메뉴 건너뛰기




Volumn 43, Issue 4, 2002, Pages 669-678

Tryptophan scanning mutagenesis in TM4 of the GABAA receptor α1 subunit: Implications for modulation by inhaled anesthetics and ion channel structure

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; 4 AMINOBUTYRIC ACID A RECEPTOR; AMINO ACID; ASPARAGINE; CHLOROFORM; HALOTHANE; INHALATION ANESTHETIC AGENT; ION CHANNEL; ISOFLURANE; ISOLEUCINE; MEMBRANE PROTEIN; MUTANT PROTEIN; TRYPTOPHAN;

EID: 0036754362     PISSN: 00283908     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0028-3908(02)00175-2     Document Type: Article
Times cited : (60)

References (38)
  • 2
    • 0035237928 scopus 로고    scopus 로고
    • Molecular modeling of ligand-gated ion channels: Progress and challenges
    • Bertaccini E., Trudell J.R. Molecular modeling of ligand-gated ion channels: progress and challenges. International Review of Neurobiology. 48:2001;141-166.
    • (2001) International Review of Neurobiology , vol.48 , pp. 141-166
    • Bertaccini, E.1    Trudell, J.R.2
  • 3
    • 0036019297 scopus 로고    scopus 로고
    • Predicting the transmembrane secondary structure of ligand-gated ion channels
    • in press
    • Bertaccini, E., Trudell, J.R., 2002. Predicting the transmembrane secondary structure of ligand-gated ion channels. Protein Engineering, in press
    • (2002) Protein Engineering
    • Bertaccini, E.1    Trudell, J.R.2
  • 4
    • 0028326435 scopus 로고
    • Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: Secondary structure implications
    • Blanton M.P., Cohen J.B. Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: secondary structure implications. Biochemistry. 33:(10):1994;2859-2872.
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 2859-2872
    • Blanton, M.P.1    Cohen, J.B.2
  • 6
    • 0031595748 scopus 로고    scopus 로고
    • Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics
    • Bouzat C., Roccamo A.M., Garbus I., Barrantes F. Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics. Molecular Pharmacology. 54:1998;146-153.
    • (1998) Molecular Pharmacology , vol.54 , pp. 146-153
    • Bouzat, C.1    Roccamo, A.M.2    Garbus, I.3    Barrantes, F.4
  • 7
    • 0034059664 scopus 로고    scopus 로고
    • Nicotinic receptor fourth transmembrane domain: Hydrogen bonding by conserved threonine contributes to channel gating kinetics
    • Bouzat C., Barrantes F., Sine S. Nicotinic receptor fourth transmembrane domain: hydrogen bonding by conserved threonine contributes to channel gating kinetics. Journal of General Physiology. 115:(5):2000;663-672.
    • (2000) Journal of General Physiology , vol.115 , Issue.5 , pp. 663-672
    • Bouzat, C.1    Barrantes, F.2    Sine, S.3
  • 9
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C., Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Molecular and Cellular Biology. 7:(8):1987;2745-2752.
    • (1987) Molecular and Cellular Biology , vol.7 , Issue.8 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 10
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng W.P., Nickoloff J.A. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Analytical Biochemistry. 200:(1):1992;81-88.
    • (1992) Analytical Biochemistry , vol.200 , Issue.1 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 11
    • 0033537884 scopus 로고    scopus 로고
    • Stoichiometry of a ligand-gated ion channel determined by fluorescence energy transfer
    • Farrar S.J., Whiting P.J., Bonnert T.P., McKernan R.M. Stoichiometry of a ligand-gated ion channel determined by fluorescence energy transfer. Journal of Biological Chemistry. 274:(15):1999;10100-10104.
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 10100-10104
    • Farrar, S.J.1    Whiting, P.J.2    Bonnert, T.P.3    McKernan, R.M.4
  • 12
    • 0028140369 scopus 로고
    • Molecular and cellular mechanisms of general anaesthesia
