Physicochemical mechanisms of aggregation and fibril formation of α-synuclein and apolipoprotein A-I
Author:
Affiliation:
1. Laboratory of Biophysical Chemistry, Kyoto Pharmaceutical 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/21/1/21_e210005/_pdf
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3. [3] Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295, 851–855 (2002). https://doi.org/10.1126/science.1067484
4. [4] Maji, S. K., Perrin, M. H., Sawaya, M. R., Jessberger, S., Vadodaria, K., Rissman, R. A., et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328–332 (2009). https://doi.org/10.1126/science.1173155
5. [5] Adler-Abramovich, L., Vaks, L., Carny, O., Trudler, D., Magno, A., Caflisch, A., et al. Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria. Nat. Chem. Biol. 8, 701–706 (2012). https://doi.org/10.1038/nchembio.1002
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