PolySia: Eine neue bioidentische Gerüstsubstanz  
line decor
     ::  GESAMTPROJEKT      
line decor

Enzymatische Herstellung

  • Keys, T.G., Fuchs, H.L., Galuska, S.P., Gerardy-Schahn, R., and Freiberger, F. (2013) A single amino acid toggles Escherischia coli polysialyltransferases between mono- and bifunctionality. Glycobiology., 23, 613-8. Highlight in Nature Chem Bio

  • Wolf, S., Warnecke, S., Ehrit, J., Freiberger, F., Gerardy-Schahn, R., and Meier, C. (2012) Chemical synthesis and enzymatic testing of CMP-sialic acid derivatives. Chembiochem., 13, 2605-15.

  • Galuska, S.P., Geyer, H., Mink, W., Kaese, P., Kuhnhardt, S., Schäfer, B., Mühlenhoff, M., Freiberger, F., Gerardy-Schahn, R., and Geyer, R. (2012) Glycomic strategy for efficient linkage analysis of di-, oligo- and polysialic acids. J. Proteomics., 75, 5266-78.

  • Keys, T.G., Freiberger, F., Ehrit, J., Krueger, J., Eggers, K., Buettner, F.F., and Gerardy-Schahn, R.(2012) A universal fluorescent acceptor for high-performance liquid chromatography analysis of pro- and eukaryotic polysialytransferases. Anal. Biochem., 427, 107-15.

  • Keys, T.G., Berger, M., and Gerardy-Schahn, R.(2012) A high-throughput screen for polysialytransferase activity. Anal. Biochem., 427, 60-68.

  • Chen, R., John, J., Rode, B., Hitzmann, B., Gerardy-Schahn, R., Kasper, C., and Scheper, T.(2011) Comparison of polysialic acid production in Escherischia coli K1 during batch cultivation and fed-batch cultivation applying two different control strategies. J. Biotechnol., 154, 222-9.

  • Galuska, S.P., Geyer, H., Weinhold, B., Kontou, M., Rohrich, R.C., Bernard, U., Gerardy-Schahn, R., Reutter, W., Münster-Kühnel, A., and Geyer, R. (2010) Quantification of nucleotide-activated sialic acids by a combination of reduction and fluorescent labeling. Anal. Chem., 82, 4591-8.

  • Schulz, E.-C., Dickmanns, A., Urlaub, H., Schmitt, A., Mühlenhoff, M., Stummeyer, K., Schwarzer, D., Gerardy-Schahn, R. and Ficner, R. (2010) Crystal structure of a novel intramolecular chaperone mediating triple ß-helix folding. Nat. Struct. Mol. Biol., 17, 210-5.

  • Schulz EC, Schwarzer D, Frank M, Stummeyer K, Mühlenhoff M, Dickmanns A, Gerardy-Schahn R*, Ficner R.* (2010). Structural basis for recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein endoNF. J. Mol. Biol., 397, 341-351.

  • Böhm, R., Freiberger, F., Stummeyer, K., Gerardy-Schahn, R., von Itzstein, M., and Haselhorst, T. (2010) Neisseria meningitides serogroup B polysialyltransferase: insights into substrate binding.. Chembiochem., 11, 170-4.

  • Schwarzer,D., Stummeyer,K., Haselhorst,T., Freiberger,F., Rode,B., Grove,M., Scheper,T., von Itzstein,M., Mühlenhoff,M., and Gerardy-Schahn,R. (2009). Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F. J. Biol. Chem., 284, 9465-9474.

  • Schulz, E.-C., Neumann, P., Gerardy-Schahn, R., Sheldrick, G.M., and Ficner, R. (2009) Crystal Structure Analysis of EndosialidaseNF at 0.98 Å Resolution. Acta Crystallogr. D Biol. Crystallogr., 66(Pt 2), 176-180.

  • Oltmann-Norden,I., Galuska,S.P., Hildebrandt,H., Geyer,R., Gerardy-Schahn,R., Geyer,H., and Mühlenhoff,M. (2008). Impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid synthesis during postnatal mouse brain development. J. Biol. Chem., 283, 1463-1471.

  • Galuska,S.P., Geyer,R., Gerardy-Schahn,R., Mühlenhoff,M., and Geyer,H. (2008). Enzyme-dependent variations in the polysialylation of the neural cell adhesion molecule (NCAM) in vivo. J. Biol. Chem., 283, 17-28.

  • Freiberger,F., Claus,H., Günzel,A., Oltmann-Norden,I., Vionnet,J., Mühlenhoff,M., Vogel,U., Vann,W.F., Gerardy-Schahn,R., and Stummeyer,K. (2007). Biochemical characterization of a Neisseria meningitidis polysialyltransferase reveals novel functional motifs in bacterial sialyltransferases. Mol. Microbiol., 65, 1258-1275.

  • Leiman,P.G., Battisti,A.J., Bowman,V.D., Stummeyer,K., Mühlenhoff,M., Gerardy-Schahn,R., Scholl,D., and Molineux,I.J. (2007). The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. J. Mol. Biol., 371, 836-849.

  • Haselhorst,T., Münster-Kühnel,A.K., Oschlies,M., Tiralongo,J., Gerardy-Schahn,R., and von Itzstein,M. (2007). Direct detection of ligand binding to Sepharose-immobilised protein using saturation transfer double difference (STDD) NMR spectroscopy. Biochem. Biophys. Res. Commun., 359, 866-870.

  • Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R., and Mühlenhoff,M. (2007). Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins. J. Biol. Chem., 282, 2821-2831.

  • Haselhorst,T., Stummeyer,K., Mühlenhoff,M., Schaper,W., Gerardy-Schahn,R., and von Itzstein,M. (2006). Endosialidase NF appears to bind polySia DP5 in a helical conformation. Chembiochem., 7, 1875-1877.

  • Stummeyer,K., Schwarzer,D., Claus,H., Vogel,U., Gerardy-Schahn,R., and Mühlenhoff,M. (2006). Evolution of bacteriophages infecting encapsulated bacteria: lessons from Escherichia coli K1-specific phages. Mol. Microbiol., 60, 1123-1135.

  • Stummeyer,K., Dickmanns,A., Mühlenhoff,M., Gerardy-Schahn,R., and Ficner,R. (2005). Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. Nat. Struct. Mol. Biol., 12, 90-96.


Gefördert durch die