메뉴 건너뛰기




Volumn 43, Issue 13, 2004, Pages 3917-3928

Improved Energy Coupling of Human P-glycoprotein by the Glycine 185 to Valine Mutation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; ADENOSINETRIPHOSPHATE; CELLS; ENTHALPY; ENTROPY; ENZYMES; MUTAGENESIS; PROTEINS; SACCHARIFICATION; THERMODYNAMIC PROPERTIES;

EID: 1842538878     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035365l     Document Type: Article
Times cited : (39)

References (60)
  • 1
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M. M., and Pastan, I. (1993) Biochemistry of multidrug resistance mediated by the multidrug transporter, Annu. Rev. Biochem. 62, 385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 3
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I. B., and Blight, M. A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans, J. Mol. Biol. 293, 381-399.
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 4
    • 0029559159 scopus 로고
    • The catalytic cycle of P-glycoprotein
    • Senior, A. E., Al-Shawi, M. K., and Urbatsch, I. L. (1995) The catalytic cycle of P-glycoprotein, FEBS Lett. 377, 285-289.
    • (1995) FEBS Lett. , vol.377 , pp. 285-289
    • Senior, A.E.1    Al-Shawi, M.K.2    Urbatsch, I.L.3
  • 5
    • 0346732289 scopus 로고    scopus 로고
    • Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein
    • Al-Shawi, M. K., Polar, M. K., Omote, H., and Figler, R. A. (2003) Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein, J. Biol. Chem. 278, 52629-52640.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52629-52640
    • Al-Shawi, M.K.1    Polar, M.K.2    Omote, H.3    Figler, R.A.4
  • 6
    • 0024292717 scopus 로고
    • An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene
    • Choi, K. H., Chen, C. J., Kriegler, M., and Roninson, I. B. (1988) An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene, Cell 53, 519-529.
    • (1988) Cell , vol.53 , pp. 519-529
    • Choi, K.H.1    Chen, C.J.2    Kriegler, M.3    Roninson, I.B.4
  • 7
    • 0025051429 scopus 로고
    • Molecular basis of preferential resistance to colchicine in multidrug-resistant human cells conferred by Gly-185 to Val-185 substitution in P-glycoprotein
    • Safa, A. R., Stern, R. K., Choi, K., Agresti, M., Tamai, I., Mehta, N. D., and Roninson, I. B. (1990) Molecular basis of preferential resistance to colchicine in multidrug-resistant human cells conferred by Gly-185 to Val-185 substitution in P-glycoprotein, Proc. Natl. Acad. Sci. U.S.A. 87, 7225-7229.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7225-7229
    • Safa, A.R.1    Stern, R.K.2    Choi, K.3    Agresti, M.4    Tamai, I.5    Mehta, N.D.6    Roninson, I.B.7
  • 8
    • 0028285002 scopus 로고
    • Kinetic evidence suggesting that the multidrug transporter differentially handles influx and efflux of its substrates
    • Stein, W. D., Cardarelli, C., Pastan, I., and Gottesman, M. M. (1994) Kinetic evidence suggesting that the multidrug transporter differentially handles influx and efflux of its substrates, Mol. Pharmacol. 45, 763-772.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 763-772
    • Stein, W.D.1    Cardarelli, C.2    Pastan, I.3    Gottesman, M.M.4
  • 9
    • 0024787142 scopus 로고
    • A new vector using the human multidrug resistance gene as a selectable marker enables overexpression of foreign genes in eukaryotic cells
    • Kane, S. E., Reinhard, D. H., Fordis, C. M., Pastan, I., and Gottesman, M. M. (1989) A new vector using the human multidrug resistance gene as a selectable marker enables overexpression of foreign genes in eukaryotic cells, Gene 84, 439-446.
    • (1989) Gene , vol.84 , pp. 439-446
    • Kane, S.E.1    Reinhard, D.H.2    Fordis, C.M.3    Pastan, I.4    Gottesman, M.M.5
  • 10
    • 0034176255 scopus 로고    scopus 로고
    • Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: High-yield expression and purification of human P-glycoprotein
    • Figler, R. A., Omote, H., Nakamoto, R. K., and Al-Shawi, M. K. (2000) Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: high-yield expression and purification of human P-glycoprotein, Arch. Biochem. Biophys. 376, 34-46.
