메뉴 건너뛰기




Volumn 2, Issue 3, 2003, Pages 588-598

A region within a lumenal loop of Saccharomyces cerevisiae Ycf1p directs proteolytic processing and substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ARSENIC TRIOXIDE; ARSENOUS ACID DERIVATIVE; CADMIUM; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 0038143251     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.2.3.588-598.2003     Document Type: Article
Times cited : (32)

References (56)
  • 2
    • 0034502842 scopus 로고    scopus 로고
    • Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1)
    • Bakos, E., R. Evers, G. Calenda, G. E. Tusnady, G. Szakacs, A. Varadi, and B. Sarkadi. 2000. Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1). J. Cell Sci. 113:4451-4461.
    • (2000) J. Cell Sci. , vol.113 , pp. 4451-4461
    • Bakos, E.1    Evers, R.2    Calenda, G.3    Tusnady, G.E.4    Szakacs, G.5    Varadi, A.6    Sarkadi, B.7
  • 4
    • 0037857348 scopus 로고
    • Effects of nucleotide binding fold mutations on STE6, a yeast ABC protein
    • L. Reuss, J. M. Russell, and M. L. Jennings (ed.). Rockefeller University Press, New York, N.Y.
    • Berkower, C., and S. Michaelis. 1993. Effects of nucleotide binding fold mutations on STE6, a yeast ABC protein, p. 130-146. In L. Reuss, J. M. Russell, and M. L. Jennings (ed.), Molecular biology and function of carrier proteins. Rockefeller University Press, New York, N.Y.
    • (1993) Molecular Biology and Function of Carrier Proteins , pp. 130-146
    • Berkower, C.1    Michaelis, S.2
  • 5
    • 0026094617 scopus 로고
    • Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP-binding cassette (ABC) protein superfamily
    • Berkower, C., and S. Michaelis. 1991. Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP-binding cassette (ABC) protein superfamily. EMBO J. 10:3777-3785.
    • (1991) EMBO J. , vol.10 , pp. 3777-3785
    • Berkower, C.1    Michaelis, S.2
  • 7
    • 0029833020 scopus 로고    scopus 로고
    • Functional and physical interactions between partial molecules of STE6, a yeast ATP-binding-cassette transport protein
    • Berkower, C., D. Taglicht, and S. Michaelis. 1996. Functional and physical interactions between partial molecules of STE6, a yeast ATP-binding-cassette transport protein. J. Biol. Chem. 271:22983-22989.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22983-22989
    • Berkower, C.1    Taglicht, D.2    Michaelis, S.3
  • 8
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14:115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 9
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., J. Ye, R. B. Rawson, and J. L. Goldstein. 2000. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100:391-398.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 10
    • 0035970021 scopus 로고    scopus 로고
    • Aquaporins in Saccharomyces: Characterization of a second functional water channel protein
    • Carbrey, J. M., M. Bonhivers, J. D. Boeke, and P. Agre. 2001. Aquaporins in Saccharomyces: characterization of a second functional water channel protein. Proc. Natl. Acad. Sci. USA 98:1000-1005.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1000-1005
    • Carbrey, J.M.1    Bonhivers, M.2    Boeke, J.D.3    Agre, P.4
  • 11
    • 0031055072 scopus 로고    scopus 로고
    • Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor
    • Chen, P., S. Sapperstein, J. D. Choi, and S. Michaelis. 1997. Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor. J. Cell Biol. 136:251-269.
    • (1997) J. Cell Biol. , vol.136 , pp. 251-269
    • Chen, P.1    Sapperstein, S.2    Choi, J.D.3    Michaelis, S.4
  • 12
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble, R. 1992. A simple and efficient procedure for transformation of yeasts. BioTechniques 13:18-20.
    • (1992) BioTechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 13
    • 0034906977 scopus 로고    scopus 로고
    • Domain interactions in the yeast ATP-binding cassette transporter Ycf1p: Intragenic suppressor analysis of mutations in the nucleotide-binding domains
    • Falcon-Perez, J. M., M. Martinez-Burgos, J. Molano, M. J. Mazon, and P. Eraso. 2001. Domain interactions in the yeast ATP-binding cassette transporter Ycf1p: intragenic suppressor analysis of mutations in the nucleotide-binding domains. J. Bacteriol. 183:4761-4770.
