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Volumn 266, Issue 3, 1997, Pages 559-575

Genetic interactions among the transmembrane segments of the G protein coupled receptor encoded by the yeast STE2 gene

Author keywords

G protein coupled receptor; Intragenic suppressor; Mating pheromone; Membrane protein; factor receptor

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MATING HORMONE ALPHA FACTOR; MEMBRANE RECEPTOR;

EID: 0031588691     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0816     Document Type: Article
Times cited : (43)

References (69)
  • 1
    • 0027506471 scopus 로고
    • The probable arrangement of helices in G protein-coupled receptors
    • Baldwin J. M. The probable arrangement of helices in G protein-coupled receptors. EMBO J. 12:1993;1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 2
    • 0028556727 scopus 로고
    • Signal propogation and regulation in the mating pheromone response pathway of the yeast
    • Bardwell L., Cook J. G., Inouye C. J., Thorner J. Signal propogation and regulation in the mating pheromone response pathway of the yeast. Saccharomyces cerevisiae. Dev. Biol. 166:1994;363-379.
    • (1994) Saccharomyces Cerevisiae. Dev. Biol. , vol.166 , pp. 363-379
    • Bardwell, L.1    Cook, J.G.2    Inouye, C.J.3    Thorner, J.4
  • 3
    • 0026080521 scopus 로고
    • Receptor G-protein signaling in yeast
    • Blumer K. J., Thorner J. Receptor G-protein signaling in yeast. Annu. Rev. Physiol. 53:1991;37-57.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 37-57
    • Blumer, K.J.1    Thorner, J.2
  • 4
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative, and single stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud N., Ozier-Kalogeropoulos O., Li G., Labouesse M., Minvielle-Sebastia L., Lacroute F. A family of low and high copy replicative, integrative, and single stranded S. cerevisiae/E. coli shuttle vectors. Yeast. 7:1991;609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 5
    • 0028674459 scopus 로고
    • Biochemical and genetic methods for analyzing specificity and activity of a precursor-processing enzyme: Yeast kex2 protease, kexin
    • Brenner C., Bevan A., Fuller R. S. Biochemical and genetic methods for analyzing specificity and activity of a precursor-processing enzyme: yeast kex2 protease, kexin. Methods Enzymol. 244:1994;152-167.
    • (1994) Methods Enzymol. , vol.244 , pp. 152-167
    • Brenner, C.1    Bevan, A.2    Fuller, R.S.3
  • 6
    • 0020040057 scopus 로고
    • Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and α factor pheromones
    • Chan R. K., Otte C. A. Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and α factor pheromones. Mol. Cell. Biol. 2:1982;11-20.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 11-20
    • Chan, R.K.1    Otte, C.A.2
  • 7
    • 0028286250 scopus 로고
    • Systematicv mutagenesis of the yeast mating pheromone receptor third intracellular loop
    • Clark C. D., Palzkill P., Botstein D. Systematicv mutagenesis of the yeast mating pheromone receptor third intracellular loop. J. Biol. Chem. 269:1994;8831-8841.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8831-8841
    • Clark, C.D.1    Palzkill, P.2    Botstein, D.3
  • 8
    • 0343170500 scopus 로고
    • Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine to isoleucine replacement at position 57
    • Das G, Hickey D., McLendon D., McLendon G., Sherman F. Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine to isoleucine replacement at position 57. Proc. Natl Acad. Sci. USA. 86:1989;496-499.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 496-499
    • Das, G.1    Hickey, D.2    McLendon, D.3    McLendon, G.4    Sherman, F.5
  • 9
    • 0023460928 scopus 로고
    • Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: A model for desensitization to pheromone
    • Dietzel C., Kurjan J. Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: a model for desensitization to pheromone. Mol. Cell. Biol. 7:1987;4169-4177.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4169-4177
    • Dietzel, C.1    Kurjan, J.2
  • 10
  • 12
    • 0029907599 scopus 로고    scopus 로고
    • Requirement for rigid body motion of transmembrane helices of light activation of rhodopsin
    • Farens D. L., Altenbach C., Yang K., Hubbell W., Khorana G. Requirement for rigid body motion of transmembrane helices of light activation of rhodopsin. Science. 274:1996;768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.4    Khorana, G.5
  • 13
    • 0024266139 scopus 로고
    • New yeast- Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Geitz R. D., Sugino A. New yeast- Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene. 74:1988;527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Geitz, R.D.1    Sugino, A.2
  • 15
    • 0028829235 scopus 로고
    • Automated method for modeling seven-helix transmembrane receptors from experimental data
    • Herzyk P., Hubbard R. E. Automated method for modeling seven-helix transmembrane receptors from experimental data. Biophys. J. 69:1995;2419-2442.
