Research
Molecular Mechanism of RAGE Ligand Recognition:
The Receptor for Advanced Glycation Endproducts (RAGE) is a pattern recognizing cell surface protein and interacts with multiple ligands,
including advanced glycation endproducts, protein amyloids and S100 proteins. We are investigating the recognition of S100 proteins by RAGE on
the molecular level. We use biophysical and genetic engineering methods to define RAGE - S100 binding interfaces and develope probes to modulate
RAGE/S100 interactions.
Role of RAGE/S100 in Cellular Signaling:
RAGE emerges as a major receptor for secreted S100 proteins and many effects of extracellular S100 proteins are RAGE dependent. More than half
of the 21 currently known S100 proteins interact with RAGE and trigger specific cellular responses that can vary between cell types. We are interested
in defining the role of RAGE on the auto- and paracrine activity of S100 proteins screted by melamona cell. We have developed epitope specific antibodies
to probe RAGE / S100 signaling in cell based assays.
Protein Dephosphorylation:
Protein phosphorylation is a major mechanism of signal transduction in eukaryotic cells. Some bacterial and viral human pathogens encode protein phosphatases
in their genomes and seem to use these to overcome defense mechanisms of host cells. We are interested in defining structural and functional differences between
eukaryotic and prokaryotic protein phosphatases.
Recent Publications
Vetter SW., Terentis AC., Osborne RL., Dawson JH., Goodin DB.; Replacement of the axial heme ligand with cysteine in nitrophorine
1: spectroscopic and crystallographic characterization, Journal of Inorganic Biochemistry, (2008), in press (reprint)
Leclerc E., Vetter SW.; Conformational changes and development of proteinase K resistance in surface-immobilized PrP;
Archive of Virology, 153 (2008), 683-691
(reprint)
Brenk R., Vetter SW., Boyce SE., Goodin DB., Stoichet BK.; Probing molecular docking in a charged model binding site;
Journal of Molecular Biology , 357 (2006), 1449-1470
(reprint)
Vetter SW., Leclerc E.; Novel aspects of calmodulin target recognition and activation; European Journal of Biochemistry, 270
(2003), 404-414 (reprint)
Vetter SW., Zhang ZY.; Combinatorial chemistry and peptide library methods to characterize protein phosphatases; Methods in Enzymology,
366 (2003), 260-282 (reprint)
Vetter SW., Zhang ZY.; Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial
library methods; Current Protein and Peptide Science, 3 (2002), 365-397
(reprint)
Vetter, S.W. and Leclerc, E. (2001), Eur. J. Biochem. , 268, 1-9. Phosphorylation of serine residues affects the conformation of
the calmodulin binding domain of human protein 4.1.
Vetter SW., Keng YF., Lawrence DS., Zhang ZY.,; Assessment of protein-tyrosine phosphatase 1B substrate specificity using "inverse
alanine scanning"; Journal of Biological Biology ; 275 (2000), 2265-2268
(reprint)
Sarimiento M., Puius YA., Vetter SW., Keng YF., Wu L., Zhao Y., Lawrence DS., Almo SC., Zhang ZY.; Structural basis for pplasticity in
protein tyrosine phosphatase 1B substrate recognition; Biochemistry, 39 (2000), 8171-8179
(reprint)
Vetter, SW. ; Proteinchemie: What's up?; Biospektrum, 6 (2000), 346
Leclerc E., Corti C., Schmid H., Vetter S., James P., Carafoli E.; Serine /threonine phosphorylation of calmodulin modulates its interaction with
the binding domains of targetr enzymes; Biochemical Journal ;344 (1999), 403-411
(reprint)
Lehmann E., Zenobi R., Vetter S.; Matrix-assisted laser desorption/ionization mass spectra reflect solution-phase zinc finger peptide complexation;
Journal of the American Society for Mass Spectrometry; 10 (1999); 27-34
(reprint)
Vetter S.; High-affinity non-inhibitory ligands for alkaline phosphatase revealed from a restricted heptapeptide library. In: Epton R (Ed)
Solid Phase Synth. Comb. Libr. (1999) Mayflower Sci. Ltd, Kingswingord, UK, pp 407-410
Vetter S., Schmid H.; High affinity binding peptides for phosphatase. In: Tam JP, Kaumaya PP (Eds) Pept. Proc. Am. Pept. Symp . 15th.
(1999) Kluwer, Dordrecht, NL, pp 71-72
Schmid H, Hoving S, Vetter S., Vorherr T, Carafoli E (1999) Synthesis and purification of unphosphorylated and phosphorylated phospholamban.
In: Tam JP, Kaumaya PP (Eds) Pept. Proc. Am. Pept. Symp. 15th. Kluwer, Dordrecht, NL, pp 709-710
Leclerc, E., Corti, C., Schmidt, H., Vetter, S., James, P. and Carafoli, E ., (1999), Biochemical J. 344, 403-411.
Serine/threonine phosphorylation of calmodulin modulates its interaction with the binding domains of target enzymes.
(reprint)
Leclerc E., Vetter S.; Characterization of a calcium-dependent calmodulin-binding domain in the 135-kD human protein 4.1 isoform;
European Journal of Biochemistry; 258 (1998), 567-571 (reprint)
Vetter S.; Direct synthesis of di-and trimethoxybenzyl thiols from the coressponding alcoholp; Synthetic Communications; 28 (1998),
3219-3223 (reprint)
Leclerc, E. and Vetter, S.(1998) Eur. J. Biochem. 258, 567-571. Characterization of a calcium-Dependent Calmodulin Binding
Domain in the 135 kD human Protein 4.1 isoform. (reprint)
Vetter S., Bayer EA., Wilchek M.; Avidin can be forced to adopt catalytic activity; Journal of the American Chemical Society ; 116 (1994),
9369-9370 (reprint)
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