    • (2001) J. Bacteriol. , vol.183 , pp. 4761-4770
    • Falcon-Perez, J.M.1    Martinez-Burgos, M.2    Molano, J.3    Mazon, M.J.4    Eraso, P.5
  • 14
    • 0039184138 scopus 로고    scopus 로고
    • Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis
    • Falcon-Perez, J. M., M. J. Mazon, J. Molano, and P. Eraso. 1999. Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis. J. Biol. Chem. 274:23584-23590.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23584-23590
    • Falcon-Perez, J.M.1    Mazon, M.J.2    Molano, J.3    Eraso, P.4
  • 15
    • 0037163124 scopus 로고    scopus 로고
    • Role of the N-terminal transmembrane region of the multidrug resistance protein MRP2 in routing to the apical membrane in MDCKII cells
    • Fernandez, S. B., Z. Hollo, A. Kern, E. Bakos, P. A. Fischer, P. Borst, and R. Evers. 2002. Role of the N-terminal transmembrane region of the multidrug resistance protein MRP2 in routing to the apical membrane in MDCKII cells. J. Biol. Chem. 277:31048-31055.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31048-31055
    • Fernandez, S.B.1    Hollo, Z.2    Kern, A.3    Bakos, E.4    Fischer, P.A.5    Borst, P.6    Evers, R.7
  • 17
    • 0033609012 scopus 로고    scopus 로고
    • Pathways of As(III) detoxification in Saccharomyces cerevisiae
    • Ghosh, M., J. Shen, and B. P. Rosen. 1999. Pathways of As(III) detoxification in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 96:5001-5006.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5001-5006
    • Ghosh, M.1    Shen, J.2    Rosen, B.P.3
  • 19
    • 0036828695 scopus 로고    scopus 로고
    • Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity
    • Haimeur, A., R. G. Deeley, and S. P. Cole. 2002. Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity. J. Biol. Chem. 277:41326-41333.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41326-41333
    • Haimeur, A.1    Deeley, R.G.2    Cole, S.P.3
  • 20
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure, and mechanism: An overview
    • Higgins, C. F. 2001. ABC transporters: physiology, structure, and mechanism: an overview. Res. Microbiol. 152:205-210.
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 22
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones, E. W. 1991. Three proteolytic systems in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 266:7963-7966.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 23
    • 0000538964 scopus 로고    scopus 로고
    • Biogenesis and function of the yeast vacuole
    • J. R. Pringle, J. R. Broach, and E. W. Jones (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Jones, E. W., G. C. Webb, and M. A. Hiller. 1997. Biogenesis and function of the yeast vacuole, p. 363-470. In J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), The molecular and cellular biology of the yeast Saccharomyces: cell cycle and cell biology, vol. 3. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) The Molecular and Cellular Biology of the Yeast Saccharomyces: Cell Cycle and Cell Biology , vol.3 , pp. 363-470
    • Jones, E.W.1    Webb, G.C.2    Hiller, M.A.3
  • 24
    • 0036860716 scopus 로고    scopus 로고
    • High-resolution genetic mapping with ordered arrays of Saccharomyces cerevisiae deletion mutants
    • Jorgensen, P., B. Nelson, M. D. Robinson, Y. Chen, B. Andrews, M. Tyers, and C. Boone. 2002. High-resolution genetic mapping with ordered arrays of Saccharomyces cerevisiae deletion mutants. Genetics 162:1091-1099.
    • (2002) Genetics , vol.162 , pp. 1091-1099
    • Jorgensen, P.1    Nelson, B.2    Robinson, M.D.3    Chen, Y.4    Andrews, B.5    Tyers, M.6    Boone, C.7
  • 26
    • 0037147341 scopus 로고    scopus 로고
    • Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1
    • Koike, K., C. J. Oleschuk, A. Haimeur, S. L. Olsen, R. G. Deeley, and S. P. Cole. 2002. Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1. J. Biol. Chem. 277:49495-49503.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49495-49503
    • Koike, K.1    Oleschuk, C.J.2    Haimeur, A.3    Olsen, S.L.4    Deeley, R.G.5    Cole, S.P.6
  • 27
    • 0030834595 scopus 로고    scopus 로고
    • Filamentous growth in budding yeast
    • Kron, S. J. 1997. Filamentous growth in budding yeast. Trends Microbiol. 5:450-454.
