- Lauren E. Ball, Ph.D.
- Joe B. Blumer, Ph.D.
- Warren Davis Jr., Ph.D.
- Scott Eblen, Ph.D.
- Perry V. Halushka, M.D., Ph.D.
- John D. Hildebrandt, Ph.D.
- Jennifer S. Isaacs, Ph.D.
- Daniel R. Knapp, Ph.D.
- David T. Kurtz, Ph.D.
- Stephen M. Lanier, Ph.D.
- Carola A. Neumann, M.D.
- John E. Oatis, Ph.D.
- Steven A. Rosenzweig, Ph.D.
- Kevin L. Schey, Ph.D.
- Kenneth D. Tew, Ph.D., D.Sc.
- Thomas Walle, Ph.D.
- Michael J. Wargovich, Ph.D.
- Jerry G. Webb, Ph.D.
John D. Hildebrandt, Ph.D.Professor
Cell and Molecular PharmacologyPh.D., University of Iowa, 1978
hildebjd@musc.edu
Tel: 843-792-3209
Fax: 843-792-2475Signal Transduction by GTP-binding Proteins
The Hildebrandt laboratory studies the structure and function of the heterotrimeric G proteins involved in mediating the effects of hormones and neurotransmitters on intracellular signaling pathways. We have particular interests in understanding the molecular mechanisms generating G protein subunit diversity and the relationship of this diversity to cellular regulation by multiple extracellular signals.
Selected Publications | Additional Publications
Hildebrandt JD. Bring your own G-Protein (Relates to article by Zhang, et al. FastForward Jan 17, 2006.) Mol Pharmacol Jan 25, 2006. [Epub ahead of print.]
Yang W and Hildebrandt JD. Genomic analysis of G protein gamma subunits in human and mouse - The relationship between conserved gene structure and G protein betagamma dimer formation. Cell Signal 18(2):194-201, 2006. [Epub 2005 Jul 11.]
Cook LA, Schey KL, Wilcox MD, Dingus J, Ettling R, Nelson T, Knapp DR and Hildebrandt JD. Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity. Mol Cell Proteomics, Dec 6, 2005 [Epub ahead of print.]
Dingus J, Wells CA, Campbell L, Cleator JH, Robinson K and Hildebrandt JD. G Protein betagamma dimer formation: Gbeta and Ggamma differentially determine efficiency of in vitro dimer formation. Biochemistry 44(35):11882-90, 2005.
Yang W, White B, Spicer EK, Weinstein BL and Hildebrandt JD. Complex haplotype structure of the human GNAS gene identifies a recombination hotspot centred on a single nucleotide polymorphism widely used in association studies. Pharmacogenetics 14(11):741-7, 2004.
Cleator JH, Ravenell R, Kurtz DT and Hildebrandt JD. A dominant negative Galphas mutant that prevents thyroid-stimulating hormone receptor activation of cAMP production and inositol 1,4,5-trisphosphate turnover: competition by different G proteins for activation by a common receptor. J Biol Chem 279(35):36601-7, 2004. (Epub 2004 Jul 02.)
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