January 9, 2016

Publications

Doncic A, Atay O, Valk E, Grande A, Bush A, Vasen G, Colman-Lerner A, Loog M, Skotheim JM. (2015) Compartmentalization of a bistable switch enables memory to cross a feedback-driven transition. Cell. Mar 12;160(6):1182-95.

Bhaduri S, Valk E, Winters MJ, Gruessner B, Loog M, Pryciak PM. (2015) A docking interface in the cyclin Cln2 promotes multi-site phosphorylation of substrates and timely cell-cycle entry. Curr Biol. Feb 2;25(3):316-25.

Valk E, Venta R, Ord M, Faustova I, Kõivomägi M, Loog M. (2014) Multistep phosphorylation systems: tunable components of biological signaling circuits. Mol Biol Cell. Nov 5;25(22):3456-60.

Kõivomägi M, Ord M, Iofik A, Valk E, Venta R, Faustova I, Kivi R, Balog ER, Rubin SM, Loog M. (2013) Multisite phosphorylation networks as signal processors for Cdk1. Nature Struct Mol Biol. 20(12), 1415-24.

McGrath DA, Balog ER, Kõivomägi M, Lucena R, Mai MV, Hirschi A, Kellogg DR, Loog M, Rubin SM. (2013) Cks confers specificity to phosphorylation-dependent CDK signaling pathways. Nature Struct Mol Biol. 20(12), 1407-14.

Venta R, Valk E, Kõivomägi M, Loog M. (2012) Double-negative feedback between S-phase cyclin-CDK and CKI generates abruptness in the G1/S switch. Front Physiol. Systems Biology 6(3), 459.

Kõivomägi, M., Valk, E., Venta, R., Iofik, A., Lepiku, M., Balog, E.R.M., Rubin, S.M., Morgan, D.O., and Loog, M. (2011). Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase. Nature, Oct 12. doi: 10.1038.

Kõivomägi, M., Valk, E., Venta, R., Iofik, A., Lepiku, M., Morgan, D., and Loog, M. (2011). Dynamics of Cdk1 substrate specificity during the cell cycle. Molecular Cell, 42(5), 610-23.

Avunie-Masala, R., Movshovich, N., Nissenkorn, Y., Gerson-Gurwitz, A., Fridman, V., Kõivomägi, M., Loog, M., Hoyt, A., Zaritsky, A., Gheber, L. (2011). Phospho-regulation of Kinesin-5 function during anaphase spindle elongation. Journal of Cell Science, 124(6), 873 – 878.

Loog, M., and Morgan, D.O. (2005). Cyclin specificity in the phosphorylation of cyclin-dependent kinase substrates. Nature, 434(7029), 104 – 108.