Author

O. C. Krokengen

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Organism:human· 5 Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Assay:protein structure· 2 Assay:proteomics· 2 Assay:cryo-EM· 1

Frequent Co-Authors

P. Kursula· 5 shared A. Raasakka· 4 shared A. Sutinen· 2 shared S. Ruskamo· 2 shared A. C. Simonsen· 1 shared A. J. Lopez Moreno· 1 shared A. Mularski· 1 shared C. Bramham· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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5 shared papersBiochemistry

P. Kursula

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Author profile →

5 papers

Recent·Most cited

The cytoplasmic tail of myelin protein zero induces morphological changes in lipid membranes

O. C. Krokengen, C. Touma, A. Mularski, A. Sutinen, R. Dunkel, M. Ytterdal, A. Raasakka, H. D. T. Mertens, A. C. Simonsen, P. Kursula

This paper investigates how the cytoplasmic tail of P0 affects lipid membrane morphology and describes the production of full-length P0 for further study.

bioRxiv · Mar 22, 2024Biochemistry

Structural characterization of two nanobodies targeting the ligand-binding pocket of human Arc

J. M. Godoy Munoz, L. Neset, S. Markusson, S. Weber, O. C. Krokengen, A. Sutinen, E. Christakou, A. J. Lopez Moreno, C. Bramham, P. Kursula

This paper characterizes two anti-Arc nanobodies that bind to the ligand-binding pocket of human Arc-NL, revealing their structural and functional properties as competitive inhibitors.

bioRxiv · Sep 6, 2023 · PreprintBiochemistry

The intrinsically disordered protein glue of myelin: Linking AlphaFold2 predictions to experimental data

O. C. Krokengen, A. Raasakka, P. Kursula

This study links AlphaFold2 predictions of myelin-specific intrinsically disordered proteins to experimental data, showing helical segments in predicted models match membrane-binding sites.

bioRxiv · Sep 13, 2022 · PreprintBiophysics

Determinants for forming a supramolecular myelin-like proteolipid lattice

S. Ruskamo, O. C. Krokengen, J. Kowal, T. Nieminen, M. Lehtimaki, A. Raasakka, V. P. Dandey, I. Vattulainen, H. Stahlberg, P. Kursula

This study uses structural and functional analyses to reveal how myelin protein P2 forms a supramolecular lattice between lipid bilayers, identifying key residues and interactions involved in membrane binding.

bioRxiv · Feb 6, 2020 · PreprintBiochemistry

Neuropathy-related mutations alter the membrane binding properties of the human myelin protein P0 cytoplasmic tail

A. Raasakka, S. Ruskamo, R. Barker, O. C. Krokengen, G. H. Vatne, C. K. Kristiansen, E. I. Hallin, M. W. Skoda, U. Bergmann, H. Wacklin-Knecht, N. C. Jones, S. V. Hoffmann, P. Kursula

This study investigates how neuropathy-related mutations in the cytoplasmic tail of the human myelin protein P0 affect its membrane binding properties and function.

bioRxiv · Jan 30, 2019Biophysics