    • (1995) Biophys. J. , vol.69 , pp. 2419-2442
    • Herzyk, P.1    Hubbard, R.E.2
  • 16
    • 0025881062 scopus 로고
    • Three-dimensional models of neurotransmitter G-binding protein-coupled receptors
    • Hibert M. F., Trumpp-Kallmeyer S., Bruinvels A., Hoflack J. Three-dimensional models of neurotransmitter G-binding protein-coupled receptors. Mol. Pharmacol. 40:1991;8-15.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 8-15
    • Hibert, M.F.1    Trumpp-Kallmeyer, S.2    Bruinvels, A.3    Hoflack, J.4
  • 18
    • 0025634390 scopus 로고
    • Information content of amino acid residues in putative helix VIII of the lac permease from Escherichia coli
    • Hinkle P. C., Hinkle P. V., Kaback H. R. Information content of amino acid residues in putative helix VIII of the lac permease from Escherichia coli. Biochemistry. 29:1990;10989-10994.
    • (1990) Biochemistry , vol.29 , pp. 10989-10994
    • Hinkle, P.C.1    Hinkle, P.V.2    Kaback, H.R.3
  • 19
    • 0026661891 scopus 로고
    • 1-ATPase from Escherichia coli: Implications for structure
    • 1-ATPase from Escherichia coli: implications for structure. Proc. Natl Acad. Sci. USA. 89:1992;9799-9803.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9799-9803
    • Howitt, S.M.1    Cox, G.B.2
  • 23
    • 0026087282 scopus 로고
    • The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of E. coli
    • King S. C., Hansen C. L., Wilson H. The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of E. coli. Biochim. Biophys. Acta. 1026:1991;177-186.
    • (1991) Biochim. Biophys. Acta , vol.1026 , pp. 177-186
    • King, S.C.1    Hansen, C.L.2    Wilson, H.3
  • 24
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodzief P. A., Young R. A. Epitope tagging and protein surveillance. Methods Enzymol. 194:1991;508-519.
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodzief, P.A.1    Young, R.A.2
  • 25
    • 0026178033 scopus 로고
    • Genetic fine-structural analysis of the Saccharomyces cerevisiaeα-pheromone receptor
    • Konopka J. B., Jenness D. D. Genetic fine-structural analysis of the Saccharomyces cerevisiaeα-pheromone receptor. Cell Regulation. 2:1991;439-452.
    • (1991) Cell Regulation , vol.2 , pp. 439-452
    • Konopka, J.B.1    Jenness, D.D.2
  • 26
    • 0023724429 scopus 로고
    • The C-terminus of the S. cerevisiaeα pheromone receptor mediates an adaptive response to pheromone
    • Konopka J. B., Jenness D. D., Hartwell L. H. The C-terminus of the S. cerevisiaeα pheromone receptor mediates an adaptive response to pheromone. Cell. 54:1988;609-620.
    • (1988) Cell , vol.54 , pp. 609-620
    • Konopka, J.B.1    Jenness, D.D.2    Hartwell, L.H.3
  • 27
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;488-492.
    • (1987) Methods Enzymol. , vol.154 , pp. 488-492
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 28
    • 85030289596 scopus 로고
    • PhD dissertation, University of Rochester, Rochester, NY
    • Laz, T. M. 1988, PhD dissertation, University of Rochester, Rochester, NY.
    • (1988)
    • Laz, T.M.1
  • 30
    • 0026757193 scopus 로고
    • Possible salt bridges between transmembrane α-helices of the lactose carrier of E. coli
    • Lee J.-I., Hwang P. P., Hansen C., Wilson T. H. Possible salt bridges between transmembrane α-helices of the lactose carrier of E. coli. J. Biol. Chem. 267:1992;20758-20764.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20758-20764
    • Lee, J.-I.1    Hwang, P.P.2    Hansen, C.3    Wilson, T.H.4
  • 31
    • 0025258442 scopus 로고
    • A simple procedure for maximum yield of high-quality plasmid DNA
    • Lee S.-Y., Rashid S. A simple procedure for maximum yield of high-quality plasmid DNA. BioTechniques. 9:1990;676-679.
