ArticleThe Journal of biological chemistry2016
Novel Antibody for the Treatment of Transthyretin Amyloidosis.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- A functional role for spontaneously occurring natural anti-transthyretin antibodies from patients with transthyretin cardiac amyloidosis.European journal of heart failure · 2025Article
- Etiological Treatment of Cardiac Amyloidosis: Standard of Care and Future Directions.Current heart failure reports · 2025Review
- Structural Basis for Monoclonal Antibody Therapy for Transthyretin Amyloidosis.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Emerging Therapies for Transthyretin Amyloidosis.Current oncology reports · 2023Review
- Treating amyloid transthyretin cardiomyopathy: lessons learned from clinical trials.Frontiers in cardiovascular medicine · 2023Review
- Cardiac amyloidosis: evolving pathogenesis, multimodal diagnostics, and principles of treatment.EXCLI journal · 2023Review
- Targeting Amyloid Fibrils by Passive Immunotherapy in Systemic Amyloidosis.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2022Review
- The Journey of Human Transthyretin: Synthesis, Structure Stability, and Catabolism.Biomedicines · 2022Review
- Hereditary Transthyretin Amyloidosis with Polyneuropathy: Monitoring and Management.International journal of general medicine · 2022Review
- Molecular Mechanisms of Cardiac Amyloidosis.International journal of molecular sciences · 2021Review
- The Ultrastructure of Tissue Damage by Amyloid Fibrils.Molecules (Basel, Switzerland) · 2021Review
- Advances in Treatment of ATTRv Amyloidosis: State of the Art and Future Prospects.Brain sciences · 2020Article
- Hereditary transthyretin amyloidosis: a model of medical progress for a fatal disease.Nature reviews. Neurology · 2019Review
- A pair of peptides inhibits seeding of the hormone transporter transthyretin into amyloid fibrils.The Journal of biological chemistry · 2019Article
- Ultrastructure in Transthyretin Amyloidosis: From Pathophysiology to Therapeutic Insights.Biomedicines · 2019Review
- Development of transgenic Caenorhabditis elegans expressing human transthyretin as a model for drug screening.Scientific reports · 2018Article
- Storage diseases with hypertrophic cardiomyopathy phenotype.Global cardiology science & practice · 2018Review
- Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Missense Variant p.Ala117Ser in the Transthyretin Gene of a Han Chinese Family with Familial Amyloid Polyneuropathy.Molecular neurobiology · 2018Article
- Diagnosis and management of transthyretin familial amyloid polyneuropathy in Japan: red-flag symptom clusters and treatment algorithm.Orphanet journal of rare diseases · 2018Review
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Familial amyloidotic polyneuropathy (FAP) is a systemic amyloidosis mainly caused by amyloidogenic transthyretin (ATTR). This incurable disease causes death ∼10 years after onset. Although it has been widely accepted that conformational change of the monomeric form of transthyretin (TTR) is very important for amyloid formation and deposition in the organs, no effective therapy targeting this step is available. In this study, we generated a mouse monoclonal antibody, T24, that recognized the cryptic epitope of conformationally changed TTR. T24 inhibited TTR accumulation in FAP model rats, which expressed human ATTR V30M in various tissues and exhibited non-fibrillar deposits of ATTR in the gastrointestinal tracts. Additionally, humanized T24 (RT24) inhibited TTR fibrillation and promoted macrophage phagocytosis of aggregated TTR. This antibody did not recognize normal serum TTR functioning properly in the blood. These results demonstrate that RT24 would be an effective novel therapeutic antibody for FAP.
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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.