Synapses are the primary points of communication between cells of the nervous system. Our laboratory is interested in synaptic receptors and ion channels. We study the molecular events that constitute agonist binding, receptor activation and ion permeation. Our research combines the approaches of pharmacology, enzymology, structural and molecular biology, electrophysiology, and mathematical modeling. Our primary goal is to understand the molecular operation of these membrane proteins in the context of their physiological roles. We also study the biophysical basis of ion channel diseases. To see a movie of AChR gating, click here
Education and Training:
PhD, Neuroscience, University of Oregon (1978)
BS, Biochemistry, University of California at Santa Barbara (1972)
Professor, University at Buffalo (1998-present)
Associate Professor, University at Buffalo (1992–1998)
Assistant Professor, University at Buffalo (1987–1992)
Research Assistant Professor, University at Buffalo (1983–1987)
Post Doctoral Fellow, University at Buffalo (1981–1983)
Post Doctoral Fellow, Neurobiology, Institute of Neurobiology San Juan, PR, Institute of Neurobiology, Puerto Rico (1978–1981)
Awards and Honors:
Chancellor's Award for Excellence in Scholarship and Creative Activities (2012)
Javits Award (2006-2014) (2006)
SUNY Chancellor's Award for Research (2003)
Chair, NIH Study Section BSCT (2003)
SUNY Research Achievement Award (2002)
Javits Award (1999-2006) (1999)
Grants and Sponsored Research:
June 2009–May 2014 Engineering a Transmitter Binding Site NIH Role: Principal Investigator
April 1986–March 2014 Multiple Activity Patterns of Acetylcholine Receptors NIH Role: Principal Investigator
Grosman C, Auerbach A. The dissociation of acetylcholine from open nicotinic receptor channels.. Proc Natl Acad Sci U S A. 2001; 98(24).
Zhu Y, Auerbach A. Na(+) occupancy and Mg(2+) block of the n-methyl-d-aspartate receptor channel.. J Gen Physiol. 2001; 117(3).
Zhu Y, Auerbach A. K(+) occupancy of the N-methyl-d-aspartate receptor channel probed by Mg(2+) block.. J Gen Physiol. 2001; 117(3).
Qin F, Auerbach A, Sachs F. A direct optimization approach to hidden Markov modeling for single channel kinetics.. Biophys J. 2000; 79(4).
Grosman C, Salamone FN, Sine SM, Auerbach A. The extracellular linker of muscle acetylcholine receptor channels is a gating control element.. J Gen Physiol. 2000; 116(3).
Grosman C, Auerbach A. Kinetic, mechanistic, and structural aspects of unliganded gating of acetylcholine receptor channels: a single-channel study of second transmembrane segment 12' mutants.. J Gen Physiol. 2000; 115(5).
Grosman C, Auerbach A. Asymmetric and independent contribution of the second transmembrane segment 12' residues to diliganded gating of acetylcholine receptor channels: a single-channel study with choline as the agonist.. J Gen Physiol. 2000; 115(5).
Grosman C, Zhou M, Auerbach A. Mapping the conformational wave of acetylcholine receptor channel gating.. Nature. 2000; 403(6771).
Akk G, Auerbach A. Activation of muscle nicotinic acetylcholine receptor channels by nicotinic and muscarinic agonists.. Br J Pharmacol. 1999; 128(7).
Zhou M, Engel AG, Auerbach A. Serum choline activates mutant acetylcholine receptors that cause slow channel congenital myasthenic syndromes.. Proc Natl Acad Sci U S A. 1999; 96(18).
Salamone FN, Zhou M, Auerbach A. A re-examination of adult mouse nicotinic acetylcholine receptor channel activation kinetics.. J Physiol. 1999; 516 (.
Akk G, Zhou M, Auerbach A. A mutational analysis of the acetylcholine receptor channel transmitter binding site.. Biophys J. 1999; 76(1 Pt).
Auerbach A, Akk G. Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism.. J Gen Physiol. 1998; 112(2).
Chen J, Auerbach A. A distinct contribution of the delta subunit to acetylcholine receptor channel activation revealed by mutations of the M2 segment.. Biophys J. 1998; 75(1).
Premkumar LS, Auerbach A. Stoichiometry of recombinant N-methyl-D-aspartate receptor channels inferred from single-channel current patterns.. J Gen Physiol. 1997; 110(5).
