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Raasakka A., Ruskamo S., Kowal J., Han H., Baumann A., Myllykoski M., Fasano A., Rossano R., Riccio P., Bürck J., Ulrich A.S., Stahlberg H. & Kursula P. (2018)ÌýMolecular structure and function of myelin protein P0 in membrane stacking. Sci. Rep., in press.

Laulumaa S., Nieminen T., Raasakka A., Krokengen O.C., Safaryan A., Hallin E.I., Brysbaert G., Lensink M.F., Ruskamo S., Vattulainen I. & Kursula P. (2018)ÌýStructure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins. BMC Struct. Biol. 18:8.

Ruskamo S., Nieminen T., Kristiansen C.K., Vatne G.H., Baumann A., Hallin E.I., Raasakka A., Joensuu P., Bergmann U., Vattulainen I. & Kursula P. (2017)ÌýMolecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2. Sci. Rep., in press.

Raasakka A., Ruskamo S., Kowal J., Barker R., Baumann A., Martel A., Tuusa J., Myllykoski M., Bürck J., Ulrich A.S., Stahlberg H. & Kursula P. (2017) Membrane association landscape of myelin basic protein portrays formationÌýof the myelin major dense line. Sci. Rep., in press.Ìý

Snaidero N., Velte C., Myllykoski M., Raasakka A., Ignatev A., Werner H.B.,ÌýErwig M.S.,ÌýMöbius W., Kursula P., Nave K.A. &ÌýSimons M.Ìý(2017) Antagonistic functions of MBP and CNP establish cytosolic channels in CNS myelin. Cell Rep. 18:314-323.Ìý

Raasakka A., Myllykoski M., Laulumaa S., Lehtimäki M., Härtlein M., Moulin M., Kursula I. & Kursula P. (2015) Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase. Sci. Rep. 5:16520.Ìý

Laulumaa S., Nieminen T., Lehtimäki M., Aggarwal S., Simons M., Koza M.M., Vattulainen I., Kursula P. & Natali F. (2015) Dynamics of the peripheral membrane protein P2 from human myelin measured by neutron scattering - a comparison between wild-type protein and a hinge mutant. PLoS ONE 10:e0128954.

Han H. & Kursula P. (2015) The olfactomedin domain from gliomedin is a beta-propeller with unique structural properties. J. Biol. Chem. 290: 3612-3621.

Zenker J., Stettner M., Ruskamo S., Domènech-Estévez E., Baloui H., Médard J.-J., Verheijen M.H.G., Brouwers J.F., Kursula P., Kieseier B.C. & Chrast R. (2014) A role of peripheral myelin protein 2 in lipid homeostasis of myelinating Schwann cells. Glia 62: 1502-1512. 


Han H. & Kursula P. (2014) Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping. J. Biol. Chem. 289: 14121-14131.


Ruskamo S., Yadav R.P., Sharma S., Lehtimäki M., Laulumaa S., Aggarwal S., Simons M., Bürck J., Ulrich A.S., Juffer A.H., Kursula I. & Kursula P. (2014) Atomic-resolution view into structure-function relationships of the human myelin peripheral membrane protein P2. Acta Cryst. D 70: 165-176.


Knoll W., Peters J., Kursula P., Gerelli Y., Ollivier J., Demé B., Telling M., Kemner E. & Natali F. (2014) Structural and dynamical properties of reconstituted myelin sheaths by myelin proteins MBP and P2 studied by neutron scattering. Soft Matter 10: 519-529.

Myllykoski M., Baumgärtel P. & Kursula P. (2012) Conformations of peptides derived from myelin-specific proteins in membrane-mimetic conditions probed by synchrotron radiation CD spectroscopy. Amino Acids, 42: 1467-1474.


Suresh S., Wang C., Nanekar R., Kursula P. & Edwardson J.M. (2010) Myelin basic protein and myelin protein 2 act synergistically to cause stacking of lipid bilayers. Biochemistry 49: 3456-3463.


Majava V., Wang C., Myllykoski M., Kangas S.M., Kang S.U., Hayashi N., Baumgärtel P., Heape A.M., Lubec G. & Kursula P. (2010) Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. Amino Acids 39:59-71.


Hallin E.I., Eriksen M.S., Baryshnikov S., Nikolaienko O., Grødem S., Hosokawa T., Hayashi Y., Bramham C.R. &ÌýKursula P. (2018)ÌýStructure of monomeric full-length ARC sheds light on molecular flexibility, protein interactions, and functional modalities. J. Neurochem., in press.

Ponna S.K., Ruskamo S., Myllykoski M., Keller C., Boeckers T.M. & Kursula P. (2018) Structural basis for PDZ domain interactions in the post-synaptic density scaffolding protein Shank3. J. Neurochem. 145:449-463.

Brockmann S.J., Freischmidt A., Oeckl P., Müller K., Ponna S.K., Helferich A.M., Paone C., Reinders J., Kojer K., Orth M., Jokela M., Auranen M., Udd B., Hermann A., Danzer K.M., Lichtner P., Walther P., Ludolph A.C., Andersen P.M., Otto M.,ÌýKursula P., Just S. &ÌýWeishaupt J.H. (2018)ÌýCHCHD10 mutations p.R15L and p.G66V cause motoneuron disease by haploinsufficiency.ÌýHum. Mol. Genet. 27:706-715.

