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Volumn 1419, Issue 2, 1999, Pages 173-185

Mutations in the white gene of Drosophila melanogaster affecting ABC transporters that determine eye colouration

Author keywords

ABC transporter; Brown gene; Pigment precursor transport; Scarlet gene; Transport ATPase; White gene

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE;

EID: 0033066317     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00064-4     Document Type: Article
Times cited : (150)

References (65)
  • 2
    • 0016186615 scopus 로고
    • Subcellular localization of the first three enzymes of the ommochrome synthetic pathway in Drosophila melanogaster
    • D.T. Sullivan, S.L. Grillo, R.J. Kilos, Subcellular localization of the first three enzymes of the ommochrome synthetic pathway in Drosophila melanogaster, J. Exp. Zool. 188 (1974) 225-234.
    • (1974) J. Exp. Zool. , vol.188 , pp. 225-234
    • Sullivan, D.T.1    Grillo, S.L.2    Kilos, R.J.3
  • 3
    • 0021693175 scopus 로고
    • DNA Sequence of the white locus of Drosophila melanogaster
    • K. O'Hare, C. Murphy, R. Levis, G.M. Rubin, DNA Sequence of the white locus of Drosophila melanogaster, J. Mol. Biol. 180 (1984) 437-455.
    • (1984) J. Mol. Biol. , vol.180 , pp. 437-455
    • O'Hare, K.1    Murphy, C.2    Levis, R.3    Rubin, G.M.4
  • 4
    • 0025287801 scopus 로고
    • Sequence of a cDNA from the Drosophila melanogaster white gene
    • M. Pepling, S.M. Mount, Sequence of a cDNA from the Drosophila melanogaster white gene, Nucleic Acids Res. 18 (1990) 1633.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1633
    • Pepling, M.1    Mount, S.M.2
  • 5
    • 0024268092 scopus 로고
    • The Brown protein of Drosophila melanogaster is similar to the White protein and to components of active transport complexes
    • T.D. Dreeson, D.H. Johnson, S. Henikoff, The Brown protein of Drosophila melanogaster is similar to the White protein and to components of active transport complexes, Mol. Cell. Biol. 8 (1988) 5206-5215.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5206-5215
    • Dreeson, T.D.1    Johnson, D.H.2    Henikoff, S.3
  • 6
    • 0024697812 scopus 로고
    • Cloning and characterisation of the scarlet gene of Drosophila melanogaster
    • R.G. Tearle, J.M. Belote, M. McKeown, B.S. Baker, A.J. Howells, Cloning and characterisation of the scarlet gene of Drosophila melanogaster, Genetics 122 (1989) 595-606.
    • (1989) Genetics , vol.122 , pp. 595-606
    • Tearle, R.G.1    Belote, J.M.2    McKeown, M.3    Baker, B.S.4    Howells, A.J.5
  • 7
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: Structure, mechanism, and evolution
    • G.F.-L. Ames, Bacterial periplasmic transport systems: structure, mechanism, and evolution, Annu. Rev. Biochem. 55 (1986) 397-425.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 397-425
    • Ames, G.F.-L.1
  • 8
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • C.F. Higgins, ABC transporters: from microorganisms to man, Annu. Rev. Cell. Biol. 8 (1992) 67-113.
    • (1992) Annu. Rev. Cell. Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 9
    • 0027132575 scopus 로고
    • ABC transporters: Bacterial exporters
    • M.J. Fath, R. Kolter, ABC transporters: bacterial exporters, Microbiol. Rev. 57 (1993) 995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 10
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • J.E. Walker, M. Saraste, M.J. Runswick, N.J. Gay, Distantly related sequences in the alpha and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, EMBO J. 1 (1982) 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 11
    • 0025954269 scopus 로고
    • Structure-functional analysis of the histidine permease and comparison with cystic fibrosis mutations
    • V. Shyamala, V. Baichwal, E. Beall, G.F.-L. Ames, Structure-functional analysis of the histidine permease and comparison with cystic fibrosis mutations, J. Biol. Chem. 266 (1991) 18714-18719.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18714-18719
    • Shyamala, V.1    Baichwal, V.2    Beall, E.3    Ames, G.F.-L.4
  • 12
    • 0021927285 scopus 로고
    • Phosphate-specific transport system of Escherichia coli: Nucleotide sequence and gene-polypeptide relationships
    • B.P. Surin, H. Rosenberg, G.B. Cox, Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships, J. Bacteriol. 161 (1985) 189-198.
