ArticleNature communications2019
A molecular mechanism for transthyretin amyloidogenesis.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
78 citing papers in PubMed, 1 synthesis or guideline pooled it, 137 citations in OpenAlex.
- Chemistry, Biological Properties, and Bio-analysis of Tafamidis, a New Transthyretin Stabilizer: A Systematic Review.Cardiovascular & hematological agents in medicinal chemistry · 2024Pooled it
- Solution Phase Protein Dynamics: Influences of ESI Buffers on Hydration.Analytical chemistry · 2026Article
- Evaluation of the Current ATTR-CM Treatment Landscape via a Mathematical Model of TTR Dissociation and Amyloid Formation.CPT: pharmacometrics & systems pharmacology · 2026Article
- Changes in the concentration of phosphatidylcholine in lipid bilayers determines the aggregation rate of transthyretin.Biophysical chemistry · 2026Article
- Synthesis, Structural Characterization, and In Silico Evaluation of the Salicylidene Schiff Base 4‑{(ACS omega · 2026Article
- Light-induced analgesia provides a drug-free optical method for pain relief via activation of TRAAK kNature communications · 2026Article
- Glycosidic scaffold bearing multiple galloyl moieties from pomegranate disrupts transthyretin amyloids.iScience · 2026Article
- A Comprehensive Review of Gene Mutations in Inherited Blood Disorders Among the Saudi Population.Human mutation · 2026Review
- Amyloidogenic phenotypical variation affects post-transplant outcome of hereditary transthyretin amyloidosis: a retrospective study.eGastroenterology · 2026Article
- Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology.Analytical chemistry · 2025Article
- Integrative structural profiling and ligand optimisation across the transthyretin mutational landscape.NPJ systems biology and applications · 2025Article
- Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR.Journal of applied crystallography · 2025Article
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- Dual modulation of amyloid beta and tau aggregation and dissociation in Alzheimer's disease: a comprehensive review of the characteristics and therapeutic strategies.Translational neurodegeneration · 2025Review
- Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.Journal of applied crystallography · 2025Article
- Management of Hereditary Transthyretin Amyloidosis (ATTRv) Patients and Asymptomatic Carriers in Spain: The EMPATIa Study.Journal of clinical medicine · 2024Article
- Global longitudinal strain in pre-symptomatic patients with mutation for transthyretin amyloidosis.Orphanet journal of rare diseases · 2024Article
- Designed Cell-Penetrating Peptide Constructs for Inhibition of Pathogenic Protein Self-Assembly.Pharmaceutics · 2024Review
- Mispacking of the F87 sidechain drives aggregation-promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer.Protein science : a publication of the Protein Society · 2024Article
- Identification of the interfacial regions in misfolded transthyretin oligomers.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human transthyretin (TTR) is implicated in several fatal forms of amyloidosis. Many mutations of TTR have been identified; most of these are pathogenic, but some offer protective effects. The molecular basis underlying the vastly different fibrillation behaviours of these TTR mutants is poorly understood. Here, on the basis of neutron crystallography, native mass spectrometry and modelling studies, we propose a mechanism whereby TTR can form amyloid fibrils via a parallel equilibrium of partially unfolded species that proceeds in favour of the amyloidogenic forms of TTR. It is suggested that unfolding events within the TTR monomer originate at the C-D loop of the protein, and that destabilising mutations in this region enhance the rate of TTR fibrillation. Furthermore, it is proposed that the binding of small molecule drugs to TTR stabilises non-amyloidogenic states of TTR in a manner similar to that occurring for the protective mutants of the protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.