Search Results - "Hanek, Ariele P"
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A Unified View of the Role of Electrostatic Interactions in Modulating the Gating of Cys Loop Receptors
Published in The Journal of biological chemistry (16-12-2005)“…In the Cys loop superfamily of ligand-gated ion channels, a global conformational change, initiated by agonist binding, results in channel opening and the…”
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A Stereochemical Test of a Proposed Structural Feature of the Nicotinic Acetylcholine Receptor
Published in Journal of the American Chemical Society (08-10-2008)“…Understanding the gating mechanism of the nicotinic acetylcholine receptor (nAChR) and similar channels constitutes a significant challenge in chemical…”
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A cation-pi interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue
Published in The Journal of neuroscience (22-10-2008)“…Cys-loop receptor binding sites characteristically contain many aromatic amino acids. In nicotinic ACh and 5-HT3 receptors, a Trp residue forms a cation-pi…”
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A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists
Published in Molecular pharmacology (01-04-2011)“…Cation-π interactions have been demonstrated to play a major role in agonist-binding in Cys-loop receptors. However, neither the aromatic amino acid…”
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Photochemical proteolysis of an unstructured linker of the GABAAR extracellular domain prevents GABA but not pentobarbital activation
Published in Molecular pharmacology (01-07-2010)“…The GABA type A receptor (GABA(A)R) is the major inhibitory receptor in the mammalian central nervous system and the target of numerous pharmaceuticals. The…”
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Unnatural Amino Acid Mutagenesis of the GABAA Receptor Binding Site Residues Reveals a Novel Cation–π Interaction between GABA and β2Tyr97
Published in The Journal of neuroscience (24-01-2007)“…The binding pockets of Cys-loop receptors are dominated by aromatic amino acids. In the GABA A receptor α 1 Phe65, β 2 Tyr97, β 2 Tyr157, and β 2 Tyr205 are…”
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Unnatural Amino Acid Mutagenesis of the GABA A Receptor Binding Site Residues Reveals a Novel Cation–π Interaction between GABA and β 2 Tyr97
Published in The Journal of neuroscience (24-01-2007)“…The binding pockets of Cys-loop receptors are dominated by aromatic amino acids. In the GABA A receptor α 1 Phe65, β 2 Tyr97, β 2 Tyr157, and β 2 Tyr205 are…”
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Unnatural Amino Acid Mutagenesis of the GABA sub(A) Receptor Binding Site Residues Reveals a Novel Cation- pi Interaction between GABA and {szligbeta} sub(2)Tyr97
Published in The Journal of neuroscience (01-01-2007)“…The binding pockets of Cys-loop receptors are dominated by aromatic amino acids. In the GABA sub(A) receptor alpha sub(1)Phe65, {szligbeta} sub(2)Tyr97,…”
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Unnatural amino acid mutagenesis of the GABA(A) receptor binding site residues reveals a novel cation-pi interaction between GABA and beta 2Tyr97
Published in The Journal of neuroscience (24-01-2007)“…The binding pockets of Cys-loop receptors are dominated by aromatic amino acids. In the GABA(A) receptor alpha1Phe65, beta2Tyr97, beta2Tyr157, and beta2Tyr205…”
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A Cation-{pi} Interaction in the Binding Site of the Glycine Receptor Is Mediated by a Phenylalanine Residue
Published in The Journal of neuroscience (22-10-2008)Get full text
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