Ponna S.K., Myllykoski M., Boeckers T.M. & Kursula P. (2017)ÌýStructure of an unconventional SH3 domain from the postsynaptic density protein Shank3 at ultrahigh resolution. Biochem. Biophys. Res. Commun., in press

Piirainen H., Taura J., Kursula P., Ciruela F. & Jaakola V.-P. (2017)ÌýCalcium modulates calmodulin/α-actinin 1 interaction with and agonist-dependent internalization of the adenosine A2AÌýreceptor. BBA Mol. Cell Res. 1864:674-686.ÌýÌý

Myllykoski M., Baumann A., Hensley K. & Kursula P. (2017)ÌýCollapsin response mediator protein 2: high-resolution crystal structure sheds light on small-molecule binding, post-translational modifications, and conformational flexibility. Amino Acids, in press.ÌýDOI 10.1007/s00726-016-2376-z.Ìý

Bezem M.T., Baumann A., Skjærven L., Meyer R.,ÌýKursula P., Martinez A., Flydal M.I. (2016)ÌýStable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme.ÌýSci. Rep. 6:30390.

Ponna S.K., Myllykoski M., Boeckers T.M. & Kursula P. (2016)ÌýSub-atomic resolution X-ray diffraction of the SH3 domain from the post-synaptic density protein Shank3. bioRxiv; DOI:Ìý.

Freischmidt A., Wieland T., Richter B., Ruf W., Schaeffer V., Müller K., Marroquin N., Nordin F., Hübers A., Weydt P., Pinto S., Press R., Millecamps S., Molko N., Bernard E., Desnuelle C., Soriani M.-H., Dorst J., Graf E., Nordström U., Feiler M.S., Putz S., Böckers T.M., Meyer T., Winkler A.S., Winkelman J., de Carvalho M., Thal D.R., Otto M., Brännström T., Volk A.E., Kursula P., Danzer K.M., Lichtner P., Dikic I., Meitinger T., Ludolph A.C., Strom T.M., Andersen P.M. & Weishaupt J.H. (2015) Haploinsufficiency of TBK1 causes familial amyotrophic lateral sclerosis and fronto-temporal dementia. Nature Neurosci. 18: 631-636.

Simon B., Huart A.-S., Temmerman K., Vahokoski J., Mertens H.D.T., Komadina D., Hoffmann J.-E., Yumerefendi H., Svergun D.I., Kursula P., Schultz C., McCarthy A.A., Hart D.J. & Wilmanns M. (2016) Death-associated protein kinase activity is regulated by coupled calcium/calmodulin binding to two distinct sites. Structure 24:851-861.

Patel A.K., Yadav R.P., Majava V., Kursula I. & Kursula P. (2011) Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase. J. Mol. Biol. 409: 369-383.


de Diego I., Kuper J., Bakalova N., Kursula P. & Wilmanns M. (2010) Molecular basis of the death associated protein kinase-calcium/calmodulin regulator complex. Science Signaling 3:ra6.


Raasakka A., Mahootchi E., Winge I., Luan W., Kursula P. & Haavik J. (2018) Structure of the mouse acidic amino acid decarboxylase GADL1. Acta Cryst. FÌý74:65-73.Ìý

Myllykoski M. & Kursula P. (2017)ÌýStructural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase. PLoS ONEÌý12:e0170355.Ìý

Koski K., Anantharajan J., Kursula P., Dhavala P., Murthy A.V., Bergmann U., Myllyharju J. & Wierenga R.K. (2017)ÌýAssembly of theÌýelongated collagen prolyl 4-hydroxylase α2β2ÌýheterotetramerÌýaround a central α2Ìýdimer. Biochem. J., 474:751-769.

Kouznetsova E., Kanno T., Karlberg T., Thorsell A.-G., Wisniewska M., Kursula P., Sjögren C. & Schüler H. (2016)ÌýSister chromatic cohesion establishment factor ESCO1 operates by substrate-assisted catalysis. Structure 24:789-796.

Bhargav S.P., Vahokoski J., Kallio J.P., Torda A., Kursula P. & Kursula I. (2015) Two independently folding units ofÌýPlasmodiumÌýprofilin suggest evolutionÌýviaÌýgene fusion. Cell. Mol. Life Sci. 72:4193-4203.Ìý

Onwukwe G.U., Kursula P., Koski M.K., Schmitz W. & Wierenga R.K. (2015) Human Δ3, Δ2-enoyl-CoA isomerase, type-2: a structural enzymology study on the catalytic role of its ACBP-domain and helix-10. FEBS J. 282: 746-768.

Kursula P. (2014) Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix. Acta Cryst. D 70: 24-30.


Anantharajan J., Koski M.K., Kursula P., Hieta R., Bergmann U., Myllyharju J. & Wierenga R.K. (2013) The unique structural motifs for substrate binding and dimerisation of the alpha subunit of collagen prolyl 4-hydroxylase. Structure 12: 2107-2118.


Forst A.H., Karlberg T., Herzog N., Thorsell A.-G., Gross A., Feijs K.L., Verheugd P., Kursula P., Nijmeijer B., Kremmer E., Kleine H., Ladurner A., Schüler H. & Lüscher B. (2013) Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains. Structure 21: 462-475.


Patton G.C., Stenmark P., Gollapalli D.R., Sevastik R., Kursula P., Flodin S., Schüler H., Swales C.T., Eklund H., Himo F., Nordlund P. & Hedstrom L. (2011) Cofactor mobility determines reaction outcome in the IMPDH amd GMPR (β-α)8 barrel enzymes. Nature Chem. Biol. 7: 950-958.


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