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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995
A cDNA library was constructed from liver RNA of the Australian diprotodont marsupial Macropus eugenii, the Tammar wallaby. A cloned full-length transthyretin cDNA was sequenced. The derived amino-acid sequence showed 68% overall similarity to that of human transthyretin, with 86% similarity in the thyroxine binding site.
C M, Brack +3 more
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A cDNA library was constructed from liver RNA of the Australian diprotodont marsupial Macropus eugenii, the Tammar wallaby. A cloned full-length transthyretin cDNA was sequenced. The derived amino-acid sequence showed 68% overall similarity to that of human transthyretin, with 86% similarity in the thyroxine binding site.
C M, Brack +3 more
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Hereditary transthyretin amyloidosis associated with a transthyretin variant Thr59Arg
Amyloid, 2017Hereditary transthyretin (TTR) amyloidosis is characterized by ATTR amyloid deposits in various tissue sites and organs, such as peripheral nerves, heart, gastrointestinal tract, kidneys, eyes, and...
Tetsuya, Watanabe +10 more
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Transthyretin amyloid cardiomyopathy
Medicina Clínica (English Edition), 2021Transthyretin (TTR) cardiac amyloidosis is a severe, progressive, infiltrative disease caused by the deposition of TTR at cardiac level. It may be due to a genetic alteration in its hereditary form (ATTRv) or as a consequence of an age-related degenerative process (ATTRwt). Thanks to advances in imaging techniques and the possibility of achieving a non-
Pablo, Garcia-Pavia +2 more
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Safety and Efficacy of RNAi Therapy for Transthyretin Amyloidosis
BACKGROUND: Transthyretin amyloidosis is caused by the deposition of hepatocyte-derived transthyretin amyloid in peripheral nerves and the heart. A therapeutic approach mediated by RNA interference (RNAi) could reduce the production of transthyretin ...
Ole B. Suhr +2 more
exaly +2 more sources
Background Transthyretin amyloidosis (ATTR) is a heterogeneous disorder with multiorgan involvement and a genetic or nongenetic basis. Objectives The goal of this study was to describe ATTR in the United States by using data from the THAOS (Transthyretin
Mathew S Maurer +2 more
exaly +2 more sources
Investigation into thiol conjugation of transthyretin in hereditary transthyretin amyloidosis
European Journal of Clinical Investigation, 1998BackgroundFor all forms of amyloidosis, the amyloid‐generating mechanism is unknown. Familial amyloidotic polyneuropathy type I is caused by a variant transthyretin (TTR Met‐30). As electrospray ionization mass spectrometry (ESI‐MS) discloses both thiol‐conjugated and ‐unconjugated forms of wild‐type and variant TTR, we wanted to investigate the ...
O B, Suhr +7 more
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Structural and functional evolution of transthyretin and transthyretin‐like proteins
Proteins: Structure, Function, and Bioinformatics, 2006AbstractTransthyretin (TTR) is a tetrameric protein involved in the distribution of thyroid hormones in vertebrates. The amino acid sequence of TTR is highly conserved across vertebrates. Hypothetical TTR‐like proteins (TLPs) were inferred from the identification of genes in nonvertebrate species. Here, we identified five motifs defining TLPs and three
Sarah C, Hennebry +3 more
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Transthyretin and the human placenta
Placenta, 2013Since its discovery, transthyretin (TTR) has been regarded as an important hepatically derived protein carrier of thyroid hormones and retinol in blood. However, in more recent years it has been shown that TTR has other important functions. TTR is abundant in cerebrospinal fluid, where it may be involved in transport of thyroid hormones into the brain.
Landers, K. A. +2 more
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Transthyretin and the Transthyretin Amyloidoses
2007Transthyretin is a normal serum protein that carries the secondary thyroid hormone thyroxine and retinol binding protein when it is loaded with retinol. It is synthesized primarily in the liver but there is also significant production in the choroid plexus and the retina. Both message and protein are found in the kidney but that site does not appear to
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Localization of transthyretin-mRNA and of immunoreactive transthyretin in the human fetus
Virchows Archiv A Pathological Anatomy and Histopathology, 1989Five human fetuses at mid-term (16-20 weeks) and one with a gestational age of 8 weeks were investigated. The cellular localization of transthyretin (TTR)-mRNA in different organs was demonstrated by in situ hybridization with a 35S-labelled, single-stranded RNA probe. Immunoreactive TTR (TTR-IR) was localized with a monoclonal antibody to TTR.
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