Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation
Author:
Affiliation:
1. Graduate School of Engineering, Osaka University
Publisher
Biophysical Society of Japan
Subject
Physiology,Molecular Biology,Biophysics,Biochemistry,Biochemistry, Genetics and Molecular Biology (miscellaneous)
Link
https://www.jstage.jst.go.jp/article/biophysico/20/1/20_e200013/_pdf
Reference74 articles.
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2. [2] Eisenberg, D. S., Sawaya, M. R. Structural studies of amyloid proteins at the molecular level. Annu. Rev. Biochem. 86, 69–95 (2017). https://doi.org/10.1146/annurev-biochem-061516-045104
3. [3] Chiti, F., Dobson, C. M. Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade. Annu. Rev. Biochem. 86, 27–68 (2017). https://doi.org/10.1146/annurev-biochem-061516-045115
4. [4] Iadanza, M. G., Silvers, R., Boardman, J., Smith, H. I., Karamanos, T. K., Debelouchina, G. T., et al. The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nat. Commun. 9, 4517 (2018). https://doi.org/10.1038/s41467-018-06761-6
5. [5] Schweighauser, M., Shi, Y., Tarutani, A., Kametani, F., Murzin, A. G., Ghetti, B., et al. Structures of α-synuclein filaments from multiple system atrophy. Nature 585, 464–469 (2020). https://doi.org/10.1038/s41586-020-2317-6
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