ReviewInternational journal of molecular sciences2024
From Molecular to Radionuclide and Pharmacological Aspects in Transthyretin Cardiac Amyloidosis.
Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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
2 citing papers in PubMed.
- [Thrombopenia and hemolytic anemia in acute and emergency medicine : Detailed view at thrombotic microangiopathies].Innere Medizin (Heidelberg, Germany) · 2025Review
- Case Report: Challenges in the diagnosis and treatment of cardiac amyloidosis: a case misdiagnosed as dual cardiac amyloidosis.Frontiers in cardiovascular medicine · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
Amyloidosis is a rare pathology characterized by protein deposits in various organs and tissues. Cardiac amyloidosis (CA) can be caused by various protein deposits, but transthyretin amyloidosis (ATTR) and immunoglobulin light chain (AL) are the most frequent pathologies. Protein misfolding can be induced by several factors such as oxidative stress, genetic mutations, aging, chronic inflammation, and neoplastic disorders. In ATTR cardiomyopathy (ATTR-CM), the amyloid fibrils can be found in the myocardium interstitial space and are associated with arrhythmias and heart failure. In pathological situations, the transthyretin (TTR) configuration is destroyed by proteolytic action, leading to monomers that further misfold and aggregate to form the amyloid fibrils.
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