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14 p, 2.4 MB Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy / Ferreira, Priscila (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica) ; Sant'Anna, Ricardo (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica) ; Varejão, Nathalia (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica) ; Lima, Cinthia (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica) ; Novis, Shenia (Centro de Estudos de Paramiloidose Antônio Rodrigues de Mello) ; Barbosa, Renata V. (Centro de Estudos de Paramiloidose Antônio Rodrigues de Mello) ; Caldeira, Concy M. (SONDA. Universidade Federal do Rio de Janeiro) ; Rumjanek, Franklin D. (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Cruz, Marcia W. (Centro de Estudos de Paramiloidose Antônio Rodrigues de Mello) ; Foguel, Debora (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Transthyretin (TTR) is a tetrameric beta-sheet-rich protein. Its deposits have been implicated in four different amyloid diseases. Although aggregation of the wild-type sequence is responsible for the senile form of the disease, more than one hundred variants have been described thus far, most of which confer a more amyloidogenic character to TTR, mainly because they compromise the stability of the protein in relation to monomer formation, which upon misfolding is intrinsically aggregation-prone. [...]
2013 - 10.1371/journal.pone.0082484
PloS one, Vol. 8, issue 12 (2013) , art. e82484  

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