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Volumn 17, Issue 42007, 1997, Pages 29-56

Introductory lecture: In vitro translation analysis of integral membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); BILE ACID; CHOLECYSTOKININ; CHOLECYSTOKININ A RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN;

EID: 0031016851     PISSN: 10799893     EISSN: None     Source Type: Journal    
DOI: 10.3109/10799899709036593     Document Type: Article
Times cited : (13)

References (70)
  • 1
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982; 157: 105 – 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 2
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg D., Schwarz E., Komaromy M., Wall R. J. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 1984; 179: 125 – 142
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.J.4
  • 3
    • 0022371456 scopus 로고
    • Amino acid sequence of the Ca2+ Mg2+ dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • MacLennan D. H., Brandl C. J., Koreczak B., Green N. M. Amino acid sequence of the Ca2+ Mg2+ dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 1985; 316: 696 – 700
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Koreczak, B.3    Green, N.M.4
  • 4
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron-cryo-microscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron-cryo-microscopy. J. Mol. Biol. 1990; 213: 899 – 929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 5
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G. F. X., Villa C., Henderson R. Projection structure of rhodopsin. Nature 1993; 362: 770 – 772
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 6
    • 0028962270 scopus 로고
    • Low resolution of bovine Rhodopsin determined by electro-cryo-microscopy
    • Vinzenz M. U., Schertler G. F. X. Low resolution of bovine Rhodopsin determined by electro-cryo-microscopy. Biophys. J. 1995; 68: 1776 – 1786
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Vinzenz, M.U.1    Schertler, G.F.X.2
  • 7
    • 0023645822 scopus 로고
    • Crystallization and preliminary X-ray and optical spectroscopic characterization of the photochemical reaction center from Rhodobacter sphaeroides strain 2.4.1
    • Frank H. A., Taremi S. S., Knox J. R. Crystallization and preliminary X-ray and optical spectroscopic characterization of the photochemical reaction center from Rhodobacter sphaeroides strain 2.4.1. J. Mol. Biol. 1987; 198: 139 – 141
    • (1987) J. Mol. Biol. , vol.198 , pp. 139-141
    • Frank, H.A.1    Taremi, S.S.2    Knox, J.R.3
  • 8
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 1995; 376: 660 – 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 9
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • (erratum: Nature 363, 286, 1993).
    • Toyoshima C., Sasabe H., Stokes D. L. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 1993; 362: 467 – 471, (erratum: Nature 363, 286, 1993).
    • (1993) Nature , vol.362 , pp. 467-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 10
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss M. S., Abele U., Weckesser J., Welte W., Schiltz E., Schulz G. E. Molecular architecture and electrostatic properties of a bacterial porin. Science 1991; 254: 1627 – 1630
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 11
    • 0028167849 scopus 로고
    • Beta-structure in the membrane-spanning part of the nicotinic acetylcholine receptor (or how helical are transmembrane helices?)
    • Hucho F., Gorne-Tschelnokow U., Strecker A. Beta-structure in the membrane-spanning part of the nicotinic acetylcholine receptor (or how helical are transmembrane helices?). Trends Biochem. Sci. 1994; 19: 383 – 387
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 383-387
    • Hucho, F.1    Gorne-Tschelnokow, U.2    Strecker, A.3
  • 12
    • 0027954627 scopus 로고
    • The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β-structures
    • Gorne-Tschelnokow U., Strecker A., Kaduk C., Naumann D., Hucho F. The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β-structures. EMBO J. 1994; 13: 338 – 341
    • (1994) EMBO J. , vol.13 , pp. 338-341
