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Stefan Vetter

Research Assistant Professor
5A Sudro Hall
Phone: 701.231.5281
Fax: 701.231.8333
Stefan.Vetter@ndsu.edu

Education:

1994 - M.S. Chemistry (Dipl-Chemiker), Technische Universität Braunschweig, Germany,
1998 - Ph.D. Biochemistry, Swiss Federal Institute of Technology (Dr. sc. ETH), Switzerland Ph.D.,

Positions:

1998-1999 - Torrey Pines Institute of Molecular Studies, San Diego, SNF Postdoctoral Research Fellow, Combinatorial Chemistry
1999-2005 - The Scripps Research Institute, La Jolla, Research Associate, Molecular and Structural Biology
2005-2009 - Florida Atlantic University, Boca Raton, Assistant Professor, Biochemistry
2010 - present - North Dakota State University, Assistant Professor, Pharmaceutical Sciences

Research Interest

Activation of the receptor for advanced glycation endproducts (RAGE) is believed to be critically involved in diabetic complications, neurodegerative disorders, and several cancers by supporting tissue inflammation. RAGE can be activated by several structurally unrelated ligands including S100 proteins, amyloid forming peptides, and advanced glycation endproducts. We are working on understanding the ligand binding properties of RAGE using biophysical and biochemical methods. We are also interested in discovering and developing small molecules and peptides that can modulate RAGE activation.

Recent Publications:

Indurthi VS, Leclerc E, Vetter SW, Calorimetric investigation of diclofenac drug binding to a panel of moderately glycated serum albumins, Eur J Pharm Sci 59 (2014) 158-168 

Otvos L Jr., Vetter SW, Koladia M, Knappe D, Schmidt R, Ostorhazi E,  Kovalszky I, Bionda N, Cudic P, Surmacz E, Wade JD, Hoffmann R, The designer leptin antagonist peptide Allo-aca compensates for short serum half-life with very tight binding to the receptor, Amino Acids 46 (2014) 873-882 

 Meghnani V, Wagh A, Indurthi VS, Koladia M, Vetter SW, Law B, Leclerc E, The Receptor for Advanced Glycation End Products influences the expression of its S100 protein ligands in melanoma tumors, Int J Biochem Cell Biol 57 (2014) 54-62 

 Meghnani V, Vetter SW, Leclerc E, RAGE overexpression confers a metastatic phenotype to the WM115 human primary melanoma cell line, Biochim Biophys Acta 1842 (2014) 1017-1027 

Vetter SW, Phage Display Selection of Peptides that Target Calcium Binding Proteins, Methods Mol. Biol. 963 (2013) 215-235 

Indurthi VS, Leclerc E, Vetter SW, Interaction Between Glycated Serum Albumin and AGE-Receptors Depends on Structural Changes and the Glycation Reagent, Arch. Biochem. Biophys. 528 (2012) 185-196 

Vetter SW, Indurthi VS, Moderate glycation of serum albumin affects folding, stability, and ligand binding, Clin Chim Acta 412 (2011) 2105-2116 

Leclerc E, Sturchler E, Vetter SW, The S100B/RAGE Axis in Alzheimer's Disease, Cardiovasc Psychiatry Neurol 2010 (2010) 539-581. 

Vetter SW, Terentis A, Osborn RL, Dawson JH, Goodin DB; Replacement of the axial histidine heme ligand with cysteine in nitrophorin I: Spectroscopic and crystallographic characterization; J. Biol. Inorg. Chem. (2009), 14(2)(2009), 179-191

Leclerc E, Fritz G, Vetter SW, Heizmann CW; Binding of S100 proteins to RAGE: An update; Biochim. Biophys. Acta. (2009), 1793, 993-1007

Leclerc E, Sturchler E, Vetter SW, Heizmann CW; Crosstalk between calcium, amyloid beta and the receptor for advanced glycation endproducts in Alzheimer’s disease.  Reviews in the Neurosciences, (2009), 20, 95-110

Leclerc E, Heizmann CW, Vetter SW, RAGE and S100 Protein Transcription Levels are Highly Variable in Human Melanoma Tumors and Cells. General Physiol. Biophys.  (2009), 28, F65-75


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North Dakota State University
Phone: +1 (701) 231-7661 / Fax: (701) 231-8333
Campus address: Sudro Hall 116
Physical/delivery address: 1401 Albrecht Blvd, Fargo, ND 58102
Mailing address: NDSU Dept. 2665 / PO Box 6050 / Fargo, ND 58108-6050
Page manager: Pharmaceutical Sciences
Published by North Dakota State University

Last Updated: Monday, March 30, 2015 3:47:55 PM