    • (1985) J. Bacteriol. , vol.161 , pp. 189-198
    • Surin, B.P.1    Rosenberg, H.2    Cox, G.B.3
  • 16
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • H.R. Bourne, D.A. Sanders, F. McCormick, The GTPase superfamily: conserved structure and molecular mechanism, Nature 349 (1991) 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 17
    • 0029883155 scopus 로고    scopus 로고
    • Characterisation and analysis of conserved motifs in a peroxisomal ATP-binding cassette transporter
    • N. Shani, A. Sapag, D. Valle, Characterisation and analysis of conserved motifs in a peroxisomal ATP-binding cassette transporter, J. Biol. Chem. 271 (1996) 8725-8730.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8725-8730
    • Shani, N.1    Sapag, A.2    Valle, D.3
  • 18
    • 0029867564 scopus 로고    scopus 로고
    • Mutations within the first LSGGQ motif of Ste6p cause defects in a-Factor transport and mating in Saccharomyces cerevisiae
    • B.L. Browne, V. McClendon, D.M. Bedwell, Mutations within the first LSGGQ motif of Ste6p cause defects in a-Factor transport and mating in Saccharomyces cerevisiae, J. Bacteriol. 178 (1996) 1712-1719.
    • (1996) J. Bacteriol. , vol.178 , pp. 1712-1719
    • Browne, B.L.1    McClendon, V.2    Bedwell, D.M.3
  • 19
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis deltaF508 mutation using STE6-CFTR chimeras in yeast
    • J.L. Teem, H.A. Berger, L.S. Ostedgaard, D.P. Rich, L.-C. Tsui, M.J. Welsh, Identification of revertants for the cystic fibrosis deltaF508 mutation using STE6-CFTR chimeras in yeast, Cell 73 (1993) 335-346.
    • (1993) Cell , vol.73 , pp. 335-346
    • Teem, J.L.1    Berger, H.A.2    Ostedgaard, L.S.3    Rich, D.P.4    Tsui, L.-C.5    Welsh, M.J.6
  • 20
    • 0028033550 scopus 로고
    • Cystic fibrosis-type mutational analysis in the ATP-binding cassette transporter signature of human P-glycoprotein MDR1
    • T. Hoof, A. Demmer, M.R. Hadam, J.R. Riordan, B. Tümmler, Cystic fibrosis-type mutational analysis in the ATP-binding cassette transporter signature of human P-glycoprotein MDR1, J. Biol. Chem. 269 (1994) 20575-20583.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20575-20583
    • Hoof, T.1    Demmer, A.2    Hadam, M.R.3    Riordan, J.R.4    Tümmler, B.5
  • 22
    • 0025310336 scopus 로고
    • A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein
    • G.R. Cutting, L.M. Kasch, B.J. Rosenstein, J. Zielenski, L.-C. Tsui, S.E. Antonarakis, H.H. Kazazian, A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein, Nature 346 (1990) 366-369.
    • (1990) Nature , vol.346 , pp. 366-369
    • Cutting, G.R.1    Kasch, L.M.2    Rosenstein, B.J.3    Zielenski, J.4    Tsui, L.-C.5    Antonarakis, S.E.6    Kazazian, H.H.7
  • 23
    • 0028177555 scopus 로고
    • Mutational analysis of the traffic ATPase (ABC) transporters involved in uptake of eye pigment precursors in Drosophila melanogaster
    • G.D. Ewart, D. Cannell, G.B. Cox, A.J. Howells, Mutational analysis of the traffic ATPase (ABC) transporters involved in uptake of eye pigment precursors in Drosophila melanogaster, J. Biol. Chem. 269 (1994) 10370-10377.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10370-10377
    • Ewart, G.D.1    Cannell, D.2    Cox, G.B.3    Howells, A.J.4
  • 24
    • 0026786329 scopus 로고
    • Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family
    • R. Kerppola, G. Ames, Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family, J. Biol. Chem. 267 (1992) 2329-2336.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2329-2336
    • Kerppola, R.1    Ames, G.2
  • 25
    • 0028240216 scopus 로고
    • Bacterial binding protein-dependent permeases: Characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins
    • W. Saurin, W. Köster, E. Dassa, Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins, Mol. Microbiol. 12 (1994) 993-1004.
