Proteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesis

Autor: Louise C. Serpell, Vittorio Bellotti, Innes R. Clatworthy, Julian D. Gillmore, Graham W. Taylor, Monica Stoppini, Philip N. Hawkins, Julien Marcoux, Maria Chiara Monti, Loredana Marchese, Sara Raimondi, Palma Mangione, Piero Pucci, Steve P. Wood, Carol V. Robinson, Mark B. Pepys, Annalisa Relini, Mattia Porcari, Sofia Giorgetti, Riccardo Porcari, Glenys A. Tennent, Wenjie Chen

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2014, 111 (4), pp.1539-1544. ⟨10.1073/pnas.1317488111⟩

The Ser52Pro variant of transthyretin (TTR) produces aggressive, highly penetrant, autosomal-dominant systemic amyloidosis in persons heterozygous for the causative mutation. Together with a minor quantity of full-length wild-type and variant TTR, th

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https://hal.archives-ouvertes.fr/hal-02335557