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 34-46
    • Figler, R.A.1    Omote, H.2    Nakamoto, R.K.3    Al-Shawi, M.K.4
  • 11
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo, T. W., and Clarke, D. M. (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
  • 13
    • 0025974219 scopus 로고
    • Tackling the protease problem in Saccharomyces cerevisiae
    • Jones, E. W. (1991) Tackling the protease problem in Saccharomyces cerevisiae, Methods Enzymol. 194, 428-453.
    • (1991) Methods Enzymol. , vol.194 , pp. 428-453
    • Jones, E.W.1
  • 15
    • 0028362501 scopus 로고
    • Charaterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch, I. L., Al-Shawi, M. K., and Senior, A. E. (1994) Charaterization of the ATPase activity of purified Chinese hamster P-glycoprotein, Biochemistry 33, 7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 16
    • 0023158563 scopus 로고
    • Inorganic and organic phosphate measurements in the nanomolar range
    • Van Veldhoven, P. P., and Mannaerts, G. P. (1987) Inorganic and organic phosphate measurements in the nanomolar range, Anal. Biochem. 161, 45-48.
    • (1987) Anal. Biochem. , vol.161 , pp. 45-48
    • Van Veldhoven, P.P.1    Mannaerts, G.P.2
  • 17
    • 0030612021 scopus 로고    scopus 로고
    • 0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway
    • 0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway, Biochemistry 36, 12961-12969.
    • (1997) Biochemistry , vol.36 , pp. 12961-12969
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 18
    • 0037160075 scopus 로고    scopus 로고
    • A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein
    • Omote, H., and Al-Shawi, M. K. (2002) A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein, J. Biol. Chem. 277, 45688-45694.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45688-45694
    • Omote, H.1    Al-Shawi, M.K.2
  • 19
    • 0024297489 scopus 로고
    • 1-ATPase and application to the study of mutant enzymes
    • 1-ATPase and application to the study of mutant enzymes, J. Biol. Chem. 263, 19640-19648.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19640-19648
    • Al-Shawi, M.K.1    Senior, A.E.2
  • 20
    • 0344443751 scopus 로고    scopus 로고
    • Identification of two different states of P-glycoprotein in its catalytic cycle. Role of the linker region in the transition between these two states
    • Rao, U. S., and Nuti, S. L. (2003) Identification of two different states of P-glycoprotein in its catalytic cycle. Role of the linker region in the transition between these two states, J. Biol. Chem. 278, 46576-46582.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46576-46582
    • Rao, U.S.1    Nuti, S.L.2
  • 21
    • 0029797074 scopus 로고    scopus 로고
    • Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system
    • Ramachandra, M., Ambudkar, S. V., Gottesman, M. M., Pastan, I., and Hrycyna, C. A. (1996) Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system, Mol. Biol. Cell 7, 1485-1498.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1485-1498
    • Ramachandra, M.1    Ambudkar, S.V.2    Gottesman, M.M.3    Pastan, I.4    Hrycyna, C.A.5
  • 22
    • 0028899422 scopus 로고
    • Mutation of glycine 185 to valine alters the ATPase function of human P-glycoprotein expressed in Sf9 cells
    • Rao, U. S. (1995) Mutation of glycine 185 to valine alters the ATPase function of human P-glycoprotein expressed in Sf9 cells, J. Biol. Chem. 270, 6686-6690.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6686-6690
    • Rao, U.S.1
  • 24
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu, R., and Sharom, F. J. (1996) Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains, Biochemistry 35, 11865-11873.
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 25
    • 0032716822 scopus 로고    scopus 로고
    • Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters
    • Krupka, R. M. (1999) Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters, J. Membr. Biol. 172, 129-143.
    • (1999) J. Membr. Biol. , vol.172 , pp. 129-143
    • Krupka, R.M.1
  • 26
    • 84983721796 scopus 로고
    • The enthalpy-entropy relationship
    • Exner, O. (1973) The enthalpy-entropy relationship, Prog. Phys. Org. Chem. 10, 411-482.
    • (1973) Prog. Phys. Org. Chem. , vol.10 , pp. 411-482
    • Exner, O.1
  • 27
    • 0027482461 scopus 로고
    • Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
    • Sharom, F. J., Yu, X., and Doige, C. A. (1993) Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein, J. Biol. Chem. 268, 24197-24202.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24197-24202
    • Sharom, F.J.1    Yu, X.2    Doige, C.A.3
  • 28
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • Loo, T. W., and Clarke, D. M. (2002) Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein, J. Biol. Chem. 277, 44332-44338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 29
    • 0033485546 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide-binding domains of the multidrug resistance transporter P-glycoprotein
    • Blott, E. J., Higgins, C. F., and Linton, K. J. (1999) Cysteine-scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide-binding domains of the multidrug resistance transporter P-glycoprotein, EMBO J. 18, 6800-6808.
