메뉴 건너뛰기




Volumn 580, Issue 4, 2006, Pages 1064-1084

Insight in eukaryotic ABC transporter function by mutation analysis

Author keywords

Membrane protein; Polymorphisms; Processing; Site directed mutagenesis; Transport

Indexed keywords

ABC TRANSPORTER; GLYCOPROTEIN P; MEMBRANE PROTEIN; MULTIDRUG RESISTANCE PROTEIN 1; MULTIDRUG RESISTANCE PROTEIN 2; PROTEIN YCF1; SULFONYLUREA RECEPTOR; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 31844452412     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.01.024     Document Type: Short Survey
Times cited : (75)

References (271)
  • 1
    • 0034917716 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • M. Dean, A. Rzhetsky, and R. Allikmets The human ATP-binding cassette (ABC) transporter superfamily Genome Res. 11 2001 1156 1166
    • (2001) Genome Res. , vol.11 , pp. 1156-1166
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 2
    • 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, and 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
  • 4
    • 0024307162 scopus 로고
    • Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance
    • M. Azzaria, E. Schurr, and P. Gross Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance Mol. Cell. Biol. 9 1989 5289 5297
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5289-5297
    • Azzaria, M.1    Schurr, E.2    Gross, P.3
  • 5
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities
    • T.W. Loo, and D.M. Clarke Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities J. Biol. Chem. 270 1995 21449 21452
    • (1995) J. Biol. Chem. , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 6
    • 0032562795 scopus 로고    scopus 로고
    • Drug stimulated nucleotide trapping in the human multidrug transporter MDR1. Cooperation of the nucleotide binding domains
    • K. Szabo, E. Welker, E. Bakos, M. Muller, I. Roninson, A. Varadi, and B. Sarkadi Drug stimulated nucleotide trapping in the human multidrug transporter MDR1. Cooperation of the nucleotide binding domains J. Biol. Chem. 273 1998 10132 10138
    • (1998) J. Biol. Chem. , vol.273 , pp. 10132-10138
    • Szabo, K.1    Welker, E.2    Bakos, E.3    Muller, M.4    Roninson, I.5    Varadi, A.6    Sarkadi, B.7
  • 7
    • 0032584289 scopus 로고    scopus 로고
    • Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotides at both sites
    • I.L. Urbatsch, L. Beaudet, I. Carrier, and P. Gros Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotides at both sites Biochemistry 37 1998 4592 4602
    • (1998) Biochemistry , vol.37 , pp. 4592-4602
    • Urbatsch, I.L.1    Beaudet, L.2    Carrier, I.3    Gros, P.4
  • 10
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • I.B. Holland, and M.A. Blight ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans J. Mol. Biol. 293 1999 381 399
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 11
    • 1242335471 scopus 로고    scopus 로고
    • The MRP-related and BCRP/ABCG2 multidrug resistance proteins: Biology, substrate specificity and regulation
    • A. Haimeur, G. Conseil, R.G. Deeley, and S.P.C. Cole The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulation Curr. Drug Metab. 5 2004 21 53
    • (2004) Curr. Drug Metab. , vol.5 , pp. 21-53
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.C.4
  • 12
    • 11844297796 scopus 로고    scopus 로고
    • Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas
    • G. Conseil, R.G. Deeley, and S.P.C. Cole Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas Biochem. Pharmacol. 69 2005 451 461
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 451-461
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.C.3
  • 14
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins in toxicology: Role of P-glycoprotein, MRP1, MRP2 and BCRP (ABCG2) in tissue defense