    • Gorne-Tschelnokow, U.1    Strecker, A.2    Kaduk, C.3    Naumann, D.4    Hucho, F.5
  • 13
    • 0027151857 scopus 로고
    • The site of action of pantoprazol in the gastric H/K ATPase
    • Shin J. M., Besancon M., Simon A., Sachs G. The site of action of pantoprazol in the gastric H/K ATPase. Biochim. Biophys. Acta 1993; 1148: 223 – 233
    • (1993) Biochim. Biophys. Acta , vol.1148 , pp. 223-233
    • Shin, J.M.1    Besancon, M.2    Simon, A.3    Sachs, G.4
  • 14
    • 0001347857 scopus 로고
    • Biochemical identification of transmembrane segments of the Ca2+-ATPase of sarcoplasmic reticulum
    • Shin J. M., Kajimura M., Arguello J. M., Kaplan J. H., Sachs G. Biochemical identification of transmembrane segments of the Ca2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 1993; 269: 22533 – 22537
    • (1993) J. Biol. Chem. , vol.269 , pp. 22533-22537
    • Shin, J.M.1    Kajimura, M.2    Arguello, J.M.3    Kaplan, J.H.4    Sachs, G.5
  • 15
    • 0028264177 scopus 로고
    • Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments
    • Shainskaya A., Karlish S. J. Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments. J. Biol. Chem. 1994; 269: 10780 – 10789
    • (1994) J. Biol. Chem. , vol.269 , pp. 10780-10789
    • Shainskaya, A.1    Karlish, S.J.2
  • 16
    • 0027732901 scopus 로고
    • Transmembrane organization of the Na,K-ATPase determined by epitope addition
    • Canfield V. A., Levenson R. Transmembrane organization of the Na,K-ATPase determined by epitope addition. Biochemistry 1993; 32: 13782 – 13786
    • (1993) Biochemistry , vol.32 , pp. 13782-13786
    • Canfield, V.A.1    Levenson, R.2
  • 17
    • 0028138863 scopus 로고
    • Studies on the membrane topology of the Na/K ATPase
    • Yoon K. L., Guidotti G. Studies on the membrane topology of the Na/K ATPase. J. Biol. Chem. 1994; 269: 28249 – 28258
    • (1994) J. Biol. Chem. , vol.269 , pp. 28249-28258
    • Yoon, K.L.1    Guidotti, G.2
  • 18
    • 0026785563 scopus 로고
    • Definition of surface-exposed and trans-membranous regions of the (Ca2+-Mg2+-ATPase of sarcoplasmic reticulum using anti-peptide antibodies
    • Mata A. M., Matthews I., Tunwell R. E., Sharma R. P., Lee A. G., East J. M. Definition of surface-exposed and trans-membranous regions of the (Ca2+-Mg2+-ATPase of sarcoplasmic reticulum using anti-peptide antibodies. Biochem. J. 1992; 286: 567 – 580
    • (1992) Biochem. J. , vol.286 , pp. 567-580
    • Mata, A.M.1    Matthews, I.2    Tunwell, R.E.3    Sharma, R.P.4    Lee, A.G.5    East, J.M.6
  • 19
    • 0025236388 scopus 로고
    • Functional consequences of alterations to polar amino acids located in the transmembrane domain of the Ca-ATPase of the Sarcoplasmic reticulum
    • Clarke D. M., Loo T. W., Maclennan D. M. Functional consequences of alterations to polar amino acids located in the transmembrane domain of the Ca-ATPase of the Sarcoplasmic reticulum. J. Biol. Chem. 1990; 265: 6262 – 6267
    • (1990) J. Biol. Chem. , vol.265 , pp. 6262-6267
    • Clarke, D.M.1    Loo, T.W.2    Maclennan, D.M.3
  • 21
    • 0028233906 scopus 로고
    • Insertional mutagenesis as a probe of rhodopsin's topography, stability and activity
    • Borjigin J., Nathans J. Insertional mutagenesis as a probe of rhodopsin's topography, stability and activity. J. Biol. Chem. 1994; 269: 14715 – 14722
    • (1994) J. Biol. Chem. , vol.269 , pp. 14715-14722
    • Borjigin, J.1    Nathans, J.2
  • 22
    • 0027728991 scopus 로고
    • Site directed mutagenesis of the Na,K ATPase: Consequences of the subtitutions of negatively charged amino acids localized in the transmembrane domains
    • Jewell E. A., Lingrel J. B. Site directed mutagenesis of the Na,K ATPase: Consequences of the subtitutions of negatively charged amino acids localized in the transmembrane domains. Biochemistry 1993; 32: 13523 – 13530
    • (1993) Biochemistry , vol.32 , pp. 13523-13530
    • Jewell, E.A.1    Lingrel, J.B.2
  • 23
    • 0028202511 scopus 로고
    • Analysis of amino acid residues in the H5-H6 transmembrane and extracellular domains of Na,K-ATPase α-subunit identifies theonine 797 as a determinant of ouabain sensitivity
