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Volumn 60, Issue 3, 2005, Pages 412-423

G-protein-coupled receptor domain overexpression in Halobacterium salinarum: Long-range transmembrane interactions in heptahelical membrane proteins

Author keywords

2b adrenergic receptor; Allosteric; Bacteriorhodopsin; Fusion proteins; G protein coupled receptors; Heterologous expression

Indexed keywords

ALPHA 2B ADRENERGIC RECEPTOR; BACTERIORHODOPSIN; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; HYBRID PROTEIN; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN;

EID: 23044489637     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20498     Document Type: Article
Times cited : (9)

References (73)
  • 1
    • 0008600208 scopus 로고    scopus 로고
    • TinyGRAP database: A bioinformatics tool to mine G-protein-coupled receptor mutant data
    • Beukers MW, Kristiansen I, IJzerman AP, Edvardsen I. TinyGRAP database: a bioinformatics tool to mine G-protein-coupled receptor mutant data. Trends Pharmacol Sci 1999;20:475-477.
    • (1999) Trends Pharmacol Sci , vol.20 , pp. 475-477
    • Beukers, M.W.1    Kristiansen, I.2    Ijzerman, A.P.3    Edvardsen, I.4
  • 5
    • 0036223247 scopus 로고    scopus 로고
    • Grafting segments from the extracellular surface of CCR5 onto a bacteriorhodopsin transmembrane scaffold confers HIV-1 coreceptor activity
    • Abdulaev NG, Strassmaier TT, Ngo T, Chen R, Luecke H, Oprian DD, Ridge KD. Grafting segments from the extracellular surface of CCR5 onto a bacteriorhodopsin transmembrane scaffold confers HIV-1 coreceptor activity. Structure (Camb) 2002;10:515-525.
    • (2002) Structure (Camb) , vol.10 , pp. 515-525
    • Abdulaev, N.G.1    Strassmaier, T.T.2    Ngo, T.3    Chen, R.4    Luecke, H.5    Oprian, D.D.6    Ridge, K.D.7
  • 7
    • 0025924636 scopus 로고
    • Properties of Asp212-Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base
    • Needleman R, Chang M, Ni B, Varo G, Fornes J, White SH, Lanyi JK. Properties of Asp212-Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base. J Biol Chem 1991;266: 11478-11484.
    • (1991) J Biol Chem , vol.266 , pp. 11478-11484
    • Needleman, R.1    Chang, M.2    Ni, B.3    Varo, G.4    Fornes, J.5    White, S.H.6    Lanyi, J.K.7
  • 10
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin JM, Schertler GF, Unger VM. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J Mol Biol 1997;272:144-164.
    • (1997) J Mol Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 11
    • 0025821645 scopus 로고
    • Functional interactions of recombinant alpha 2 adrenergic receptor subtypes and G proteins in reconstituted phospholipid vesicles
    • Kurose H, Regan JW, Caron MG, Lefkowitz RJ. Functional interactions of recombinant alpha 2 adrenergic receptor subtypes and G proteins in reconstituted phospholipid vesicles. Biochemistry 1991;30:3335-3341.
    • (1991) Biochemistry , vol.30 , pp. 3335-3341
    • Kurose, H.1    Regan, J.W.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 12
    • 0031633388 scopus 로고    scopus 로고
    • Alpha 2-adrenergic receptor subtypes: Subtle mutation of the alpha 2A-adrenergic receptor in vivo by gene targeting strategies reveals the role of this subtype in multiple physiological settings
    • MacMillan LB, Lakhlani P, Lovinger D, Limbird LE. Alpha 2-adrenergic receptor subtypes: subtle mutation of the alpha 2A-adrenergic receptor in vivo by gene targeting strategies reveals the role of this subtype in multiple physiological settings. Recent Prog Horm Res 1998;53:25-42.
    • (1998) Recent Prog Horm Res , vol.53 , pp. 25-42
    • MacMillan, L.B.1    Lakhlani, P.2    Lovinger, D.3    Limbird, L.E.4
  • 13
    • 0027081142 scopus 로고
    • Pharmacological characteristics of alpha 2-adrenergic receptors: Comparison of pharmacologically defined subtypes with subtypes identified by molecular cloning
    • Bylund DB, Blaxall HS, Iversen LJ, Caron MG, Lefkowitz RJ, Lomasney JW. Pharmacological characteristics of alpha 2-adrenergic receptors: comparison of pharmacologically defined subtypes with subtypes identified by molecular cloning. Mol Pharmacol 1992;42:1-5.
