Thomas Näsström

Artikel i tid­skrift (Referee­granskat)

• Näsström, T., Ådén, J., Shibata, F., Andersson, P.O., Karlsson, B.C.G. (2020). A Capped Peptide of the Aggregation Prone NAC 71–82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations. International Journal of Molecular Sciences. 21. 1-14.
• Näsström, T., Andersson, P.O., Lejon, C., Karlsson, B.C.G. (2019). Amyloid fibrils prepared using an acetylated and methyl amidated peptide model of the alpha-Synuclein NAC 71-82 amino acid stretch contain an additional cross-beta structure also found in prion proteins. Scientific Reports. 9. 1-14.
• Fagerqvist, T., Lindström, V., Nordström, E., Lord, A., Tucker, S.M.E., et al. (2013). Monoclonal antibodies selective for α-synuclein oligomers/protofibrils recognize brain pathology in Lewy body disorders and α-synuclein transgenic mice with the disease-causing A30P mutation. Journal of Neurochemistry. 126. 131-144.
• Fagerqvist, T., Näsström, T., Ihse, E., Lindström, V., Sahlin, C., et al. (2013). Off-pathway α-synuclein oligomers seem to alter α-synuclein turnover in a cell model but lack seeding capability in vivo. Amyloid : Journal of Protein Folding Disorders. 20. 233-244.