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QRB Discovery|December 25, 2025
The low complexity linker of DNAJB6b is key to its anti-amyloid functionTimas Merkelis, Ulf Olsson, Sara LinseBiophysical Journal|November 8, 2025
Does amyloid fibril nucleation occur at surfaces only?Jon Pallbo, Sara Linse, Ulf OlssonThe Journal of Biological Chemistry|October 5, 2023
The C-terminal domain of the antiamyloid chaperone DNAJB6 binds to amyloid-β peptide fibrils and inhibits secondary nucleationNicklas Österlund, Rebecca Frankel, Andreas Carlsson, et al.Langmuir : the ACS Journal of Surfaces and Colloids|November 15, 2019
Fibril Charge Affects α-Synuclein Hydrogel Rheological PropertiesBrett H Pogostin, Sara Linse, Ulf OlssonACS Chemical Neuroscience|November 21, 2022
Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary NucleationDev Thacker, Amanda Willas, Alexander J Dear, et al.Biophysical Chemistry|February 12, 2025
On the thermal and chemical stability of DNAJB6b and its globular domainsCelia Fricke, Jelica Milošević, Andreas Carlsson, et al.Proceedings of the National Academy of Sciences of the United States of America|June 12, 2023
Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptideDev Thacker, Mohammad Barghouth, Mara Bless, et al.International Journal of Molecular Sciences|February 15, 2022
A Palette of Fluorescent Aβ42 Peptides Labelled at a Range of Surface-Exposed SitesDev Thacker, Mara Bless, Mohammad Barghouth, et al.Langmuir : the ACS Journal of Surfaces and Colloids|July 16, 2025
Air-Water Interfacial Adsorption of the Chaperone Protein DNAJB6bJon Pallbo, Marco Fornasier, Sara Linse, et al.Proceedings of the National Academy of Sciences of the United States of America|April 20, 2026
The temperature dependence of amyloid β solubility reveals the hydrophobic effect as the main driving force for fibril formationMax Lindberg, Jing Hu, Dev Thacker, et al.Pageof 43