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Preininger, Anita

Anita M. Preininger, Ph.D.
Research Assistant Professor
Department of  Pharmacology
Vanderbilt University Medical Center
RRB 444
2200 Pierce Avenue
Nashville, TN    37232

PhD, IGP/Pharmacology, Northwestern  University, 2003 (Evanston, IL)

Research Interests: 
GPCR signaling using biophysical approaches to study dynamics and function of G-protein activation.  In particular, we are interested in pursuing the role of myristoylation in receptor mediated G-protein activation, in an extension of earlier work suggesting the amino terminus may function as a myristoyl switch.

Preininger, AM, *Kaya, AI, Busenlehner, LS, Armstrong, RN and HE Hamm. Myristoylation alters conformation and dynamics of Galphai proteins. Biochemistry, 51:1911-24 (2012). *contributed equally

Van Eps, N, *Preininger, AM, Alexander, NS, Kaya, AI, Meier, SM, Meiler, J, Hamm HE and WL Hubbell. Interaction of a Galpha protein with an activated receptor opens the inter-domain interface. PNAS, 108; 9420-9424 (2011). *contributed equally

Kaya, AI, Thaker,TM, Preininger, AM, Iverson, TM, and HE Hamm. Efficient rhodopsin and transducin coupling depends on negatively-charged phospholipids. Biochemistry, 50: 3193-203 (2011).

Hamm, HE, Meier, SM, Liao, G, and AM Preininger*.  Trp fluorescence reveals an activation-dependent cation-pi intereaction in the Switch II region of Gai proteins.  Protein Science, 18:2326-2335 (2009). *Corresponding author.

*Holinstat, M, *Preininger, AM, Milne, SB,Hudson, WJ, Brown, HA and HE Hamm. Irreversible platelet activation requires PAR1-mediated signaling through phosphatidylinositol phosphates, Mol. Pharm,, 76: 30-313 (2009).  *Contributed equally to this work.
*Anita M. Preininger,  *Michael A. Funk, Scott M. Meier , William M. Oldham, Christopher A. Johnston, Suraj Adhikary, Adam Kimple, David P. Siderovski, Heidi E. Hamm and Tina M. Iverson, A helix dipole movement contributes to allosteric GDP release in Gαi1, Biochemistry, 48:2630 (2009).*Contributed equally to this work
Preininger, AM, Parello, J, Meier, SM, Liao, G and Hamm, HE. Receptor-mediated changes at the myristoylated amino terminus of Gai proteins, Biochemistry  47; 10281–10293 (2008).
Preininger, AM, Oldham, WM and Hamm, HE. Biophysical approaches to the study of G-protein structure and function, Chapter,  Signal Transduction in the Retina, Fliesler and Kisselev (ed), CRC Press, (1/24/08).
Brown, HA, Henage, LG, Preininger, AM., Xiang, Y and Exton, JH.  Biochemical analysis of Phospholipase D, Methods in Enzymology, Lipidomics and Bioactive Lipids, 434:49-87 (2007).
Oldham, W, Van Eps, N, Preininger, AM, Hubbell, WL, Hamm, HE. Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins.Oldham, PNAS, 104: 7927-7932 (2007).
Callender, H, Forrester, JS, Ivanova, P, Preininger, A, Milne, S and HA Brown, Quantification of diacylglycerol species from cellular extracts by ESI MS using a linear regression algorithm, Analytical Chemistry, 79:311, 2006.
A. M. Preininger, L. G. Henage, W. M. Oldham, E. J. Yoon, H. E. Hamm, and H. A. Brown, Direct Modulation of Phospholipase D Activity by Gbeta{gamma}, Molecular Pharmacology,  70: 311-318, 2006.
W.M.  Oldham, N. Van Eps, A.M. Preininger,  W.L. Hubbell and H.E. Hamm, Mechanism of the receptor-catalyzed activation of heterotrimeric  G proteins, in press, Nature Structural and Molecular Biology,  July 2006.
Blackmer, T., Larsen, E., Bartleson, C., Kowalchyk,  J., Yoon, E., Preininger, A.,Alford,  S., Hamm, H., Martin, T.  G-protein bg directly regulates SNARE protein  fusion machinery for secretory granule exocytosis, Nature NeuroscienceNature 8, 421-425, 2005.
Preininger,  A.M. and Hamm, H.E.  G protein signaling:  insights  from new structures.  Sci STKE, 2004,  Jan. 27.
Cabera-Vera, TM, Vanhauwe,  J., Thomas, T., Medkova, M., Preininger, A.,  Mazzoni, MR, Hamm, HE.  Insights into G protein structure,  function, and regulation. Endocrine  Reviews, 24 (6) 765, 2003, Dec. 24.
Preininger AM. Van Eps N. Yu NJ. Medkova  M. Hubbell WL. Hamm, HE. The myristoylated amino terminus of Galpha(i)(1) plays  a critical role in the structure and function of Galpha(i)(1) subunits in  solution. Biochemistry. 42(26):7931-41,  2003 Jul 8.


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