메뉴 건너뛰기




Volumn 64, Issue 1, 2000, Pages 13-33

Membrane topology and insertion of membrane proteins: Search for topogenic signals

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BETA GALACTOSIDASE; BETA LACTAMASE; CYSTEINE; MEMBRANE PROTEIN; PROLACTIN; PROTEIN BAD;

EID: 0034057802     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.64.1.13-33.2000     Document Type: Review
Times cited : (169)

References (212)
  • 1
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha-subunit
    • Akabas, M. H., and A. Karlin. 1995. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha-subunit. Biochemistry 34:12496-12500.
    • (1995) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2
  • 2
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit
    • Akabas, M. H., C. Kaufmann, P. Archdeacon, and A. Karlin. 1994. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit. Neuron 13:919-927.
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 3
    • 0028264188 scopus 로고
    • Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator
    • Akabas, M. H., C. Kaufmann, T. A. Cook, and P. Archdeacon. 1994. Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269:14865-14868.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14865-14868
    • Akabas, M.H.1    Kaufmann, C.2    Cook, T.A.3    Archdeacon, P.4
  • 4
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., D. A. Stauffer, M. Xu, and A. Karlin. 1992. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 5
    • 0027456615 scopus 로고
    • Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo
    • Akiyama, Y., and K. Ito. 1993. Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo. J. Biol. Chem. 268:8146-8150.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8146-8150
    • Akiyama, Y.1    Ito, K.2
  • 6
    • 0026657163 scopus 로고
    • Membrane topology of the pBR322 tetracycline resistance protein. TetA-PhoA gene fusions and implications for the mechanism of TetA membrane insertion
    • Allard, J. D., and K. P. Bertrand. 1992. Membrane topology of the pBR322 tetracycline resistance protein. TetA-PhoA gene fusions and implications for the mechanism of TetA membrane insertion. J. Biol. Chem. 267:17809-17819.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17809-17819
    • Allard, J.D.1    Bertrand, K.P.2
  • 7
    • 0026529067 scopus 로고
    • Different positively charged amino acids have similar effects on the topology of a polytopic transmembrane protein in Escherichia coli
    • Andersson, H., E. Bakker, and G. von Heijne. 1992. Different positively charged amino acids have similar effects on the topology of a polytopic transmembrane protein in Escherichia coli. J. Biol. Chem. 267:1491-1495.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1491-1495
    • Andersson, H.1    Bakker, E.2    Von Heijne, G.3
  • 8
    • 0027439249 scopus 로고
    • Position-specific Asp-Lys pairing can affect signal sequence function and membrane protein topology
    • Andersson, H., and G. von Heijne. 1993. Position-specific Asp-Lys pairing can affect signal sequence function and membrane protein topology. J. Biol. Chem. 268:21389-21393.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21389-21393
    • Andersson, H.1    Von Heijne, G.2
  • 9
    • 0027473683 scopus 로고
    • Sec dependent and sec independent assembly of E. coli inner membrane proteins: The topological rules depend on chain length
    • Andersson, H., and G. von Heijne. 1993. Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length. EMBO J. 12:683-691.
    • (1993) EMBO J. , vol.12 , pp. 683-691
    • Andersson, H.1    Von Heijne, G.2
  • 10
    • 0028291426 scopus 로고
    • Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane
    • Andersson, H., and G. von Heijne. 1994. Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane. FEBS Lett. 347:169-172.
    • (1994) FEBS Lett. , vol.347 , pp. 169-172
    • Andersson, H.1    Von Heijne, G.2
  • 11
    • 0029646091 scopus 로고
    • Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing
    • Athappilly, F. K., and W. A. Hendrickson. 1995. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3:1407-1419.
    • (1995) Structure , vol.3 , pp. 1407-1419
    • Athappilly, F.K.1    Hendrickson, W.A.2
  • 12
    • 0029963973 scopus 로고    scopus 로고
    • Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
    • Bacher, G., H. Lutcke, B. Jungnickel, T. A. Rapoport, and B. Dobberstein. 1996. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 381:248-251.
    • (1996) Nature , vol.381 , pp. 248-251
    • Bacher, G.1    Lutcke, H.2    Jungnickel, B.3    Rapoport, T.A.4    Dobberstein, B.5
  • 13
    • 0028361579 scopus 로고
    • +-ATPase using in vitro translation
    • +-ATPase using in vitro translation. J. Biol. Chem. 269:16909-16919.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16909-16919
    • Bamberg, K.1    Sachs, G.2
  • 14
    • 0029790978 scopus 로고    scopus 로고
    • In vivo membrane assembly of the E. coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force
    • Bassilana, M., and C. Gwizdek. 1996. In vivo membrane assembly of the E. coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force. EMBO J. 15:5202-5208.
    • (1996) EMBO J. , vol.15 , pp. 5202-5208
    • Bassilana, M.1    Gwizdek, C.2
  • 16
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle, D., D. Weeks, and G. Sachs. 1995. The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J. Biol. Chem. 270:25678-25684.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 17
    • 0030762504 scopus 로고    scopus 로고
    • Identification of membrane insertion sequences of the rabbit gastric cholecystokinin-A receptor by in vitro translation
    • Bayle, D., D. Weeks, and G. Sachs. 1997. Identification of membrane insertion sequences of the rabbit gastric cholecystokinin-A receptor by in vitro translation. J. Biol. Chem. 272:19697-19707.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19697-19707
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 18
    • 0031021424 scopus 로고    scopus 로고
    • -)-coupled gamma-aminobutyric acid transporter from rat brain
    • -)-coupled gamma-aminobutyric acid transporter from rat brain. J. Biol. Chem. 272:1203-1210.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1203-1210
    • Bennett, E.R.1    Kanner, B.I.2
  • 19
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein, H. D., M. A. Poritz, K. Strub, P. J. Hoben, S. Brenner, and P. Walter. 1989. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340:482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 20
    • 0032006712 scopus 로고    scopus 로고
    • The role of the ribosome-translocon complex in translation and assembly of polytopic membrane proteins
    • Bibi, E. 1998. The role of the ribosome-translocon complex in translation and assembly of polytopic membrane proteins. Trends Biochem. Sci. 23: 51-55.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 51-55
    • Bibi, E.1
  • 21
    • 0028098714 scopus 로고
    • Membrane topology of multidrug resistance protein expressed in Escherichia coli N-terminal domain
    • Bibi, E., and O. Beja. 1994. Membrane topology of multidrug resistance protein expressed in Escherichia coli N-terminal domain. J. Biol. Chem. 269:19910-19915.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19910-19915
    • Bibi, E.1    Beja, O.2
  • 22
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. 1980. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77:1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 23
    • 0029894267 scopus 로고    scopus 로고
    • Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration
    • Borel, A. C., and S. M. Simon. 1996. Biogenesis of polytopic membrane proteins: membrane segments assemble within translocation channels prior to membrane integration. Cell 85:379-389.
    • (1996) Cell , vol.85 , pp. 379-389
    • Borel, A.C.1    Simon, S.M.2
  • 24
    • 0003158441 scopus 로고
    • Use of gene fusions to determine membrane protein topology
    • S. H. White (ed.). Oxford University Press, Oxford, United Kingdom
    • Boyd, D. 1994. Use of gene fusions to determine membrane protein topology, p. 144-163. In S. H. White (ed.), Membrane protein structure. Experimental approaches. Oxford University Press, Oxford, United Kingdom.
    • (1994) Membrane Protein Structure. Experimental Approaches , pp. 144-163
    • Boyd, D.1
  • 25
    • 0025059797 scopus 로고
    • The role of charged amino acids in the localization of secreted and membrane proteins
    • Boyd, D., and J. Beckwith. 1990. The role of charged amino acids in the localization of secreted and membrane proteins. Cell 62:1031-1033.
    • (1990) Cell , vol.62 , pp. 1031-1033
    • Boyd, D.1    Beckwith, J.2
  • 26
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd, D., B. Traxler, and J. Beckwith. 1993. Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J. Bacteriol. 175:553-556.
    • (1993) J. Bacteriol. , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 27
    • 0022869217 scopus 로고
    • A vector for the construction of translational fusions to TEM beta-lactamase and the analysis of protein export signals and membrane protein topology
    • Broome-Smith, J. K., and B. G. Spratt. 1986. A vector for the construction of translational fusions to TEM beta-lactamase and the analysis of protein export signals and membrane protein topology. Gene 49:341-349.