    • Franks N.P., Lieb W.R. Molecular and cellular mechanisms of general anaesthesia. Nature. 367:(6464):1994;607-614.
    • (1994) Nature , vol.367 , Issue.6464 , pp. 607-614
    • Franks, N.P.1    Lieb, W.R.2
  • 13
    • 0027282161 scopus 로고
    • Positive modulation of human gamma-aminobutyric acid type A and glycine receptors by the inhalation anesthetic isoflurane
    • Harrison N.L., Kugler J.L., Jones M.V., Greenblatt E.P., Pritchett D.B. Positive modulation of human gamma-aminobutyric acid type A and glycine receptors by the inhalation anesthetic isoflurane. Molecular Pharmacology. 44:(3):1993;628-632.
    • (1993) Molecular Pharmacology , vol.44 , Issue.3 , pp. 628-632
    • Harrison, N.L.1    Kugler, J.L.2    Jones, M.V.3    Greenblatt, E.P.4    Pritchett, D.B.5
  • 15
    • 0030339414 scopus 로고    scopus 로고
    • Chimeric GABAA/glycine receptors: Expression and barbiturate pharmacology
    • Koltchine V.V., Ye Q., Finn S.E., Harrison N.L. Chimeric GABAA/glycine receptors: expression and barbiturate pharmacology. Neuropharmacology. 35:(9-10):1996;1445-1456.
    • (1996) Neuropharmacology , vol.35 , Issue.9-10 , pp. 1445-1456
    • Koltchine, V.V.1    Ye, Q.2    Finn, S.E.3    Harrison, N.L.4
  • 16
    • 0032707446 scopus 로고    scopus 로고
    • Agonist gating and isoflurane potentiation in the human gamma-aminobutyric acid type A receptor determined by the volume of a second transmembrane domain residue
    • Koltchine V.V., Finn S.E., Jenkins A., Nikolaeva N., Lin A., Harrison N.L. Agonist gating and isoflurane potentiation in the human gamma-aminobutyric acid type A receptor determined by the volume of a second transmembrane domain residue. Molecular Pharmacology. 56:(5):1999;1087-1093.
    • (1999) Molecular Pharmacology , vol.56 , Issue.5 , pp. 1087-1093
    • Koltchine, V.V.1    Finn, S.E.2    Jenkins, A.3    Nikolaeva, N.4    Lin, A.5    Harrison, N.L.6
  • 18
    • 0033567181 scopus 로고    scopus 로고
    • General anaesthetic actions on ligand-gated ion channels
    • Krasowski M.D., Harrison N.L. General anaesthetic actions on ligand-gated ion channels. Cell. Mol. Life. Sci. 55:(10):1999;1278-1303.
    • (1999) Cell. Mol. Life. Sci , vol.55 , Issue.10 , pp. 1278-1303
    • Krasowski, M.D.1    Harrison, N.L.2
  • 19
    • 0029849201 scopus 로고    scopus 로고
    • Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating
    • Lasalde J.A., Tamamizu S., Butler D.H., Vibat C.R., Hung B., McNamee M.G. Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating. Biochemistry. 35:(45):1996;14139-14148.
    • (1996) Biochemistry , vol.35 , Issue.45 , pp. 14139-14148
    • Lasalde, J.A.1    Tamamizu, S.2    Butler, D.H.3    Vibat, C.R.4    Hung, B.5    McNamee, M.G.6
  • 20
    • 0034607718 scopus 로고    scopus 로고
    • Coupled proteolytic and mass spectrometry studies indicate a novel topology for the glycine receptor
    • Leite J.F., Amoscato A.A., Cascio M. Coupled proteolytic and mass spectrometry studies indicate a novel topology for the glycine receptor. Journal of Biological Chemistry. 275:(18):2000;13683-13689.
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13683-13689
    • Leite, J.F.1    Amoscato, A.A.2    Cascio, M.3
  • 22
    • 0035968206 scopus 로고    scopus 로고
    • Structure of the pore-forming transmembrane domain of a ligand-gated ion channel
    • Methot N., Ritchie B.D., Blanton M.P., Baenziger J.E. Structure of the pore-forming transmembrane domain of a ligand-gated ion channel. Journal of Biological Chemistry. 276:(26):2001;23726-23732.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.26 , pp. 23726-23732
    • Methot, N.1    Ritchie, B.D.2    Blanton, M.P.3    Baenziger, J.E.4
  • 24
    • 0030302114 scopus 로고    scopus 로고
    • Inhibition of rho1 receptor GABAergic currents by alcohols and volatile anesthetics