    • E.M. Leslie, R.G. Deeley, and S.P.C. Cole Multidrug resistance proteins in toxicology: Role of P-glycoprotein, MRP1, MRP2 and BCRP (ABCG2) in tissue defense Toxicol. Appl. Pharmacol. 204 2004 216 237
    • (2004) Toxicol. Appl. Pharmacol. , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 15
    • 85163548581 scopus 로고    scopus 로고
    • MRP2, the apical export pump for anionic conjugates
    • I.B. Holland S.P.C. Cole K. Kuchler C.F. Higgins Academic Press London
    • J. Konig, A.T. Nies, Y. Cui, and D. Keppler MRP2, the apical export pump for anionic conjugates I.B. Holland S.P.C. Cole K. Kuchler C.F. Higgins ABC Transporters: From Bacteria to Man 2003 Academic Press London 423 443
    • (2003) ABC Transporters: From Bacteria to Man , pp. 423-443
    • Konig, J.1    Nies, A.T.2    Cui, Y.3    Keppler, D.4
  • 16
    • 0034072174 scopus 로고    scopus 로고
    • Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions
    • E. Bakos, R. Evers, J.A. Sinkule, A. Varadi, P. Borst, and B. Sarkadi Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions Mol. Pharmacol. 57 2000 760 768
    • (2000) Mol. Pharmacol. , vol.57 , pp. 760-768
    • Bakos, E.1    Evers, R.2    Sinkule, J.A.3    Varadi, A.4    Borst, P.5    Sarkadi, B.6
  • 19
    • 0032936619 scopus 로고    scopus 로고
    • Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis
    • D.C. Gadsby, and A.C. Nairn Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis Physiol. Rev. 79 1999 S77 S107
    • (1999) Physiol. Rev. , vol.79
    • Gadsby, D.C.1    Nairn, A.C.2
  • 20
    • 0026759418 scopus 로고
    • + channel regulators on CFTR chloride currents
    • + channel regulators on CFTR chloride currents J. Gen. Physiol. 100 1992 573 591
    • (1992) J. Gen. Physiol. , vol.100 , pp. 573-591
    • Sheppard, D.N.1    Welsh, M.J.2
  • 24
    • 0029561629 scopus 로고
    • Cloning and functional expression of the cDNA encoding a novel ATP-sensitive potassium channel subunit expressed in pancreatic β-cells, brain, heart and skeletal muscle
    • H. Sakura, C. Ãmmãlã, P.A. Smith, F.M. Gribble, and F.M. Ashcroft Cloning and functional expression of the cDNA encoding a novel ATP-sensitive potassium channel subunit expressed in pancreatic β-cells, brain, heart and skeletal muscle FEBS Lett. 377 1995 338 344
    • (1995) FEBS Lett. , vol.377 , pp. 338-344
    • Sakura, H.1    Ãmmãlã, C.2    Smith, P.A.3    Gribble, F.M.4    Ashcroft, F.M.5
  • 27
    • 0023911193 scopus 로고
    • Adenosine 5′-triphosphate-sensitive potassium channels
    • F.M. Ashcroft Adenosine 5′-triphosphate-sensitive potassium channels Annu. Rev. Neurosci. 11 1988 97 118
    • (1988) Annu. Rev. Neurosci. , vol.11 , pp. 97-118
    • Ashcroft, F.M.1
  • 29
    • 0032788372 scopus 로고    scopus 로고
    • Molecular biology of adenosine triphosphate-sensitive potassium channels
    • L. Aguilar-Bryan, and J. Bryan Molecular biology of adenosine triphosphate-sensitive potassium channels Endocrinol. Rev. 20 1999 101 135
    • (1999) Endocrinol. Rev. , vol.20 , pp. 101-135
    • Aguilar-Bryan, L.1    Bryan, J.2
  • 30
    • 0033037098 scopus 로고    scopus 로고
    • ATP-sensitive potassium channels: A model of heteromultimeric potassium channel/receptor assemblies
    • S. Seino ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies Annu. Rev. Physiol. 61 1999 337 362
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 337-362
    • Seino, S.1
  • 33
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • M.M. Gottesman, T. Fojo, and S.E. Bates Multidrug resistance in cancer: role of ATP-dependent transporters Nat. Rev. Cancer 2 2002 48 58
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 34
    • 3843140625 scopus 로고    scopus 로고
    • Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly
    • G. Tombline, L.A. Bartholomew, I.L. Urbatsch, and A.E. Senior Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly J. Biol. Chem. 279 2004 31212 31220
