Author

S. Ruskamo

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· 7 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Organism:human· 7 Research Focus:protein folding & dynamics· 6 Assay:structural biology· 5 Assay:protein structure· 2 Approach:statistical model· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

P. Kursula· 8 shared A. Raasakka· 5 shared A. Sutinen· 3 shared G. T. T. Nguyen· 2 shared H. Stahlberg· 2 shared J. Kowal· 2 shared N. C. Jones· 2 shared O. C. Krokengen· 2 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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8 shared papersBiochemistry

P. Kursula

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Author profile →

8 papers

Recent·Most cited

Conformational analysis of membrane-proximal segments of GDAP1 in a lipidic environment using synchrotron radiation suggests a mode of assembly at the mitochondrial outer membrane

A. Sutinen, N. C. Jones, S. V. Hoffmann, S. Ruskamo, P. Kursula

This study uses synchrotron radiation and spectroscopy to model GDAP1 assembly at the mitochondrial outer membrane, suggesting a single transmembrane helix flanked by peripheral helices.

bioRxiv · May 8, 2023Biochemistry

Conserved intramolecular networks in GDAP1 are closely connected to CMT-linked mutations and protein stability

A. Sutinen, D. Paffenholz, G. T. T. Nguyen, S. Ruskamo, A. E. Torda, P. Kursula

This study analyzes GDAP1 mutations linked to CMT, showing they affect protein stability and conserved intramolecular networks, potentially leading to mitochondrial dysfunction and neuronal degeneration.

bioRxiv · Sep 9, 2022Biochemistry

Human myelin proteolipid protein structure and lipid bilayer stacking

S. Ruskamo, A. Raasakka, J. S. Pedersen, A. Martel, K. Skubnik, T. Darwish, L. Porcar, P. Kursula

This study determines the structure of human myelin proteolipid protein (PLP) and its isoform DM20, revealing their dimeric conformation and role in membrane stacking and organization.

bioRxiv · Mar 14, 2022Biochemistry

Structural insights into Charcot-Marie-Tooth disease-linked mutations in human GDAP1

A. Sutinen, G. T. T. Nguyen, A. Raasakka, G. Muruganandam, R. Loris, E. Ylikallio, H. Tyynismaa, L. Bartesaghi, S. Ruskamo, P. Kursula

This study investigates the structural and biochemical effects of CMT-linked GDAP1 mutations, finding reduced thermal stability and disrupted interaction networks that may impair neuronal function.

bioRxiv · Feb 18, 2022Biochemistry

Human myelin protein P2: From crystallography to time-lapse membrane imaging and neuropathy-associated variants

M. Uusitalo, M. B. Klenow, S. Laulumaa, M. P. Blakeley, A. C. Simonsen, S. Ruskamo, P. Kursula

This study investigates the structural and functional properties of P2 variants associated with Charcot-Marie-Tooth disease using crystallography, spectroscopy, and imaging techniques.

bioRxiv · Apr 15, 2021Biochemistry

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

Molecular structure and function of myelin protein P0 in membrane stacking

A. Raasakka, S. Ruskamo, J. Kowal, H. Han, A. Baumann, M. Myllykoski, A. Fasano, R. Rossano, P. Riccio, J. Buerck, A. S. Ulrich, H. Stahlberg, P. Kursula

This study characterizes the molecular structure and function of myelin protein P0, showing how its extracellular domains stack lipid membranes and stabilize the intraperiod line in peripheral myelin.

bioRxiv · Aug 19, 2018Biochemistry