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Volumn 45, Issue 13, 2006, Pages 4182-4189

Site-directed alkylation of cysteine replacements in the lactose permease of Escherichia coli: Helices I, III, VI, and XI

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; AMINES; BINDING ENERGY; ESCHERICHIA COLI; MUTAGENESIS; SOLVENTS; SUGARS; X RAY ANALYSIS;

EID: 33645537372     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052631h     Document Type: Article
Times cited : (23)

References (59)
  • 1
    • 0022558555 scopus 로고
    • Purification, reconstitution, and characterization of the lac permease of Escherichia coli
    • Viitanen, P., Newman, M. J., Foster, D. L., Wilson, T. H., and Kaback, H. R. (1986) Purification, reconstitution, and characterization of the lac permease of Escherichia coli, Methods Enzymol. 125, 429-452.
    • (1986) Methods Enzymol. , vol.125 , pp. 429-452
    • Viitanen, P.1    Newman, M.J.2    Foster, D.L.3    Wilson, T.H.4    Kaback, H.R.5
  • 2
    • 0028291250 scopus 로고
    • Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli
    • Sahin-Tóth, M., Lawrence, M. C., and Kaback, H. R. (1994) Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 91, 5421-5425.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5421-5425
    • Sahin-Tóth, M.1    Lawrence, M.C.2    Kaback, H.R.3
  • 3
    • 0025938223 scopus 로고
    • Characterization of purified, reconstituted site-directed cysteine mutants of the lactose permease of Escherichia coli
    • van Iwaarden, P. R., Driessen, A. J., Menick, D. R., Kaback, H. R., and Konings, W. N. (1991) Characterization of purified, reconstituted site-directed cysteine mutants of the lactose permease of Escherichia coli, J. Biol. Chem. 266, 15688-15692.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15688-15692
    • Van Iwaarden, P.R.1    Driessen, A.J.2    Menick, D.R.3    Kaback, H.R.4    Konings, W.N.5
  • 4
    • 0024368803 scopus 로고
    • A five-residue sequence near the carboxyl terminus of the polytopic membrane protein lac permease is required for stability within the membrane
    • Roepe, P. D., Zbar, R. I., Sarkar, H. K., and Kaback, H. R. (1989) A five-residue sequence near the carboxyl terminus of the polytopic membrane protein lac permease is required for stability within the membrane, Proc. Natl. Acad. Sci. U.S.A. 86, 3992-3996.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 3992-3996
    • Roepe, P.D.1    Zbar, R.I.2    Sarkar, H.K.3    Kaback, H.R.4
  • 5
    • 0026322834 scopus 로고
    • Sequential truncation of the lactose permease over a three-amino acid sequence near the carboxyl terminus leads to progressive loss of activity and stability
    • McKenna, E., Hardy, D., Pastore, J. C., and Kaback, H. R. (1991) Sequential truncation of the lactose permease over a three-amino acid sequence near the carboxyl terminus leads to progressive loss of activity and stability, Proc. Natl. Acad. Sci. U.S.A. 88, 2969-2973.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2969-2973
    • McKenna, E.1    Hardy, D.2    Pastore, J.C.3    Kaback, H.R.4
  • 6
    • 0026688406 scopus 로고
    • Evidence that the final turn of the last transmembrane helix in the lactose permease is required for folding
    • McKenna, E., Hardy, D., and Kaback, H. R. (1992) Evidence that the final turn of the last transmembrane helix in the lactose permease is required for folding, J. Biol. Chem. 267, 6471-6474.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6471-6474
    • McKenna, E.1    Hardy, D.2    Kaback, H.R.3
  • 7
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins
    • Frillingos, S., Sahin-Toth, M., Wu, J., and Kaback, H. R. (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
  • 8
    • 33751385088 scopus 로고
    • Cysteine scanning mutagenesis of putative helix XI in the lactose permease of Escherichia coli
    • Dunten, R. L., Sahin-Toth, M., and Kaback, H. R. (1993) Cysteine scanning mutagenesis of putative helix XI in the lactose permease of Escherichia coli, Biochemistry 32, 12644-12650.
