ReviewInternational journal of molecular sciences2021
A Brief Journey through Protein Misfolding in Transthyretin Amyloidosis (ATTR Amyloidosis).
Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 2 of them syntheses 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
22 citing papers in PubMed, 2 syntheses or guidelines pooled it, 37 citations in OpenAlex.
- Pharmacological Interventions for Hereditary Transthyretin-Related Amyloidosis With Polyneuropathy: Systematic Review and Network Meta-Analysis.European journal of neurology · 2026Pooled it
- Direct Oral Anticoagulants vs. Vitamin K Antagonists for Atrial Fibrillation in Cardiac Amyloidosis: A Systematic Review and Meta-analysis.Reviews in cardiovascular medicine · 2025Pooled it
- Pathogenesis and kidney prognosis of renal amyloidosis.Cellular and molecular life sciences : CMLS · 2026Review
- Association Between Occupational Physical Work Exposure and Wild-Type Transthyretin Cardiomyopathy.JACC. Advances · 2026Article
- Synthesis, Structural Characterization, and In Silico Evaluation of the Salicylidene Schiff Base 4‑{(ACS omega · 2026Article
- The Arrhythmic Burden of Cardiac Amyloidosis: A Comprehensive Review.Heart views : the official journal of the Gulf Heart Association · 2026Review
- Clinical and genetic analysis of a family with transthyretin amyloid polyneuropathy caused by a TTR Lys55Asn mutation.Orphanet journal of rare diseases · 2025Article
- Survival in a Contemporary, Real-World Cohort of Patients with Mixed-Phenotype Transthyretin Amyloid Cardiomyopathy Treated with Tafamidis: An Analysis from THAOS.Cardiology and therapy · 2025Article
- Unravelling the myriad physiologic roles of transthyretin: critical considerations for treating transthyretin amyloidosis.Annals of medicine · 2025Review
- Polyneuropathy in hereditary and wildtype transthyretin amyloidosis, comparison of key clinical features and red flags.Scientific reports · 2025Article
- Effectiveness and Utility of Genetic Testing in Establishing a Diagnosis of Hereditary Transthyretin Amyloidosis.Journal of clinical medicine · 2025Article
- Real-world treatment management in hereditary transthyretin amyloidosis - an experience report and proposal for therapy switch decision criteria.Neurological research and practice · 2025Article
- Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.Journal of applied crystallography · 2025Article
- From Molecular to Radionuclide and Pharmacological Aspects in Transthyretin Cardiac Amyloidosis.International journal of molecular sciences · 2024Review
- Molecular mechanisms and emerging therapies in wild-type transthyretin amyloid cardiomyopathy.Heart failure reviews · 2024Review
- Case Report: A rare transthyretin mutation p.D58Y in a Chinese case of transthyretin amyloid cardiomyopathy.Frontiers in cardiovascular medicine · 2024Article
- Examining the Difficulties in Identifying and Handling Cardiac Amyloidosis; Acquiring Important Knowledge and Robust Treatment Methods.Cardiovascular & hematological disorders drug targets · 2024Review
- EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates.International journal of molecular sciences · 2023Article
- Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins.Molecules (Basel, Switzerland) · 2023Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transthyretin (TTR) amyloidogenesis involves the formation, aggregation, and deposition of amyloid fibrils from tetrameric TTR in different organs and tissues. While the result of amyloidoses is the accumulation of amyloid fibrils resulting in end-organ damage, the nature, and sequence of the molecular causes leading to amyloidosis may differ between the different variants. In addition, fibril accumulation and toxicity vary between different mutations. Structural changes in amyloidogenic TTR have been difficult to identify through X-ray crystallography; but nuclear magnetic resonance spectroscopy has revealed different chemical shifts in the backbone structure of mutated and wild-type TTR, resulting in diverse responses to the cellular conditions or proteolytic stress. Toxic mechanisms of TTR amyloidosis have different effects on different tissues. Therapeutic approaches have evolved from orthotopic liver transplants to novel disease-modifying therapies that stabilize TTR tetramers and gene-silencing agents like small interfering RNA and antisense oligonucleotide therapies. The underlying molecular mechanisms of the different TTR variants could be responsible for the tropisms to specific organs, the age at onset, treatment responses, or disparities in the prognosis.
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.