    • (1992) Mol Pharmacol , vol.42 , pp. 1-5
    • Bylund, D.B.1    Blaxall, H.S.2    Iversen, L.J.3    Caron, M.G.4    Lefkowitz, R.J.5    Lomasney, J.W.6
  • 14
    • 0033522903 scopus 로고    scopus 로고
    • Role for the third intracellular loop in cell surface stabilization of the alpha2A-adrenergic receptor
    • Edwards SW, Limbird LE. Role for the third intracellular loop in cell surface stabilization of the alpha2A-adrenergic receptor. J Biol Chem 1999;274:16331-16336.
    • (1999) J Biol Chem , vol.274 , pp. 16331-16336
    • Edwards, S.W.1    Limbird, L.E.2
  • 15
    • 0028178404 scopus 로고
    • Unique structural features important for stabilization versus polarization of the alpha 2A-adrenergic receptor on the basolateral membrane of Madin-Darby canine kidney cells
    • Keefer JR, Kennedy ME, Limbird LE. Unique structural features important for stabilization versus polarization of the alpha 2A-adrenergic receptor on the basolateral membrane of Madin-Darby canine kidney cells. J Biol Chem 1994;269:16425-16432.
    • (1994) J Biol Chem , vol.269 , pp. 16425-16432
    • Keefer, J.R.1    Kennedy, M.E.2    Limbird, L.E.3
  • 16
    • 0033531936 scopus 로고    scopus 로고
    • The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes
    • Prezeau L, Richman JG, Edwards SW, Limbird LE. The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes. J Biol Chem 1999;274:13462-13469.
    • (1999) J Biol Chem , vol.274 , pp. 13462-13469
    • Prezeau, L.1    Richman, J.G.2    Edwards, S.W.3    Limbird, L.E.4
  • 17
    • 0036078874 scopus 로고    scopus 로고
    • Mutagenesis and peptide analysis of the DRY motif in the alpha2A adrenergic receptor: Evidence for alternate mechanisms in G protein-coupled receptors
    • Chung DA, Wade SM, Fowler CB, Woods DD, Abada PB, Mosberg HI, Neubig RR. Mutagenesis and peptide analysis of the DRY motif in the alpha2A adrenergic receptor: evidence for alternate mechanisms in G protein-coupled receptors. Biochem Biophys Res Commun 2002;293:1233-1241.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 1233-1241
    • Chung, D.A.1    Wade, S.M.2    Fowler, C.B.3    Woods, D.D.4    Abada, P.B.5    Mosberg, H.I.6    Neubig, R.R.7
  • 18
    • 0034142184 scopus 로고    scopus 로고
    • Mechanisms regulating the cell surface residence time of the alpha 2A-adrenergic receptor
    • Wilson MH, Limbird LE. Mechanisms regulating the cell surface residence time of the alpha 2A-adrenergic receptor. Biochemistry 2000;39:693-700.
    • (2000) Biochemistry , vol.39 , pp. 693-700
    • Wilson, M.H.1    Limbird, L.E.2
  • 22
    • 0037184945 scopus 로고    scopus 로고
    • Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3
    • Wang Q, Limbird LE. Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3. J Biol Chem 2002;277:50589-50596.
    • (2002) J Biol Chem , vol.277 , pp. 50589-50596
    • Wang, Q.1    Limbird, L.E.2
  • 23
    • 0025723894 scopus 로고
    • Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle
    • Varo G, Lanyi JK. Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle. Biochemistry 1991;30:7165-7171.
    • (1991) Biochemistry , vol.30 , pp. 7165-7171
    • Varo, G.1    Lanyi, J.K.2
  • 24
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S, Gerstein M, Oesterhelt D, Henderson R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J 1993;12:1-8.
    • (1993) EMBO J , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 25
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 1997;277:1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 26
    • 0037285261 scopus 로고    scopus 로고
    • Structural clues to the mechanism of ion pumping in bacteriorhodopsin
    • Luecke H, Lanyi JK. Structural clues to the mechanism of ion pumping in bacteriorhodopsin. Adv Protein Chem 2003;63:111-130.