    • Feng J., Lingrel J. B. Analysis of amino acid residues in the H5-H6 transmembrane and extracellular domains of Na,K-ATPase α-subunit identifies theonine 797 as a determinant of ouabain sensitivity. Biochemistry 1994; 33: 4218 – 4224
    • (1994) Biochemistry , vol.33 , pp. 4218-4224
    • Feng, J.1    Lingrel, J.B.2
  • 24
    • 0028816888 scopus 로고
    • Structure-function relationships of cation translocation by Ca2+ and Na,K-ATPases studied by site directed mutagenesis
    • Andersen J., Vilsen B. Structure-function relationships of cation translocation by Ca2+ and Na,K-ATPases studied by site directed mutagenesis. FEBS Letters 1995; 359: 101 – 106
    • (1995) FEBS Letters , vol.359 , pp. 101-106
    • Andersen, J.1    Vilsen, B.2
  • 25
    • 0027263492 scopus 로고
    • Characterization of yeast plasma membrane H+-ATPase mutant pmal-A135V and its revertants
    • Na S., Perlin D. S., Seto-Young D., Wang G., Haber J. E. Characterization of yeast plasma membrane H+-ATPase mutant pmal-A135V and its revertants. J. Biol. Chem. 1993; 268: 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.E.5
  • 26
    • 0026787464 scopus 로고
    • Ouabain-resistant transfectants of the murine ouabain resistance gene contain mutations in the α-subunit of the Na,K-ATPase
    • Cantley L. G., Zhou X. M., Cunha M. J., Epstein J., Cantley L. C. Ouabain-resistant transfectants of the murine ouabain resistance gene contain mutations in the α-subunit of the Na,K-ATPase. J. Biol. Chem. 1992; 267: 17271 – 17278
    • (1992) J. Biol. Chem. , vol.267 , pp. 17271-17278
    • Cantley, L.G.1    Zhou, X.M.2    Cunha, M.J.3    Epstein, J.4    Cantley, L.C.5
  • 27
    • 0027464932 scopus 로고
    • Membrane topology and omeprazole labeling of the gastric H,K-adenosinetriphosphatase
    • Besancon M., Shin J. M., Mercier F., Munson K., Miller M., Hersey S., Sachs G. Membrane topology and omeprazole labeling of the gastric H,K-adenosinetriphosphatase. Biochemistry 1993; 32: 2345 – 2355
    • (1993) Biochemistry , vol.32 , pp. 2345-2355
    • Besancon, M.1    Shin, J.M.2    Mercier, F.3    Munson, K.4    Miller, M.5    Hersey, S.6    Sachs, G.7
  • 28
    • 0025947113 scopus 로고
    • Identification of an extracytoplasmic region of the H,K ATPase labelled by a K-competitive photoinhibitor
    • Munson K. B., Balaji V. N., Ramnayaran K., Sachs G. Identification of an extracytoplasmic region of the H,K ATPase labelled by a K-competitive photoinhibitor. J. Biol. Chem. 1991; 266: 18976 – 18988
    • (1991) J. Biol. Chem. , vol.266 , pp. 18976-18988
    • Munson, K.B.1    Balaji, V.N.2    Ramnayaran, K.3    Sachs, G.4
  • 30
    • 0028977979 scopus 로고
    • Four hydrophobic segments in the NH2-terminal third (H1-H4) of the Na,K-ATPase α-subunit alternately initiate and halt membrane translocation of the newly synthesized polypeptide
    • Xie Y., Morimoto T. Four hydrophobic segments in the NH2-terminal third (H1-H4) of the Na,K-ATPase α-subunit alternately initiate and halt membrane translocation of the newly synthesized polypeptide. J. Biol. Chem. 1995; 270: 11985 – 11991
    • (1995) J. Biol. Chem. , vol.270 , pp. 11985-11991
    • Xie, Y.1    Morimoto, T.2
  • 31
    • 0030029807 scopus 로고
    • Only the first and the last hydrophobic segments in the COOH-terminal third of Na,K-ATPase α-subunit initiate and halt, respectively, membrane translocation of the newly synthesized polypeptide. Implications for the membrane topology
    • Xie Y., Lanhans-Ralasekaran S. A., Bellovino D., Morimito T. J. Only the first and the last hydrophobic segments in the COOH-terminal third of Na,K-ATPase α-subunit initiate and halt, respectively, membrane translocation of the newly synthesized polypeptide. Implications for the membrane topology. Biol. Chem. 1995; 271: 2563 – 2573
    • (1995) Biol. Chem. , vol.271 , pp. 2563-2573
    • Xie, Y.1    Lanhans-Ralasekaran, S.A.2    Bellovino, D.3    Morimito, T.J.4
  • 32
    • 0027444708 scopus 로고
    • Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium
    • Smith D. L., Tao T., Maguire M. E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 1993; 268: 22469 – 22479
