Guideline of transthyretin-related hereditary amyloidosis for clinicians

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Guideline of transthyretin-related hereditary amyloidosis for clinicians

Transthyretin amyloidosis is a progressive and eventually fatal disease primarily characterized by sensory, motor, and autonomic neuropathy and/or cardiomyopathy. Given its phenotypic unpredictability and variability, transthyretin amyloidosis can be difficult to recognize and manage. Misdiagnosis is common, and patients may wait several years before accurate diagnosis, risking additional signi...

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Early identification of transthyretin-related hereditary cardiac amyloidosis.

Amyloidosis is characterized by the extracellular deposition of highly-organized fibrillar aggregates showing a cross-beta super-secondary structure (1). Several proteins are amyloidogenic in humans, resulting in different clinical presentations, either systemic or localized. Transthyretin-related hereditary amyloidosis (ATTR) is a late-onset, dominantly inherited systemic amyloidosis. Heterozy...

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[Familial approach in hereditary transthyretin cardiac amyloidosis].

Cardiac amyloidosis is a disease of complex diagnosis and treatment. Some subtypes of cardiac amyloidosis are inherited. Among these, the most common variant is caused by mutations in the transthyretin gene. Correct identification of amyloidosis produced by a genetic defect is of great importance because it modifies the diagnostic and therapeutic approach in patients and their families. We desc...

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Hereditary Transthyretin Amyloidosis in Eight Chinese Families

BACKGROUND Mutations of transthyretin (TTR) cause the most common type of autosomal-dominant hereditary systemic amyloidosis, which occurs worldwide. To date, more and more mutations in the TTR gene have been reported. Some variations in the clinical presentation are often observed in patients with the same mutation or the patients in the same family. The purpose of this study was to find out t...

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ژورنال

عنوان ژورنال: Orphanet Journal of Rare Diseases

سال: 2013

ISSN: 1750-1172

DOI: 10.1186/1750-1172-8-31