    • (2004) J. Biol. Chem. , vol.279 , pp. 31212-31220
    • Tombline, G.1    Bartholomew, L.A.2    Urbatsch, I.L.3    Senior, A.E.4
  • 35
    • 1242272074 scopus 로고    scopus 로고
    • Synergy between conserved ABC signature Ser residues in P-glycoprotein catalysis
    • G. Tombline, L.A. Bartholomew, K. Gimi, G.A. Tyndall, and A.E. Senior Synergy between conserved ABC signature Ser residues in P-glycoprotein catalysis J. Biol. Chem. 279 2004 5363 5373
    • (2004) J. Biol. Chem. , vol.279 , pp. 5363-5373
    • Tombline, G.1    Bartholomew, L.A.2    Gimi, K.3    Tyndall, G.A.4    Senior, A.E.5
  • 36
    • 8744266443 scopus 로고    scopus 로고
    • Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues
    • G. Tombline, L.A. Bartholomew, G.A. Tyndall, K. Gimi, I.L. Urbatsch, and A.E. Senior Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues J. Biol. Chem. 279 2004 46518 46526
    • (2004) J. Biol. Chem. , vol.279 , pp. 46518-46526
    • Tombline, G.1    Bartholomew, L.A.2    Tyndall, G.A.3    Gimi, K.4    Urbatsch, I.L.5    Senior, A.E.6
  • 37
    • 0028064872 scopus 로고
    • A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein
    • M.S. Szczypka, J.A. Wemmie, W.S. Moye-Rowley, and D.S. Thiele A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein J. Biol. Chem. 269 1994 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.S.4
  • 39
    • 0039184138 scopus 로고    scopus 로고
    • Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis
    • J.M. Falcon-Perez, M.J. Mazon, J. Molano, and P. Eraso Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis J. Biol. Chem. 274 1999 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
  • 41
    • 0031026369 scopus 로고    scopus 로고
    • Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters
    • G.E. Tusnady, E. Bakos, A. Varadi, and B. Sarkadi Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters FEBS Lett. 402 1997 1 3
    • (1997) FEBS Lett. , vol.402 , pp. 1-3
    • Tusnady, G.E.1    Bakos, E.2    Varadi, A.3    Sarkadi, B.4
  • 42
    • 22944446748 scopus 로고    scopus 로고
    • Polymorphisms of MRP1 (ABCC1) and related ATP-dependent drug transporters
    • G. Conseil, R.G. Deeley, and S.P.C. Cole Polymorphisms of MRP1 (ABCC1) and related ATP-dependent drug transporters Pharmacogenet. Genomics 15 2005 523 533
    • (2005) Pharmacogenet. Genomics , vol.15 , pp. 523-533
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.C.3
  • 43
    • 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
    • K.P. Hopfner, A. Karcher, D.S. Shin, L. Craig, L.M. Arthur, J.P. Carney, and J.A. Tainer Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA-double strand break repair and the ABC-ATPase superfamily Cell 101 2000 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
  • 44
    • 0025954269 scopus 로고
    • Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations
    • V. Shyamala, V. Baichwal, E. Beall, and G.F. Ames Structure-function 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.4
  • 46
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and open channel block
    • S. McDonough, N. Davidson, H.A. Lester, and 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
  • 47
    • 0030051032 scopus 로고    scopus 로고
    • Identification of cystic fibrosis transmembrane conductance regulator channel-lining residues in and flanking the M6 membrane-spanning segment
    • M. Cheung, and M.H. Akabas Identification of cystic fibrosis transmembrane conductance regulator 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
  • 49
    • 0030886246 scopus 로고    scopus 로고
    • Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel
    • P. Linsdell, J.A. Tabcharani, and J.W. Hanrahan Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel J. Gen. Physiol. 110 1997 365 377
    • (1997) J. Gen. Physiol. , vol.110 , pp. 365-377
