These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
139 related articles for article (PubMed ID: 31421227)
1. Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation. Najarzadeh Z; Pedersen JN; Christiansen G; Shojaosadati SA; Pedersen JS; Otzen DE Biochim Biophys Acta Proteins Proteom; 2019 Nov; 1867(11):140263. PubMed ID: 31421227 [TBL] [Abstract][Full Text] [Related]
2. Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC. Nagaraj M; Ahmed M; Lyngsø J; Vad BS; Bøggild A; Fillipsen A; Pedersen JS; Otzen DE; Akbey Ü J Mol Biol; 2020 Mar; 432(7):2232-2252. PubMed ID: 32084414 [TBL] [Abstract][Full Text] [Related]
3. Interaction of membrane vesicles with the Najarzadeh Z; Mohammad-Beigi H; Pedersen JN; Christiansen G; Pedersen JS; Nielsen J; Otzen DE BBA Adv; 2022; 2():100055. PubMed ID: 37082589 [TBL] [Abstract][Full Text] [Related]
5. Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC. Rasmussen HØ; Otzen DE; Pedersen JS J Biol Chem; 2022 Feb; 298(2):101569. PubMed ID: 35007533 [TBL] [Abstract][Full Text] [Related]
6. Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Rasmussen CB; Christiansen G; Vad BS; Lynggaard C; Enghild JJ; Andreasen M; Otzen D Protein Sci; 2019 Mar; 28(3):633-642. PubMed ID: 30592554 [TBL] [Abstract][Full Text] [Related]
12. 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]
13. Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation. Christensen LFB; Jensen KF; Nielsen J; Vad BS; Christiansen G; Otzen DE ACS Omega; 2019 Feb; 4(2):4029-4039. PubMed ID: 31459612 [TBL] [Abstract][Full Text] [Related]
14. 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. Byeon CH; Wang PC; Byeon IL; Akbey Ü Biomol NMR Assign; 2023 Dec; 17(2):159-165. PubMed ID: 37162737 [TBL] [Abstract][Full Text] [Related]
15. Influence of the macromolecular crowder alginate in the fibrillar organization of the functional amyloid FapC from Pseudomonas aeruginosa. Siri M; Herrera M; Moyano AJ; Celej MS Arch Biochem Biophys; 2021 Nov; 713():109062. PubMed ID: 34688606 [TBL] [Abstract][Full Text] [Related]
16. A multimethod approach for analyzing FapC fibrillation and determining mass per length. Rasmussen HØ; Otzen DE; Pedersen JS Biophys J; 2021 Jun; 120(11):2262-2275. PubMed ID: 33812849 [TBL] [Abstract][Full Text] [Related]
17. 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]
18. Functional amyloid in a lipid-like environment: a merry dance of many steps. Otzen DE Essays Biochem; 2022 Dec; 66(7):1035-1046. PubMed ID: 36205438 [TBL] [Abstract][Full Text] [Related]
19. Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS. Mortensen HG; Madsen JK; Andersen KK; Vosegaard T; Deen GR; Otzen DE; Pedersen JS Biophys J; 2017 Dec; 113(12):2621-2633. PubMed ID: 29262357 [TBL] [Abstract][Full Text] [Related]
20. Tannin-controlled micelles and fibrils of κ-casein. Ma W; Tribet C; Guyot S; Zanchi D J Chem Phys; 2019 Dec; 151(24):245103. PubMed ID: 31893889 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]