pathogenic process is caused by a heritable TTR point mutation in cases of familial TTR-related amyloidosis or wild-type TTR in cases of age-associated amyloidosis (previously called senile systemic amyloidosis). The TTR amyloid...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Anti-Inflammatory Agents, Non-Steroidal
Share to Clusterin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prealbumin

Share to Protein Stability

Share to Protein Structure, Secondary

Share to Protein Unfolding

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 25478940
DOI: 10.1021/bi5011249
PMCID: PMC4303310

Genes

TTR
CLU

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cooperative stabilization of transthyretin by clusterin and diflunisal.PMID 25478940Read ↗

Transthyretin: Its function and amyloid formation.Semantic proximity Read ↗

Disease-Modifying Treatments for Transthyretin Amyloidosis.Semantic proximity Read ↗

A Brief Journey through Protein Misfolding in Transthyretin Amyloidosis (ATTR Amyloidosis).Semantic proximity Read ↗

Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology.Semantic proximity Read ↗

Thermodynamic Stability and Aggregation Kinetics of EF Helix and EF Loop Variants of Transthyretin.Semantic proximity Read ↗

Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis.Semantic proximity Read ↗

Transthyretin (ATTR) amyloidosis nephropathy: lessons from a TTR stabilizer molecule.Semantic proximity Read ↗

Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.Semantic proximity Read ↗

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

AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin.Semantic proximity Read ↗

Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants.Semantic proximity Read ↗

Unusual duplication mutation in a surface loop of human transthyretin leads to an aggressive drug-resistant amyloid disease.Semantic proximity Read ↗

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