    • (1993) Biochemistry , vol.32 , pp. 12644-12650
    • Dunten, R.L.1    Sahin-Toth, M.2    Kaback, H.R.3
  • 9
    • 0029983491 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of helix VI and the flanking hydrophilic domains in the lactose permease of Escherichia coli
    • Frillingos, S., and Kaback, H. R. (1996) Cysteine-scanning mutagenesis of helix VI and the flanking hydrophilic domains in the lactose permease of Escherichia coli, Biochemistry 35, 5333-5338.
    • (1996) Biochemistry , vol.35 , pp. 5333-5338
    • Frillingos, S.1    Kaback, H.R.2
  • 10
    • 0031056670 scopus 로고    scopus 로고
    • The role of helix VIII in the lactose permease of Escherichia coli. I. Cys-scanning mutagenesis
    • Frillingos, S., Ujwal, M. L., Sun, J., and Kaback, H. R. (1997) The role of helix VIII in the lactose permease of Escherichia coli. I. Cys-scanning mutagenesis, Protein Sci. 6, 431-437.
    • (1997) Protein Sci. , vol.6 , pp. 431-437
    • Frillingos, S.1    Ujwal, M.L.2    Sun, J.3    Kaback, H.R.4
  • 11
    • 0030681217 scopus 로고    scopus 로고
    • Site-directed spin-labeling of transmembrane domain VII and the 4B1 antibody epitope in the lactose permease of Escherichia coli
    • Voss, J., Hubbell, W. L., Hernandez, J., and Kaback, H. R. (1997) Site-directed spin-labeling of transmembrane domain VII and the 4B1 antibody epitope in the lactose permease of Escherichia coli, Biochemistry 36, 15055-15061.
    • (1997) Biochemistry , vol.36 , pp. 15055-15061
    • Voss, J.1    Hubbell, W.L.2    Hernandez, J.3    Kaback, H.R.4
  • 12
    • 0032474478 scopus 로고    scopus 로고
    • Sulfhydryl oxidation of mutants with cysteine in place of acidic residues in the lactose permease
    • Voss, J., Sun, J., and Kaback, H. R. (1998) Sulfhydryl oxidation of mutants with cysteine in place of acidic residues in the lactose permease, Biochemistry 37, 8191-8196.
    • (1998) Biochemistry , vol.37 , pp. 8191-8196
    • Voss, J.1    Sun, J.2    Kaback, H.R.3
  • 13
    • 0033619698 scopus 로고    scopus 로고
    • Nitroxide scanning electron paramagnetic resonance of helices IV, V and the intervening loop in the lactose permease of Escherichia coli
    • Zhao, M., Zen, K.-C., Hernandez-Borrell, J., Altenbach, C., Hubbell, W. L., and Kaback, H. R. (1999) Nitroxide scanning electron paramagnetic resonance of helices IV, V and the intervening loop in the lactose permease of Escherichia coli, Biochemistry 38, 15970-15977.
    • (1999) Biochemistry , vol.38 , pp. 15970-15977
    • Zhao, M.1    Zen, K.-C.2    Hernandez-Borrell, J.3    Altenbach, C.4    Hubbell, W.L.5    Kaback, H.R.6
  • 14
    • 0030747620 scopus 로고    scopus 로고
    • Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking
    • Wu, J., and Kaback, H. R. (1997) Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking, J. Mol. Biol. 270, 285-293.
    • (1997) J. Mol. Biol. , vol.270 , pp. 285-293
    • Wu, J.1    Kaback, H.R.2
  • 15
    • 0029789304 scopus 로고    scopus 로고
    • Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli
    • Wu, J., Voss, J., Hubbell, W. L., and Kaback, H. R. (1996) Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 93, 10123-10127.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10123-10127
    • Wu, J.1    Voss, J.2    Hubbell, W.L.3    Kaback, H.R.4
  • 16
    • 0030760970 scopus 로고    scopus 로고
    • Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed cross-linking
    • Sun, J., and Kaback, H. R. (1997) Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed cross-linking. Biochemistry 36, 11959-11965.
    • (1997) Biochemistry , vol.36 , pp. 11959-11965
    • Sun, J.1    Kaback, H.R.2
  • 18
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli, Science 301, 610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 19
    • 0037452911 scopus 로고    scopus 로고
    • A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability
    • Smirnova, I. N., and Kaback, H. R. (2003) A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability, Biochemistry 42, 3025-3031.
