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Journal Abstract Search
177 related items for PubMed ID: 35290118
1. Single-molecule fluorescence imaging and deep learning reveal highly heterogeneous aggregation of amyloid-β 42. Meng F, Yoo J, Chung HS. Proc Natl Acad Sci U S A; 2022 Mar 22; 119(12):e2116736119. PubMed ID: 35290118 [Abstract] [Full Text] [Related]
2. Direct evidence for self-propagation of different amyloid-β fibril conformations. Spirig T, Ovchinnikova O, Vagt T, Glockshuber R. Neurodegener Dis; 2014 Mar 22; 14(3):151-9. PubMed ID: 25300967 [Abstract] [Full Text] [Related]
4. Conserved S/T Residues of the Human Chaperone DNAJB6 Are Required for Effective Inhibition of Aβ42 Amyloid Fibril Formation. Månsson C, van Cruchten RTP, Weininger U, Yang X, Cukalevski R, Arosio P, Dobson CM, Knowles T, Akke M, Linse S, Emanuelsson C. Biochemistry; 2018 Aug 14; 57(32):4891-4902. PubMed ID: 30024736 [Abstract] [Full Text] [Related]
8. Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril Surface. Barz B, Strodel B. Chemistry; 2016 Jun 20; 22(26):8768-72. PubMed ID: 27135646 [Abstract] [Full Text] [Related]
10. Automatic identification of crossovers in cryo-EM images of murine amyloid protein A fibrils with machine learning. Weber M, Bäuerle A, Schmidt M, Neumann M, Fändrich M, Ropinski T, Schmidt V. J Microsc; 2020 Jan 20; 277(1):12-22. PubMed ID: 31859366 [Abstract] [Full Text] [Related]
11. Understanding amyloid fibril nucleation and aβ oligomer/drug interactions from computer simulations. Nguyen P, Derreumaux P. Acc Chem Res; 2014 Feb 18; 47(2):603-11. PubMed ID: 24368046 [Abstract] [Full Text] [Related]
18. Polymorphic Aβ42 fibrils adopt similar secondary structure but differ in cross-strand side chain stacking interactions within the same β-sheet. Wang H, Duo L, Hsu F, Xue C, Lee YK, Guo Z. Sci Rep; 2020 Mar 31; 10(1):5720. PubMed ID: 32235842 [Abstract] [Full Text] [Related]