A
Arne Raasakka
Researcher at University of Bergen
Publications - 47
Citations - 628
Arne Raasakka is an academic researcher from University of Bergen. The author has contributed to research in topics: Myelin & Biology. The author has an hindex of 11, co-authored 37 publications receiving 419 citations. Previous affiliations of Arne Raasakka include University of Oulu & Flanders Institute for Biotechnology.
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Journal ArticleDOI
Antagonistic Functions of MBP and CNP Establish Cytosolic Channels in CNS Myelin
Nicolas Snaidero,Nicolas Snaidero,Caroline Velte,Matti Myllykoski,Arne Raasakka,Arne Raasakka,Alexander Ignatev,Hauke B. Werner,Michelle S Erwig,Wiebke Möbius,Wiebke Möbius,Petri Kursula,Petri Kursula,Klaus-Armin Nave,Klaus-Armin Nave,Mikael Simons +15 more
TL;DR: This study identified 2,′3′-cyclic nucleotide 3′-phosphodiesterase (CNP), an oligodendrocyte-specific protein previously implicated in the maintenance of axonal integrity, as an essential factor in generating and maintaining cytoplasm within the myelin compartment.
Journal ArticleDOI
Membrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Line.
Arne Raasakka,Arne Raasakka,Salla Ruskamo,Julia Kowal,Robert Barker,Anne Baumann,Anne Baumann,Anne L. Martel,Jussi T. Tuusa,Matti Myllykoski,Jochen Bürck,Anne S. Ulrich,Henning Stahlberg,Petri Kursula,Petri Kursula +14 more
TL;DR: The results support the formation of an amorphous protein phase of MBP between two membrane bilayers and provide a molecular model for MDL formation during myelination, which is of importance when understanding myelin assembly and demyelinating conditions.
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The myelin membrane-associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: on a highway to structure and function.
TL;DR: The membrane-anchored myelin enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase is found to be involved in local adenosine production in traumatic brain injury and possibly has a regulatory function in mitochondrial membrane permeabilization.
Journal ArticleDOI
Molecular structure and function of myelin protein P0 in membrane stacking
Arne Raasakka,Arne Raasakka,Salla Ruskamo,Julia Kowal,Julia Kowal,Huijong Han,Anne Baumann,Anne Baumann,Matti Myllykoski,A. Fasano,Rocco Rossano,Paolo Riccio,Jochen Bürck,Anne S. Ulrich,Henning Stahlberg,Petri Kursula,Petri Kursula +16 more
TL;DR: Transmission electron cryomicroscopy of native full-length P0 showed that P0 stacks lipid membranes by forming antiparallel dimers between the extracellular Ig-like domains, which explains the double structure of the myelin intraperiod line.
Journal ArticleDOI
Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation.
TL;DR: A detailed picture of the CNPase active site during its catalytic cycle is provided, and a specific function for the previously uncharacterized N-terminal domain is suggested.