A fractional-order yeast prion mathematical model and its solution
Author:
Funder
University Grants Commission
Department of Science and Technology
Publisher
Springer Science and Business Media LLC
Link
https://link.springer.com/content/pdf/10.1007/s12190-024-02063-x.pdf
Reference30 articles.
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2. Wickner, R.B., Edskes, H.K., Wu, S., Gregg, K.: Prions are the greatest protein misfolding problem, and yeast has several solutions. PLoS Pathog. 19(5), e1011333 (2023)
3. Chernoff, Y.O., Grizel, A.V., Rubel, A.A., Zelinsky, A.A., Chandramowlishwaran, P., Chernova, T.A.: Application of yeast to studying amyloid and prion diseases. Adv. Genet. 105, 293–380 (2020)
4. Kushnirov, V.V., Kochneva-Pervukhova, N.V., Chechenova, M.B., Frolova, N.S., Ter-Avanesyan, M.D.: Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J. 19(3), 324–331 (2000)
5. Kryndushkin, D.S., Alexandrov, I.M., Ter-Avanesyan, M.D., Kushnirov, V.V.: Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278(49), 49636–49643 (2003)
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