| Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates S Chia, P Flagmeier, J Habchi, V Lattanzi, S Linse, CM Dobson, ... Proceedings of the National Academy of Sciences 114 (30), 8005-8010, 2017 | 60 | 2017 |
| Amyloid β 42 fibril structure based on small-angle scattering V Lattanzi, I André, U Gasser, M Dubackic, U Olsson, S Linse Proceedings of the National Academy of Sciences 118 (48), e2112783118, 2021 | 42 | 2021 |
| Surface-catalyzed secondary nucleation dominates the generation of toxic IAPP aggregates DC Rodriguez Camargo, S Chia, J Menzies, B Mannini, G Meisl, ... Frontiers in Molecular Biosciences 8, 757425, 2021 | 28 | 2021 |
| Sphere–Tubule Superstructures through Supramolecular and Supracolloidal Assembly Pathways J Cautela, V Lattanzi, LK Månsson, L Galantini, JJ Crassous Small 14 (50), 1803215, 2018 | 21 | 2018 |
| Solubility of Aβ40 peptide V Lattanzi, K Bernfur, E Sparr, U Olsson, S Linse JCIS Open 4, 100024, 2021 | 14 | 2021 |
| On the cluster formation of α-synuclein fibrils M Dubackic, I Idini, V Lattanzi, Y Liu, A Martel, A Terry, M Haertlein, ... Frontiers in molecular biosciences 8, 768004, 2021 | 3 | 2021 |
| Serine phosphorylation mimics of Aβ form distinct, non-cross-seeding fibril morphs K Sanagavarapu, G Meisl, V Lattanzi, K Bernfur, B Frohm, U Olsson, ... Chemical Science 15 (45), 19142-19159, 2024 | | 2024 |
| Amyloid β peptide: from monomer solubility to fibril structure V Lattanzi | | 2021 |