    • (2003) Adv Protein Chem , vol.63 , pp. 111-130
    • Luecke, H.1    Lanyi, J.K.2
  • 27
    • 0024730742 scopus 로고
    • Transformation of the archaebacterium Halobacterium volcano, with genomic DNA
    • Cline SW, Schalkwyk LC, Doolittle WF. Transformation of the archaebacterium Halobacterium volcano, with genomic DNA. J Bacteriol 1989;171:4987-4991.
    • (1989) J Bacteriol , vol.171 , pp. 4987-4991
    • Cline, S.W.1    Schalkwyk, L.C.2    Doolittle, W.F.3
  • 28
    • 0031786572 scopus 로고    scopus 로고
    • Functional expression of green fluorescent protein derivatives in Halobacterium salinarum
    • Nomura S, Harada Y. Functional expression of green fluorescent protein derivatives in Halobacterium salinarum. FEMS Microbiol Lett 1998;167:287-293.
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 287-293
    • Nomura, S.1    Harada, Y.2
  • 29
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D, Stoeckenius W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol 1974;31:667-678.
    • (1974) Methods Enzymol , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979;76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0033780328 scopus 로고    scopus 로고
    • Production and purification of recombinant human alpha 2C2 adrenergic receptor using Saccharomyces cerevisiae
    • Kapat A, Jaakola VP, Heimo H, Liitti S, Heikinheimo P, Glumoff T, Goldman A. Production and purification of recombinant human alpha 2C2 adrenergic receptor using Saccharomyces cerevisiae. Bioseparation 2000;9:167-172.
    • (2000) Bioseparation , vol.9 , pp. 167-172
    • Kapat, A.1    Jaakola, V.P.2    Heimo, H.3    Liitti, S.4    Heikinheimo, P.5    Glumoff, T.6    Goldman, A.7
  • 33
    • 0031557676 scopus 로고    scopus 로고
    • Subtype specific recognition of human alpha2C2 adrenergic receptor using monoclonal antibodies against the third intracellular loop
    • Liitti S, Narva H, Marjamaki A, Hellman J, Kallio J, Jalkanen M, Matikainen MT. Subtype specific recognition of human alpha2C2 adrenergic receptor using monoclonal antibodies against the third intracellular loop. Biochem Biophys Res Commun 1997;233:166-172.
    • (1997) Biochem Biophys Res Commun , vol.233 , pp. 166-172
    • Liitti, S.1    Narva, H.2    Marjamaki, A.3    Hellman, J.4    Kallio, J.5    Jalkanen, M.6    Matikainen, M.T.7
  • 34
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau EM, Rosenbusch JP. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc Natl Acad Sci USA 1996;93:14532-14535.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 35
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Faham S, Bowie JU. Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J Mol Biol 2002;316:1-6.
    • (2002) J Mol Biol , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 36
    • 0037706939 scopus 로고    scopus 로고
    • Compatibility of detergents with the microbatch-under-oil crystallization method
    • Loll PJ, Tretiakova A, Soderblom E. Compatibility of detergents with the microbatch-under-oil crystallization method. Acta Crystallogr D Biol Crystallogr 2003;59:1114-1116.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 1114-1116
    • Loll, P.J.1    Tretiakova, A.2    Soderblom, E.3
  • 37
    • 0018805369 scopus 로고
    • Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient
    • Rehorek M, Heyn MP. Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient. Biochemistry 1979;18:4977-4983.
    • (1979) Biochemistry , vol.18 , pp. 4977-4983
    • Rehorek, M.1    Heyn, M.P.2
  • 38
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • Otto H, Marti T, Holz M, Mogi T, Lindau M, Khorana HG, Heyn MP. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc Natl Acad Sci USA 1989;86:9228-9232.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 39
    • 0034607683 scopus 로고    scopus 로고
    • Evidence for long range allosteric interactions between the extracellular and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C
    • Alexiev U, Mollaaghababa R, Khorana HG, Heyn MP. Evidence for long range allosteric interactions between the extracellular and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C. J Biol Chem 2000;275: 13431-13440.
