Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants.

@article{Quintas2001TetramerDA,
  title={Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants.},
  author={Alexandre Quintas and Daniela C Vaz and Isabel Cardoso and Maria Jo{\~a}o Saraiva and Rui M. M. Brito},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 29},
  pages={27207-13}
}
Amyloid fibril formation and deposition is a common feature of a wide range of fatal diseases including spongiform encephalopathies, Alzheimer's disease, and familial amyloidotic polyneuropathies (FAP), among many others. In certain forms of FAP, the amyloid fibrils are mostly constituted by variants of transthyretin (TTR), a homotetrameric plasma protein. Recently, we showed that transthyretin in solution may undergo dissociation to a non-native monomer, even under close to physiological… CONTINUE READING

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Transthyretin Stability and Amyloidogenesis

M. R. Almeida, A. M. Damas, M. C. Lans, A. Brouwer, M.J.M. Saraiva
Biochemistry • 1997

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