Amyloids and prions in the light of evolution
Author:
Funder
Russian Science Foundation
Publisher
Springer Science and Business Media LLC
Subject
Genetics,General Medicine
Link
https://link.springer.com/content/pdf/10.1007/s00294-023-01270-6.pdf
Reference127 articles.
1. Ahmed AB, Znassi N, Château MT, Kajava AV (2015) A structure-based approach to predict predisposition to amyloidosis. Alzheimers Dement 11:681–690. https://doi.org/10.1016/j.jalz.2014.06.007
2. Akbey Ü, Andreasen M (2022) Functional amyloids from bacterial biofilms - structural properties and interaction partners. Chem Sci 13:6457–6477. https://doi.org/10.1039/d2sc00645f
3. Alberti S, Halfmann R, King O, Kapila A, Lindquist S (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137:146–158. https://doi.org/10.1016/j.cell.2009.02.044
4. Al-Garawi ZS, Morris KL, Marshall KE, Eichler J, Serpell LC (2017) The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides. Interface Focus 7:20170027. https://doi.org/10.1098/rsfs.2017.0027
5. Ali M, Chernova TA, Newnam GP et al (2014) Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion. J Biol Chem 289:27625–27639. https://doi.org/10.1074/jbc.M114.582429
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