    • (2003) Biochemistry , vol.42 , pp. 3025-3031
    • Smirnova, I.N.1    Kaback, H.R.2
  • 22
    • 0035807025 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helices IV and V that contain the major determinants for substrate binding
    • Kwaw, I., Zen, K. C., Hu, Y., and Kaback, H. R. (2001) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helices IV and V that contain the major determinants for substrate binding, Biochemistry 40, 10491-10499.
    • (2001) Biochemistry , vol.40 , pp. 10491-10499
    • Kwaw, I.1    Zen, K.C.2    Hu, Y.3    Kaback, H.R.4
  • 23
    • 0029043941 scopus 로고
    • Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopy
    • Wu, J., Frillingos, S., and Kaback, H. R. (1995) Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopy, Biochemistry 34, 8257-8263.
    • (1995) Biochemistry , vol.34 , pp. 8257-8263
    • Wu, J.1    Frillingos, S.2    Kaback, H.R.3
  • 24
    • 0034609514 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix X
    • Venkatesan, P., Hu, Y., and Kaback, H. R. (2000) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix X, Biochemistry 39, 10656-10661.
    • (2000) Biochemistry , vol.39 , pp. 10656-10661
    • Venkatesan, P.1    Hu, Y.2    Kaback, H.R.3
  • 25
    • 0034609555 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix VII
    • Venkatesan, P., Kwaw, I., Hu, Y., and Kaback, H. R. (2000) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix VII, Biochemistry 39, 10641-10648.
    • (2000) Biochemistry , vol.39 , pp. 10641-10648
    • Venkatesan, P.1    Kwaw, I.2    Hu, Y.3    Kaback, H.R.4
  • 26
    • 0034609552 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix II
    • Venkatesan, P., Liu, Z., Hu, Y., and Kaback, H. R. (2000) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix II, Biochemistry 39, 10649-10655.
    • (2000) Biochemistry , vol.39 , pp. 10649-10655
    • Venkatesan, P.1    Liu, Z.2    Hu, Y.3    Kaback, H.R.4
  • 27
    • 0030614685 scopus 로고    scopus 로고
    • The role of helix VIII in the lactose permease of Escherichia coli. II. Site-directed sulfhydryl modification
    • Frillingos, S., and Kaback, H. R. (1997) The role of helix VIII in the lactose permease of Escherichia coli. II. Site-directed sulfhydryl modification, Protein Sci. 6, 438-443.
    • (1997) Protein Sci. , vol.6 , pp. 438-443
    • Frillingos, S.1    Kaback, H.R.2
  • 28
    • 0038333417 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of helix IX in the lactose permease of Escherichia coli
    • Zhang, W., Hu, Y., and Kaback, H. R. (2003) Site-directed sulfhydryl labeling of helix IX in the lactose permease of Escherichia coli, Biochemistry 42, 4904-4908.
    • (2003) Biochemistry , vol.42 , pp. 4904-4908
    • Zhang, W.1    Hu, Y.2    Kaback, H.R.3
  • 29
    • 0009651669 scopus 로고
    • Site-directed sulfhydryl chemistry and spectroscopy: Applications in the aspartate receptor system
    • Falke, J. J., Sternberg, D. E., and Koshland, D. E. (1986) Site-directed sulfhydryl chemistry and spectroscopy: Applications in the aspartate receptor system, Biophys. J. 49, 20a.
    • (1986) Biophys. J. , vol.49
    • Falke, J.J.1    Sternberg, D.E.2    Koshland, D.E.3
  • 30
    • 0026670486 scopus 로고
    • + antiporter of Escherichia coli encoded by transposon Tn10. The role of a conserved sequence motif, GXXXXRXGRR, in a putative cytoplasmic loop between helices 2 and 3
    • + antiporter of Escherichia coli encoded by transposon Tn10. The role of a conserved sequence motif, GXXXXRXGRR, in a putative cytoplasmic loop between helices 2 and 3, J. Biol. Chem. 267, 19155-19162.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19155-19162
    • Yamaguchi, A.1    Someya, Y.2    Sawai, T.3
  • 32
    • 0031451150 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor
    • Danielson, M. A., Bass, R. B., and Falke, J. J. (1997) Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor, J. Biol. Chem. 272, 32878-32888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32878-32888
    • Danielson, M.A.1    Bass, R.B.2    Falke, J.J.3
  • 33
    • 0032575326 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor
    • Butler, S. L., and Falke, J. J. (1998) Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor, Biochemistry 37, 10746-10756.
