Gregg B. Wells

Gregg B. Wells

Associate Professor

Department of Molecular and Cellular Medicine
Room 204 Reynolds Medical Building
College Station, TX   77843

Education and Post-Graduate Training

Dr. Gregg B. Wells received his BA (with distinction) in chemistry from Northwestern University in 1981. He earned his PhD in biophysical and theoretical biology from the University of Chicago Pritzker School of Medicine in 1987 and his MD was awarded from the University of Chicago Pritzker School of Medicine in 1989. From 1989 to 1996 he completed his residency in anatomic pathology and fellowship in neuropathology at the Hospital of the University of Pennsylvania. He is certified in anatomic pathology with special certification in neuropathology by the American Board of Pathology. He joined the faculty at the Texas A&M University Health Science Center in 1999.

Research Interests

The general theme of the research in my laboratory is the role of protein structure in disease, particularly in neurological disease. One area of study is the structure and function of the superfamily of neurotransmitter-gated ion channels that includes nicotinic acetylcholine, serotonin 5HT3, glycine, and GABAA receptors. Members of this superfamily are involved in drug addiction and alcoholism, neurodegenerative diseases such as Alzheimer disease and Parkinson disease, genetic forms of epilepsy, and neuropsychiatric disorders such as schizophrenia and depression. We are developing new approaches to elucidating the molecular structures of these ion channels from animals and bacteria. Cyclic nucleotide gated channels (CNGCs) are a second area of study. We are interpreting their electrophysiological properties in terms of structure and thermodynamics. Hearing is a third area of study. We are using computational models of calcium and potassium ion channels and mechanotransduction to explain electrophysiological function of cochlear hair cells. Fourth, analysis of genomes and tissue-specific transcriptomes of electrogenic animals (e.g., electric fish) is expected reveal new aspects of lifecycles of ion channels. Explaining neurological diseases in terms of protein structure is a theme linking our neuroscience research with neuropathology, my medical specialty.

Graduate training is available through the Medical Science PhD program (College of Medicine), through the MD/PhD program (College of Medicine) and other programs that our faculty are affiliated with joint research.


  • Wells, GB and Tanaka, JC. (1997) "Ion Selectivity Predictions from a Two Site Permeation Model for the Cyclic Nucleotide-Gated Channel of Retinal Rod Cells." Biophysical Journal. 72, 127-140. PMID: 8994598.
  • Wells, GB, Anand, R, Wang, F and Lindstrom, J. (1998) "Water-soluble Nicotinic Acetylcholine Receptor Formed by alpha7 Subunit Extracellular Domains." Journal of Biological Chemistry. 273, 964-973. PMID: 9422757.
  • Wells, G. B., Lin, L., Jeanclos, E. M., and Anand, R. (2001) “Assembly and Ligand Binding Properties of the Water-Soluble Extracellular Domains of the Glutamate Receptor GluR1 Subunit.” Journal of Biological Chemistry. 276, 3031-3036. PMID: 11076939.
  • Person, A.M., Bills, K.L., Liu, H., Botting, S.K., Lindstrom, J., and Wells, GB. (2005) Extracellular Domain Nicotinic Acetylcholine Receptors formed by Alpha4 and Beta2 Subunits. J. Biol. Chem. 280, 39990-40002. PMID: 1617463.
  • Farris HE, Wells GB, and Ricci AJ. (2006) "Steady-State Adaptation of Mechanotransduction Modulates the Resting Potential of Auditory Hair Cells, Providing an Assay for Endolymph [Ca2+]." Journal of Neuroscience. 26, 12526-12536. PMID: 17135414.
  • Wells, G.B. (2008) Structural answers and persistent questions about how nicotinic receptors work. Front Biosci. 13:5479-5510. Review. PMID: 18508600.
  • Person, A.M. and Wells, G.B. (2011) Characterizing low affinity epibatidine binding to α4β2 nicotinic acetylcholine receptors with ligand depletion and nonspecific binding. BMC Biophysics 4: 19. PMID: 22112852.
  • Amici SA, McKay SB, Wells GB, Robson JI, Nasir M, Ponath G, Anand R. (2012), "A highly conserved cytoplasmic cysteine residue in the α4 nicotinic acetylcholine receptor is palmitoylated and regulates protein expression, Journal of Biological Chemistry 287: 23119-23127. PMID: 22593584.
  • Gallant JR, Traeger LL, Volkening JD, Moffett H, Chen P-H, Novina CD, Phillips GN Jr, Anand R, Wells GB, Pinch M, Güth R, Unguez GA, Albert JS, Zakon HH, Samanta MP, and Sussman MR (2014), "Genomic basis for the convergent evolution of electric organs," Science 344: 1522-1525. PMID: 24970089.