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6. Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation. Klein RD; Shu Q; Cusumano ZT; Nagamatsu K; Gualberto NC; Lynch AJL; Wu C; Wang W; Jain N; Pinkner JS; Amarasinghe GK; Hultgren SJ; Frieden C; Chapman MR mBio; 2018 Jul; 9(4):. PubMed ID: 30018113 [TBL] [Abstract][Full Text] [Related]
7. Amyloid peptides derived from CsgA and FapC modify the viscoelastic properties of biofilm model matrices. Lembré P; Di Martino P; Vendrely C Biofouling; 2014; 30(4):415-26. PubMed ID: 24592895 [TBL] [Abstract][Full Text] [Related]
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13. Intrinsically disordered Pseudomonas chaperone FapA slows down the fibrillation of major biofilm-forming functional amyloid FapC. Byeon CH; Hansen KH; Jeffrey J; Saricayir H; Andreasen M; Akbey Ü FEBS J; 2024 May; 291(9):1925-1943. PubMed ID: 38349812 [TBL] [Abstract][Full Text] [Related]
14. The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Hammer ND; Schmidt JC; Chapman MR Proc Natl Acad Sci U S A; 2007 Jul; 104(30):12494-9. PubMed ID: 17636121 [TBL] [Abstract][Full Text] [Related]
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20. Folding Steps in the Fibrillation of Functional Amyloid: Denaturant Sensitivity Reveals Common Features in Nucleation and Elongation. Sønderby TV; Rasmussen HØ; Frank SA; Skov Pedersen J; Otzen DE J Mol Biol; 2022 Jan; 434(2):167337. PubMed ID: 34748745 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]