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FEBS Letters|December 23, 2008
The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivityDaniel Agren, Robert Schnell, Gunter SchneiderActa Crystallographica. Section F, Structural Biology and Crystallization Communications|December 5, 2008
1.9 A structure of the signal receiver domain of the putative response regulator NarL from Mycobacterium tuberculosisRobert Schnell, Daniel Agren, Gunter SchneiderOptics Express|June 5, 2009
Arrays of vertical-cavity electroabsorption modulators for parallel signal processingQin Wang, Stéphane Junique, Daniel Agren, et al.The Journal of Biological Chemistry|September 19, 2008
Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteriaDaniel Agren, Robert Schnell, Wulf Oehlmann, et al.Journal of Molecular Biology|February 29, 2008
Three-dimensional structures of apo- and holo-L-alanine dehydrogenase from Mycobacterium tuberculosis reveal conformational changes upon coenzyme bindingDaniel Agren, Matthias Stehr, Catrine L Berthold, et al.Experimental Cell Research|January 6, 2009
WAFL, a new protein involved in regulation of early endocytic transport at the intersection of actin and microtubule dynamicsIng-Marie Viklund, Pontus Aspenström, Vannary Meas-Yedid, et al.Pageof 1