    • (1998) Biochemistry , vol.37 , pp. 10746-10756
    • Butler, S.L.1    Falke, J.J.2
  • 34
    • 0032566732 scopus 로고    scopus 로고
    • Detection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning
    • Bass, R. B., and Falke, J. J. (1998) Detection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning, J. Biol. Chem. 273, 25006-25014.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25006-25014
    • Bass, R.B.1    Falke, J.J.2
  • 35
    • 0033565446 scopus 로고    scopus 로고
    • The aspartate receptor cytoplasmic domain: In situ chemical analysis of structure, mechanism and dynamics
    • Bass, R. B., and Falke, J. J. (1999) The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics, Struct. Folding Des. 7, 829-840.
    • (1999) Struct. Folding Des. , vol.7 , pp. 829-840
    • Bass, R.B.1    Falke, J.J.2
  • 36
    • 0032575609 scopus 로고    scopus 로고
    • Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger
    • Tang, X.-O., Fujinaga, J., Kopito, R., and Casey, J. R. (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.-O.1    Fujinaga, J.2    Kopito, R.3    Casey, J.R.4
  • 37
    • 0033516475 scopus 로고    scopus 로고
    • +-coupled multidrug transporter from Escherichia coli, reveals a hydrophobic pathway for solutes
    • +-coupled multidrug transporter from Escherichia coli, reveals a hydrophobic pathway for solutes, J. Biol. Chem. 274, 19480-19486.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19480-19486
    • Mordoch, S.S.1    Granot, D.2    Lebendiker, M.3    Schuldiner, S.4
  • 41
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., Stauffer, D. A., Xu, M., and Karlin, A. (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
  • 42
    • 0028355745 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Stauffer, D. A., and Karlin, A. (1994) Acetylcholine receptor channel structure probed in cysteine-substitution mutants, Biochemistry 33, 6840-6849.
    • (1994) Biochemistry , vol.33 , pp. 6840-6849
    • Stauffer, D.A.1    Karlin, A.2
  • 43
    • 0029593370 scopus 로고
    • Towards a structural basis for the function of the nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and Akabas, M. H. (1995) Towards a structural basis for the function of the nicotinic acetylcholine receptors and their cousins, Neuron 15, 1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 44
    • 0032544066 scopus 로고    scopus 로고
    • The substrate-binding site in the lactose permease of Escherichia coli
    • Venkatesan, P., and Kaback, H. R. (1998) The substrate-binding site in the lactose permease of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 95, 9802-9807.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9802-9807
    • Venkatesan, P.1    Kaback, H.R.2
  • 45
    • 0026553380 scopus 로고
    • The N-terminal 22 amino acid residues in the lactose permease of Escherichia coli are not obligatory for membrane insertion or transport activity
    • Bibi, E., Stearns, S. M., and Kaback, H. R. (1992) The N-terminal 22 amino acid residues in the lactose permease of Escherichia coli are not obligatory for membrane insertion or transport activity, Proc. Natl. Acad. Sci. U.S.A. 89, 3180-3184.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 3180-3184
    • Bibi, E.1    Stearns, S.M.2    Kaback, H.R.3
  • 47
    • 0024357187 scopus 로고
    • Site-directed mutagenesis of tyrosine residues in the lac permease of Escherichia coli
    • Roepe, P. D., and Kaback, H. R. (1989) Site-directed mutagenesis of tyrosine residues in the lac permease of Escherichia coli, Biochemistry 28, 6127-6132.
    • (1989) Biochemistry , vol.28 , pp. 6127-6132
    • Roepe, P.D.1    Kaback, H.R.2
  • 48
    • 0028206024 scopus 로고
    • Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli
    • Sahin-Tóth, M., Persson, B., Schwieger, J., Cohan, M., and Kaback, H. R. (1994) Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli, Protein Sci. 3, 240-247.
