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Fibril in senile systemic amyloidosis is derived from normal transthyretin.

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Westermark, P, Sletten, K, Johansson, B, Cornwell, G G·1990·Proceedings of the National Academy of Sciences

Abstract

The amyloid fibril in senile systemic amyloidosis (SSA), like that of familial amyloidotic polyneuropathy, is derived from transthyretin (TTR). SSA, however, is a common disease, affecting to some degree 25% of the population greater than 80 years old. In familial amyloidotic polyneuropathy, the amyloidogenesis has been considered to depend on point mutations leading to TTR variants. We show that the TTR molecule in SSA, on the other hand, has a normal primary structure. Factors other than the primary structure of TTR must therefore be important in the pathogenesis of TTR-derived amyloid.

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Metadata

Authors
Westermark, P., Sletten, K., Johansson, B., & Cornwell, G. G.
Venue
Proceedings of the National Academy of Sciences
Published
1990-04
Volume
87
Issue
7
Pages
2843-2845
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2022945618
Cited by
696
References
0
FWCI
4.86
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Fibril in senile systemic amyloidosis is derived from normal transthyretin. https://app.cochat.ai/papers/10.1073/pnas.87.7.2843
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Westermark, P., Sletten, K., Johansson, B., & Cornwell, G. G. (1990). Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.87.7.2843

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.