    • (1986) Gene , vol.49 , pp. 341-349
    • Broome-Smith, J.K.1    Spratt, B.G.2
  • 28
    • 0025053613 scopus 로고
    • Beta-lactamase as a probe of membrane protein assembly and protein export
    • Broome-Smith, J. K., M. Tadayyon, and Y. Zhang. 1990. Beta-lactamase as a probe of membrane protein assembly and protein export. Mol. Microbiol. 4:1637-1644.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1637-1644
    • Broome-Smith, J.K.1    Tadayyon, M.2    Zhang, Y.3
  • 29
    • 0025330038 scopus 로고
    • lac permease of Escherichia coli: Topology and sequence elements promoting membrane insertion
    • Calamia, J., and C. Manoil. 1990. lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion. Proc. Natl. Acad. Sci. USA 87:4937-4941.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4937-4941
    • Calamia, J.1    Manoil, C.2
  • 30
    • 0022446237 scopus 로고
    • Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli
    • Chang, C. N., W. J. Kuang, and E. Y. Chen. 1986. Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene 44:121-125.
    • (1986) Gene , vol.44 , pp. 121-125
    • Chang, C.N.1    Kuang, W.J.2    Chen, E.Y.3
  • 31
    • 0030775990 scopus 로고    scopus 로고
    • Topology of NAT2, a prototypical example of a new family of amino acid transporters
    • Chang, H. C., and D. R. Bush. 1997. Topology of NAT2, a prototypical example of a new family of amino acid transporters. J. Biol. Chem. 272: 30552-30557.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30552-30557
    • Chang, H.C.1    Bush, D.R.2
  • 32
    • 0028241858 scopus 로고
    • Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion
    • Chang, X. B., Y. X. Hou, T. J. Jensen, and J. R. Riordan. 1994. Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion. J. Biol. Chem. 269:18572-18575.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18572-18575
    • Chang, X.B.1    Hou, Y.X.2    Jensen, T.J.3    Riordan, J.R.4
  • 33
    • 0028108943 scopus 로고
    • Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase
    • Chapman-Smith, A., D. L. Turner, J. E. Cronan, Jr., T. W. Morris, and J. C. Wallace. 1994. Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochem. J. 302:881-887.
    • (1994) Biochem. J. , vol.302 , pp. 881-887
    • Chapman-Smith, A.1    Turner, D.L.2    Cronan J.E., Jr.3    Morris, T.W.4    Wallace, J.C.5
  • 34
    • 0025745313 scopus 로고
    • The transmembrane topology of the amino terminus of the alpha subunit of the nicotinic acetylcholine receptor
    • Chavez, R. A., and Z. W. Hall. 1991. The transmembrane topology of the amino terminus of the alpha subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 266:15532-15538.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15532-15538
    • Chavez, R.A.1    Hall, Z.W.2
  • 35
    • 0032524637 scopus 로고    scopus 로고
    • Determination of external loop topology in the serotonin transporter by site-directed chemical labeling
    • Chen, J. G., S. Liu-Chen, and G. Rudnick. 1998. Determination of external loop topology in the serotonin transporter by site-directed chemical labeling. J. Biol. Chem. 273:12675-12681.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12675-12681
    • Chen, J.G.1    Liu-Chen, S.2    Rudnick, G.3
  • 36
    • 0025306403 scopus 로고
    • The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli
    • Chepuri, V., and R. B. Gennis. 1990. The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli. J. Biol. Chem. 265:12978-12986.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12978-12986
    • Chepuri, V.1    Gennis, R.B.2
  • 37
    • 0030940847 scopus 로고    scopus 로고
    • Analysis of the transmembrane topology and membrane assembly of the GAT-1 gamma-aminobutyric acid transporter
    • Clark, J. A. 1997. Analysis of the transmembrane topology and membrane assembly of the GAT-1 gamma-aminobutyric acid transporter. J. Biol. Chem. 272:14695-14704.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14695-14704
    • Clark, J.A.1
  • 38
    • 0031666046 scopus 로고    scopus 로고
    • Analysis of transporter topology using deletion and epitope tagging
    • Clark, J. A. 1998. Analysis of transporter topology using deletion and epitope tagging. Methods Enzymol. 296:293-307.
    • (1998) Methods Enzymol. , vol.296 , pp. 293-307
    • Clark, J.A.1
  • 39
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and G. von Heijne. 1994. TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10:685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 40
    • 0027361668 scopus 로고
    • GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor
    • Connolly, T., and R. Gilmore. 1993. GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor. J. Cell Biol. 123:799-807.
    • (1993) J. Cell Biol. , vol.123 , pp. 799-807
    • Connolly, T.1    Gilmore, R.2
  • 42
    • 0030977049 scopus 로고    scopus 로고
    • A topological model for the general aromatic amino acid permease, AroP, of Escherichia coli
    • Cosgriff, A. J., and A. J. Pittard. 1997. A topological model for the general aromatic amino acid permease, AroP, of Escherichia coli. J. Bacteriol. 179:3317-3323.
    • (1997) J. Bacteriol. , vol.179 , pp. 3317-3323
    • Cosgriff, A.J.1    Pittard, A.J.2
  • 43
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins
    • Cronan, J. E., Jr. 1990. Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins. J. Biol. Chem. 265:10327-10333.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10327-10333
    • Cronan J.E., Jr.1
  • 44
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K. S., S. Liao, V. E. Worrell, G. D. Reinhart, and A. E. Johnson. 1994. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78:461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 45
    • 0028865328 scopus 로고
    • Membrane topology analysis of the Escherichia coli cytosine permease
    • Danielsen, S., D. Boyd, and J. Neuhard. 1995. Membrane topology analysis of the Escherichia coli cytosine permease. Microbiology 141:2905-2913.
    • (1995) Microbiology , vol.141 , pp. 2905-2913
    • Danielsen, S.1    Boyd, D.2    Neuhard, J.3
  • 46
    • 0032430831 scopus 로고    scopus 로고
    • Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli
    • De Gier, J. W., P. A. Scotti, A. Saaf, Q. A. Valent, A. Kuhn, J. Luirink, and G. von Heijne. 1998. Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli. Proc. Natl. Acad. Sci. USA 95:14646-14651.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14646-14651
    • De Gier, J.W.1    Scotti, P.A.2    Saaf, A.3    Valent, Q.A.4    Kuhn, A.5    Luirink, J.6    Von Heijne, G.7
  • 47
    • 0025836761 scopus 로고
    • Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm
    • Derman, A. I., and J. Beckwith. 1991. Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. J. Bacteriol. 173:7719-7722.
    • (1991) J. Bacteriol. , vol.173 , pp. 7719-7722
    • Derman, A.I.1    Beckwith, J.2
  • 48
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman, A. I., W. A. Prinz, D. Belin, and J. Beckwith. 1993. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262:1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 49
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do, H., D. Falcone, J. Lin, D. W. Andrews, and A. E. Johnson. 1996. The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85:369-378.
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 51
    • 77956776810 scopus 로고    scopus 로고
    • Translocation of proteins across the bacterial cytoplasmic membrane
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.). Elsevier Biomedical Press, Amsterdam, The Netherlands
    • Driessen, A. J. M. 1996. Translocation of proteins across the bacterial cytoplasmic membrane, p. 759-790. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Transport processes in membranes. Elsevier Biomedical Press, Amsterdam, The Netherlands.
    • (1996) Transport Processes in Membranes , pp. 759-790
    • Driessen, A.J.M.1
  • 52
    • 0030827619 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial envelope
    • Duong, F., J. Eichler, A. Price, M. R. Leonard, and W. Wickner. 1997. Biogenesis of the gram-negative bacterial envelope. Cell 91:567-573.
    • (1997) Cell , vol.91 , pp. 567-573
    • Duong, F.1    Eichler, J.2    Price, A.3    Leonard, M.R.4    Wickner, W.5
  • 53
    • 0030745847 scopus 로고    scopus 로고
    • The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
    • Duong, F., and W. Wickner. 1997. The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling. EMBO J. 16:4871-4879.
    • (1997) EMBO J. , vol.16 , pp. 4871-4879
    • Duong, F.1    Wickner, W.2
  • 54
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A., and W. Wickner. 1994. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78:835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 55
    • 0025052350 scopus 로고
    • Genetic analysis of membrane protein topology by a sandwich gene fusion approach
    • Ehrmann, M., D. Boyd, and J. Beckwith. 1990. Genetic analysis of membrane protein topology by a sandwich gene fusion approach. Proc. Natl. Acad. Sci. USA 87:7574-7578.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7574-7578
    • Ehrmann, M.1    Boyd, D.2    Beckwith, J.3
  • 56
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., E. Schwarz, M. Komaromy, and R. Wall. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 57
    • 0028364949 scopus 로고
    • A topological model for the high-affinity nickel transporter of alcaligenes eutrophus
    • Eitinger, T., and B. Friedrich. 1994. A topological model for the high-affinity nickel transporter of Alcaligenes eutrophus. Mol. Microbiol. 12:1025-1032.