    • Mihic S.J., Harris R.A. Inhibition of rho1 receptor GABAergic currents by alcohols and volatile anesthetics. Journal of Pharmacology and Experimental Therapeutics. 277:(1):1996;411-416.
    • (1996) Journal of Pharmacology and Experimental Therapeutics , vol.277 , Issue.1 , pp. 411-416
    • Mihic, S.J.1    Harris, R.A.2
  • 26
    • 0034663286 scopus 로고    scopus 로고
    • Membrane and synaptic actions of halothane on rat hippocampal pyramidal neurons and inhibitory interneurons
    • Nishikawa K., MacIver M.B. Membrane and synaptic actions of halothane on rat hippocampal pyramidal neurons and inhibitory interneurons. Journal of Neuroscience. 20:(16):2000;5915-5923.
    • (2000) Journal of Neuroscience , vol.20 , Issue.16 , pp. 5915-5923
    • Nishikawa, K.1    MacIver, M.B.2
  • 28
    • 0030873046 scopus 로고    scopus 로고
    • Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing
    • Ortiz-Miranda S.I., Lasalde J.A., Pappone P.A., McNamee M.G. Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing. Journal of Membrane Biology. 158:(1):1997;17-30.
    • (1997) Journal of Membrane Biology , vol.158 , Issue.1 , pp. 17-30
    • Ortiz-Miranda, S.I.1    Lasalde, J.A.2    Pappone, P.A.3    McNamee, M.G.4
  • 29
    • 0024424165 scopus 로고
    • Effect of volatile anesthetics on synaptic transmission in the rat hippocampus
    • Pearce R.A., Stringer J.L., Lothman E.W. Effect of volatile anesthetics on synaptic transmission in the rat hippocampus. Anesthesiology. 71:(4):1989;591-598.
    • (1989) Anesthesiology , vol.71 , Issue.4 , pp. 591-598
    • Pearce, R.A.1    Stringer, J.L.2    Lothman, E.W.3
  • 31
    • 0034712698 scopus 로고    scopus 로고
    • Functional effects of periodic tryptophan substitutions in the alpha M4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor
    • Tamamizu S., Guzman G.R., Santiago J., Rojas L.V., McNamee M.G., Lasalde-Dominicci J.A. Functional effects of periodic tryptophan substitutions in the alpha M4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor. Biochemistry. 39:(16):2000;4666-4673.
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4666-4673
    • Tamamizu, S.1    Guzman, G.R.2    Santiago, J.3    Rojas, L.V.4    McNamee, M.G.5    Lasalde-Dominicci, J.A.6
  • 32
    • 0032772075 scopus 로고    scopus 로고
    • Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain
    • Tamamizu S., Lee Y., Hung B., McNamee M.G., Lasalde-Dominicci J.A. Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain. Journal of Membrane Biology. 170:(2):1999;157-164.
    • (1999) Journal of Membrane Biology , vol.170 , Issue.2 , pp. 157-164
    • Tamamizu, S.1    Lee, Y.2    Hung, B.3    McNamee, M.G.4    Lasalde-Dominicci, J.A.5
  • 34
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature. 373:(6509):1995;37-43.
    • (1995) Nature , vol.373 , Issue.6509 , pp. 37-43
    • Unwin, N.1
  • 35
    • 0019316535 scopus 로고
    • Structural and functional diversity in 4-alpha-helical proteins
    • Weber P.C., Salemme F.R. Structural and functional diversity in 4-alpha-helical proteins. Nature. 287:(5777):1980;82-84.
    • (1980) Nature , vol.287 , Issue.5777 , pp. 82-84
    • Weber, P.C.1    Salemme, F.R.2
  • 36
    • 0033046508 scopus 로고    scopus 로고
    • The GABA-A receptor gene family: New targets for therapeutic intervention
    • Whiting P.J. The GABA-A receptor gene family: new targets for therapeutic intervention. Neurochemistry International. 34:(5):1999;387-390.
    • (1999) Neurochemistry International , vol.34 , Issue.5 , pp. 387-390
    • Whiting, P.J.1
  • 37
    • 0029865892 scopus 로고    scopus 로고
    • Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alpha1 subunit
    • Xu M., Akabas M.H. Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alpha1 subunit. Journal of General Physiology. 107:(2):1996;195-205.
    • (1996) Journal of General Physiology , vol.107 , Issue.2 , pp. 195-205
    • Xu, M.1    Akabas, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.