Dr. Anja Münster-Kühnel

 

Dr. rer. nat.

1.Staatsexamen Biologie/Chemie für Lehramt an Gymnasien

 

 

Geb. J3, Ebene 04, Raum 1291 (Büro) oder 1050 (Labor)

Tel.: +49(0)511/532-8245 (Büro) oder -9302 (Labor)

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

 

E-Mail: muenster.anja(at)mh-hannover.de

 

 

Research interests

 

- Identification and characterization of vertebrate CMP-sialic acid synthetases (CMAS)

Biological function of CMAS in the cell nucleus. Structure-function-relationships. Identification of inhibitors.

 

- Functional role of sialic acid

The role of sialic acids in kidney development and function. The role of sialic acids in vertebrate development.

 

 

Publications

 

Galuska SP, Geyer H, Weinhold B, Kontou M, Röhrich RC, Bernard U, Gerardy-Schahn R, Reutter W, Münster-Kühnel A, Geyer R. (2010) Quantification of nucleotide-activated sialic acids by a combination of reduction and fluorescent labeling. Anal Chem. 82(11):4591-8.

 

Oschlies M, Dickmanns A, Haselhorst T, Schaper W, Stummeyer K, Tiralongo J, Weinhold B, Gerardy-Schahn R, von Itzstein M, Ficner R, Münster-Kühnel AK. (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.

 

Hartlieb S, Günzel A, Gerardy-Schahn R, Münster-Kühnel AK, Kirschning A, Dräger G (2008) Chemoenzymatic synthesis of CMP-N-acetyl-7-fluoro-7-deoxy-neuraminic acid. Carbohydr Res. 343(12):2075-82.

 

Tiralongo J, Fujita A, Sato C, Kitajima K, Lehmann F, Oschlies M, Gerardy-Schahn R, Münster-Kühnel AK (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 AK, 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 MJ, Tiralongo J, Münster-Kühnel AK, 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.

 

 

Fujita A, Sato C, Münster-Kühnel AK, Gerardy-Schahn R, Kitajima K (2005) Development of a simple and efficient method for assaying cytidine monophosphate sialic acid synthetase activity using an enzymatic reduced nicotinamide adenine dinucleotide/oxidized nicotinamide adenine dinucleotide converting system. Anal Biochem 337(1):12-21.

 

 

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

 

Kean EL, Münster-Kühnel AK and Gerardy-Schahn R (2004): CMP-sialic acid synthetase of the nucleus. Biochim Biophys Acta. 1673:56-65.

 

Münster-Kühnel AK, Tiralongo J, Krapp S, Weinhold B, Ritz-Sedlacek V, Jacob U and Gerardy-Schahn R (2004): Structure and function of vertebrate CMP-sialic acid synthetases. Glycobiology. 14:43R-51R.

 

Krapp S, Münster-Kühnel AK, Kaiser JT, Huber R, Tiralongo J, Gerardy-Schahn R and Jacob U: The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase. J Mol Biol. 334:625-37 (2003).

 

Münster AK, Weinhold B, Gotza B, Mühlenhoff M, Frosch M, and Gerardy-Schahn R: Nuclear localization signal of murine CMP-Neu5Ac synthetase includes residues required for both nuclear targeting and enzymatic activity. J. Biol. Chem. 277:19688-19696 (2002).

 

Nakata D, Münster AK, Gerardy-Schahn R, Aoki N, Matsuda T, Kitajima K: Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates. Glycobiology, 11(8):685-692 (2001).

 

Münster AK, Eckhardt M, Potvin B, Mühlenhoff M, Stanley P, Gerardy-Schahn R: Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs. Proc. Natl. Acad. Sci. USA, 95:9140-9145 (1998).