    • (1990) BioTechniques , vol.9 , pp. 676-679
    • Lee, S.-Y.1    Rashid, S.2
  • 33
    • 0028965496 scopus 로고
    • Long-range, small magnitude nonadditivity of mutational effects in proteins
    • LiCata V. J., Ackers G. K. Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry. 34:1995;3133-3139.
    • (1995) Biochemistry , vol.34 , pp. 3133-3139
    • Licata, V.J.1    Ackers, G.K.2
  • 34
    • 0029096818 scopus 로고
    • Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors
    • Liu J., Schoneberg T., van Rhee M., Wess J. Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors. J. Biol. Chem. 270:1995;19532-19539.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19532-19539
    • Liu, J.1    Schoneberg, T.2    Van Rhee, M.3    Wess, J.4
  • 35
    • 0026681102 scopus 로고
    • 2adrenergic receptor protein based on computer modeling studies
    • 2adrenergic receptor protein based on computer modeling studies. J. Mol. Biol. 225:1992;859-871.
    • (1992) J. Mol. Biol. , vol.225 , pp. 859-871
    • Maloneyhuss, K.1    Lybrand, T.P.2
  • 36
    • 0028076771 scopus 로고
    • Genetic studies of the lac repressor: XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues as well as "spacers" which do not require a specific sequence
    • Markiewicz P., Kleina L. G., Cruz C., Ehret S., Miller J. H. Genetic studies of the lac repressor: XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues as well as "spacers" which do not require a specific sequence. J. Mol. Biol. 240:1994;421-433.
    • (1994) J. Mol. Biol. , vol.240 , pp. 421-433
    • Markiewicz, P.1    Kleina, L.G.2    Cruz, C.3    Ehret, S.4    Miller, J.H.5
  • 37
    • 0026761601 scopus 로고
    • Substitutions in the hydrophobic core of the α-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluveriα-factor and to antagonist
    • Marsh L. Substitutions in the hydrophobic core of the α-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluveriα-factor and to antagonist. Mol. Cell. Biol. 12:1992;3959-3966.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3959-3966
    • Marsh, L.1
  • 38
    • 0023395343 scopus 로고
    • Identification and regulation of a gene required for cell fusion during mating of the yeast Saccharomyces cerevisiae
    • McCaffrey G., Clay F. J., Kelsay K., Sprague G. Identification and regulation of a gene required for cell fusion during mating of the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 7:1987;2680-2690.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2680-2690
    • McCaffrey, G.1    Clay, F.J.2    Kelsay, K.3    Sprague, G.4
  • 40
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad D., Hunter R., Parker R. A rapid method for localized mutagenesis of yeast genes. Yeast. 8:1992;79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 41
    • 0027263492 scopus 로고
    • Characterization of yeast plasma membrane H-ATPase mutant pma-A135V and its revertants
    • Na S., Perlin D. S., Seto-Young D., Wang G., Haber J. Characterization of yeast plasma membrane H-ATPase mutant pma-A135V and its revertants. J. Biol. Chem. 268:1993;11792-11797.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11792-11797
    • Na, S.1    Perlin, D.S.2    Seto-Young, D.3    Wang, G.4    Haber, J.5
  • 43
    • 0026605299 scopus 로고
    • Determination of transmembrane protein structure by disulfide cross-linking: The E. coli Tar receptor
    • Pakula A. A., Simon M. Determination of transmembrane protein structure by disulfide cross-linking: the E. coli Tar receptor. Proc. Natl Acad. Sci. USA. 89:1992;4144-4148.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4144-4148
    • Pakula, A.A.1    Simon, M.2
  • 44
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane α-helices as autonomous folding domains
    • Popot J.-L. Integral membrane protein structure: transmembrane α-helices as autonomous folding domains. Curr. Opn. Struct. Biol. 3:1993;532-540.