    • (1994) Mol. Microbiol. , vol.12 , pp. 1025-1032
    • Eitinger, T.1    Friedrich, B.2
  • 58
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • Engelman, D. M., and T. A. Steitz. 1981. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23:411-422.
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 59
    • 0018369848 scopus 로고
    • Analysis of microbial biotin proteins
    • Fall, R. R. 1979. Analysis of microbial biotin proteins. Methods Enzymol. 62:390-398.
    • (1979) Methods Enzymol. , vol.62 , pp. 390-398
    • Fall, R.R.1
  • 60
    • 0033008601 scopus 로고    scopus 로고
    • Protein targeting to the bacterial cytoplasmic membrane
    • Fekkes, P., and A. J. Driessen. 1999. Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev. 63:161-173.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 161-173
    • Fekkes, P.1    Driessen, A.J.2
  • 61
    • 0022358406 scopus 로고
    • Bovine opsin has more than one signal sequence
    • Friedlander, M., and G. Blobel. 1985. Bovine opsin has more than one signal sequence. Nature 318:338-343.
    • (1985) Nature , vol.318 , pp. 338-343
    • Friedlander, M.1    Blobel, G.2
  • 62
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins
    • Frillingos, S., M. Sahin-toth, J. Wu, and H. R. Kaback. 1998. Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins. FASEB J. 12:1281-1299.
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 63
    • 0023883641 scopus 로고
    • Genetic analysis of the membrane insertion and topology of Ma1F, a cytoplasmic membrane protein of Escherichia coli
    • Froshauer, S., G. N. Green, D. Boyd, K. McGovern, and J. Beckwith. 1988. Genetic analysis of the membrane insertion and topology of Ma1F, a cytoplasmic membrane protein of Escherichia coli. J. Mol. Biol. 200:501-511.
    • (1988) J. Mol. Biol. , vol.200 , pp. 501-511
    • Froshauer, S.1    Green, G.N.2    Boyd, D.3    McGovern, K.4    Beckwith, J.5
  • 64
    • 0032504246 scopus 로고    scopus 로고
    • Structure-function relationships in OxlT, the oxalate/formate transporter of Oxalobacter formigenes. Topological features of transmembrane helix 11 as visualized by site-directed fluorescent labeling
    • Fu, D., and P. C. Maloney. 1998. Structure-function relationships in OxlT, the oxalate/formate transporter of Oxalobacter formigenes. Topological features of transmembrane helix 11 as visualized by site-directed fluorescent labeling. J. Biol. Chem. 273:17962-17967.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17962-17967
    • Fu, D.1    Maloney, P.C.2
  • 65
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eukaryotic cells
    • Gafvelin, G., M. Sakaguchi, H. Andersson, and G. von Heijne. 1997. Topological rules for membrane protein assembly in eukaryotic cells. J. Biol. Chem. 272:6119-6127.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6119-6127
    • Gafvelin, G.1    Sakaguchi, M.2    Andersson, H.3    Von Heijne, G.4
  • 66
    • 0028175016 scopus 로고
    • Topological "frustration" in multispanning E. coli inner membrane proteins
    • Gafvelin, G., and G. von Heijne. 1994. Topological "frustration" in multispanning E. coli inner membrane proteins. Cell 77:401-412.
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    Von Heijne, G.2
  • 67
    • 0030011712 scopus 로고    scopus 로고
    • Comparative topology studies in Saccharomyces cerevisiae and in Escherichia coli. The N-terminal half of the yeast ABC protein Ste6
    • Geller, D., D. Taglicht, R. Edgar, A. Tam, O. Pines, S. Michaelis, and E. Bibi. 1996. Comparative topology studies in Saccharomyces cerevisiae and in Escherichia coli. The N-terminal half of the yeast ABC protein Ste6. J. Biol. Chem. 271:13746-13753.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13746-13753
    • Geller, D.1    Taglicht, D.2    Edgar, R.3    Tam, A.4    Pines, O.5    Michaelis, S.6    Bibi, E.7
  • 68
    • 0023750080 scopus 로고
    • Beta-galactosidase gene fusions as probes for the cytoplasmic regions of subunits I and II of the membrane-bound cytochrome d terminal oxidase from Escherichia coli
    • Georgiou, C. D., T. J. Dueweke, and R. B. Gennis. 1988. Beta-galactosidase gene fusions as probes for the cytoplasmic regions of subunits I and II of the membrane-bound cytochrome d terminal oxidase from Escherichia coli. J. Biol. Chem. 263:13130-13137.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13130-13137
    • Georgiou, C.D.1    Dueweke, T.J.2    Gennis, R.B.3
  • 69
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore, R., and G. Blobel. 1985. Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell 42:497-505.
    • (1985) Cell , vol.42 , pp. 497-505
    • Gilmore, R.1    Blobel, G.2
  • 70
    • 0024083858 scopus 로고
    • The transmembrane topology of the sn-glycerol-3-phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions
    • Gott, P., and W. Boos. 1988. The transmembrane topology of the sn-glycerol-3-phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions. Mol. Microbiol. 2:655-663.
    • (1988) Mol. Microbiol. , vol.2 , pp. 655-663
    • Gott, P.1    Boos, W.2
  • 71
    • 0024522434 scopus 로고
    • Nucleotide sequence of the osmoregulatory proU operon of Escherichia coli
    • Gowrishankar, J. 1989. Nucleotide sequence of the osmoregulatory proU operon of Escherichia coli. J. Bacteriol. 171:1923-1931.
    • (1989) J. Bacteriol. , vol.171 , pp. 1923-1931
    • Gowrishankar, J.1
  • 73
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer, R., and C. G. Tate. 1995. Overexpression of integral membrane proteins for structural studies. Q. Rev. Biophys. 28:315-422.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 74
    • 0028248240 scopus 로고
    • Role of N-glycosylation in the expression of human band 3-mediated anion transport
    • Groves, J. D., and M. J. Tanner. 1994. Role of N-glycosylation in the expression of human band 3-mediated anion transport. Mol. Membr. Biol. 11:31-38.
    • (1994) Mol. Membr. Biol. , vol.11 , pp. 31-38
    • Groves, J.D.1    Tanner, M.J.2
  • 75
    • 0032169137 scopus 로고    scopus 로고
    • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology
    • Grunewald, M., A. Bendahan, and B. I. Kanner. 1998. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron 21:623-632.
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 76
    • 0029810929 scopus 로고    scopus 로고
    • Use of phoA and lacZ fusions to study the membrane topology of ProW, a component of the osmoregulated ProU transport system of Escherichia coli
    • Haardt, M., and E. Bremer. 1996. Use of phoA and lacZ fusions to study the membrane topology of ProW, a component of the osmoregulated ProU transport system of Escherichia coli. J. Bacteriol. 178:5370-5381.
    • (1996) J. Bacteriol. , vol.178 , pp. 5370-5381
    • Haardt, M.1    Bremer, E.2
  • 77
    • 0030952745 scopus 로고    scopus 로고
    • Membrane topology of the di-and tripeptide transport protein of Lactococcus lactis
    • Hagting, A., J. van der Velde, B. Poolman, and W. N. Konings. 1997. Membrane topology of the di-and tripeptide transport protein of Lactococcus lactis. Biochemistry 36:6777-6785.
    • (1997) Biochemistry , vol.36 , pp. 6777-6785
    • Hagting, A.1    Van Der Velde, J.2    Poolman, B.3    Konings, W.N.4
  • 78
    • 0032566277 scopus 로고    scopus 로고
    • Mechanism involved in generating the carboxyl-terminal half topology of P-glycoprotein
    • Han, E. S., and J. T. Zhang. 1998. Mechanism involved in generating the carboxyl-terminal half topology of P-glycoprotein. Biochemistry 37:11996-12004.
    • (1998) Biochemistry , vol.37 , pp. 11996-12004
    • Han, E.S.1    Zhang, J.T.2
  • 79
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann, E., T. A. Rapoport, and H. F. Lodish. 1989. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 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
  • 80
    • 0027449053 scopus 로고
    • Assembly of eukaryotic class III (N-out, C-in) membrane proteins into the Escherichia coli cytoplasmic membrane
    • Hennessey, E. S., L. Hashemzadeh-Bonehi, L. A. Hunt, and J. K. Broome-Smith. 1993. Assembly of eukaryotic class III (N-out, C-in) membrane proteins into the Escherichia coli cytoplasmic membrane. FEBS Lett. 331: 159-161.
