ReviewFrontiers in molecular neuroscience2020
Modulation of the Mechanisms Driving Transthyretin Amyloidosis.
Review in Frontiers in molecular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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
25 citing papers in PubMed, 43 citations in OpenAlex.
- Disease-Modifying Therapies for Hereditary Transthyretin Amyloidosis with Polyneuropathy: Current Status and Future Perspectives.Neurology and therapy · 2026Review
- Transthyretin at the crossroads of neurodegeneration: a silent guardian in Parkinson's disease.Metabolic brain disease · 2026Review
- Amyloid fibril polymorphism in the heart and liver of a patient with polyneuropathic ATTRv-V122Δ amyloidosis.Communications biology · 2026Article
- Amyloidogenic phenotypical variation affects post-transplant outcome of hereditary transthyretin amyloidosis: a retrospective study.eGastroenterology · 2026Article
- Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.Nature communications · 2025Article
- Article
- The Concise Guide to PHARMACOLOGY 2025/26: Introduction and Other Protein Targets.British journal of pharmacology · 2025Review
- Exploring Genetic Silencing: RNAi and CRISPR-Cas Potential against Drug Resistance in Malaria.Mini reviews in medicinal chemistry · 2025Review
- ATTRv-V30M amyloid fibrils from heart and nerves exhibit structural homogeneity.Structure (London, England : 1993) · 2024Article
- Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.Communications biology · 2024Article
- ATTRv-V30M Type A amyloid fibrils from heart and nerves exhibit structural homogeneity.bioRxiv : the preprint server for biology · 2024Article
- Amyloid fibril polymorphism in the heart of an ATTR amyloidosis patient with polyneuropathy attributed to the V122Δ variant.bioRxiv : the preprint server for biology · 2024Article
- Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.bioRxiv : the preprint server for biology · 2024Article
- Molecular mechanisms and emerging therapies in wild-type transthyretin amyloid cardiomyopathy.Heart failure reviews · 2024Review
- Characterization of heterozygous ATTR Tyr114Cys amyloidosis-specific induced pluripotent stem cells.Heliyon · 2024Article
- Iatrogenic intramuscular hematoma of the oblique muscles as a complication of technetium-99m-labeled pyrophosphate imaging-based computed tomography-guided core-needle biopsy in a patient with wild-type transthyretin cardiac amyloidosis.Radiology case reports · 2024Article
- The Concise Guide to PHARMACOLOGY 2023/24: Introduction and Other Protein Targets.British journal of pharmacology · 2023Review
- Transthyretin Stabilizers and Seeding Inhibitors as Therapies for Amyloid Transthyretin Cardiomyopathy.Pharmaceutics · 2023Review
- A molecular basis for tetramer destabilization and aggregation of transthyretin Ala97Ser.Protein science : a publication of the Protein Society · 2023Article
- Amyloid seeding as a disease mechanism and treatment target in transthyretin cardiac amyloidosis.Heart failure reviews · 2022Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transthyretin (TTR) amyloidoses are systemic diseases associated with TTR aggregation and extracellular deposition in tissues as amyloid. The most frequent and severe forms of the disease are hereditary and associated with amino acid substitutions in the protein due to single point mutations in the
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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.