    • (1999) EMBO J. , vol.18 , pp. 6800-6808
    • Blott, E.J.1    Higgins, C.F.2    Linton, K.J.3
  • 30
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics, Biochemistry 35, 7692-7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 31
    • 0024388720 scopus 로고
    • Evolutionary optimization of the catalytic effectiveness of an enzyme
    • Burbaum, J. J., Raines, R. T., Albery, W. J., and Knowles, J. R. (1989) Evolutionary optimization of the catalytic effectiveness of an enzyme, Biochemistry 28, 9293-9305.
    • (1989) Biochemistry , vol.28 , pp. 9293-9305
    • Burbaum, J.J.1    Raines, R.T.2    Albery, W.J.3    Knowles, J.R.4
  • 32
    • 0024362996 scopus 로고
    • P-glycoprotein gene (MDR1) cDNA from human adrenal: Normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance
    • Kioka, N., Tsubota, J., Kakehi, Y., Komano, T., Gottesman, M. M., Pastan, I., and Ueda, K. (1989) P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance, Biochem. Biophys. Res. Commun. 162, 224-231.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 224-231
    • Kioka, N.1    Tsubota, J.2    Kakehi, Y.3    Komano, T.4    Gottesman, M.M.5    Pastan, I.6    Ueda, K.7
  • 33
    • 0035836495 scopus 로고    scopus 로고
    • Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein
    • Ruth, A., Stein, W. D., Rose, E., and Roninson, I. B. (2001) Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein, Biochemistry 40, 4332-4339.
    • (2001) Biochemistry , vol.40 , pp. 4332-4339
    • Ruth, A.1    Stein, W.D.2    Rose, E.3    Roninson, I.B.4
  • 34
    • 0031027579 scopus 로고    scopus 로고
    • 1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits
    • 1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits, J. Biol. Chem. 272, 2300-2306.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2300-2306
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 36
    • 0025185116 scopus 로고
    • Towards an understanding of the structural basis of 'forbidden' transport pathways in the Escherichia coli lactose carrier: Mutations probing the energy barriers to uncoupled transport
    • King, S. C., and Wilson, T. H. (1990) Towards an understanding of the structural basis of 'forbidden' transport pathways in the Escherichia coli lactose carrier: mutations probing the energy barriers to uncoupled transport, Mol. Microbiol. 4, 1433-1438.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1433-1438
    • King, S.C.1    Wilson, T.H.2
  • 37
    • 37049153631 scopus 로고
    • Analytical description of the effects of modifiers and of enzyme multivalency upon the steady-state catalyzed reaction rate
    • Botts, J., and Morales, M. (1953) Analytical description of the effects of modifiers and of enzyme multivalency upon the steady-state catalyzed reaction rate, Trans. Faraday Soc. 49, 696-707.
    • (1953) Trans. Faraday Soc. , vol.49 , pp. 696-707
    • Botts, J.1    Morales, M.2
  • 41
    • 0033539603 scopus 로고    scopus 로고
    • Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: Probing the role of hydrophobic residue size in the central region of the fusion peptide
    • Han, X., Steinhauer, D. A., Wharton, S. A., and Tamm, L. K. (1999) Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: probing the role of hydrophobic residue size in the central region of the fusion peptide, Biochemistry 38, 15052-15059.
    • (1999) Biochemistry , vol.38 , pp. 15052-15059
    • Han, X.1    Steinhauer, D.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 42
    • 0024415109 scopus 로고
    • Conformational effects of amino acid substitutions in the P-glycoprotein of the mdr 1 gene
    • Brandt-Rauf, P. W., Lee, G., Carty, R. P., Pincus, M. R., and Chen, J. M. (1989) Conformational effects of amino acid substitutions in the P-glycoprotein of the mdr 1 gene, J. Protein Chem. 8, 563-573.