    • (1993) FEBS Lett. , vol.331 , pp. 159-161
    • Hennessey, E.S.1    Hashemzadeh-Bonehi, L.2    Hunt, L.A.3    Broome-Smith, J.K.4
  • 81
    • 0027229977 scopus 로고
    • Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion
    • High, S., S. S. Andersen, D. Gorlich, E. Hartmann, S. Prehn, T. A. Rapoport, and B. Dobberstein. 1993. Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. J. Cell Biol. 121:743-750.
    • (1993) J. Cell Biol. , vol.121 , pp. 743-750
    • High, S.1    Andersen, S.S.2    Gorlich, D.3    Hartmann, E.4    Prehn, S.5    Rapoport, T.A.6    Dobberstein, B.7
  • 83
    • 0030863293 scopus 로고    scopus 로고
    • Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus
    • Hipfner, D. R., K. C. Almquist, E. M. Leslie, J. H. Gerlach, C. E. Grant, R. G. Deeley, and S. P. Cole. 1997. Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus. J. Biol. Chem. 272:23623-23630.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23623-23630
    • Hipfner, D.R.1    Almquist, K.C.2    Leslie, E.M.3    Gerlach, J.H.4    Grant, C.E.5    Deeley, R.G.6    Cole, S.P.7
  • 84
    • 0028131474 scopus 로고
    • Topology of the Glut 1 glucose transporter deduced from glycosylation scanning mutagenesis
    • Hresko, R. C., M. Kruse, M. Strube, and M. Mueckler. 1994. Topology of the Glut 1 glucose transporter deduced from glycosylation scanning mutagenesis. J. Biol. Chem. 269:20482-20488.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20482-20488
    • Hresko, R.C.1    Kruse, M.2    Strube, M.3    Mueckler, M.4
  • 86
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 87
    • 0030014628 scopus 로고    scopus 로고
    • Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion
    • Jander, G., J. E. Cronan, Jr., and J. Beckwith. 1996. Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion. J. Bacteriol. 178:3049-3058.
    • (1996) J. Bacteriol. , vol.178 , pp. 3049-3058
    • Jander, G.1    Cronan J.E., Jr.2    Beckwith, J.3
  • 88
    • 0031660683 scopus 로고    scopus 로고
    • Probing structure of neurotransmitter transporters by substituted-cysteine accessibility method
    • Javitch, J. A. 1998. Probing structure of neurotransmitter transporters by substituted-cysteine accessibility method. Methods Enzymol. 296:331-346.
    • (1998) Methods Enzymol. , vol.296 , pp. 331-346
    • Javitch, J.A.1
  • 89
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
    • Johansson, M., I. Nilsson, and G. von Heijne. 1993. Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol. Gen. Genet. 239:251-256.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    Von Heijne, G.3
  • 90
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D. T., W. R. Taylor, and J. M. Thornton. 1994. A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry 33:3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 91
    • 0032321679 scopus 로고    scopus 로고
    • +/solute cotransporter family
    • +/solute cotransporter family. Biochim. Biophys. Acta 1365:60-64.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 60-64
    • Jung, H.1
  • 93
    • 77956817521 scopus 로고    scopus 로고
    • The lactose permease of Escherichia coli: Past, present and future
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.). Elsevier Science, Amsterdam, The Netherlands
    • Kaback, H. R. 1996. The lactose permease of Escherichia coli: past, present and future, p. 203-227. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Handbook of biological physics. Transport processes in eukaryotic and prokaryotic organisms. Elsevier Science, Amsterdam, The Netherlands.
    • (1996) Handbook of Biological Physics. Transport Processes in Eukaryotic and Prokaryotic Organisms , pp. 203-227
    • Kaback, H.R.1
  • 94
    • 0028950653 scopus 로고
    • Membrane topology of P-glycoprotein as determined by epitope insertion: Transmembrane organization of the N-terminal domain of mdr3
    • Kast, C., V. Canfield, R. Levenson, and P. Gros. 1995. Membrane topology of P-glycoprotein as determined by epitope insertion: transmembrane organization of the N-terminal domain of mdr3. Biochemistry 34:4402-4411.
    • (1995) Biochemistry , vol.34 , pp. 4402-4411
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 95
    • 0029918133 scopus 로고    scopus 로고
    • Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence
    • Kast, C., V. Canfield, R. Levenson, and P. Gros. 1996. Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence. J. Biol. Chem. 271:9240-9248.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9240-9248
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 96
    • 0032562137 scopus 로고    scopus 로고
    • Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein
    • Kast, C., and P. Gros. 1998. Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein. Biochemistry 37:2305-2313.
    • (1998) Biochemistry , vol.37 , pp. 2305-2313
    • Kast, C.1    Gros, P.2
  • 99
    • 0021847027 scopus 로고
    • The detection and classification of membrane-spanning proteins
    • Klein, P., M. Kanehisa, and C. DeLisi. 1985. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta 815:468-476.
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 468-476
    • Klein, P.1    Kanehisa, M.2    DeLisi, C.3
  • 100
    • 0025202897 scopus 로고
    • Structural requirements for interruption of protein translocation across rough endoplasmic reticulum membrane
    • Kuroiwa, T., M. Sakaguchi, K. Mihara, and T. Omura. 1990. Structural requirements for interruption of protein translocation across rough endoplasmic reticulum membrane. J. Biochem. 108:829-834.
    • (1990) J. Biochem. , vol.108 , pp. 829-834
    • Kuroiwa, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 101
    • 0025882870 scopus 로고
    • Systematic analysis of stop-transfer sequence for microsomal membrane
    • Kuroiwa, T., M. Sakaguchi, K. Mihara, and T. Omura. 1991. Systematic analysis of stop-transfer sequence for microsomal membrane. J. Biol. Chem. 266:9251-9255.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9251-9255
    • Kuroiwa, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 102
    • 0029960038 scopus 로고    scopus 로고
    • Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins
    • Kuroiwa, T., M. Sakaguchi, T. Omura, and K. Mihara. 1996. Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins. J. Biol. Chem. 271: 6423-6428.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6423-6428
    • Kuroiwa, T.1    Sakaguchi, M.2    Omura, T.3    Mihara, K.4
  • 103
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 104
    • 0028040839 scopus 로고
    • Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multispan membrane glycoproteins
    • Landolt-Marticorena, C., and R. A. Reithmeier. 1994. Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multispan membrane glycoproteins. Biochem. J. 302:253-260.
    • (1994) Biochem. J. , vol.302 , pp. 253-260
    • Landolt-Marticorena, C.1    Reithmeier, R.A.2
  • 105
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena, C., K. A. Williams, C. M. Deber, and R. A. Reithmeier. 1993. Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol. 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
  • 106
    • 0029742631 scopus 로고    scopus 로고
    • Topological analysis of the Rhodobacter capsulatus PucC protein and effects of C-terminal deletions on light-harvesting complex II
    • LeBlanc, H. N., and J. T. Beatty. 1996. Topological analysis of the Rhodobacter capsulatus PucC protein and effects of C-terminal deletions on light-harvesting complex II. J. Bacteriol. 178:4801-4806.
    • (1996) J. Bacteriol. , vol.178 , pp. 4801-4806
    • LeBlanc, H.N.1    Beatty, J.T.2
  • 107
    • 0028134990 scopus 로고
    • Mutations eliminating the protein export function of a membrane-spanning sequence
    • Lee, E., and C. Manoil. 1994. Mutations eliminating the protein export function of a membrane-spanning sequence. J. Biol. Chem. 269:28822-28828.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28822-28828
    • Lee, E.1    Manoil, C.2
  • 108
    • 77956734988 scopus 로고    scopus 로고
    • Molecular genetic analysis of membrane protein topology
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.). Elsevier Science, Amsterdam, The Netherlands
    • Lee, M., and C. Manoil. 1996. Molecular genetic analysis of membrane protein topology, p. 189-201. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Handbook of biological physics. Transport processes of eukaryotic and prokaryotic organisms. Elsevier Science, Amsterdam, The Netherlands.
    • (1996) Handbook of Biological Physics. Transport Processes of Eukaryotic and Prokaryotic Organisms , pp. 189-201
    • Lee, M.1    Manoil, C.2
  • 109
    • 0025367345 scopus 로고
    • A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments
    • Lewis, M. J., J. A. Chang, and R. D. Simoni. 1990. A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments. J. Biol. Chem. 265:10541-10550.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10541-10550
    • Lewis, M.J.1    Chang, J.A.2    Simoni, R.D.3
  • 110
    • 0026502763 scopus 로고
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
    • Li, S. J., and J. E. J. Cronan. 1992. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267:855-863.