    • (1997) Trends Microbiol. , vol.5 , pp. 450-454
    • Kron, S.J.1
  • 28
    • 0035834145 scopus 로고    scopus 로고
    • PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling
    • Levitan, D., J. Lee, L. Song, R. Manning, G. Wong, E. Parker, and L. Zhang. 2001. PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling. Proc. Natl. Acad. Sci. USA 98:12186-12190.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12186-12190
    • Levitan, D.1    Lee, J.2    Song, L.3    Manning, R.4    Wong, G.5    Parker, E.6    Zhang, L.7
  • 29
    • 0029983266 scopus 로고    scopus 로고
    • The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump
    • Li, Z., M. Szczypka, Y. Lu, D. Thiele, and P. Rea. 1996. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271:6509-6517.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6509-6517
    • Li, Z.1    Szczypka, M.2    Lu, Y.3    Thiele, D.4    Rea, P.5
  • 30
    • 0031013876 scopus 로고    scopus 로고
    • A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalyzed transport of bis(glutathionato)cadmium
    • Li, Z. S., Y. P. Lu, R. G. Zhen, M. Szczypka, D. J. Thiele, and P. A. Rea. 1997. A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalyzed transport of bis(glutathionato)cadmium. Proc. Natl. Acad. Sci. USA 94:42-47.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 42-47
    • Li, Z.S.1    Lu, Y.P.2    Zhen, R.G.3    Szczypka, M.4    Thiele, D.J.5    Rea, P.A.6
  • 32
    • 0036911113 scopus 로고    scopus 로고
    • Requirement of the N-terminal extension for vacuolar trafficking and transport activity of yeast Ycf1p, an ATP-binding cassette transporter
    • Mason, D. L., and S. Michaelis. 2002. Requirement of the N-terminal extension for vacuolar trafficking and transport activity of yeast Ycf1p, an ATP-binding cassette transporter. Mol. Biol. Cell 13:4443-4455.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4443-4455
    • Mason, D.L.1    Michaelis, S.2
  • 33
    • 0023974052 scopus 로고
    • The a-factor pheromone of Saccharomyces cerevisiae is essential for mating
    • Michaelis, S., and I. Herskowitz. 1988. The a-factor pheromone of Saccharomyces cerevisiae is essential for mating. Mol. Cell. Biol. 8:1309-1318.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 34
    • 0030873221 scopus 로고    scopus 로고
    • Recombination-mediated PCR-directed plasmid construction in vivo in yeast
    • Oldenburg, K. R., K. T. Vo, S. Michaelis, and C. Paddon. 1997. Recombination-mediated PCR-directed plasmid construction in vivo in yeast. Nucleic Acids Res. 25:451-452.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 451-452
    • Oldenburg, K.R.1    Vo, K.T.2    Michaelis, S.3    Paddon, C.4
  • 37
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1). Crystallization and single-particle analysis
    • Rosenberg, M. F., Q. Mao, A. Holzenburg, R. C. Ford, R. G. Deeley, and S. P. Cole. 2001. The structure of the multidrug resistance protein 1 (MRP1/ABCC1). crystallization and single-particle analysis. J. Biol. Chem. 276:16076-16082.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16076-16082
    • Rosenberg, M.F.1    Mao, Q.2    Holzenburg, A.3    Ford, R.C.4    Deeley, R.G.5    Cole, S.P.6
  • 38
    • 0036255533 scopus 로고    scopus 로고
    • The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex formation
    • Salerno, M., M. Petroutsa, and A. Garnier-Suillerot. 2002. The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex formation. J. Bioenerg. Biomembr. 34:135-145.
    • (2002) J. Bioenerg. Biomembr. , vol.34 , pp. 135-145
    • Salerno, M.1    Petroutsa, M.2    Garnier-Suillerot, A.3
  • 39
    • 0036616623 scopus 로고    scopus 로고
    • Localization, regulation, and substrate transport properties of Bpt1p, a Saccharomyces cerevisiae MRP-type ABC transporter
    • Sharma, K. G., D. L. Mason, G. Liu, P. A. Rea, A. K. Bachhawat, and S. Michaelis. 2002. Localization, regulation, and substrate transport properties of Bpt1p, a Saccharomyces cerevisiae MRP-type ABC transporter. Eukaryot. Cell 1:391-400.
    • (2002) Eukaryot. Cell , vol.1 , pp. 391-400
    • Sharma, K.G.1    Mason, D.L.2    Liu, G.3    Rea, P.A.4    Bachhawat, A.K.5    Michaelis, S.6
  • 40
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 41
    • 0021713895 scopus 로고
    • Transcription and regulatory signals at the mating type locus in yeast
    • Siliciano, P., and K. Tatchell. 1984. Transcription and regulatory signals at the mating type locus in yeast. Cell 37:969-978.
