Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation

Autor: Gunna Christiansen, Line Friis Bakmann Christensen, Daniel E. Otzen, Brian S. Vad, Janni Nielsen, Kirstine Friis Jensen

Publikováno v: ACS Omega
Christensen, L F B, Jensen, K F, Nielsen, J, Vad, B S, Christiansen, G & Otzen, D E 2019, ' Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation ', ACS Omega, vol. 4, no. 2, pp. 4029-4039 . https://doi.org/10.1021/acsomega.8b03590
ACS Omega, Vol 4, Iss 2, Pp 4029-4039 (2019)

Functional amyloid (FA) proteins have evolved to assemble into fibrils with a characteristic cross-β structure, which stabilizes biofilms and contributes to bacterial virulence. Some of the most studied bacterial FAs are the curli protein CsgA, expr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b7aa29f20783394b40ed7baa825953
https://pubmed.ncbi.nlm.nih.gov/31459612