    • (1992) J. Biol. Chem. , vol.267 , pp. 855-863
    • Li, S.J.1    Cronan, J.E.J.2
  • 111
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., J. Lin, H. Do, and A. E. Johnson. 1997. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90:31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 112
    • 0018789510 scopus 로고
    • Chicken ovalbumin contains an internal signal sequence
    • Lingappa, V. R., J. R. Lingappa, and G. Blobel. 1979. Chicken ovalbumin contains an internal signal sequence. Nature 281:117-121.
    • (1979) Nature , vol.281 , pp. 117-121
    • Lingappa, V.R.1    Lingappa, J.R.2    Blobel, G.3
  • 113
    • 0031920140 scopus 로고    scopus 로고
    • Estimation of structural similarity of membrane proteins by hydropathy profile alignment
    • Lolkema, J. S., and D. J. Slotboom. 1998. Estimation of structural similarity of membrane proteins by hydropathy profile alignment. Mol. Membr. Biol. 15:33-42.
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 33-42
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 114
    • 0032568845 scopus 로고    scopus 로고
    • Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues
    • Long, J. C., S. Wang, and S. B. Vik. 1998. Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273:16235-16240.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 115
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo, T. W., and D. M. Clarke. 1995. Membrane topology of a cysteine-less mutant of human P-glycoprotein. J. Biol. Chem. 270:843-848.
    • (1995) J. Biol. Chem. , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 116
    • 0031983038 scopus 로고    scopus 로고
    • Co-and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly
    • Lu, Y., X. Xiong, A. Helm, K. Kimani, A. Bragin, and W. R. Skach. 1998. Co-and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly. J. Biol. Chem. 273:568-576.
    • (1998) J. Biol. Chem. , vol.273 , pp. 568-576
    • Lu, Y.1    Xiong, X.2    Helm, A.3    Kimani, K.4    Bragin, A.5    Skach, W.R.6
  • 117
    • 0025020688 scopus 로고
    • Analysis of protein localization by use of gene fusions with complementary properties
    • Manoil, C. 1990. Analysis of protein localization by use of gene fusions with complementary properties. J. Bacteriol. 172:1035-1042.
    • (1990) J. Bacteriol. , vol.172 , pp. 1035-1042
    • Manoil, C.1
  • 118
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and J. Beckwith. 1986. A genetic approach to analyzing membrane protein topology. Science 233:1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 119
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., M. W. Hofmann, J. Brunner, and B. Dobberstein. 1995. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81:207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 120
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K. E., W. Mothes, and T. A. Rapoport. 1998. Protein translocation: tunnel vision. Cell 92:381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.1    Mothes, W.2    Rapoport, T.A.3
  • 121
    • 0014027648 scopus 로고
    • Further studies on the properties of liver propionyl coenzyme A holocarboxylase synthetase and the specificity of holocarboxylase formation
    • McAllister, H. C., and M. J. Coon. 1966. Further studies on the properties of liver propionyl coenzyme A holocarboxylase synthetase and the specificity of holocarboxylase formation. J. Biol. Chem. 241:2855-2861.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2855-2861
    • McAllister, H.C.1    Coon, M.J.2
  • 122
    • 0027087217 scopus 로고
    • Insertional mutagenesis of hydrophilic domains in the lactose permease of Escherichia coli
    • McKenna, E., D. Hardy, and H. R. Kaback. 1992. Insertional mutagenesis of hydrophilic domains in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA 89:11954-11958.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11954-11958
    • McKenna, E.1    Hardy, D.2    Kaback, H.R.3
  • 124
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli
    • Michaelis, S., H. Inouye, D. Oliver, and J. Beckwith. 1983. Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J. Bacteriol. 154:366-374.
    • (1983) J. Bacteriol. , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 125
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller, J. D., H. Wilhelm, L. Gierasch, R. Gilmore, and P. Walter. 1993. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366:351-354.
    • (1993) Nature , vol.366 , pp. 351-354
    • Miller, J.D.1    Wilhelm, H.2    Gierasch, L.3    Gilmore, R.4    Walter, P.5
  • 126
    • 0031686961 scopus 로고    scopus 로고
    • Coupled translocation events generate topological heterogeneity at the endoplasmic reticulum membrane
    • Moss, K., A. Helm, Y. Lu, A. Bragin, and W. R. Skach. 1998. Coupled translocation events generate topological heterogeneity at the endoplasmic reticulum membrane. Mol. Biol. Cell 9:2681-2697.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2681-2697
    • Moss, K.1    Helm, A.2    Lu, Y.3    Bragin, A.4    Skach, W.R.5
  • 128
    • 0032524342 scopus 로고    scopus 로고
    • A mutation in the Escherichia coli secy gene that produces distinct effects on inner membrane protein insertion and protein export
    • Newitt, J. A., and H. D. Bernstein. 1998. A mutation in the Escherichia coli secY gene that produces distinct effects on inner membrane protein insertion and protein export. J. Biol. Chem. 273:12451-12456.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12451-12456
    • Newitt, J.A.1    Bernstein, H.D.2
  • 129
    • 0025015646 scopus 로고
    • Fine-tuning the topology of a polytopic membrane protein: Role of positively and negatively charged amino acids
    • Nilsson, I., and G. von Heijne. 1990. Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids. Cell 62:1135-1141.
    • (1990) Cell , vol.62 , pp. 1135-1141
    • Nilsson, I.1    Von Heijne, G.2
  • 130
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I. M., and G. von Heijne. 1993. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268:5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 131
    • 0026673416 scopus 로고
    • The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Olender, E. H., and R. D. Simon. 1992. The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267:4223-4235.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4223-4235
    • Olender, E.H.1    Simon, R.D.2
  • 132
    • 0031030990 scopus 로고    scopus 로고
    • Analysis of the transmembrane topology of the glycine transporter GLYT1
    • Olivares, L., C. Aragon, C. Gimenez, and F. Zafra. 1997. Analysis of the transmembrane topology of the glycine transporter GLYT1. J. Biol. Chem. 272:1211-1217.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1211-1217
    • Olivares, L.1    Aragon, C.2    Gimenez, C.3    Zafra, F.4
  • 133
    • 0032561457 scopus 로고    scopus 로고
    • Assessment of topogenic functions of anticipated transmembrane segments of human band 3
    • Ota, K., M. Sakaguchi, N. Hamasaki, and K. Mihara. 1998. Assessment of topogenic functions of anticipated transmembrane segments of human band 3. J. Biol. Chem. 273:28286-28291.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28286-28291
    • Ota, K.1    Sakaguchi, M.2    Hamasaki, N.3    Mihara, K.4
  • 134
    • 0032185234 scopus 로고    scopus 로고
    • Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins
    • Ota, K., M. Sakaguchi, G. von Heijne, N. Hamasaki, and K. Mihara. 1998. Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins. Mol. Cell 2:495-503.
    • (1998) Mol. Cell , vol.2 , pp. 495-503
    • Ota, K.1    Sakaguchi, M.2    Von Heijne, G.3    Hamasaki, N.4    Mihara, K.5
  • 136
    • 0029097866 scopus 로고
    • Multiple residues specify external tetraethylammonium blockade in voltage-gated potassium channels
    • Pascual, J. M., C. C. Shieh, G. E. Kirsch, and A. M. Brown. 1995. Multiple residues specify external tetraethylammonium blockade in voltage-gated potassium channels. Biophys. J. 69:428-434.
    • (1995) Biophys. J. , vol.69 , pp. 428-434
    • Pascual, J.M.1    Shieh, C.C.2    Kirsch, G.E.3    Brown, A.M.4
  • 137
    • 0029966330 scopus 로고    scopus 로고
    • Topology of the phenylalanine-specific permease of Escherichia coli
    • Pi, J., and A. J. Pittard. 1996. Topology of the phenylalanine-specific permease of Escherichia coli. J. Bacteriol. 178:2650-2655.
    • (1996) J. Bacteriol. , vol.178 , pp. 2650-2655
    • Pi, J.1    Pittard, A.J.2
  • 138
    • 0038415649 scopus 로고    scopus 로고
    • Protein translocation in the three domains of life: Variations on a theme
    • Pohlschroder, M., W. A. Prinz, E. Hartmann, and J. Beckwith. 1997. Protein translocation in the three domains of life: variations on a theme. Cell 91:563-566.
