Article
A new isoleucine substitution of Val-20 in transthyretin tetramers selectively impairs dimer-dimer contacts and causes systemic amyloidosis.
Proceedings of the National Academy of Sciences of the United States of America - 25 Jun 1996
Jenne D E, Denzel K, Blätzinger P, Winter P, Obermaier B, Linke R P, Altland K
Abstract excerpt
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...
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