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1
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0029005830
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Nicotinic receptor-binding site probed with unnatural amino-acid incorporation in intact cells
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Nowak M.W., Kearney P.C., Sampson J.R., Saks M.E., Labarca C.G., Silverman S.K., Zhong W., Thorson J., Abelson J.N., Davidson N.et al. Nicotinic receptor-binding site probed with unnatural amino-acid incorporation in intact cells. Science. 268:1995;439-442.
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Nowak, M.W.1
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Zhong, W.7
Thorson, J.8
Abelson, J.N.9
Davidson, N.10
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0028088192
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A new tool for studying protein structure and function
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Cornish V.W., Schultz P.G. A new tool for studying protein structure and function. Curr. Opin. Struct. Biol. 4:1994;601-607.
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Cornish, V.W.1
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A general method for site-specific incorporation of unnatural amino acids into proteins
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Noren C.J., Anthonycahill S.J., Griffith M.C., Schultz P.G. A general method for site-specific incorporation of unnatural amino acids into proteins. Science. 244:1989;182-188.
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Noren, C.J.1
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4
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0003104160
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Incorporation of noncoded amino acids by in vitro protein biosynthesis
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Gilmore M.A., Steward L.E., Chamberlin A.R. Incorporation of noncoded amino acids by in vitro protein biosynthesis. Top Curr. Chem. 202:1999;77-99.
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Gilmore, M.A.1
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Unnatural amino acids as probes of protein structure and function
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Dougherty D.A. Unnatural amino acids as probes of protein structure and function. Curr. Opin. Chem. Biol. 4:2000;645-652.
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Incorporation of non-natural amino acids into proteins
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Hohsaka T., Sisido M. Incorporation of non-natural amino acids into proteins. Curr. Opin. Chem. Biol. 6:2002;809-815.
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0032311418
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In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system
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Nowak M.W., Gallivan J.P., Silverman S.K., Labarca C.G., Dougherty D.A., Lester H.A. In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system. Methods Enzymol. 293:1998;504-529.
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Nowak, M.W.1
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Silverman, S.K.3
Labarca, C.G.4
Dougherty, D.A.5
Lester, H.A.6
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8
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0029811223
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Agonist-binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists
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Kearney P.C., Nowak M.W., Zhong W., Silverman S.K., Lester H.A., Dougherty D.A. Agonist-binding site of the nicotinic acetylcholine receptor: tests with novel side chains and with several agonists. Mol. Pharmacol. 50:1996;1401-1412.
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Kearney, P.C.1
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Dougherty, D.A.6
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9
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0032514762
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From ab initio quantum mechanics to molecular neurobiology: A cation-π binding site in the nicotinic receptor
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Zhong W.G., Gallivan J.P., Zhang Y.O., Li L.T., Lester H.A., Dougherty D.A. From ab initio quantum mechanics to molecular neurobiology: a cation-π binding site in the nicotinic receptor. Proc. Natl. Acad. Sci. U.S.A. 95:1998;12088-12093.
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Zhong, W.G.1
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Lester, H.A.5
Dougherty, D.A.6
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10
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0030043489
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Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
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Dougherty D.A. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science. 271:1996;163-168.
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Dougherty, D.A.1
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The cation-π interaction
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Ma J.C., Dougherty D.A. The cation-π interaction. Chem. Rev. 97:1997;1303-1324.
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Ma, J.C.1
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12
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0037072311
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Cation-π interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: The anomalous binding properties of nicotine
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A demonstration of the fluoro-Trp series as a general method for systematically varying the strength of cation-π interactions; this work provides further evidence that this interaction represents a general biological strategy for the recognition of neurotransmitters.
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Beene D.L., Brandt G.S., Zhong W.G., Zacharias N.M., Lester H.A., Dougherty D.A. Cation-π interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: the anomalous binding properties of nicotine. Biochemistry. 41:2002;10262-10269 A demonstration of the fluoro-Trp series as a general method for systematically varying the strength of cation-π interactions; this work provides further evidence that this interaction represents a general biological strategy for the recognition of neurotransmitters.
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Biochemistry
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Beene, D.L.1
Brandt, G.S.2
Zhong, W.G.3
Zacharias, N.M.4
Lester, H.A.5
Dougherty, D.A.6
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13
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0035113738
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The tethered agonist approach to mapping ion channel proteins toward a structural model for the agonist binding site of the nicotinic acetylcholine receptor
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An effective illustration of the tethered-agonist approach for the spatial mapping of ligand-receptor relationships.