    • (1997) Cell , vol.91 , pp. 563-566
    • Pohlschroder, M.1    Prinz, W.A.2    Hartmann, E.3    Beckwith, J.4
  • 139
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L., and D. M. Engelman. 1990. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 140
    • 0030745799 scopus 로고    scopus 로고
    • Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3
    • Popov, M., L. Y. Tam, J. Li, and R. A. Reithmeier. 1997. Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3. J. Biol. Chem. 272:18325-18332.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18325-18332
    • Popov, M.1    Tam, L.Y.2    Li, J.3    Reithmeier, R.A.4
  • 141
    • 0028241136 scopus 로고
    • Purification of two active fusion proteins of the Na(+)-dependent citrate carrier of Klebsiella pneumoniae
    • Pos, K. M., M. Bott, and P. Dimroth. 1994. Purification of two active fusion proteins of the Na(+)-dependent citrate carrier of Klebsiella pneumoniae. FEBS Lett. 347:37-41.
    • (1994) FEBS Lett. , vol.347 , pp. 37-41
    • Pos, K.M.1    Bott, M.2    Dimroth, P.3
  • 142
    • 0032506039 scopus 로고    scopus 로고
    • In vitro biotinylation provides quantitative recovery of highly purified active lactose permease in a single step
    • Pouny, Y., C. Weitzman, and H. R. Kaback. 1998. In vitro biotinylation provides quantitative recovery of highly purified active lactose permease in a single step. Biochemistry 37:15713-15719.
    • (1998) Biochemistry , vol.37 , pp. 15713-15719
    • Pouny, Y.1    Weitzman, C.2    Kaback, H.R.3
  • 143
    • 0029932862 scopus 로고    scopus 로고
    • Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysis
    • Pourcher, T., E. Bibi, H. R. Kaback, and G. Leblanc. 1996. Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysis. Biochemistry 35:4161-4168.
    • (1996) Biochemistry , vol.35 , pp. 4161-4168
    • Pourcher, T.1    Bibi, E.2    Kaback, H.R.3    Leblanc, G.4
  • 144
    • 0028148705 scopus 로고
    • Gene fusion analysis of membrane protein topology: A direct comparison of alkaline phosphatase and beta-lactamase fusions
    • Prinz, W. A., and J. Beckwith. 1994. Gene fusion analysis of membrane protein topology: a direct comparison of alkaline phosphatase and beta-lactamase fusions. J. Bacteriol. 176:6410-6413.
    • (1994) J. Bacteriol. , vol.176 , pp. 6410-6413
    • Prinz, W.A.1    Beckwith, J.2
  • 145
    • 0032478813 scopus 로고    scopus 로고
    • The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli
    • Prinz, W. A., D. H. Boyd, M. Ehrmann, and J. Beckwith. 1998. The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli. J. Biol. Chem. 273:8419-8424.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8419-8424
    • Prinz, W.A.1    Boyd, D.H.2    Ehrmann, M.3    Beckwith, J.4
  • 146
    • 0027956144 scopus 로고
    • Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP
    • Rapiejko, P. J., and R. Gilmore. 1994. Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP. Mol. Biol. Cell 5:887-897.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 887-897
    • Rapiejko, P.J.1    Gilmore, R.2
  • 147
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T. A., B. Jungnickel, and U. Kutay. 1996. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65:271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 148
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees, D. C., L. DeAntonio, and D. Eisenberg. 1989. Hydrophobic organization of membrane proteins. Science 245:510-513.
    • (1989) Science , vol.245 , pp. 510-513
    • Rees, D.C.1    DeAntonio, L.2    Eisenberg, D.3
  • 149
    • 0024366667 scopus 로고
    • The bacterial photosynthetic reaction center as a model for membrane proteins
    • Rees, D. C., H. Komiya, T. O. Yeates, J. P. Allen, and G. Feher. 1989. The bacterial photosynthetic reaction center as a model for membrane proteins. Annu. Rev. Biochem. 58:607-633.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 607-633
    • Rees, D.C.1    Komiya, H.2    Yeates, T.O.3    Allen, J.P.4    Feher, G.5
  • 150
    • 0024400708 scopus 로고
    • Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
    • Romisch, K., J. Webb, J. Herz, S. Prehn, R. Frank, M. Vingron, and B. Dobberstein. 1989. Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Nature 340:478-482.
    • (1989) Nature , vol.340 , pp. 478-482
    • Romisch, K.1    Webb, J.2    Herz, J.3    Prehn, S.4    Frank, R.5    Vingron, M.6    Dobberstein, B.7
  • 151
    • 0029758264 scopus 로고    scopus 로고
    • Topological analysis of NhaA, a Na+/H+ antiporter from Escherichia coli
    • Rothman, A., E. Padan, and S. Schuldiner. 1996. Topological analysis of NhaA, a Na+/H+ antiporter from Escherichia coli. J. Biol. Chem. 271: 32288-32292.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32288-32292
    • Rothman, A.1    Padan, E.2    Schuldiner, S.3
  • 152
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa oxa1p homologue from Escherichia coli
    • Saaf, A., M. Monne, J. W. De Gier, and G. von Heijne. 1998. Membrane topology of the 60-kDa oxa1p homologue from Escherichia coli. J. Biol. Chem. 273:30415-30418.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30415-30418
    • Saaf, A.1    Monne, M.2    De Gier, J.W.3    Von Heijne, G.4
  • 153
    • 0032006057 scopus 로고    scopus 로고
    • Stop-transfer function of pseudo-random amino acid segments during translocation across prokaryotic and eukaryotic membranes
    • Saaf, A., E. Wallin, and G. von Heijne. 1998. Stop-transfer function of pseudo-random amino acid segments during translocation across prokaryotic and eukaryotic membranes. Eur. J. Biochem. 251:821-829.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 821-829
    • Saaf, A.1    Wallin, E.2    Von Heijne, G.3
  • 154
    • 0028921415 scopus 로고
    • Design of a membrane protein for site-specific proteolysis: Properties of engineered factor Xa protease sites in the lactose permease of Escherichia coli
    • Sahin-Toth, M., R. L. Dunten, and H. R. Kaback. 1995. Design of a membrane protein for site-specific proteolysis: properties of engineered factor Xa protease sites in the lactose permease of Escherichia coli. Biochemistry 34:1107-1112.
    • (1995) Biochemistry , vol.34 , pp. 1107-1112
    • Sahin-Toth, M.1    Dunten, R.L.2    Kaback, H.R.3
  • 156
    • 0024465189 scopus 로고
    • Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase
    • San Millan, J. L., D. Boyd, R. Dalbey, W. Wickner, and J. Beckwith. 1989. Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase. J. Bacteriol. 171:5536-5541.
    • (1989) J. Bacteriol. , vol.171 , pp. 5536-5541
    • San Millan, J.L.1    Boyd, D.2    Dalbey, R.3    Wickner, W.4    Beckwith, J.5
  • 157
    • 0028857635 scopus 로고
    • Membrane topology analysis of Escherichia coli K-12 Mtr permease by alkaline phosphatase and beta-galactosidase fusions
    • Sarsero, J. P., and A. J. Pittard. 1995. Membrane topology analysis of Escherichia coli K-12 Mtr permease by alkaline phosphatase and beta-galactosidase fusions. J. Bacteriol. 177:297-306.
    • (1995) J. Bacteriol. , vol.177 , pp. 297-306
    • Sarsero, J.P.1    Pittard, A.J.2
  • 158
    • 0032566739 scopus 로고    scopus 로고
    • Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein
    • Sato, M., R. Hresko, and M. Mueckler. 1998. Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein. J. Biol. Chem. 273:25203-25208.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25203-25208
    • Sato, M.1    Hresko, R.2    Mueckler, M.3
  • 159
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and B. Dobberstein. 1996. Common principles of protein translocation across membranes. Science 271:1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 160
    • 0032434691 scopus 로고    scopus 로고
    • A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation
    • Seal, R. P., and S. G. Amara. 1998. A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation. Neuron 21:1487-1498.
    • (1998) Neuron , vol.21 , pp. 1487-1498
    • Seal, R.P.1    Amara, S.G.2
  • 161
    • 0028047906 scopus 로고
    • An amphipathic sequence determinant of membrane protein topology
    • Seligman, L., and C. Manoil. 1994. An amphipathic sequence determinant of membrane protein topology. J. Biol. Chem. 269:19888-19896.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19888-19896
    • Seligman, L.1    Manoil, C.2
  • 162
    • 0031020515 scopus 로고    scopus 로고
    • FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins
    • Seluanov, A., and E. Bibi. 1997. FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins. J. Biol. Chem. 272:2053-2055.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2053-2055
    • Seluanov, A.1    Bibi, E.2
  • 163
    • 0023939327 scopus 로고
    • Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii
    • Shenoy, B. C., and H. G. Wood. 1988. Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii. FASEB J. 2:2396-2401.