    • (2000) J Biol Chem , vol.275 , pp. 13431-13440
    • Alexiev, U.1    Mollaaghababa, R.2    Khorana, H.G.3    Heyn, M.P.4
  • 41
    • 0025096943 scopus 로고
    • Large scale preparation of homogeneous bacteriorhodopsin
    • Lorber B, DeLucas LJ. Large scale preparation of homogeneous bacteriorhodopsin. FEBS Lett 1990;261:14-18.
    • (1990) FEBS Lett , vol.261 , pp. 14-18
    • Lorber, B.1    Delucas, L.J.2
  • 42
    • 0742288411 scopus 로고    scopus 로고
    • The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors
    • Yohannan S, Faham S, Yang D, Whitelegge JP, Bowie JU. The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors. Proc Natl Acad Sci USA 2004;101:959-963.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 959-963
    • Yohannan, S.1    Faham, S.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 45
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    • Balashov SP, Imasheva ES, Govindjee R, Ebrey TG. Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys J 1996;70:473-481.
    • (1996) Biophys J , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 46
    • 0024977340 scopus 로고
    • Retinal isomer ratio in dark-adapted purple membrane and bacteriorhodopsin monomers
    • Scherrer P, Mathew MK, Sperling W, Stoeckenius W. Retinal isomer ratio in dark-adapted purple membrane and bacteriorhodopsin monomers. Biochemistry 1989;28:829-834.
    • (1989) Biochemistry , vol.28 , pp. 829-834
    • Scherrer, P.1    Mathew, M.K.2    Sperling, W.3    Stoeckenius, W.4
  • 47
    • 0027940310 scopus 로고
    • Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and e and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles
    • Alexiev U, Marti T, Heyn MP, Khorana HG, Scherrer P. Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles. Biochemistry 1994; 33:13693-13699.
    • (1994) Biochemistry , vol.33 , pp. 13693-13699
    • Alexiev, U.1    Marti, T.2    Heyn, M.P.3    Khorana, H.G.4    Scherrer, P.5
  • 48
    • 0026725522 scopus 로고
    • Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle
    • Heberle J, Dencher NA. Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle. Proc Natl Acad Sci USA 1992;89: 5996-6000.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5996-6000
    • Heberle, J.1    Dencher, N.A.2
  • 49
    • 0029665673 scopus 로고    scopus 로고
    • A linkage of the pKa's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • Richter HT, Brown LS, Needleman R, Lanyi JK. A linkage of the pKa's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry 1996;35:4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 50
    • 1542357653 scopus 로고    scopus 로고
    • Conformational and molecular modeling studies of beta-cyclodextrin- heptagastrin and the third extracellular loop of the cholecystokinin 2 receptor
    • Giragossian C, Schaschke N, Moroder L, Mierke DF. Conformational and molecular modeling studies of beta-cyclodextrin-heptagastrin and the third extracellular loop of the cholecystokinin 2 receptor. Biochemistry 2004;43:2724-2731.
    • (2004) Biochemistry , vol.43 , pp. 2724-2731
    • Giragossian, C.1    Schaschke, N.2    Moroder, L.3    Mierke, D.F.4
  • 51
    • 0034257936 scopus 로고    scopus 로고
    • Structure of tuberoinfundibular peptide of 39 residues
    • Piserchio A, Usdin T, Mierke DF. Structure of tuberoinfundibular peptide of 39 residues. J Biol Chem 2000;275:27284-27290.
    • (2000) J Biol Chem , vol.275 , pp. 27284-27290
    • Piserchio, A.1    Usdin, T.2    Mierke, D.F.3
  • 52
    • 0030841110 scopus 로고    scopus 로고
    • Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin
    • Yeagle PL, Alderfer JL, Albert AD. Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin. Biochemistry 1997;36:9649-9654.
    • (1997) Biochemistry , vol.36 , pp. 9649-9654
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 53
    • 0028804818 scopus 로고
    • The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin
    • Adler M, Seto MH, Nitecki DE, Lin JH, Light DR, Morser J. The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin. J Biol Chem 1995;270:23366-23372.
    • (1995) J Biol Chem , vol.270 , pp. 23366-23372
    • Adler, M.1    Seto, M.H.2    Nitecki, D.E.3    Lin, J.H.4    Light, D.R.5    Morser, J.6
  • 54
    • 0033229834 scopus 로고    scopus 로고
    • Expression, purification, and structural characterization of the bacteriorhodopsin-aspartyl transcarbamylase fusion protein
    • Turner GJ, Miercke LJ, Mitra AK, Stroud RM, Betlach MC, Winter-Vann A. Expression, purification, and structural characterization of the bacteriorhodopsin-aspartyl transcarbamylase fusion protein. Protein Expr Purif 1999;17:324-338.
