Darren L. Beene, Ph.D. - Publications

2004 California Institute of Technology, Pasadena, CA 
physical organic chemistry to systems of biological importance

6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2012 Lummis SC, Harrison NJ, Wang J, Ashby JA, Millen KS, Beene DL, Dougherty DA. Multiple Tyrosine Residues Contribute to GABA Binding in the GABA(C) Receptor Binding Pocket. Acs Chemical Neuroscience. 3: 186-192. PMID 22448304 DOI: 10.1021/cn200103n  0.6
2005 Lummis SC, Beene DL, Lee LW, Lester HA, Broadhurst RW, Dougherty DA. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature. 438: 248-52. PMID 16281040 DOI: 10.1038/nature04130  0.6
2005 Lummis SC, L Beene D, Harrison NJ, Lester HA, Dougherty DA. A cation-pi binding interaction with a tyrosine in the binding site of the GABAC receptor. Chemistry & Biology. 12: 993-7. PMID 16183023 DOI: 10.1016/j.chembiol.2005.06.012  0.6
2004 Beene DL, Price KL, Lester HA, Dougherty DA, Lummis SC. Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 24: 9097-104. PMID 15483128 DOI: 10.1523/JNEUROSCI.2429-04.2004  0.6
2003 Beene DL, Dougherty DA, Lester HA. Unnatural amino acid mutagenesis in mapping ion channel function. Current Opinion in Neurobiology. 13: 264-70. PMID 12850209 DOI: 10.1016/S0959-4388(03)00068-0  0.6
2002 Beene DL, Brandt GS, Zhong W, Zacharias NM, Lester HA, Dougherty DA. Cation-pi interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: the anomalous binding properties of nicotine. Biochemistry. 41: 10262-9. PMID 12162741 DOI: 10.1021/bi020266d  0.6
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