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Li L.T., Zhong W.G., Zacharias N., Gibbs C., Lester H.A., Dougherty D.A. The tethered agonist approach to mapping ion channel proteins toward a structural model for the agonist binding site of the nicotinic acetylcholine receptor. Chem. Biol. 8:2001;47-58 An effective illustration of the tethered-agonist approach for the spatial mapping of ligand-receptor relationships.
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Li, L.T.1
Zhong, W.G.2
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Lester, H.A.5
Dougherty, D.A.6
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14
-
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0037202217
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A perturbed pK(a) at the binding site of the nicotinic acetylcholine receptor: Implications for nicotine binding
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a of the nAChR binding site; the work demonstrates how the method can identify the specific chemistry of ligand-receptor interactions.
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a of the nAChR binding site; the work demonstrates how the method can identify the specific chemistry of ligand-receptor interactions.
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J. Am. Chem. Soc.
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Petersson, E.J.1
Choi, A.2
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Dougherty, D.A.5
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15
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0030922940
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An experimental approach to evaluating the role of backbone interactions in proteins using unnatural amino acid mutagenesis
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Koh J.T., Cornish V.W., Schultz P.G. An experimental approach to evaluating the role of backbone interactions in proteins using unnatural amino acid mutagenesis. Biochemistry. 36:1997;11314-11322.
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Biochemistry
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Koh, J.T.1
Cornish, V.W.2
Schultz, P.G.3
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16
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0032495762
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Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogues
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Killian J.A., Van Cleve M.D., Shayo Y.F., Hecht S.M. Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogues. J. Am. Chem. Soc. 120:1998;3032-3042.
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Killian, J.A.1
Van Cleve, M.D.2
Shayo, Y.F.3
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17
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0037167581
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Site-specific incorporation of (aminooxy)acetic acid into proteins
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Eisenhauer B.M., Hecht S.M. Site-specific incorporation of (aminooxy)acetic acid into proteins. Biochemistry. 41:2002;11472-11478.
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Biochemistry
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Eisenhauer, B.M.1
Hecht, S.M.2
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18
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0033607250
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Mapping disulfide connectivity using backbone ester hydrolysis
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England P.M., Lester H.A., Dougherty D.A. Mapping disulfide connectivity using backbone ester hydrolysis. Biochemistry. 38:1999;14409-14415.
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(1999)
Biochemistry
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England, P.M.1
Lester, H.A.2
Dougherty, D.A.3
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19
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0034046304
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Probing the role of a conserved M1 proline residue in 5-hydroxytryptamine(3) receptor gating
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Dang H., England P.M., Farivar S.S., Dougherty D.A., Lester H.A. Probing the role of a conserved M1 proline residue in 5-hydroxytryptamine(3) receptor gating. Mol. Pharmacol. 57:2000;1114-1122.
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Mol. Pharmacol.
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Dang, H.1
England, P.M.2
Farivar, S.S.3
Dougherty, D.A.4
Lester, H.A.5
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20
-
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0033534674
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Backbone mutations in transmembrane domains of a ligand-gated ion channel: Implications for the mechanism of gating
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England P.M., Zhang Y.N., Dougherty D.A., Lester H.A. Backbone mutations in transmembrane domains of a ligand-gated ion channel: implications for the mechanism of gating. Cell. 96:1999;89-98.
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(1999)
Cell
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, pp. 89-98
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England, P.M.1
Zhang, Y.N.2
Dougherty, D.A.3
Lester, H.A.4
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21
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0035119276
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+ channel with backbone mutations in the selectivity filter
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+ ion selectivity filter and to identify interactions between the filter and permeant ions that contribute to channel gating.
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+ ion selectivity filter and to identify interactions between the filter and permeant ions that contribute to channel gating.
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Nat. Neurosci.
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Lu, T.1
Ting, A.Y.2
Mainland, J.3
Jan, L.Y.4
Schultz, P.G.5
Yang, J.6
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22
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0034816479
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Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor
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Philipson K.D., Gallivan J.P., Brandt G.S., Dougherty D.A., Lester H.A. Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor. Am. J. Physiol. Cell Physiol. 281:2001;C195-C206.
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Am. J. Physiol. Cell Physiol.
, vol.281
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Philipson, K.D.1
Gallivan, J.P.2
Brandt, G.S.3
Dougherty, D.A.4
Lester, H.A.5
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23
-
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0032055921
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Flash decaging of tyrosine sidechains in an ion channel
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Miller J.C., Silverman S.K., England P.M., Dougherty D.A., Lester H.A. Flash decaging of tyrosine sidechains in an ion channel. Neuron. 20:1998;619-624.
