Hrle, A., A. A. H. Su, J. Ebert, C. Benda, L. Randau and E. Conti: Structure and RNA-binding properties of the Type III-A CRISPR-associated protein Csm3. In: RNA Biology 10, 11, 1670-1678 (2013).
Jeyaprakash, A. A., A. Santamaria, U. Jayachandran, Y. W. Chan, C. Benda, E. A. Nigg and E. Conti: Structural and Functional Organization of the Ska Complex, a Key Component of the Kinetochore-Microtubule Interface. In: Molecular Cell 46, 3, 274-286 (2012).
Lin, T. C., L. Gombos, A. Neuner, D. Sebastian, J. V. Olsen, A. Hrle, C. Benda and E. Schiebel: Phosphorylation of the Yeast gamma-Tubulin Tub4 Regulates Microtubule Function. In: PLoS ONE 6, 5, [1]-[17], Seq. No.: e19700 (2011).
Macek, B., C. Benda, A. Jestel, K. Maskos, M. Mann and A. Messerschmidt: Phosphorylation of the human full-length protein kinase C iota. In: Journal of Proteome Research 7, 7, 2928-2935 (2008).
Messerschmidt, A., S. Macieira, M. Velarde, M. Badeker, C. Benda, A. Jestel, H. Brandstetter, T. Neuefeind and M. Blaesse: Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. In: Journal of Molecular Biology 352, 4, 918-931 (2005).
Benda, C., C. Scheufler, N. T. de Marsac and W. Gärtner: Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators. In: Biophysical Journal 87, 1, 476-487 (2004).
Benda, C., C. Scheufler, N. Tandeau de Marsac and W. Gärtner: Crystal Structures of Two Cyanobacterial Response Regulators in Apo- and Phosphorylated Form Reveal a Novel Dimerization Motif of Phytochrome-Associated Response Regulators. In: Biophysical Journal 87, 1, 476-487 (2004).
doi: 10.1529/biophysj.103.033696
Benda, C.: Studies on structure and dynamics of components of phytochrome-mediated light signalling in plants and bacteria.. Doktorarbeit, Ludwig-Maximilians-Universität, München (2003).
The Max Planck Society does not take any responsibility for the content of this export.