    • (1993) J. Biol. Chem. , vol.268 , pp. 22469-22479
    • Smith, D.L.1    Tao, T.2    Maguire, M.E.3
  • 33
    • 0029960789 scopus 로고    scopus 로고
    • Glutamate residues in the second extracellular loop of the human A2a adenosine receptor are required for ligand recognition
    • Kim K., Jiang Q., Glashofer M., Yehle S., Wess J., Jacobson K. A. Glutamate residues in the second extracellular loop of the human A2a adenosine receptor are required for ligand recognition. Mol. Pharmacol. 1996; 49: 683 – 691
    • (1996) Mol. Pharmacol. , vol.49 , pp. 683-691
    • Kim, K.1    Jiang, Q.2    Glashofer, M.3    Yehle, S.4    Wess, J.5    Jacobson, K.A.6
  • 34
    • 0029995284 scopus 로고    scopus 로고
    • Molecular mechanisms involved in muscarinic aetylcholine receptor-mediated G protein activation studied by insertion mutagenesis
    • Liu J., Blin N., Conklin B. R., Wess J. Molecular mechanisms involved in muscarinic aetylcholine receptor-mediated G protein activation studied by insertion mutagenesis. J. Biol. Chem. 1996; 271: 6172 – 6178
    • (1996) J. Biol. Chem. , vol.271 , pp. 6172-6178
    • Liu, J.1    Blin, N.2    Conklin, B.R.3    Wess, J.4
  • 35
    • 0030041761 scopus 로고    scopus 로고
    • Amino acid side chains that define muscarinic receptor/G-protein coupling. Studies of the third intracellular loop
    • Burstein E. S., Spalding T. A., Brann M. R. Amino acid side chains that define muscarinic receptor/G-protein coupling. Studies of the third intracellular loop. Biol. Chem. 1996; 271: 2882 – 2885
    • (1996) Biol. Chem. , vol.271 , pp. 2882-2885
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 37
    • 0028568176 scopus 로고
    • TopPred II: an improtved software for membrane protein structure predictions
    • Claros M. G., von Heijne G. TopPred II: an improtved software for membrane protein structure predictions. Comput. Appl. Biosci. 1994; 10: 685 – 686
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    von Heijne, G.2
  • 38
    • 0022358406 scopus 로고
    • Bovine opsine has more than one signal sequence
    • Friedlander M., Blobel G. Bovine opsine has more than one signal sequence. Nature 1985; 318: 338 – 343
    • (1985) Nature , vol.318 , pp. 338-343
    • Friedlander, M.1    Blobel, G.2
  • 39
    • 0029077235 scopus 로고
    • Plasma membrane localization and fonctionnal rescue of truncated forms of a G-protein coupled receptor
    • Schöneberg T., Liu J., Wess J. Plasma membrane localization and fonctionnal rescue of truncated forms of a G-protein coupled receptor. J. Biol. Chem. 1995; 270: 18000 – 18006
    • (1995) J. Biol. Chem. , vol.270 , pp. 18000-18006
    • Schöneberg, T.1    Liu, J.2    Wess, J.3
  • 40
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of proteine translocation across membranes
    • Schatz G., Dobberstein B. Common principles of proteine translocation across membranes. Science 1996; 271: 1519 – 1526
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 42
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels H. P., Spiess M. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 1988; 55: 61 – 70
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.P.1    Spiess, M.2
  • 43
    • 0027935404 scopus 로고
    • In vitro translation and membrane topology of the rat recombinant mGliR1α
    • Seal A. J., Collingridge G. L., Hemley J. M. In vitro translation and membrane topology of the rat recombinant mGliR1α. Neuropharmarcology 1994; 33: 1065 – 1070
    • (1994) Neuropharmarcology , vol.33 , pp. 1065-1070
    • Seal, A.J.1    Collingridge, G.L.2    Hemley, J.M.3
  • 44
    • 0028175016 scopus 로고
    • Topological frustration in multispanning E. coli inner membrane proteins
    • Gafvelin G., von Heijne G. Topological frustration in multispanning E. coli inner membrane proteins. Cell 1994; 77: 401 – 412
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    von Heijne, G.2
  • 45
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 1992; 225: 487 – 494
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 46