    • (1994) Mol. Microbiol. , vol.12 , pp. 993-1004
    • Saurin, W.1    Köster, W.2    Dassa, E.3
  • 26
    • 0029011568 scopus 로고
    • PXA1, a possible Saccharomyces cerevisiae ortholog of the human adrenoleukodystrophy gene
    • N. Shani, P.A. Watkins, D. Valle, PXA1, a possible Saccharomyces cerevisiae ortholog of the human adrenoleukodystrophy gene, Proc. Natl. Acad. Sci. USA 92 (1995) 6012-6016.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6012-6016
    • Shani, N.1    Watkins, P.A.2    Valle, D.3
  • 27
    • 0020181397 scopus 로고
    • Regulation of white locus expression: The structure of mutant alleles at the white locus of Drosophila melanogaster
    • Z. Zachar, P.M. Bingham, Regulation of white locus expression: the structure of mutant alleles at the white locus of Drosophila melanogaster, Cell 30 (1982) 529-541.
    • (1982) Cell , vol.30 , pp. 529-541
    • Zachar, Z.1    Bingham, P.M.2
  • 28
    • 0023932531 scopus 로고
    • The nature of N-ethyl-N-nitrosourea-induced mutations at the white locus of Drosophila melanogaster
    • A. Pastink, C. Vreeken, E.W. Vogel, The nature of N-ethyl-N-nitrosourea-induced mutations at the white locus of Drosophila melanogaster, Mutat. Res. 199 (1988) 47-53.
    • (1988) Mutat. Res. , vol.199 , pp. 47-53
    • Pastink, A.1    Vreeken, C.2    Vogel, E.W.3
  • 32
    • 0021112316 scopus 로고
    • Chromosomal walking and jumping to isolate DNA from the Ace and rosy loci and the bithorax complex in Drosophila melanogaster
    • W. Bender, P. Spierer, D.S. Hogness, Chromosomal walking and jumping to isolate DNA from the Ace and rosy loci and the bithorax complex in Drosophila melanogaster, J. Mol. Biol. 168 (1983) 17-33.
    • (1983) J. Mol. Biol. , vol.168 , pp. 17-33
    • Bender, W.1    Spierer, P.2    Hogness, D.S.3
  • 33
    • 0025788241 scopus 로고
    • High fidelity amplification using thermostable DNA polymerase from Pyrococcus furiosus
    • K.S. Lundberg, D.D. Shoemaker, M.W.W. Adams, J.M. Short, J.A. Sorge, E.J. Mathur, High fidelity amplification using thermostable DNA polymerase from Pyrococcus furiosus, Gene 108 (1991) 1-8.
    • (1991) Gene , vol.108 , pp. 1-8
    • Lundberg, K.S.1    Shoemaker, D.D.2    Adams, M.W.W.3    Short, J.M.4    Sorge, J.A.5    Mathur, E.J.6
  • 35
    • 0005803615 scopus 로고
    • Ommochrome biosynthetic pathway of Drosophila melanogaster: Variations in the levels of enzyme activities and intermediates during adult development
    • R.L. Ryall, A.J. Howells, Ommochrome biosynthetic pathway of Drosophila melanogaster: Variations in the levels of enzyme activities and intermediates during adult development, Insect Biochem. 6 (1974) 135-142.
    • (1974) Insect Biochem. , vol.6 , pp. 135-142
    • Ryall, R.L.1    Howells, A.J.2
  • 36
    • 0017818003 scopus 로고
    • Control of drosopterin synthesis in Drosophila melanogaster: Mutants showing an altered pattern of GTP cyclohydrolase activity during development, Biochem
    • B.A. Evans, A.J. Howells, Control of drosopterin synthesis in Drosophila melanogaster: mutants showing an altered pattern of GTP cyclohydrolase activity during development, Biochem. Genet. 16 (1978) 13-26.
    • (1978) Genet. , vol.16 , pp. 13-26
    • Evans, B.A.1    Howells, A.J.2
  • 37
  • 38
    • 0019965825 scopus 로고
    • Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium
    • C.F. Higgins, P.D. Haag, K. Nikaido, F. Ardeshir, G. Garcia, G.F.-L. Ames, Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium, Nature 298 (1982) 723-727.