    • (1988) FASEB J. , vol.2 , pp. 2396-2401
    • Shenoy, B.C.1    Wood, H.G.2
  • 164
    • 0017681846 scopus 로고
    • Use of gene fusions to study outer membrane protein localization in Escherichia coli
    • Silhavy, T. J., H. A. Shuman, J. Beckwith, and M. Schwartz. 1977. Use of gene fusions to study outer membrane protein localization in Escherichia coli. Proc. Natl. Acad. Sci. USA 74:5411-5415.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5411-5415
    • Silhavy, T.J.1    Shuman, H.A.2    Beckwith, J.3    Schwartz, M.4
  • 165
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S. M., and G. Blobel. 1991. A protein-conducting channel in the endoplasmic reticulum. Cell 65:371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 166
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • Sipos, L., and G. von Heijne. 1993. Predicting the topology of eukaryotic membrane proteins. Eur. J. Biochem. 213:1333-1340.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1333-1340
    • Sipos, L.1    Von Heijne, G.2
  • 167
    • 0028318283 scopus 로고
    • Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum
    • Skach, W. R., L. B. Shi, M. C. Calayag, A. Frigeri, V. R. Lingappa, and A. S. Verkman. 1994. Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum. J. Cell Biol. 125:803-815.
    • (1994) J. Cell Biol. , vol.125 , pp. 803-815
    • Skach, W.R.1    Shi, L.B.2    Calayag, M.C.3    Frigeri, A.4    Lingappa, V.R.5    Verkman, A.S.6
  • 168
    • 0028807145 scopus 로고
    • Topology analysis of the colicin V export protein CvaA in Escherichia coli
    • Skvirsky, R. C., S. Reginald, and X. Shen. 1995. Topology analysis of the colicin V export protein CvaA in Escherichia coli. J. Bacteriol. 177:6153-6159.
    • (1995) J. Bacteriol. , vol.177 , pp. 6153-6159
    • Skvirsky, R.C.1    Reginald, S.2    Shen, X.3
  • 169
    • 0029913959 scopus 로고    scopus 로고
    • Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family
    • Slotboom, D. J., J. S. Lolkema, and W. N. Konings. 1996. Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family. J. Biol. Chem. 271:31317-31321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31317-31321
    • Slotboom, D.J.1    Lolkema, J.S.2    Konings, W.N.3
  • 170
    • 0025805276 scopus 로고
    • Membrane topography of ColE1 gene products: The immunity protein
    • Song, H. Y., and W. A. Cramer. 1991. Membrane topography of ColE1 gene products: the immunity protein. J. Bacteriol. 173:2935-2943.
    • (1991) J. Bacteriol. , vol.173 , pp. 2935-2943
    • Song, H.Y.1    Cramer, W.A.2
  • 171
    • 0029819510 scopus 로고    scopus 로고
    • Glycosylation of multiple extracytosolic loops in Band 3, a model polytopic membrane protein
    • Tam, L. Y., C. Landolt-Marticorena, and R. A. Reithmeier. 1996. Glycosylation of multiple extracytosolic loops in Band 3, a model polytopic membrane protein. Biochem. J. 318:645-648.
    • (1996) Biochem. J. , vol.318 , pp. 645-648
    • Tam, L.Y.1    Landolt-Marticorena, C.2    Reithmeier, R.A.3
  • 172
    • 0032575609 scopus 로고    scopus 로고
    • Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger
    • Tang, X. B., J. Fujinaga, R. Kopito, and J. R. Casey. 1998. Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger. J. Biol. Chem. 273:22545-22553.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22545-22553
    • Tang, X.B.1    Fujinaga, J.2    Kopito, R.3    Casey, J.R.4
  • 173
    • 0031466796 scopus 로고    scopus 로고
    • The structure and function of band 3 (AE1): Recent developments
    • Tanner, M. J. 1997. The structure and function of band 3 (AE1): recent developments. Mol. Membr. Biol. 14:155-165.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 155-165
    • Tanner, M.J.1
  • 174
    • 0027752961 scopus 로고
    • + transport protein (RhaT) from enterobacteria
    • + transport protein (RhaT) from enterobacteria. J. Biol. Chem. 268:26850-26857.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26850-26857
    • Tate, C.G.1    Henderson, P.J.2
  • 175
    • 0027478779 scopus 로고
    • The topological analysis of integral cytoplasmic membrane proteins
    • Traxler, B., D. Boyd, and J. Beckwith. 1993. The topological analysis of integral cytoplasmic membrane proteins. J. Membr. Biol. 132:1-11.
    • (1993) J. Membr. Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 176
    • 15844393588 scopus 로고    scopus 로고
    • Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery
    • Traxler, B., and C. Murphy. 1996. Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery. J. Biol. Chem. 271:12394-12400.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12394-12400
    • Traxler, B.1    Murphy, C.2
  • 179
    • 0029566085 scopus 로고
    • Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli
    • Uchida, K., H. Mori, and S. Mizushima. 1995. Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270:30862-30868.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30862-30868
    • Uchida, K.1    Mori, H.2    Mizushima, S.3
  • 180
    • 0028849634 scopus 로고
    • Membrane topology of helices VII and XI in the lactose permease of Escherichia coli studied by lacY-phoA fusion analysis and site-directed spectroscopy
    • Ujwal, M. L., H. Jung, E. Bibi, C. Manoil, C. Altenbach, W. L. Hubbell, and H. R. Kaback. 1995. Membrane topology of helices VII and XI in the lactose permease of Escherichia coli studied by lacY-phoA fusion analysis and site-directed spectroscopy. Biochemistry 34:14909-14917.
    • (1995) Biochemistry , vol.34 , pp. 14909-14917
    • Ujwal, M.L.1    Jung, H.2    Bibi, E.3    Manoil, C.4    Altenbach, C.5    Hubbell, W.L.6    Kaback, H.R.7
  • 181
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt, N. D., J. A. Newitt, and H. D. Bernstein. 1997. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88:187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 183
    • 0032568818 scopus 로고    scopus 로고
    • Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase
    • Valiyaveetil, F. I., and R. H. Fillingame. 1998. Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase. J. Biol. Chem. 273:16241-16247.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16241-16247
    • Valiyaveetil, F.I.1    Fillingame, R.H.2
  • 184
    • 0029843116 scopus 로고    scopus 로고
    • Membrane topology of the sodium ion-dependent citrate carrier of Klebsiella pneumoniae. Evidence for a new structural class of secondary transporters
    • van Geest, M., and J. S. Lolkema. 1996. Membrane topology of the sodium ion-dependent citrate carrier of Klebsiella pneumoniae. Evidence for a new structural class of secondary transporters. J. Biol. Chem. 271:25582-25589.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25582-25589
    • Van Geest, M.1    Lolkema, J.S.2
  • 185
    • 85038049002 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 186
    • 0033569920 scopus 로고    scopus 로고
    • +/citrate transporter CitS requires downstream TMS IX for insertion in the Escherichia coli membrane
    • +/citrate transporter CitS requires downstream TMS IX for insertion in the Escherichia coli membrane. J. Biol. Chem. 274:29705-29711.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29705-29711
    • Van Geest, M.1    Lolkema, J.S.2
  • 187
    • 0033613965 scopus 로고    scopus 로고
    • Insertion of a bacterial secondary transport protein in the endoplasmic reticulum membrane
    • van Geest, M., I. Nilsson, G. von Heijne, and J. S. Lolkema. 1999. Insertion of a bacterial secondary transport protein in the endoplasmic reticulum membrane. J. Biol. Chem. 274:2816-2823.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2816-2823
    • Van Geest, M.1    Nilsson, I.2    Von Heijne, G.3    Lolkema, J.S.4
  • 188
    • 0025940840 scopus 로고
    • Construction of a functional lactose permease devoid of cysteine residues
    • van Iwaarden, P. R., J. C. Pastore, W. N. Konings, and H. R. Kaback. 1991. Construction of a functional lactose permease devoid of cysteine residues. Biochemistry 30:9595-9600.