    • (1999) Protein Expr Purif , vol.17 , pp. 324-338
    • Turner, G.J.1    Miercke, L.J.2    Mitra, A.K.3    Stroud, R.M.4    Betlach, M.C.5    Winter-Vann, A.6
  • 55
    • 0027401509 scopus 로고
    • Homologous overexpression of a light-driven anion pump in an archaebacterium
    • Heymann JA, Havelka WA, Oesterhelt D. Homologous overexpression of a light-driven anion pump in an archaebacterium. Mol Microbiol 1993;7:623-630.
    • (1993) Mol Microbiol , vol.7 , pp. 623-630
    • Heymann, J.A.1    Havelka, W.A.2    Oesterhelt, D.3
  • 56
    • 0032938307 scopus 로고    scopus 로고
    • Saturation mutagenesis of the TATA box: And upstream activator sequence in the haloarchaeal bop gene promoter
    • Baliga NS, DasSarma S. Saturation mutagenesis of the TATA box: and upstream activator sequence in the haloarchaeal bop gene promoter. J Bacteriol 1999;181:2513-2518.
    • (1999) J Bacteriol , vol.181 , pp. 2513-2518
    • Baliga, N.S.1    Dassarma, S.2
  • 57
    • 0026558591 scopus 로고
    • Association of the halobacterial 7S RNA to the polysome correlates with expression of the membrane protein bacterioopsin
    • Gropp R, Gropp F, Betlach MC. Association of the halobacterial 7S RNA to the polysome correlates with expression of the membrane protein bacterioopsin. Proc Natl Acad Sci USA 1992;89:1204-1208.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1204-1208
    • Gropp, R.1    Gropp, F.2    Betlach, M.C.3
  • 58
    • 0025875784 scopus 로고
    • Expression of the bop gene cluster of Halobacterium halobium is induced by low oxygen tension and by light
    • Shand RF, Betlach MC. Expression of the bop gene cluster of Halobacterium halobium is induced by low oxygen tension and by light. J Bacteriol 1991;173:4692-4699.
    • (1991) J Bacteriol , vol.173 , pp. 4692-4699
    • Shand, R.F.1    Betlach, M.C.2
  • 59
    • 0033602998 scopus 로고    scopus 로고
    • Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin
    • Brown LS, Needleman R, Lanyi JK. Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin. Biochemistry 1999;38:6855-6861.
    • (1999) Biochemistry , vol.38 , pp. 6855-6861
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3
  • 60
    • 0036681347 scopus 로고    scopus 로고
    • Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the reprotonation mechanism
    • Martinez LC, Thurmond RL, Jones PG, Turner GJ. Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the reprotonation mechanism. Proteins 2002; 48:269-282.
    • (2002) Proteins , vol.48 , pp. 269-282
    • Martinez, L.C.1    Thurmond, R.L.2    Jones, P.G.3    Turner, G.J.4
  • 61
    • 0035957510 scopus 로고    scopus 로고
    • Structure and function in bacteriorhodopsin: The role of the interhelical loops in the folding and stability of bacteriorhodopsin
    • Kim JM, Booth PJ, Allen SJ, Khorana HG. Structure and function in bacteriorhodopsin: the role of the interhelical loops in the folding and stability of bacteriorhodopsin. J Mol Biol 2001;308:409-422.
    • (2001) J Mol Biol , vol.308 , pp. 409-422
    • Kim, J.M.1    Booth, P.J.2    Allen, S.J.3    Khorana, H.G.4
  • 62
    • 0035957523 scopus 로고    scopus 로고
    • Structure and function in bacteriorhodopsin: The effect of the interhelical loops on the protein folding kinetics
    • Allen SJ, Kim JM, Khorana HG, Lu H, Booth PJ. Structure and function in bacteriorhodopsin: the effect of the interhelical loops on the protein folding kinetics. J Mol Biol 2001;308:423-435.
