Bonnefond, L., P. Schellenberger, J. Basquin, G. Demangeat, C. Ritzenthaler, R. Chenevert, C. Balg, M. Frugier, J. Rudinger-Thirion, R. Giege, B. Lorber and C. Sauter: Exploiting Protein Engineering and Crystal Polymorphism for Successful X-ray Structure Determination. In: Crystal Growth & Design 11, 10, 4334-4343 (2011).
Buckle, A. M., M. A. Bate, S. Androulakis, M. Cinquanta, J. Basquin, F. Bonneau, D. K. Chatterjee, D. Cittaro, S. Graslund, A. Gruszka, R. Page, S. Suppmann, J. X. Wheeler, D. Agostini, M. Taussig, C. F. Taylor, S. P. Bottomley, A. Villaverde and A. de Marco: Recombinant protein quality evaluation: proposal for a minimal information standard. In: Standards in Genomic Sciences 5, 2, 195-197 (2011).
Malet, H., M. Topf, D. K. Clare, J. Ebert, F. Bonneau, J. Basquin, K. Drazkowska, R. Tomecki, A. Dziembowski, E. Conti, H. R. Saibil and E. Lorentzen: RNA channelling by the eukaryotic exosome. In: EMBO Reports 11, 12, 936-942 (2010).
Bonneau, F., J. Basquin, J. Ebert, E. Lorentzen and E. Conti: The Yeast Exosome Functions as a Macromolecular Cage to Channel RNA Substrates for Degradation. In: Cell 139, 3, 547-559 (2009).
Conti, E., F. Bonneau, J. Ebert, J. Basquin and E. Lorentzen: Molecular mechanisms of RNA degradation by the exosome. In: FEBS Journal 276, Suppl. 1, 37-38 (2009).
Lorentzen, E., J. Basquin and E. Conti: Structural organization of the RNA-degrading exosome. In: Current Opinion in Structural Biology 18, 6, 709-713 (2008).
Lorentzen, E., J. Basquin, R. Tomecki, A. Dziembowski and E. Conti: Structure of the active subunit of the yeast exosome core, Rrp44: Diverse modes of substrate recruitment in the RNase II nuclease family. In: MOLECULAR CELL 29, 6, 717-728 (2008).
Oddone, A., E. Lorentzen, J. Basquin, A. Gasch, V. Rybin, E. Conti and M. Sattler: Structural and biochemical characterization of the yeast exosome component Rrp40. In: EMBO Reports 8, 1, 63-69 (2007).
doi: 10.1038/sj.embor.7400856
Ennifar, E., J. Basquin, R. Birkenbihl and D. Suck: Purification, crystallization and preliminary X-ray diffraction studies of the archaeal virus resolvase SIRV2. In: Acta Crystallographica Section F-Structural Biology and Crystallization Communications 61, 507-509 (2005).
The Max Planck Society does not take any responsibility for the content of this export.