    • (1989) J. Protein Chem. , vol.8 , pp. 563-573
    • Brandt-Rauf, P.W.1    Lee, G.2    Carty, R.P.3    Pincus, M.R.4    Chen, J.M.5
  • 43
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homologue in a closed conformation
    • Chang, G. (2003) Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homologue in a closed conformation, J. Mol. Biol. 330, 419-430.
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 44
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F.-L., and Kim, S. H. (1998) Crystal structure of the ATP-binding subunit of an ABC transporter, Nature 396, 703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.-L.5    Kim, S.H.6
  • 45
    • 0034682894 scopus 로고    scopus 로고
    • An integrated approach to the analysis and modeling of protein sequences and structures. II. On the relationship between sequence and structural similarity for proteins that are not obviously related in sequence
    • Yang, A. S., and Honig, B. (2000) An integrated approach to the analysis and modeling of protein sequences and structures. II. On the relationship between sequence and structural similarity for proteins that are not obviously related in sequence, J. Mol. Biol. 301, 679-689.
    • (2000) J. Mol. Biol. , vol.301 , pp. 679-689
    • Yang, A.S.1    Honig, B.2
  • 46
    • 0042531543 scopus 로고    scopus 로고
    • A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure
    • Seigneuret, M., and Garnier-Suillerot, A. (2003) A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure, J. Biol. Chem. 278, 30115-30124.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30115-30124
    • Seigneuret, M.1    Garnier-Suillerot, A.2
  • 47
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A Homolog of the Multidrug Resistance ATP Binding Cassette (ABC) Transporters
    • Chang, G., and Roth, C. B. (2001) Structure of MsbA from E. coli: A Homolog of the Multidrug Resistance ATP Binding Cassette (ABC) Transporters, Science 293, 1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 48
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling
    • Stenham, D. R., Campbell, J. D., Sansom, M. S., Higgins, C. F., Kerr, I. D., and Linton, K. J. (2003) An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling, FASEB J. 17, 2287-2289.
    • (2003) FASEB J. , vol.17 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 49
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T., and Rees, D. C. (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism, Science 296, 1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 50
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P., Karcher, A., Shin, D. S., Craig, L., Arthur, L. M., Carney, J. P., and Tainer, J. A. (2000) Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily, Cell 101, 789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 51
    • 0036789902 scopus 로고    scopus 로고
    • Mechanism of ABC transporters: A molecular dynamics simulation of a well characterized nucleotide-binding subunit
    • Jones, P. M., and George, A. M. (2002) Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit, Proc. Natl. Acad. Sci. U.S.A. 99, 12639-12644.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12639-12644
    • Jones, P.M.1    George, A.M.2
  • 52
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Schmitt, L., and Tampe, R. (2002) Structure and mechanism of ABC transporters, Curr. Opin. Struct. Biol. 12, 754-760.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 754-760
    • Schmitt, L.1    Tampe, R.2
  • 53
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • Urbatsch, I. L., Gimi, K., Wilke-Mounts, S., and Senior, A. E. (2000) Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein, Biochemistry 39, 11921-11927.
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 54
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., Hofnung, M., and Dassa, E. (1997) Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits, EMBO J. 16, 3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 55
    • 0026473238 scopus 로고
    • Identification of residues in the first cytoplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters
    • Currier, S. J., Kane, S. E., Willingham, M. C., Cardarelli, C. O., Pastan, I., and Gottesman, M. M. (1992) Identification of residues in the first cytoplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters, J. Biol. Chem. 267, 25153-25159.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25153-25159
    • Currier, S.J.1    Kane, S.E.2    Willingham, M.C.3    Cardarelli, C.O.4    Pastan, I.5    Gottesman, M.M.6
  • 56
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser, A., Do, R. K. G., and Sali, A. (2000) Modeling of loops in protein structures, Protein Sci. 9, 1753-1773.
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.G.2    Sali, A.3
  • 57
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins, D. G., and Sharp, P. M. (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer, Gene 73, 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 58
    • 0027375587 scopus 로고
    • Secondary structure prediction of all-helical proteins in two states
    • Rost, B., and Sander, C. (1993) Secondary structure prediction of all-helical proteins in two states, Protein Eng. 6, 831-836.
    • (1993) Protein Eng. , vol.6 , pp. 831-836
    • Rost, B.1    Sander, C.2
  • 59
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. (1996) PHD: predicting one-dimensional protein structure by profile-based neural networks, Methods Enzymol. 266, 525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 60
    • 0026244229 scopus 로고
    • A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.