    • (1994) Protein Sci. , vol.3 , pp. 240-247
    • Sahin-Tóth, M.1    Persson, B.2    Schwieger, J.3    Cohan, M.4    Kaback, H.R.5
  • 49
    • 0028574138 scopus 로고
    • The role of transmembrane domain III in the lactose permease of Escherichia coli
    • Sahin-Tóth, M., Frillingos, S., Bibi, E., Gonzalez, A., and Kaback, H. R. (1994) The role of transmembrane domain III in the lactose permease of Escherichia coli, Protein Sci. 3, 2302-2310.
    • (1994) Protein Sci. , vol.3 , pp. 2302-2310
    • Sahin-Tóth, M.1    Frillingos, S.2    Bibi, E.3    Gonzalez, A.4    Kaback, H.R.5
  • 51
    • 77957010716 scopus 로고
    • Bacterial membranes
    • Kaback, H. R. (1971) Bacterial Membranes, Methods Enzymol. 22, 99-120.
    • (1971) Methods Enzymol. , vol.22 , pp. 99-120
    • Kaback, H.R.1
  • 52
    • 0016750458 scopus 로고
    • Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles
    • Short, S. A., Kaback, H. R., and Kohn, L. D. (1975) Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles, J. Biol. Chem. 250, 4291-4296.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4291-4296
    • Short, S.A.1    Kaback, H.R.2    Kohn, L.D.3
  • 53
    • 19644392529 scopus 로고    scopus 로고
    • Interhelical packing modulates conformational flexibility in the lactose permease of Escherichia coli
    • Ermolova, N. V., Smirnova, I. N., Kasho, V. N., and Kaback, H. R. (2005) Interhelical packing modulates conformational flexibility in the lactose permease of Escherichia coli, Biochemistry 44, 7669-7677.
    • (2005) Biochemistry , vol.44 , pp. 7669-7677
    • Ermolova, N.V.1    Smirnova, I.N.2    Kasho, V.N.3    Kaback, H.R.4
  • 54
    • 0035823221 scopus 로고    scopus 로고
    • Helix packing in the lactose permease of Escherichia coli: Localization of helix VI
    • Guan, L., Weinglass, A. B., and Kaback, H. R. (2001) Helix packing in the lactose permease of Escherichia coli: Localization of helix VI, J. Mol. Biol. 312, 69-77.
    • (2001) J. Mol. Biol. , vol.312 , pp. 69-77
    • Guan, L.1    Weinglass, A.B.2    Kaback, H.R.3
  • 55
    • 20444419395 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease
    • Kaback, H. R. (2005) Structure and mechanism of the lactose permease, C. R. Biol. 328, 557-567.
    • (2005) C. R. Biol. , vol.328 , pp. 557-567
    • Kaback, H.R.1
  • 56
    • 0027289570 scopus 로고
    • Cysteine scanning mutagenesis of putative transmembrane helices IX and X in the lactose permease of Escherichia coli
    • Sahin-Tóth, M., and Kaback, H. R. (1993) Cysteine scanning mutagenesis of putative transmembrane helices IX and X in the lactose permease of Escherichia coli, Protein Sci. 2, 1024-1033.
    • (1993) Protein Sci. , vol.2 , pp. 1024-1033
    • Sahin-Tóth, M.1    Kaback, H.R.2
  • 57
    • 0030685033 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential
    • Frillingos, S., Gonzalez, A., and Kaback, H. R. (1997) Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential, Biochemistry 36, 14284-14290.
    • (1997) Biochemistry , vol.36 , pp. 14284-14290
    • Frillingos, S.1    Gonzalez, A.2    Kaback, H.R.3
  • 58
    • 0028200090 scopus 로고
    • Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli
    • Frillingos, S., Sahin-Tóth, M., Persson, B., and Kaback, H. R. (1994) Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli, Biochemistry 33, 8074-8081.
    • (1994) Biochemistry , vol.33 , pp. 8074-8081
    • Frillingos, S.1    Sahin-Tóth, M.2    Persson, B.3    Kaback, H.R.4
  • 59
    • 0031029785 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli
    • Frillingos, S., Sun, J., Gonzalez, A., and Kaback, H. R. (1997) Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli, Biochemistry 36, 269-273.
    • (1997) Biochemistry , vol.36 , pp. 269-273
    • Frillingos, S.1    Sun, J.2    Gonzalez, A.3    Kaback, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.