Sutinen, Aleksi

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

Sutinen, A., Nguyen, G. T. T., Raasakka, A., Muruganandam, G., Loris, R., Ylikallio, E., Tyynismaa, H., Bartesaghi, L., Ruskamo, S., & Kursula, P. (2022) · FEBS Open Bio

Hereditary Neurological DisordersPeripheral Neuropathies and Disorders

Cited by 13

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

Sutinen, A., Nguyen, G. T. T., Raasakka, A., Muruganandam, G., Loris, R., Ylikallio, E., Tyynismaa, H., Bartesaghi, L., Ruskamo, S., & Kursula, P. (2022) · FEBS Open Bio

Hereditary Neurological DisordersPeripheral Neuropathies and Disorders

Cited by 13

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

Sutinen, A., Paffenholz, D., Nguyen, G. T. T., Ruskamo, S., Torda, A. E., & Kursula, P. (2023) · PLOS ONE

Hereditary Neurological DisordersProtein Structure and Dynamics

Cited by 8

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

Krokengen, O. C., Touma, C., Mularski, A., Sutinen, A., Dunkel, R., Ytterdal, M., Raasakka, A., Mertens, H. D. T., Simonsen, A. C., & Kursula, P. (2024) · Biochimica et Biophysica Acta (BBA) - Biomembranes

Lipid Membrane Structure and BehaviorHereditary Neurological Disorders

Cited by 7

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

Krokengen, O. C., Touma, C., Mularski, A., Sutinen, A., Dunkel, R., Ytterdal, M., Raasakka, A., Mertens, H. D. T., Simonsen, A. C., & Kursula, P. (2024) · Biochimica et Biophysica Acta (BBA) - Biomembranes

Lipid Membrane Structure and BehaviorHereditary Neurological Disorders

Cited by 7

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

Sutinen, A., Jones, N. C., Hoffmann, S. V., Ruskamo, S., & Kursula, P. (2023) · Biophysical Chemistry

Protein Structure and DynamicsMitochondrial Function and Pathology

Cited by 3

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

Sutinen, A., Jones, N. C., Hoffmann, S. V., Ruskamo, S., & Kursula, P. (2023) · Biophysical Chemistry

Protein Structure and DynamicsMitochondrial Function and Pathology

Cited by 3

Nanobodies against the myelin enzyme CNPase as tools for structural and functional studies

Markusson, S., Raasakka, A., Schröder, M., Sograte‐Idrissi, S., Rahimi, A. M., Asadpour, O., Körner, H., Lodygin, D., Eichel‐Vogel, M. A., Chowdhury, R., et al. (2025) · Journal of Neurochemistry

Phosphodiesterase function and regulationMonoclonal and Polyclonal Antibodies Research

Cited by 1

Nanobodies against the myelin enzyme CNPase as tools for structural and functional studies

Markusson, S., Raasakka, A., Schröder, M., Sograte-Idrissi, S., Rahimi, A. M., Asadpour, O., Körner, H., Lodygin, D., Eichel-Vogel, M. A., Chowdhury, R., et al. (2024) · Journal of Neurochemistry

Phosphodiesterase function and regulationMonoclonal and Polyclonal Antibodies Research

Cited by 1

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

Sutinen, A., Paffenholz, D., Nguyen, G. T. T., Ruskamo, S., Torda, A. E., & Kursula, P. (2022) · bioRxiv (Cold Spring Harbor Laboratory)

Hereditary Neurological DisordersProtein Structure and Dynamics

Cited by 0