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

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

Laboratory investigation; a journal of technical methods and pathology - 1 May 2004

Miller Sean R, Sekijima Yoshiki, Kelly Jeffery W

Abstract excerpt

Transthyretin (TTR) tetramer dissociation and misfolding affords a monomeric amyloidogenic intermediate that misassembles into aggregates including amyloid fibrils. Amyloidogenesis of wild-type (WT) TTR causes senile systemic amyloidosis (SSA), whereas fibril formation from one of the more than 80 TTR variants leads to familial amyloidosis, typically with earlier onset than SSA. Several nonsteroidal...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidosis
Share to Anti-Inflammatory Agents, Non-Steroidal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Stability

Share to In Vitro Techniques

Share to Kinetics

Share to Prealbumin

Share to Protein Folding

Share to Protein Structure, Quaternary

Source

Identifiers

PMID: 14968122
DOI: 10.1038/labinvest.3700059

Genes

TTR

Variants

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

Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants.PMID 14968122Read ↗

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

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

Structural stabilization of transthyretin by a new compound, 6-benzoyl-2-hydroxy-1H-benzo[de]isoquinoline-1,3(2H)-dione.Semantic proximity Read ↗

Transthyretin (ATTR) amyloidosis: clinical spectrum, molecular pathogenesis and disease-modifying treatments.Semantic proximity Read ↗

Inhibition of the Amyloidogenesis of Transthyretin by Natural Products and Synthetic Compounds.Semantic proximity Read ↗

Systemic optimization and structural evaluation of quinoline derivatives as transthyretin amyloidogenesis inhibitors.Semantic proximity Read ↗

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

Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design.Semantic proximity Read ↗

Targeting Amyloid Aggregation: An Overview of Strategies and MechanismsSemantic proximity Read ↗

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

Tafamidis in transthyretin amyloid cardiomyopathy: effects on transthyretin stabilization and clinical outcomes.Semantic proximity Read ↗

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

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