Dr. Melanie Sellmeier

 

geb. Oschlies

Dr. rer. nat.

Diplom-Biochemikerin

Post-Doc　

 

Geb. J3, Ebene 04, Raum 1240

Tel.: +49(0)511/532-8303

FAX: +49(0)511/532-8801

 

E-Mail: Oschlies.Melanie(at)mh-hannover.de

 

 

 

Research interests

 

CMP-Sialic acid synthetase (CMAS):

 - Biological function of CMAS in the cell nucleus.

 - X-ray crystallography of CMAS protein-domains.

 - Structure-function-relationships.

 - Identification of inhibitors.

 - Identification of interacting proteins.

 

 

Publications

 

Oschlies, M.; Dickmanns, A.; Haselhorst, T.; Schaper, W.; Stummeyer, K.; Tiralongo, J.; Weinhold, B.;　Gerardy-Schahn, R.; von Itzstein, M.; Ficner, R. ; Münster-Kühnel, A.-K., (2009) A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme. J. Mol. Biol. 393(1):83–97.　

 

Tiralongo, J.; Fujita, A.; Sato, C.; Kitajima, K.; Lehmann, F.; Oschlies, M.; Gerardy-Schahn, R.; Münster-Kühnel, A. K., (2007) The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme. Glycobiology 17(9):945-54.

 

Haselhorst, T.; Münster-Kühnel, A. K.; Oschlies, M.; Tiralongo, J.; Gerardy-Schahn, R.; 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(4):866-70.

 

Haselhorst, T.; Oschlies, M.; Abu-Izneid, T.; Kiefel, M. J.; Tiralongo, J.; Münster-Kühnel, A. K.; Gerardy-Schahn, R.; von Itzstein, M., (2006) A 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetase. Glycoconj J. 23(5-6):371-5.

 

Haselhorst. T.; Münster-Kühnel, A. K.; Stolz, A.; Oschlies, M.; Tiralongo, J.; Kitajima, K.; Gerardy-Schahn, R.; von Itzstein, M., (2005) Probing a CMP-Kdn synthetase by (1)H, (31)P, and STD NMR spectroscopy. Biochem Biophys Res Commun. 327(2):565-70.