    • (1993) Curr. Opn. Struct. Biol. , vol.3 , pp. 532-540
    • Popot, J.-L.1
  • 45
    • 0028840683 scopus 로고
    • Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway
    • Price L. A., Kajkowski E. M., Hadcock J. R., Ozenberger B. A., Pausch M. H. Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway. Mol. Cell. Biol. 15:1995;6188-6195.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6188-6195
    • Price, L.A.1    Kajkowski, E.M.2    Hadcock, J.R.3    Ozenberger, B.A.4    Pausch, M.H.5
  • 46
    • 0024297275 scopus 로고
    • Peptide analogues compete with the binding of α-factor to its receptor in Saccharomyces cerevisiae
    • Raths S. K., Naider F., Becker J. M. Peptide analogues compete with the binding of α-factor to its receptor in Saccharomyces cerevisiae. J. Biol. Chem. 263:1988;17333-17341.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17333-17341
    • Raths, S.K.1    Naider, F.2    Becker, J.M.3
  • 47
    • 0024294018 scopus 로고
    • The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain
    • Reneke J. E., Blumer K. J., Courchesne W. E., Thorner J. The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain. Cell. 55:1988;221-234.
    • (1988) Cell , vol.55 , pp. 221-234
    • Reneke, J.E.1    Blumer, K.J.2    Courchesne, W.E.3    Thorner, J.4
  • 48
    • 0028931922 scopus 로고
    • In vivo assembly of rhodopsin from expressed polypeptide fragments
    • Ridge K. D., Lee S. S. J., Yao L. L. In vivo assembly of rhodopsin from expressed polypeptide fragments. Proc. Natl Acad. Sci. USA. 92:1995;3204-3208.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3204-3208
    • Ridge, K.D.1    Lee, S.S.J.2    Yao, L.L.3
  • 49
    • 0026767250 scopus 로고
    • Kinesin-related proteins required for assembly of the mitotic spindle
    • Roof D. M., Meluh P. B., Rose M. D. Kinesin-related proteins required for assembly of the mitotic spindle. J. Cell. Biol. 118:1992;95-108.
    • (1992) J. Cell. Biol. , vol.118 , pp. 95-108
    • Roof, D.M.1    Meluh, P.B.2    Rose, M.D.3
  • 51
    • 0026439214 scopus 로고
    • Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli
    • Sahin-Toth M., Dunten R. L., Gonzalez A., Kaback H. R. Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli. Proc. Natl Acad. Sci. USA. 89:1992;10547-10551.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10547-10551
    • Sahin-Toth, M.1    Dunten, R.L.2    Gonzalez, A.3    Kaback, H.R.4
  • 53
  • 54
    • 0029090142 scopus 로고
    • Proline in a transmembrane helix compensates for cavities in the photosynthetic reaction center
    • Schiffer M., Ainsworth C. F., Deng Y.-L., Johnson G., Pascoe F., Hanson D. K. Proline in a transmembrane helix compensates for cavities in the photosynthetic reaction center. J. Mol. Biol. 252:1995;472-482.
    • (1995) J. Mol. Biol. , vol.252 , pp. 472-482
    • Schiffer, M.1    Ainsworth, C.F.2    Deng, Y.-L.3    Johnson, G.4    Pascoe, F.5    Hanson, D.K.6
  • 55
    • 0028174038 scopus 로고
    • Noncontiguous domains of the α-factor receptor of yeasts confer ligand specificity
    • Sen M., Marsh L. Noncontiguous domains of the α-factor receptor of yeasts confer ligand specificity. J. Biol. Chem. 269:1994;968-973.
    • (1994) J. Biol. Chem. , vol.269 , pp. 968-973
    • Sen, M.1    Marsh, L.2
  • 56
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh S. P., Zvyaga T. A., Lichtarge O., Sakmar T. P., Bourne H. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature. 383:1996;347-350.
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.5
  • 57
    • 0026654252 scopus 로고
    • Mutational studies of protein structures and stabilities
    • Shortle D. Mutational studies of protein structures and stabilities. Quart Rev. Biophys. 25:1992;205-250.
    • (1992) Quart Rev. Biophys. , vol.25 , pp. 205-250
    • Shortle, D.1
  • 58
    • 0021968408 scopus 로고
    • Genetic analysis of staphlococcal nuclease: Identification of three intragenic "global" suppressors of nuclease-minus mutants
    • Shortle D., Lin B. Genetic analysis of staphlococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutants. Genetics. 110:1985;539-555.
