Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-023-10155-1.pdf
Reference17 articles.
1. Akbey U, Andreasen M (2022) Functional amyloids from bacterial biofilms - structural properties and interaction partners. Chem Sci 13(22):6457–6477
2. Bohush A, Filipek A (2020) HSP90 Co-Chaperone, CacyBP/SIP, protects alpha-synuclein from aggregation. Cells 9(10):2254
3. Byeon C-H et al (2023) Initial steps of chaperone-aided fibrillation of Pseudomonas aeruginosa biofilm forming functional amyloid FapC. bioRxiv. https://doi.org/10.1101/2023.03.14.530334
4. Byeon CH et al (2023b) Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa. Biomolecular Nmr Assign. https://doi.org/10.1101/2023.03.14.530334
5. Chapman MR et al (2002) Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295(5556):851–855
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1. Intrinsically disordered Pseudomonas chaperone FapA slows down the fibrillation of major biofilm‐forming functional amyloid FapC;The FEBS Journal;2024-02-13
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