    • (1984) Cell , vol.37 , pp. 969-978
    • Siliciano, P.1    Tatchell, K.2
  • 42
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae
    • E. W. Jones, J. R. Pringle, and J. R. Broach (ed.). Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Sprague, G. F., and J. W. Thorner. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae, p. 657-744. In E. W. Jones, J. R. Pringle, and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression , pp. 657-744
    • Sprague, G.F.1    Thorner, J.W.2
  • 43
    • 0033529672 scopus 로고    scopus 로고
    • Localization of a substrate specificity domain in the multidrug resistance protein
    • Stride, B. D., S. P. Cole, and R. G. Deeley. 1999. Localization of a substrate specificity domain in the multidrug resistance protein. J. Biol. Chem. 274:22877-22883.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22877-22883
    • Stride, B.D.1    Cole, S.P.2    Deeley, R.G.3
  • 44
    • 0028064872 scopus 로고
    • A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein
    • Szczypka, M. S., J. A. Wemmie, W. S. Moye-Rowley, and D. J. Thiele. 1994. A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein. J. Biol. Chem. 269:22853-22857.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22853-22857
    • Szczypka, M.S.1    Wemmie, J.A.2    Moye-Rowley, W.S.3    Thiele, D.J.4
  • 45
    • 0032322715 scopus 로고    scopus 로고
    • A complete catalogue of Saccharomyces cerevisiae ABC proteins and their relevance to human health and disease
    • S. V. Ambudkar and M. M. Gottesman (ed.). Academic Press, Inc., New York, N.Y.
    • Taglicht, D., and S. Michaelis. 1998. A complete catalogue of Saccharomyces cerevisiae ABC proteins and their relevance to human health and disease, p. 130-162. In S. V. Ambudkar and M. M. Gottesman (ed.), Methods in enzymology. Academic Press, Inc., New York, N.Y.
    • (1998) Methods in Enzymology , pp. 130-162
    • Taglicht, D.1    Michaelis, S.2
  • 46
    • 0024459376 scopus 로고
    • Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival
    • Teichert, U., B. Mechler, H. Muller, and D. H. Wolf. 1989. Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. J. Biol. Chem. 264:16037-16045.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16037-16045
    • Teichert, U.1    Mechler, B.2    Muller, H.3    Wolf, D.H.4
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specific gap penalties, and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specific gap penalties, and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0030771930 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae ATP-binding cassette transporter protein Ycf1p
    • Wemmie, J., and W. Moye-Rowley. 1997. Mutational analysis of the Saccharomyces cerevisiae ATP-binding cassette transporter protein Ycf1p. Mol. Microbiol. 25:683-694.
    • (1997) Mol. Microbiol. , vol.25 , pp. 683-694
    • Wemmie, J.1    Moye-Rowley, W.2
  • 49
    • 0028575444 scopus 로고
    • Cadmium tolerance mediated by the yeast AP-1 protein requires the presence of an ATP-binding cassette transporter-encoding gene, YCF1
    • Wemmie, J., M. Szczypka, D. Thiele, and W. Moye-Rowley. 1994. Cadmium tolerance mediated by the yeast AP-1 protein requires the presence of an ATP-binding cassette transporter-encoding gene, YCF1. J. Biol. Chem. 269:32592-32597.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32592-32597
    • Wemmie, J.1    Szczypka, M.2    Thiele, D.3    Moye-Rowley, W.4
  • 51
    • 0035937153 scopus 로고    scopus 로고
    • The role of presenilins in gamma-secretase activity
    • Wolfe, M. S., and C. Haass. 2001. The role of presenilins in gamma-secretase activity. J. Biol. Chem. 276:5413-5416.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5413-5416
    • Wolfe, M.S.1    Haass, C.2
  • 52
    • 0037150534 scopus 로고    scopus 로고
    • Intramembrane proteases: Mixing oil and water
    • Wolfe, M. S., and D. J. Selkoe. 2002. Intramembrane proteases: mixing oil and water. Science 296:2156-2157.
    • (2002) Science , vol.296 , pp. 2156-2157
    • Wolfe, M.S.1    Selkoe, D.J.2
  • 54
    • 0037036427 scopus 로고    scopus 로고
    • Determinants of the substrate specificity of multidrug resistance protein 1: Role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17
    • Zhang, D. W., S. P. Cole, and R. G. Deeley. 2002. Determinants of the substrate specificity of multidrug resistance protein 1: role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17. J. Biol. Chem. 277:20934-20941.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20934-20941
    • Zhang, D.W.1    Cole, S.P.2    Deeley, R.G.3
  • 55
    • 0035860688 scopus 로고    scopus 로고
    • Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: Evidence for functional interaction between transmembrane helices 14 and 17
    • Zhang, D. W., S. P. Cole, and R. G. Deeley. 2001. Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: evidence for functional interaction between transmembrane helices 14 and 17. J. Biol. Chem. 276:34966-34974.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34966-34974
    • Zhang, D.W.1    Cole, S.P.2    Deeley, R.G.3
  • 56
    • 0035918322 scopus 로고    scopus 로고
    • Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines
    • Zhang, D. W., S. P. Cole, and R. G. Deeley. 2001. Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines. J. Biol. Chem. 276:13231-13239.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13231-13239
    • Zhang, D.W.1    Cole, S.P.2    Deeley, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.