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne G., Gavel Y. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 1988; 174: 671 – 678
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • von Heijne, G.1    Gavel, Y.2
  • 47
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann E., Rapoport T. A., Lodish H. F. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 1989; 86: 5786 – 5790
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 48
    • 0028341737 scopus 로고
    • Reversible topology of a bifunctional transmembrane protein
    • Kim H., Paul S., Jennity J., Inouye M. Reversible topology of a bifunctional transmembrane protein. Mol. Microbiol. 1994; 11: 819 – 831
    • (1994) Mol. Microbiol. , vol.11 , pp. 819-831
    • Kim, H.1    Paul, S.2    Jennity, J.3    Inouye, M.4
  • 49
    • 0028361579 scopus 로고
    • Topological analysis of the HK ATPase using in vitro translation
    • Bamberg K., Sachs G. Topological analysis of the HK ATPase using in vitro translation. J. Biol. Chem. 1994; 269: 16909 – 16919
    • (1994) J. Biol. Chem. , vol.269 , pp. 16909-16919
    • Bamberg, K.1    Sachs, G.2
  • 50
    • 0025054302 scopus 로고
    • Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins
    • Brasseur R., Vanderbranden M., Cornet B., Burny A., Ruysschaert J. M. Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins. Biochim. Biophys. Acta 1990; 1029: 267 – 273
    • (1990) Biochim. Biophys. Acta , vol.1029 , pp. 267-273
    • Brasseur, R.1    Vanderbranden, M.2    Cornet, B.3    Burny, A.4    Ruysschaert, J.M.5
  • 51
    • 0027056047 scopus 로고
    • A molecular model for membrane fusion based on solution studies of a amphiphilic peptide from HIVgp41
    • Fujii G., Horvath S., Woodward S., Eiserling F., Eisenberg D. A molecular model for membrane fusion based on solution studies of a amphiphilic peptide from HIVgp41. Protein Sci. 1992; 1: 1454 – 1464
    • (1992) Protein Sci. , vol.1 , pp. 1454-1464
    • Fujii, G.1    Horvath, S.2    Woodward, S.3    Eiserling, F.4    Eisenberg, D.5
  • 52
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segment of human type I single span membrane proteins
    • Landolt-Marticorena C., Williams K. A., Deber C. M., Reithmeier R. A. Non-random distribution of amino acids in the transmembrane segment of human type I single span membrane proteins. J. Mol. Biol. 1993; 229: 602 – 608
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.4
  • 54
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do H., Falcone D., Lin J., Andrews D. W., Johnsom A. E. The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 1996; 85: 369 – 378
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnsom, A.E.5
  • 55
    • 0026684458 scopus 로고
    • Signal peptides open protein-conducting channel
    • Simon S. M., Blobel G. Signal peptides open protein-conducting channel. Cell 1992; 69: 677 – 684
    • (1992) Cell , vol.69 , pp. 677-684
    • Simon, S.M.1    Blobel, G.2
  • 56
    • 0023855416 scopus 로고
    • Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)
    • Merlie J. P., Fagan D., Mudd J., Needleman P. Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase). J. Biol. Chem. 1988; 263: 3550 – 3553
    • (1988) J. Biol. Chem. , vol.263 , pp. 3550-3553
    • Merlie, J.P.1    Fagan, D.2    Mudd, J.3    Needleman, P.4
  • 57
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot D., Loo P. J., Garavito R. M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 1993; 367: 243 – 249
    • (1993) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loo, P.J.2    Garavito, R.M.3
  • 58
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle D., Weeks D., Sachs G. The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J. Biol. Chem. 1995; 270: 25678 – 25684
    • (1995) J. Biol. Chem. , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 59
    • 0029561894 scopus 로고
    • Transmembrane orientation of signal/anchor proteins is affected by the folding state but not the size of the N-terminal domain
    • Denzer A. J., Nabholz C. E., Spiess M. Transmembrane orientation of signal/anchor proteins is affected by the folding state but not the size of the N-terminal domain. EMBO J. 1995; 14: 6311 – 6317