    • (1985) Genetics , vol.110 , pp. 539-555
    • Shortle, D.1    Lin, B.2
  • 59
    • 0029785464 scopus 로고    scopus 로고
    • Potential use of additivity of mutational effects in simplifying protein engineering
    • Skinner M. M., Terwilliger T. C. Potential use of additivity of mutational effects in simplifying protein engineering. Proc. Natl Acad. Sci. USA. 93:1996;10753-10757.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10753-10757
    • Skinner, M.M.1    Terwilliger, T.C.2
  • 60
    • 33751156442 scopus 로고
    • Site-specificity of the second-site suppressor mutation of the Asp-285 to Asn mutant of metal-tetracycline/Hantiporter of Escherichia coli and the effects of amino acid substitutions at the first and second sites
    • Someya Y., Niwa A., Sawai T., Yamaguchi A. Site-specificity of the second-site suppressor mutation of the Asp-285 to Asn mutant of metal-tetracycline/Hantiporter of Escherichia coli and the effects of amino acid substitutions at the first and second sites. Biochemistry. 34:1995;7-12.
    • (1995) Biochemistry , vol.34 , pp. 7-12
    • Someya, Y.1    Niwa, A.2    Sawai, T.3    Yamaguchi, A.4
  • 61
    • 0025971103 scopus 로고
    • Assay of yeast mating reaction
    • Sprague G. Assay of yeast mating reaction. Methods Enzymol. 194:1991;77-93.
    • (1991) Methods Enzymol. , vol.194 , pp. 77-93
    • Sprague, G.1
  • 62
    • 0027434008 scopus 로고
    • Generation of temperature-sensitive cbp1 strains of Saccharomyces cerevisiae by PCR mutagenesis and in vivo recombination: Characteristics of the mutant strains imply that CBP1 is involved in stabilization and processing of cytochrome b pre-mRNA
    • Staples R. R., Diekman C. L. Generation of temperature-sensitive cbp1 strains of Saccharomyces cerevisiae by PCR mutagenesis and in vivo recombination: characteristics of the mutant strains imply that CBP1 is involved in stabilization and processing of cytochrome b pre-mRNA. Genetics. 135:1992;981-991.
    • (1992) Genetics , vol.135 , pp. 981-991
    • Staples, R.R.1    Diekman, C.L.2
  • 63
    • 0026071908 scopus 로고
    • Structure/function relationship of proteins belonging to the family of receptors coupled to GTP-binding proteins
    • Strosberg A. D. Structure/function relationship of proteins belonging to the family of receptors coupled to GTP-binding proteins. Eur. J. Biochem. 196:1991;1-10.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 1-10
    • Strosberg, A.D.1
  • 64
    • 0026592867 scopus 로고
    • Identification of intramolecular interactions in adrenergic receptors
    • Suryanarayana S., von Zastrow M., Kobilka B. K. Identification of intramolecular interactions in adrenergic receptors. J. Biol. Chem. 267:1992;21991-21994.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21991-21994
    • Suryanarayana, S.1    Von Zastrow, M.2    Kobilka, B.K.3
  • 65
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • Unger V. M., Schertler G. F. X. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68:1995;1776-1786.
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.X.2
  • 66
    • 0030025319 scopus 로고    scopus 로고
    • Exploring the allowed sequence space of a membrane protein
    • Wen J., Chen X., Bowie J. U. Exploring the allowed sequence space of a membrane protein. Nature Struct. Biol. 3:1996;141-148.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 141-148
    • Wen, J.1    Chen, X.2    Bowie, J.U.3
  • 67
    • 0027317361 scopus 로고
    • Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping
    • Whitley P., Nilsson L., von Heijne G. Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping. Biochemistry. 32:1993;8534-8539.
    • (1993) Biochemistry , vol.32 , pp. 8534-8539
    • Whitley, P.1    Nilsson, L.2    Von Heijne, G.3
  • 68
    • 0029897724 scopus 로고    scopus 로고
    • MRNA sequences influencing translation and the selection of AUG initiator codons in the yeast Saccharomyces cerevisiae
    • Yun D.-F., Laz T. M., Clements J. M., Sherman F. mRNA sequences influencing translation and the selection of AUG initiator codons in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 19:1996;1225-1239.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1225-1239
    • Yun, D.-F.1    Laz, T.M.2    Clements, J.M.3    Sherman, F.4


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