    • (1982) Nature , vol.298 , pp. 723-727
    • Higgins, C.F.1    Haag, P.D.2    Nikaido, K.3    Ardeshir, F.4    Garcia, G.5    Ames, G.F.-L.6
  • 39
    • 0027497594 scopus 로고
    • Gene SNQ2 of Saccharomyces cerevisiae, which confers resistance to 4-nitroquinoline-N-oxide and other chemicals, encodes a 169 kDa protein homologous to ATP-dependent permeases
    • J. Servos, E. Haase, M. Brendel, Gene SNQ2 of Saccharomyces cerevisiae, which confers resistance to 4-nitroquinoline-N-oxide and other chemicals, encodes a 169 kDa protein homologous to ATP-dependent permeases, Mol. Gen. Genet. 236 (1993) 214-218.
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 214-218
    • Servos, J.1    Haase, E.2    Brendel, M.3
  • 40
    • 0028111508 scopus 로고
    • Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene product. A yeast ABC transporter conferring mycotoxin resistance
    • P.H. Bissinger, K. Kuchler, Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene product. A yeast ABC transporter conferring mycotoxin resistance, J. Biol. Chem. 269 (1994) 4180-4186.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4180-4186
    • Bissinger, P.H.1    Kuchler, K.2
  • 41
    • 0028957971 scopus 로고
    • bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin a resistance, is structurally related to the ATP-binding cassette superfamily
    • K. Nagao, Y. Taguchi, M. Arioka, H. Kadokura, A. Takatsuki, K. Yoda, M. Yamasaki, bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily, J. Bacteriol. 177 (1995) 1536-1543.
    • (1995) J. Bacteriol. , vol.177 , pp. 1536-1543
    • Nagao, K.1    Taguchi, Y.2    Arioka, M.3    Kadokura, H.4    Takatsuki, A.5    Yoda, K.6    Yamasaki, M.7
  • 43
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • C.J. Chen, J.E. Chin, K. Ueda, D.P. Clark, I. Pastan, M.M. Gottesman, I.B. Roninson, Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells, Cell 47 (1986) 381-389.
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6    Roninson, I.B.7
  • 44
    • 0025191307 scopus 로고
    • Genomic organization of the human multidrug resistance (MDR1) gene and origin of P-glycoproteins
    • C.-J. Chen, D. Clark, K. Ueda, I. Pastan, M.M. Gottesman, I.B. Roninson, Genomic organization of the human multidrug resistance (MDR1) gene and origin of P-glycoproteins, J. Biol. Chem. 265 (1990) 506-514.
    • (1990) J. Biol. Chem. , vol.265 , pp. 506-514
    • Chen, C.-J.1    Clark, D.2    Ueda, K.3    Pastan, I.4    Gottesman, M.M.5    Roninson, I.B.6
  • 45
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, R.F. Doolittle, A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157 (1982) 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 47
    • 0023931551 scopus 로고
    • DNA sequence analysis of X-ray-induced deletions at the white locus of Drosophila melanogaster
    • A. Pastink, C. Vreeken, A. Schalet, J. Eeken, DNA sequence analysis of X-ray-induced deletions at the white locus of Drosophila melanogaster, Mutat. Res. 207 (1988) 23-28.
    • (1988) Mutat. Res. , vol.207 , pp. 23-28
    • Pastink, A.1    Vreeken, C.2    Schalet, A.3    Eeken, J.4
  • 48
    • 0032322691 scopus 로고    scopus 로고
    • ABC transporters involved in transport of eye pigment precursors in Drosophila melanogaster
    • G.D. Ewart, A.J. Howells, ABC transporters involved in transport of eye pigment precursors in Drosophila melanogaster, Methods Enzymol 292 (1998) 213-224.
    • (1998) Methods Enzymol , vol.292 , pp. 213-224
    • Ewart, G.D.1    Howells, A.J.2
  • 49
    • 0028245416 scopus 로고
    • Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein
    • T.W. Loo, D.M. Clarke, Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein, J. Biol. Chem. 269 (1994) 7243-7248.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7243-7248
    • Loo, T.W.1    Clarke, D.M.2
  • 50
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenisis of transmembrane domain 11 of P-glycoprotein by alanine scanning
    • M. Hanna, M. Brault, T. Kwan, C. Kast, P. Gros, Mutagenisis of transmembrane domain 11 of P-glycoprotein by alanine scanning, Biochemistry 35 (1996) 3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1    Brault, M.2    Kwan, T.3    Kast, C.4    Gros, P.5
  • 52
    • 0030051032 scopus 로고    scopus 로고
    • Identification of CFTR channel-lining residues in and flanking the M6 membrane-spanning segment
    • M. Cheung, M.H. Akabas, Identification of CFTR channel-lining residues in and flanking the M6 membrane-spanning segment, Biophys. J. 70 (1996) 2688-2695.