    • (2001) J Mol Biol , vol.308 , pp. 423-435
    • Allen, S.J.1    Kim, J.M.2    Khorana, H.G.3    Lu, H.4    Booth, P.J.5
  • 63
    • 0034212219 scopus 로고    scopus 로고
    • Solution structure of the loops of bacteriorhodopsin closely resembles the crystal structure
    • Katragadda M, Alderfer JL, Yeagle PL. Solution structure of the loops of bacteriorhodopsin closely resembles the crystal structure. Biochim Biophys Acta 2000;1466:1-6.
    • (2000) Biochim Biophys Acta , vol.1466 , pp. 1-6
    • Katragadda, M.1    Alderfer, J.L.2    Yeagle, P.L.3
  • 64
    • 0025830694 scopus 로고
    • Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure
    • Gilles-Gonzalez MA, Engelman DM, Khorana HG. Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure. J Biol Chem 1991;266:8545-8550.
    • (1991) J Biol Chem , vol.266 , pp. 8545-8550
    • Gilles-Gonzalez, M.A.1    Engelman, D.M.2    Khorana, H.G.3
  • 66
    • 0026469352 scopus 로고
    • Subtype-selective desensitization of alpha 2-adrenergic receptors. Different mechanisms control short and long term agonist-promoted desensitization of alpha 2C10, alpha 2C4, and alpha 2C2
    • Eason MG, Liggett SB. Subtype-selective desensitization of alpha 2-adrenergic receptors. Different mechanisms control short and long term agonist-promoted desensitization of alpha 2C10, alpha 2C4, and alpha 2C2. J Biol Chem 1992;267:25473-25479.
    • (1992) J Biol Chem , vol.267 , pp. 25473-25479
    • Eason, M.G.1    Liggett, S.B.2
  • 67
    • 0028973233 scopus 로고
    • Identification of a Gs coupling domain in the amino terminus of the third intracellular loop of the alpha 2A-adrenergic receptor. Evidence for distinct structural determinants that confer Gs versus Gi coupling
    • Eason MG, Liggett SB. Identification of a Gs coupling domain in the amino terminus of the third intracellular loop of the alpha 2A-adrenergic receptor. Evidence for distinct structural determinants that confer Gs versus Gi coupling. J Biol Chem 1995;270: 24753-24760.
    • (1995) J Biol Chem , vol.270 , pp. 24753-24760
    • Eason, M.G.1    Liggett, S.B.2
  • 68
    • 0026756371 scopus 로고
    • Sites in the third intracellular loop of the alpha 2A-adrenergic receptor confer short term agonist-promoted desensitization. Evidence for a receptor kinase-mediated mechanism
    • Liggett SB, Ostrowski J, Chesnut LC, Kurose H, Raymond JR, Caron MG, Lefkowitz RJ. Sites in the third intracellular loop of the alpha 2A-adrenergic receptor confer short term agonist-promoted desensitization. Evidence for a receptor kinase-mediated mechanism. J Biol Chem 1992;267:4740-4746.
    • (1992) J Biol Chem , vol.267 , pp. 4740-4746
    • Liggett, S.B.1    Ostrowski, J.2    Chesnut, L.C.3    Kurose, H.4    Raymond, J.R.5    Caron, M.G.6    Lefkowitz, R.J.7
  • 69
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 1996;274:768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 71
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • Radzwill N, Gerwert K, Steinhoff HJ. Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin. Biophys J 2001;80:2856-2866
    • (2001) Biophys J , vol.80 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.J.3
  • 72
    • 0037414446 scopus 로고    scopus 로고
    • Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: A time-resolved fluorescence depolarization study
    • Alexiev U, Rimke I, Pohlmann T. Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: a time-resolved fluorescence depolarization study. J Mol Biol 2003;328:705-719.
    • (2003) J Mol Biol , vol.328 , pp. 705-719
    • Alexiev, U.1    Rimke, I.2    Pohlmann, T.3
  • 73
    • 0036299067 scopus 로고    scopus 로고
    • Conformational change of the E-F interhelical loop in the M photointermediate of bacteriorhodopsin
    • Brown LS, Needleman R, Lanyi JK. Conformational change of the E-F interhelical loop in the M photointermediate of bacteriorhodopsin. J Mol Biol 2002;317:471-478.
    • (2002) J Mol Biol , vol.317 , pp. 471-478
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3


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