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QRB Discovery|August 18, 2023
On the micelle formation of DNAJB6bAndreas Carlsson, Ulf Olsson, Sara LinseLangmuir : 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.Frontiers in Molecular Biosciences|November 5, 2021
On the Cluster Formation of α-Synuclein FibrilsMarija Dubackic, Ilaria Idini, Veronica Lattanzi, 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.ACS Chemical Neuroscience|April 19, 2024
The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation StateAndreas Carlsson, Emil Axell, Cecilia Emanuelsson, et al.Proceedings of the National Academy of Sciences of the United States of America|October 2, 2020
The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrilsDev Thacker, Kalyani Sanagavarapu, Birgitta Frohm, et al.Pageof 42