    • (1991) Biochemistry , vol.30 , pp. 9595-9600
    • Van Iwaarden, P.R.1    Pastore, J.C.2    Konings, W.N.3    Kaback, H.R.4
  • 189
    • 0032502787 scopus 로고    scopus 로고
    • The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry
    • Vannier, B., X. Zhu, D. Brown, and L. Birnbaumer. 1998. The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry. J. Biol. Chem. 273:8675-8679.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8675-8679
    • Vannier, B.1    Zhu, X.2    Brown, D.3    Birnbaumer, L.4
  • 190
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341: 456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 191
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. 1992. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 192
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G. 1994. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:167-192.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 193
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne, G., and Y. Gavel. 1988. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:671-678.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 194
    • 0030471958 scopus 로고    scopus 로고
    • Membrane topology of the high-affinity L-glutamate transporter (GLAST-1) of the central nervous system
    • Wahle, S., and W. Stoffel. 1996. Membrane topology of the high-affinity L-glutamate transporter (GLAST-1) of the central nervous system. J. Cell Biol. 135:1867-1877.
    • (1996) J. Cell Biol. , vol.135 , pp. 1867-1877
    • Wahle, S.1    Stoffel, W.2
  • 195
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and A. E. Johnson. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10:87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 196
    • 0021100147 scopus 로고
    • Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides
    • Welply, J. K., P. Shenbagamurthi, W. J. Lennarz, and F. Naider. 1983. Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides. J. Biol. Chem. 258:11856-11863.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11856-11863
    • Welply, J.K.1    Shenbagamurthi, P.2    Lennarz, W.J.3    Naider, F.4
  • 197
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels, H. P., and M. Spiess. 1988. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 55:61-70.
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.P.1    Spiess, M.2
  • 198
    • 0028018421 scopus 로고
    • Sec-independent translocation of a 100-residue periplasmic N-terminal tail in the E. coli inner membrane protein proW
    • Whitley, P., T. Zander, M. Ehrmann, M. Haardt, E. Bremer, and G. von Heijne. 1994. Sec-independent translocation of a 100-residue periplasmic N-terminal tail in the E. coli inner membrane protein proW. EMBO J. 13:4653-4661.
    • (1994) EMBO J. , vol.13 , pp. 4653-4661
    • Whitley, P.1    Zander, T.2    Ehrmann, M.3    Haardt, M.4    Bremer, E.5    Von Heijne, G.6
  • 199
    • 0029817931 scopus 로고    scopus 로고
    • Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
    • Wilkinson, B. M., A. J. Critchley, and C. J. Stirling. 1996. Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J. Biol. Chem. 271:25590-25597.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25590-25597
    • Wilkinson, B.M.1    Critchley, A.J.2    Stirling, C.J.3
  • 200
    • 0026683052 scopus 로고
    • TnphoA and TnphoA′ elements for making and switching fusions for study of transcription, translation, and cell surface localization
    • Wilmes-Riesenberg, M. R., and B. L. Wanner. 1992. TnphoA and TnphoA′ elements for making and switching fusions for study of transcription, translation, and cell surface localization. J. Bacteriol. 174:4558-4575.
    • (1992) J. Bacteriol. , vol.174 , pp. 4558-4575
    • Wilmes-Riesenberg, M.R.1    Wanner, B.L.2
  • 201
    • 0022001799 scopus 로고
    • Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli
    • Wolfe, P. B., M. Rice, and W. Wickner. 1985. Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli. J. Biol. Chem. 260:1836-1841.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1836-1841
    • Wolfe, P.B.1    Rice, M.2    Wickner, W.3
  • 202
    • 0026622930 scopus 로고
    • Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase
    • Wu, J., L. S. Tisa, and B. P. Rosen. 1992. Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase. J. Biol. Chem. 267:12570-12576.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12570-12576
    • Wu, J.1    Tisa, L.S.2    Rosen, B.P.3
  • 203
    • 0027501362 scopus 로고
    • Amino acids lining the channel of the gamma-aminobutyric acid type A receptor identified by cysteine substitution
    • Xu, M., and M. H. Akabas. 1993. Amino acids lining the channel of the gamma-aminobutyric acid type A receptor identified by cysteine substitution. J. Biol. Chem. 268:21505-21508.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21505-21508
    • Xu, M.1    Akabas, M.H.2
  • 204
    • 0028970548 scopus 로고
    • Interaction of picrotoxin with GABAA receptor channel-lining residues probed in cysteine mutants
    • Xu, M., D. F. Covey, and M. H. Akabas. 1995. Interaction of picrotoxin with GABAA receptor channel-lining residues probed in cysteine mutants. Biophys. J. 69:1858-1867.
    • (1995) Biophys. J. , vol.69 , pp. 1858-1867
    • Xu, M.1    Covey, D.F.2    Akabas, M.H.3
  • 205
    • 0029076423 scopus 로고
    • Residues in the pathway through a membrane transporter
    • Yan, R. T., and P. C. Maloney. 1995. Residues in the pathway through a membrane transporter. Proc. Natl. Acad. Sci. USA 92:5973-5976.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5973-5976
    • Yan, R.T.1    Maloney, P.C.2
  • 206
    • 0031751327 scopus 로고    scopus 로고
    • Topological model of the Rhodobacter capsulatus light-harvesting complex I assembly protein LhaA (previously known as ORF1696)
    • Young, C. S., and J. T. Beatty. 1998. Topological model of the Rhodobacter capsulatus light-harvesting complex I assembly protein LhaA (previously known as ORF1696). J. Bacteriol. 180:4742-4745.
    • (1998) J. Bacteriol. , vol.180 , pp. 4742-4745
    • Young, C.S.1    Beatty, J.T.2
  • 207
    • 0032540513 scopus 로고    scopus 로고
    • Topological localization of cysteine 74 in the GABA transporter, GAT1, and its importance in ion binding and permeation
    • Yu, N., Y. Cao, S. Mager, and H. A. Lester. 1998. Topological localization of cysteine 74 in the GABA transporter, GAT1, and its importance in ion binding and permeation. FEBS Lett. 426:174-178.
    • (1998) FEBS Lett. , vol.426 , pp. 174-178
    • Yu, N.1    Cao, Y.2    Mager, S.3    Lester, H.A.4
  • 208
    • 0025884704 scopus 로고
    • The use of gene fusions to examine the membrane topology of the L subunit of the photosynthetic reaction center and of the cytochrome b subunit of the bc1 complex from Rhodobacter sphaeroides
    • Yun, C. H., S. R. Van Doren, A. R. Crofts, and R. B. Gennis. 1991. The use of gene fusions to examine the membrane topology of the L subunit of the photosynthetic reaction center and of the cytochrome b subunit of the bc1 complex from Rhodobacter sphaeroides. J. Biol. Chem. 266:10967-10973.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10967-10973
    • Yun, C.H.1    Van Doren, S.R.2    Crofts, A.R.3    Gennis, R.B.4
  • 209
    • 0028926860 scopus 로고
    • Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms
    • Zen, K. H., T. G. Consler, and H. R. Kaback. 1995. Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms. Biochemistry 34:3430-3437.
    • (1995) Biochemistry , vol.34 , pp. 3430-3437
    • Zen, K.H.1    Consler, T.G.2    Kaback, H.R.3
  • 210
    • 0031946150 scopus 로고    scopus 로고
    • Dissection of de novo membrane insertion activities of internal transmembrane segments of ATP-binding-cassette transporters: Toward understanding topological rules for membrane assembly of polytopic membrane proteins
    • Zhang, J. T., M. Chen, E. Han, and C. Wang. 1998. Dissection of de novo membrane insertion activities of internal transmembrane segments of ATP-binding-cassette transporters: toward understanding topological rules for membrane assembly of polytopic membrane proteins. Mol. Biol. Cell 9:853-863.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 853-863
    • Zhang, J.T.1    Chen, M.2    Han, E.3    Wang, C.4
  • 211
    • 0028938775 scopus 로고
    • Topological determinants of internal transmembrane segments in P-glycoprotein sequences
    • Zhang, J. T., C. H. Lee, M. Duthie, and V. Ling. 1995. Topological determinants of internal transmembrane segments in P-glycoprotein sequences. J. Biol. Chem. 270:1742-1746.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1742-1746
    • Zhang, J.T.1    Lee, C.H.2    Duthie, M.3    Ling, V.4
  • 212
    • 0029165325 scopus 로고
    • Membrane topology of the MotA protein of Escherichia coli
    • Zhou, J., R. T. Fazzio, and D. F. Blair. 1995. Membrane topology of the MotA protein of Escherichia coli. J. Mol. Biol. 251:237-242.
    • (1995) J. Mol. Biol. , vol.251 , pp. 237-242
    • Zhou, J.1    Fazzio, R.T.2    Blair, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.