    • (1996) Biophys. J. , vol.70 , pp. 2688-2695
    • Cheung, M.1    Akabas, M.H.2
  • 53
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and open-channel block
    • S. McDonough, N. Davidson, H.A. Lester, N.A. McCarty, Novel pore-lining residues in CFTR that govern permeation and open-channel block, Neuron 13 (1994) 623-634.
    • (1994) Neuron , vol.13 , pp. 623-634
    • McDonough, S.1    Davidson, N.2    Lester, H.A.3    McCarty, N.A.4
  • 55
    • 0032323641 scopus 로고    scopus 로고
    • Evolutionary relationships among ABC transporters
    • J.M. Croop, Evolutionary relationships among ABC transporters, Methods Enzymol. 292 (1998) 101-116.
    • (1998) Methods Enzymol. , vol.292 , pp. 101-116
    • Croop, J.M.1
  • 56
    • 0028858490 scopus 로고
    • Intracellular loop between transmembrane segments IV and V of cystic fibrosis transmembrane conductance regulator is involved in regulation of chloride channel conductance state
    • J. Xie, M.L. Drumm, J. Ma, P.B. Davis, Intracellular loop between transmembrane segments IV and V of cystic fibrosis transmembrane conductance regulator is involved in regulation of chloride channel conductance state, J. Biol. Chem. 270 (1995) 28084-28091.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28084-28091
    • Xie, J.1    Drumm, M.L.2    Ma, J.3    Davis, P.B.4
  • 57
    • 0029835571 scopus 로고    scopus 로고
    • Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator
    • J.F. Cotten, L.S. Ostedgaard, M.R. Carson, M.J. Welsh, Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator, J. Biol. Chem. 271 (1996) 21279-21284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21279-21284
    • Cotten, J.F.1    Ostedgaard, L.S.2    Carson, M.R.3    Welsh, M.J.4
  • 58
    • 0028901538 scopus 로고
    • Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR 1
    • X. Zhang, K.I. Collins, L.M. Greenberger, Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR 1, J. Biol. Chem. 270 (1995) 5441-5448.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5441-5448
    • Zhang, X.1    Collins, K.I.2    Greenberger, L.M.3
  • 59
    • 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
    • M. Mourez, M. Hofnung, E. Dassa, 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 (1997) 3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 60
    • 0031007555 scopus 로고    scopus 로고
    • Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region
    • É. Bakos, I. Klein, E. Welker, K. Szabó, M. Müller, B. Sarkadi, A. Váradi, Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region, Biochem. J. 323 (1997) 777-783.
    • (1997) Biochem. J. , vol.323 , pp. 777-783
    • Bakos, É.1    Klein, I.2    Welker, E.3    Szabó, K.4    Müller, M.5    Sarkadi, B.6    Váradi, A.7
  • 62
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter, the histidine permease of Salmonella typhimurium
    • L.-W. Hung, I.X. Wang, K. Nikaido, P.-Q. Liu, G.F.-L. Ames, S.-H. Kim, Crystal structure of the ATP-binding subunit of an ABC transporter, the histidine permease of Salmonella typhimurium, Nature 396 (1998) 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
  • 63
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • I.L. Urbatsch, B. Sankaran, J. Weber, A.E. Senior, P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site, J. Biol. Chem. 270 (1995) 19383-19390.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 64
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • I.L. Urbatsch, B. Sankaran, S. Bhagat, A.E. Senior, Both P-glycoprotein nucleotide-binding sites are catalytically active, J. Biol. Chem. 270 (1995) 26956-26961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 65
    • 0029559159 scopus 로고
    • Mini-review. The catalytic cycle of P-glycoprotein
    • A.E. Senior, M.K. Al-Shawi, I.L. Urbatsch, Mini-review. The catalytic cycle of P-glycoprotein, FEBS Lett. 377 (1995) 285-289.
    • (1995) FEBS Lett. , vol.377 , pp. 285-289
    • Senior, A.E.1    Al-Shawi, M.K.2    Urbatsch, I.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.