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Juha Vahokoski

Researcher
  1. 4.Ruskamo S, Chukhlieb M, Vahokoski J, Bhargav SP, Liang F, Kursula I & Kursula P (2012) Juxtanodin is an intrinsically disordered F-actin binding protein. Sci Rep 2: 899.

  2. 5.Esch D, Vahokoski J, Groves MR, Pogenberg V, Cojocaru V, vom Bruch H, Han D, Dexler HCA, Araúzo-Bravo MJ, Ng CKL, Jauch R, Wilmanns M, Schöler HR (2013) A unique Oct4 interface is crucial for reprogramming to pluripotency. Nat Cell Biol 15: 295-301.

  3. 6.Bhargav SP, Vahokoski J, Kumpula EP & Kursula I (2013) Crystallization and preliminary structural characterization of the two actin isoforms of the malaria parasite. Acta Cryst F 69: 1171-1176.

  4. 7.Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Muñico Martinez S, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C & Kursula I (2014) Structural differences explain diverse functions of Plasmodium actins. PLoS Pathog 10: e1004091.

  5. 8.Bhargav SP, Vahokoski J, Kallio JP, Torda AE, Kursula P & Kursula I (2015) Two independently folding units of Plasmodium profilin suggest evolution via gene fusion. Cell Mol Life Sci 72: 4193-4203.

  6. 9.Green JL, Wall RJ, Vahokoski J, Yusuf NA, Ridzuan MAM, Stanway RR, Stock J, Knuepfer E, Brady D, Martin SR, Howell SA, Pires IP, Moon RW, Molloy JE, Kursula I, Tewari R & Holder AA (2017) Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility. J Biol Chem 292: 17857-17875.

  7. 10.Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I & Raunser S (2017) Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proc Natl Acad Sci 114: 10636-10641. 

  8. 11.Kumpula EP, Pires IP, Lasiwa D, Piirainen H, Bergmann U, Vahokoski J & Kursula I (2017) Apicomplexan actin polymerization depends on nucleation. Sci Rep 7: 12137.

  9. 12.Pino P, Caldelari R, Mukherjee B, Vahokoski J, Klages N, Maco B, Collins CR, Kursula I, Blackman MJ, Heussler V, Brochet M & Soldati-Favre D (2017) A multi-stage antiplasmodial targets the plasmepsins IX and X essential for invasion and egress. Science 358: 522-528.

Journal articles
  • Green, Judith L.; Wall, Richard J. Wall; Vahokoski, Juha; Yusuf, Noor A.; Ridzuan, Mohd A. Mohd; Stanway, Rebekka R.; Stock, Jessica; Knuepfer, Ellen; Brady, Declan; Martin, Stephen R.; Howell, Steven A.; Pires, Isa P.; Moon, Robert W.; Molloy, Justin E.; Kursula, Inari; Tewari, Rita; Holder, Anthony A. 2017. Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility. Journal of Biological Chemistry. 292: 17857-17875. doi: 10.1074/jbc.M117.802769
  • Kumpula, Esa-Pekka; Pires, Isa; Lasiwa, Davki; Piirainen, Henni; Bergmann, Ulrich; Vahokoski, Juha; Kursula, Inari. 2017. Apicomplexan actin polymerization depends on nucleation. Scientific Reports. 7. doi: 10.1038/s41598-017-11330-w
  • Pino, Paco; Caldelari, Reto; Mukerhjee, Budhaditya; Vahokoski, Juha; Klages, Natacha; Maco, Bohumil; Collins, Christine R.; Blackman, Michael J.; Kursula, Inari; Heussler, Volker; Brochet, Mathieu; Soldati-Favre, Dominique. 2017. A multistage antimalarial targets the plasmepsins IX and X essential for invasion and egress. Science. 358: 522-528. doi: 10.1126/science.aaf8675
  • Pospich, Sabrina; Kumpula, Esa-Pekka; Von Der Ecken, Julian; Vahokoski, Juha; Kursula, Inari; Raunser, Stefan. 2017. Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proceedings of the National Academy of Sciences of the United States of America. 114: 10636-10641. doi: 10.1073/pnas.1707506114
  • Simon, Bertrand; Huart, Anne-Sophie; Temmerman, Koen; Vahokoski, Juha; Mertens, Haydyn D.T.; Komadina, Dana; Hoffmann, Jan-Erik; Yumerefendi, Hayretin; Svergun, Dmitri I.; Kursula, Petri; Schultz, Carsten; McCarthy, Andrew A.; Hart, Darren J.; Wilmanns, Matthias. 2016. Death-associated protein kinase activity is regulated by coupled calcium/calmodulin binding to two distinct sites. Structure. 24: 851-861. doi: 10.1016/j.str.2016.03.020

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