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Arthur Karlin, Ph.D. Higgins Professor of Biochemistry & Molecular Biophysics, Physiology & Cellular Biophysics, and Neurology Email: ak12@columbia.edu Tel: (212) 305-3973 Office: P&S 11-401 Fax: (212) 305-5594 |
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CURRENT RESEARCH THE FUNCTION OF RECPTORS IN TERMS OF MOLECULAR STRUCTURES The research of the laboratory is aimed at the function of receptors in terms of molecular structures. We try to understand how receptors recognize specific ligands, how the binding of these ligands is converted into the opening of ion-conducting channels (or into an interaction with GTP-binding proteins), how the selectivity of the channels is determined, and how ions are conducted through the channels. The main approaches are to identify the residues that line the binding sites and conduction pathways, to determine the three-dimensional structures, to locate the critical residues in these three-dimensional structures, and to detect changes in the functional states. To reach these goals, we use the methods of protein chemistry, molecular biology, and electrophysiology. SELECTED PUBLICATIONS Karlin, A., Wang, C., Li, J., and Xu, Q. 2004. Transfer in SDS of biotinylated proteins from acrylamide gels to an avidin coated membrane filter. BioTechniques 36:1010-1016. Karlin, A. 2004. A touching picture of nicotinic binding. Neuron 41:841-842 Li, Y., Karlin, A., Loike, J.D., Silverstein, S.C. 2004. Determination of the critical concentration of neutrophils required to block bacterial growth in tissues. J Exp Med. 200:613-22. Karlin, A., Wang, C., Li, J., and Xu, Q. 2004. Transfer in SDS of biotinylated proteins from acrylamide gels to an avidin-coated membrane filter. Biotechniques.36:1010-6. Li, J., Shi, L., and Karlin, A. 2003. A photochemical approach to the lipid accessibility of engineered cysteinyl residues. Proc. Natl. Acad. Sci. USA 100: 886-891. Yu, Y., Shi, L., and Karlin, A. 2003. Structural effects of quinacrine binding in the open channel of the acetylcholine receptor. Proc. Natl. Acad. Sci. USA 100: 3907-3912. Karlin, A. 2002. Emerging structure of the nicotinic acetylcholine receptors. Nature Reviews Neuroscience 3: 102-114. Li, Y., Karlin, A., Loike, J.D., and Silverstein, S. C. 2002. A critical concentration of neutrophils is required for effective bacterial killing in suspension. Proc. Natl. Acad. Sci. USA 99: 8289-8294. Li, J., Xu, Q., Cortes, D. M., Perozo, E., Laskey, A., and Karlin, A. 2002. Reactions of cysteines substituted in the amphipathic N terminal tail of a bacterial potassium channel with hydrophilic and hydrophobic maleimides. Proc. Natl. Acad. Sci. USA 99:11605-11610. Pascual, J.M., and Karlin, A. 1998. State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor: Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the a subunit. J. Gen. Physiol. 111:717-739. Zhang, H., and Karlin, A. 1998. Contribution of the b subunit M2 segment to the ion-conducting pathway of the acetylcholine receptor. Biochemistry 37: 7952-7964. Wilson GG, and Karlin A (1998) The location of the gate in the acetylcholine receptor channel. Neuron 20:1269-1281. Martin MD, and Karlin, A. 1997. The functional effects on the acetylcholine receptor of multiple mutations of g Asp174 and d Asp180. Biochemistry 36:10742-10750. Zhang, H., and Karlin, A. 1997. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the b subunit. Biochemistry 36:15856-15864. |
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