Research in our laboratory focuses on the structure and function of neurotransmitter receptors, in particular glutamate receptors. These receptors are the primary excitatory neurotransmitter receptors in the central nervous system and are implicated in the molecular basis of learning and memory as well as a variety of neurological disorders. The laboratory uses a variety of methods including NMR spectroscopy, X-ray crystallography, small-angle X-ray scattering, isothermal titration calorimetry, and electrophysiology to study the biophysics of drug binding. These multiple approaches provide a view of the binding site that includes both the structure and dynamics. This provides more detailed information for further drug development and understanding of the mechanism channel activation. Ongoing collaborative projects include work on protein recognition factors in leptospirosis, and experimental drugs for the treatment of Alzheimer’s disease.

• Ph D, Biochemistry, Vanderbilt University, 1979
• MA, Psychology, University of Alabama, 1975
• BS, Chemistry, University of Alabama, 1974

• 1998-Present, Professor, Department of Molecular Medicine, Cornell University
• 1993-1998, Professor of Pharmacology, Department of Pharmacology, Cornell University
• 1994-1995, Visiting Professor, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School
• 1987-1993, Associate Professor of Pharmacology, Department of Pharmacology, Cornell University
• 1988-1989, Visiting Professor, Inorganic Chemistry Laboratory, University of Oxford
• 1981-1987, Assistant Professor, Department of Pharmacology, Cornell University
• 1979-1981, Postdoctoral Fellow, Muscular Dystrophy Association and Collège de France
• 1979, Postdoctoral Fellow, Department of Anatomy, Vanderbilt University
• 1976-1979, Predoctoral Fellow of the NIMH and NIH, Department of Biochemistry, Vanderbilt University
• 1975, Predoctoral Fellow of the NIMH , Department of Biochemistry, Vanderbilt University

1. Ptak, C., Hsieh, C., Weiland, G., Oswald, R. (2014) Role of stoichiometry in the dimer-stabilizing effect of AMPA receptor allosteric modulators. 9:128-133.
2. Jenkins, M., Wells, G., Bachman, J., Snyder, J., Jenkins, A., Huganir, R., Oswald, R., Traynelis, S. (2014) Regulation of GluA1 AMPA receptor function by protein kinase C at serine-818 and threonine-840. 85:618-629.
3. Ahmed, A., Ptak, C., Fenwick, M., Hsieh, C., Weiland, G., Oswald, R. (2013) Dynamics of cleft closure of the GluA2 ligand binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange. 288:27658-27666.
4. Holley, S., Ahmed, A., Srinivasan, J., Murthy, S., Weiland, G., Oswald, R., Nowak, L. (2012) The loss of an electrostatic contact unique to AMPA receptor ligand binding domain 2 slows channel activation. 51:4015-4027.

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• Alfred P. Sloan Fellow, Cornell University
• Alumni Honors Scholarship, University of Alabama
• Fullbright Fellowship, University of Oxford
• Graduate Council Fellowship, University of Alabama
• Guggenheim Fellowship, Cornell University/Harvard University
• Harold S. Vanderbilt Scholar, Vanderbilt University
• Phi Beta Kappa, University of Alabama