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Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis.
Hum Mutat
March 1997
Department of Medicine, New York University and Research Service, New York Veterans Administration Medical Center, New York 10010, USA.
A new isoleucine substitution of Val-20 in transthyretin tetramers selectively impairs dimer-dimer contacts and causes systemic amyloidosis.
Proc Natl Acad Sci U S A
June 1996
Max-Planck-Institut für Psychiatrie, Abteilung Neuroimmunologie, Martinsried, Germany.
The most frequent form of inherited amyloidoses is associated with mutations in the transthyretin (TTR) gene coding for 127-amino acid residues of four identical, noncovalently linked subunits that form a pair of dimers in the plasma protein complex. Amyloid fibrils containing the variant and to a lesser extent the wild-type form of the TTR molecule are deposited in various organs, including peripheral nerves and the myocardium, with polyneuropathy and cardiomyopathy as major clinical manifestations. So far, more than 40 distinct amino acid substitutions distributed throughout the TTR sequence over 30 positions have been found to be correlated with an increased amyloidogenicity of TTR.
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