• Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice 

      Ruskamo, Salla; Krokengen, Oda Caspara; Kowal, Julia; Nieminen, Tuomo; Lehtimäki, Mari; Raasakka, Arne; Dandey, Venkata P; Vattulainen, Ilpo; Stahlberg, Henning; Kursula, Petri (Journal article; Peer reviewed, 2020)
      Myelin protein P2 is a peripheral membrane protein of the fatty acid–binding protein family that functions in the formation and maintenance of the peripheral nerve myelin sheath. Several P2 gene mutations cause human ...
    • Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease 

      Raasakka, Arne; Kursula, Petri (Journal article; Peer reviewed, 2020)
      Myelin ensheathes selected axonal segments within the nervous system, resulting primarily in nerve impulse acceleration, as well as mechanical and trophic support for neurons. In the central and peripheral nervous systems, ...
    • How Does Protein Zero Assemble Compact Myelin? 

      Raasakka, Arne; Kursula, Petri (Journal article; Peer reviewed, 2020-08)
      Myelin protein zero (P0), a type I transmembrane protein, is the most abundant protein in peripheral nervous system (PNS) myelin—the lipid-rich, periodic structure of membrane pairs that concentrically encloses long axonal ...
    • Structure of the ALS Mutation Target Annexin A11 Reveals a Stabilising N-Terminal Segment 

      Lillebostad, Peder August Gudmundsen; Raasakka, Arne; Hjellbrekke, Silje Johannessen; Patil, Sudarshan; Røstbø, Trude Kvalnes; Hollås, Hanne; Sakya, Siri; Szigetvari, Peter Daniel; Vedeler, Anni; Kursula, Petri (Journal article; Peer reviewed, 2020)
      The functions of the annexin family of proteins involve binding to Ca2+, lipid membranes, other proteins, and RNA, and the annexins share a common folded core structure at the C terminus. Annexin A11 (AnxA11) has a long ...