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Cinnamic acid derivatives as the potential modulators of prion aggregation

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Tishina S. A. et al. Cinnamic acid derivatives as the potential modulators of prion aggregation // Mendeleev Communications. 2017. Vol. 27. No. 5. pp. 493-494.
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Tishina S. A., Stroylov V. S., Zanyatkin I. A., Melnikova A. K., Muronetz V. I., Stroylova Y. Y. Cinnamic acid derivatives as the potential modulators of prion aggregation // Mendeleev Communications. 2017. Vol. 27. No. 5. pp. 493-494.
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TY - JOUR
DO - 10.1016/j.mencom.2017.09.021
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2017.09.021
TI - Cinnamic acid derivatives as the potential modulators of prion aggregation
T2 - Mendeleev Communications
AU - Tishina, Sofia Andreevna
AU - Stroylov, Viktor Sergeevich
AU - Zanyatkin, Ivan Andreevich
AU - Melnikova, Aleksandra Kirillovna
AU - Muronetz, Vladimir Izrailevich
AU - Stroylova, Yulia Yur'evna
PY - 2017
DA - 2017/09/07
PB - Mendeleev Communications
SP - 493-494
IS - 5
VL - 27
ER -
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@article{2017_Tishina,
author = {Sofia Andreevna Tishina and Viktor Sergeevich Stroylov and Ivan Andreevich Zanyatkin and Aleksandra Kirillovna Melnikova and Vladimir Izrailevich Muronetz and Yulia Yur'evna Stroylova},
title = {Cinnamic acid derivatives as the potential modulators of prion aggregation},
journal = {Mendeleev Communications},
year = {2017},
volume = {27},
publisher = {Mendeleev Communications},
month = {Sep},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2017.09.021},
number = {5},
pages = {493--494},
doi = {10.1016/j.mencom.2017.09.021}
}
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Tishina, Sofia Andreevna, et al. “Cinnamic acid derivatives as the potential modulators of prion aggregation.” Mendeleev Communications, vol. 27, no. 5, Sep. 2017, pp. 493-494. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2017.09.021.

Abstract

Eight cinnamic acid derivatives were studied as prion inhibitors in vitro and their cytotoxicity was evaluated. Ferulic (3-methoxy-4-hydroxycinnamic) acid, 3,4,5-trimethoxycin- namic acid and methyl 3-ethoxy-4-acetamidoxycinnamate were found to inhibit amyloid fibril formation, seeding, and spontaneous aggregation of recombinant ovine prion protein. None of the compounds demonstrated cytotoxicity on human neuroblastoma SH-SY5Y cells.

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