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Showing 1–3 of 3 results
Advanced filters: Author: Leif Antonschmidt Clear advanced filters

  • An atomistic structure of a toxic pre-fibrillar α-Synuclein intermediate is presented, highlighting structural changes that drive amyloid fibril formation.

    • Vrinda Sant
    • Dirk Matthes
    • Loren B. Andreas
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • Interactions between α-synuclein fibrils and lipids have been associated with the development of Parkinson’s disease. This cryo-EM study reveals structural details of these interactions and suggests a mechanism for fibril-induced lipid extraction.

    • Benedikt Frieg
    • Leif Antonschmidt
    • Gunnar F. Schröder
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • Understanding how small molecules bind to pathological aggregates is of importance for therapeutic and diagnostic development in diseases such as Parkinson’s Disease. Here, the authors reveal a binding site of anle138b to lipid-induced α-synuclein fibrils.

    • Leif Antonschmidt
    • Dirk Matthes
    • Loren B. Andreas
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10