Wang HL, Auerbach A, Bren N, Ohno K, Engel AG, Sine SM. Mutation in the M1 domain of the acetylcholine receptor alpha subunit decreases the rate of agonist dissociation.. J Gen Physiol. 1997; 109(6).
Qin F, Auerbach A, Sachs F. Maximum likelihood estimation of aggregated Markov processes.. Proc R Soc Lond B Biol Sci. 1997; 264(1380).
Qin F, Auerbach A. 1997; 109(2).
Akk G, Sine S, Auerbach A. Binding sites contribute unequally to the gating of mouse nicotinic alpha D200N acetylcholine receptors.. J Physiol. 1996; 496 (.
Auerbach A, Sigurdson W, Chen J, Akk G. Voltage dependence of mouse acetylcholine receptor gating: different charge movements in di-, mono- and unliganded receptors.. J Physiol. 1996; 494 (.
Akk G, Auerbach A. Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors.. Biophys J. 1996; 70(6).
Premkumar LS, Auerbach A. Identification of a high affinity divalent cation binding site near the entrance of the NMDA receptor channel.. Neuron. 1996; 16(4).
Qin F, Auerbach A, Sachs F. Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events.. Biophys J. 1996; 70(1).
Chen J, Zhang Y, Akk G, Sine S, Auerbach A. Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of alpha-subunit tyrosine 190 affect both binding and gating.. Biophys J. 1995; 69(3).
Zhang Y, Auerbach A. Kinetic properties of NMDA receptors in embryonic Xenopus spinal neurons.. J Neurophysiol. 1995; 74(1).
Gao J, Chou LW, Auerbach A. The nature of cation-pi binding: interactions between tetramethylammonium ion and benzene in aqueous solution.. Biophys J. 1993; 65(1).
Auerbach A. A statistical analysis of acetylcholine receptor activation in Xenopus myocytes: stepwise versus concerted models of gating.. J Physiol. 1993; 461.
Auerbach A. Single-channel dose-response studies in single, cell-attached patches.. Biophys J. 1991; 60(3).
Davidson RM, Tatakis DW, Auerbach AL. Multiple forms of mechanosensitive ion channels in osteoblast-like cells.. Pflugers Arch. 1990; 416(6).
Auerbach A, Lingle CJ. Activation of the primary kinetic modes of large- and small-conductance cholinergic ion channels in Xenopus myocytes.. J Physiol. 1987; 393.
Auerbach A, Lingle CJ. Heterogeneous kinetic properties of acetylcholine receptor channels in Xenopus myocytes.. J Physiol. 1986; 378.
Auerbach A, Sachs F. Single-channel currents from acetylcholine receptors in embryonic chick muscle. Kinetic and conductance properties of gaps within bursts.. Biophys J. 1984; 45(1).
Auerbach A, del Castillo J, Specht PC, Titmus M. Correlation of agonist structure with acetylcholine receptor kinetics: studies on the frog end-plate and on chick embryo muscle.. J Physiol. 1983; 343.
Lingle C, Auerbach A. Comparison of excitatory currents activated by different transmitters on crustacean muscle. II. Glutamate-activated currents and comparison with acetylcholine currents present on the same muscle.. J Gen Physiol. 1983; 81(4).
Lingle C, Auerbach A. Comparison of excitatory currents activated by different transmitters on crustacean muscle. I. Acetylcholine-activated channels.. J Gen Physiol. 1983; 81(4).
Auerbach A, Sachs F. Flickering of a nicotinic ion channel to a subconductance state.. Biophys J. 1983; 42(1).
Auerbach A, Barker DL. [(3)H]Choline uptake and metabolism in nonsynaptic regions of a crustacean sensory nerve.. J Neurochem. 1981; 36(5).
Sachs F, Auerbach A. Single-channel electrophysiology: use of the patch clamp.. Methods Enzymol. ; 103.
del Castillo J, Specht P, Auerbach A. Automatic control of potential and agonist-induced current across the endplate membrane by drug electrophoresis.. J Neurosci Res. ; 8(1).
Auerbach A, Sachs F, Neil J, McGarrigle R. Temperature measurement and control of small volumes: applications for single channel recording.. Methods Enzymol. ; 124.
Auerbach A, Sachs F. Patch clamp studies of single ionic channels.. Annu Rev Biophys Bioeng. ; 13.
Auerbach A. Acetylcholine receptors, between closed and open.. Novartis Found Symp. ; 245.