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(1998)
Neuron
, vol.20
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Miller, J.C.1
Silverman, S.K.2
England, P.M.3
Dougherty, D.A.4
Lester, H.A.5
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24
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0032541289
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A photochemical switch for controlling protein-protein interactions
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Pollitt S.K., Schultz P.G. A photochemical switch for controlling protein-protein interactions. Angew. Chem. Int. Ed. Engl. 37:1998;2104-2107.
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Angew. Chem. Int. Ed. Engl.
, vol.37
, pp. 2104-2107
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Pollitt, S.K.1
Schultz, P.G.2
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25
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0035003359
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Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel
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The incorporation of caged tyrosine identifies a key modulatory role for phosphorylation in both channel function and trafficking.
-
Tong Y.H., Brandt G.S., Li M., Shapovalov G., Slimko E., Karschin A., Dougherty D.A., Lester H.A. Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel. J. Gen. Physiol. 117:2001;103-118 The incorporation of caged tyrosine identifies a key modulatory role for phosphorylation in both channel function and trafficking.
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J. Gen. Physiol.
, vol.117
, pp. 103-118
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Tong, Y.H.1
Brandt, G.S.2
Li, M.3
Shapovalov, G.4
Slimko, E.5
Karschin, A.6
Dougherty, D.A.7
Lester, H.A.8
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26
-
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0030923523
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Site-specific, photochemical proteolysis applied to ion channels in vivo
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England P.M., Lester H.A., Davidson N., Dougherty D.A. Site-specific, photochemical proteolysis applied to ion channels in vivo. Proc. Natl. Acad. Sci. U.S.A. 94:1997;11025-11030.
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(1997)
Proc. Natl. Acad. Sci. U.S.A.
, vol.94
, pp. 11025-11030
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England, P.M.1
Lester, H.A.2
Davidson, N.3
Dougherty, D.A.4
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27
-
-
0037151668
-
Fluorescence resonance energy transfer between unnatural amino acids in a structurally modified dihydrofolate reductase
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The first use of suppressor tRNAs to incorporate a donor and acceptor pair of unnatural amino acids for fluorescence energy transfer studies.
-
Anderson R.D., Zhou J., Hecht S.M. Fluorescence resonance energy transfer between unnatural amino acids in a structurally modified dihydrofolate reductase. J. Am. Chem. Soc. 124:2002;9674-9675 The first use of suppressor tRNAs to incorporate a donor and acceptor pair of unnatural amino acids for fluorescence energy transfer studies.
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J. Am. Chem. Soc.
, vol.124
, pp. 9674-9675
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Anderson, R.D.1
Zhou, J.2
Hecht, S.M.3
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28
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0037204951
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Probing protein electrostatics with a synthetic fluorescent amino acid
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Cohen B.E., McAnaney T.B., Park E.S., Jan Y.N., Boxer S.G., Jan L.Y. Probing protein electrostatics with a synthetic fluorescent amino acid. Science. 296:2002;1700-1703.
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Science
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Cohen, B.E.1
McAnaney, T.B.2
Park, E.S.3
Jan, Y.N.4
Boxer, S.G.5
Jan, L.Y.6
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29
-
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0032486776
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Site-directed incorporation of p-nitrophenylalanine into streptavidin and site-to-site photoinduced electron transfer from a pyrenyl group to a nitrophenyl group on the protein framework
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Murakami H., Hohsaka T., Ashizuka Y., Sisido M. Site-directed incorporation of p-nitrophenylalanine into streptavidin and site-to-site photoinduced electron transfer from a pyrenyl group to a nitrophenyl group on the protein framework. J. Am. Chem. Soc. 120:1998;7520-7529.
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J. Am. Chem. Soc.
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Murakami, H.1
Hohsaka, T.2
Ashizuka, Y.3
Sisido, M.4
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30
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0037065314
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Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs
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Elaboration of a four-base codon strategy to incorporate two fluorescent amino acids into a single protein.
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Taki M., Hohsaka T., Murakami H., Taira K., Sisido M. Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs. J. Am. Chem. Soc. 124:2002;14586-14590 Elaboration of a four-base codon strategy to incorporate two fluorescent amino acids into a single protein.
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Taki, M.1
Hohsaka, T.2
Murakami, H.3
Taira, K.4
Sisido, M.5
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31
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0029838186
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Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites
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Turcatti G., Nemeth K., Edgerton M.D., Meseth U., Talabot F., Peitsch M., Knowles J., Vogel H., Chollet A. Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites. J. Biol. Chem. 271:1996;19991-19998.
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Turcatti, G.1
Nemeth, K.2
Edgerton, M.D.3
Meseth, U.4
Talabot, F.5
Peitsch, M.6
Knowles, J.7
Vogel, H.8
Chollet, A.9
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