    • (1995) EMBO J. , vol.14 , pp. 6311-6317
    • Denzer, A.J.1    Nabholz, C.E.2    Spiess, M.3
  • 60
    • 0028360414 scopus 로고
    • A copper-transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus species PCC7942
    • Kanamaru T., Kashiwagi S., Mizuno T. A copper-transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus species PCC7942. Mol. Microbiol. 1994; 13: 369 – 377
    • (1994) Mol. Microbiol. , vol.13 , pp. 369-377
    • Kanamaru, T.1    Kashiwagi, S.2    Mizuno, T.3
  • 61
    • 0026537420 scopus 로고
    • ATP-dependent cadmium transport by the cadA cadmium resistance determinant in everted membrane vesicles of Bacillus subtilis
    • Tsai K. J., Yoon K. P., Lynn A. R. ATP-dependent cadmium transport by the cadA cadmium resistance determinant in everted membrane vesicles of Bacillus subtilis. J. Bacteriol. 1992; 174: 116 – 121
    • (1992) J. Bacteriol. , vol.174 , pp. 116-121
    • Tsai, K.J.1    Yoon, K.P.2    Lynn, A.R.3
  • 63
    • 0025149361 scopus 로고
    • The epitope for monoclonal antibody A20 (amino acids 870–890) is located on the luminal surface of the Ca22+-ATPase of sarcoplasmic reticulum
    • Clarke D. M., Loo T. W., MacLennan D. H. The epitope for monoclonal antibody A20 (amino acids 870–890) is located on the luminal surface of the Ca22+-ATPase of sarcoplasmic reticulum. J Biol Chem 1990; 265: 17405 – 17408
    • (1990) J Biol Chem , vol.265 , pp. 17405-17408
    • Clarke, D.M.1    Loo, T.W.2    MacLennan, D.H.3
  • 64
    • 0023819315 scopus 로고
    • A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site
    • Gunteski-Hamblin A. M., Greeb J., Shull G. E. A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site. J. Biol. Chem. 1988; 263: 15032 – 15040
    • (1988) J. Biol. Chem. , vol.263 , pp. 15032-15040
    • Gunteski-Hamblin, A.M.1    Greeb, J.2    Shull, G.E.3
  • 65
    • 0026786784 scopus 로고
    • The alternative carboxyl termini of avian cardiac and brain sarcoplasmic reticulum/endoplasmic reticulum Ca2+-ATPases are on opposite sides of the membrane
    • Campbell A. M., Kessler P. D., Fambrough D. M. The alternative carboxyl termini of avian cardiac and brain sarcoplasmic reticulum/endoplasmic reticulum Ca2+-ATPases are on opposite sides of the membrane. J. Biol. Chem. 1992; 267: 9321 – 9325
    • (1992) J. Biol. Chem. , vol.267 , pp. 9321-9325
    • Campbell, A.M.1    Kessler, P.D.2    Fambrough, D.M.3
  • 66
    • 0028900576 scopus 로고
    • A Novel integration signal that is composed of two transmembrane segments is required to integrate the Neurospora plasma membrane H+ ATPase into microsomes
    • Lin J., Addison R. A Novel integration signal that is composed of two transmembrane segments is required to integrate the Neurospora plasma membrane H+ ATPase into microsomes. J. Biol. Chem. 1995; 270: 6935 – 6941
    • (1995) J. Biol. Chem. , vol.270 , pp. 6935-6941
    • Lin, J.1    Addison, R.2
  • 67
    • 0028941553 scopus 로고
    • The membrane topology of the carboxyl-terminal third of the Neurospora plasma membrane H+-ATPase
    • Lin J., Addison R. The membrane topology of the carboxyl-terminal third of the Neurospora plasma membrane H+-ATPase. J. Biol. Chem. 1995; 270: 694 – 6948
    • (1995) J. Biol. Chem. , vol.270 , pp. 694-6948
    • Lin, J.1    Addison, R.2
  • 68
    • 0030029790 scopus 로고    scopus 로고
    • Membrane topology of the human Na+/glucose cotransporter SGLT1
    • Turk E., Kerner C. J., Lostao M. P., Wright E. M. Membrane topology of the human Na+/glucose cotransporter SGLT1. J. Biol. Chem. 1996; 271: 1925 – 1934
    • (1996) J. Biol. Chem. , vol.271 , pp. 1925-1934
    • Turk, E.1    Kerner, C.J.2    Lostao, M.P.3    Wright, E.M.4
  • 70
    • 0028929094 scopus 로고
    • The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum
    • Oliver J., Jungnickel B., Gorlich D., Rapoport T. A., High S. The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Lett 1995; 362: 126 – 130
    • (1995) FEBS Lett , vol.362 , pp. 126-130
    • Oliver, J.1    Jungnickel, B.2    Gorlich, D.3    Rapoport, T.A.4    High, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.