    • Linsdell, P.1    Tabcharani, J.A.2    Hanrahan, J.W.3
  • 51
    • 0028276430 scopus 로고
    • ATP alters current fluctuations of cystic fibrosis transmembrane conductance regulator: Evidence for a three-state activation mechanism
    • C.J. Venglarik, B.D. Schultz, R.A. Frizzell, and R.J. Bridges ATP alters current fluctuations of cystic fibrosis transmembrane conductance regulator: evidence for a three-state activation mechanism J. Gen. Physiol. 104 1994 123 146
    • (1994) J. Gen. Physiol. , vol.104 , pp. 123-146
    • Venglarik, C.J.1    Schultz, B.D.2    Frizzell, R.A.3    Bridges, R.J.4
  • 52
    • 0029117303 scopus 로고
    • Conformational states of CFTR associated with channel gating: The role of ATP binding and hydrolysis
    • K.L. Gunderson, and R.R. Kopito Conformational states of CFTR associated with channel gating: the role of ATP binding and hydrolysis Cell 82 1995 231 239
    • (1995) Cell , vol.82 , pp. 231-239
    • Gunderson, K.L.1    Kopito, R.R.2
  • 53
    • 0346636602 scopus 로고    scopus 로고
    • The cystic fibrosis transmembrane conductance regulator (ABCC7)
    • I.B. Holland S.P.C. Cole K. Kuchler C.F. Higgins Academic Press Amsterdam
    • J.W. Hanrahan, M. Gentzsch, and J.R. Riordan The cystic fibrosis transmembrane conductance regulator (ABCC7) I.B. Holland S.P.C. Cole K. Kuchler C.F. Higgins ABC Proteins from Bacteria to Man 2003 Academic Press Amsterdam 589 618
    • (2003) ABC Proteins from Bacteria to Man , pp. 589-618
    • Hanrahan, J.W.1    Gentzsch, M.2    Riordan, J.R.3
  • 54
    • 0027311276 scopus 로고
    • Protein kinase a (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • X.B. Chang, J.A. Tabcharani, Y.X. Hou, T.J. Hensen, N. Kartner, N. Alon, J.W. Hanrahan, and J.R. Riordan Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites J. Biol. Chem. 268 1993 11304 11311
    • (1993) J. Biol. Chem. , vol.268 , pp. 11304-11311
    • Chang, X.B.1    Tabcharani, J.A.2    Hou, Y.X.3    Hensen, T.J.4    Kartner, N.5    Alon, N.6    Hanrahan, J.W.7    Riordan, J.R.8
  • 58
    • 0030931648 scopus 로고    scopus 로고
    • Stimulation of CFTR activity by its phosphorylated R domain
    • M.C. Winter, and M.J. Welsh Stimulation of CFTR activity by its phosphorylated R domain Nature 389 1997 294 296
    • (1997) Nature , vol.389 , pp. 294-296
    • Winter, M.C.1    Welsh, M.J.2
  • 59
    • 0032876843 scopus 로고    scopus 로고
    • Function of the second nucleotide binding fold in the CFTR chloride channel
    • B. Zerhusen, and J. Ma Function of the second nucleotide binding fold in the CFTR chloride channel FEBS Lett. 459 1999 177 185
    • (1999) FEBS Lett. , vol.459 , pp. 177-185
    • Zerhusen, B.1    Ma, J.2
  • 60
    • 0027364318 scopus 로고
    • Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator
    • L.S. Smit, D.J. Wilkinson, M.K. Mansoura, F.S. Collins, and D.C. Dawson Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator Proc. Natl. Acad. Sci. USA 90 1993 9963 9967
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9963-9967
    • Smit, L.S.1    Wilkinson, D.J.2    Mansoura, M.K.3    Collins, F.S.4    Dawson, D.C.5
  • 61
    • 0037013262 scopus 로고    scopus 로고
    • The first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a rapid turnover
    • L. Aleksandrov, A. Aleksandrov, X.B. Chang, and J.R. Riordan The first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a rapid turnover J. Biol. Chem. 277 2002 15419 15425
    • (2002) J. Biol. Chem. , vol.277 , pp. 15419-15425
    • Aleksandrov, L.1    Aleksandrov, A.2    Chang, X.B.3    Riordan, J.R.4
  • 62
    • 0033514315 scopus 로고    scopus 로고
    • Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator)
    • M. Ramjeesingh, C. Li, E. Garami, L.J. Huan, K. Galley, Y. Wang, and C.E. Bear Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator) Biochemistry 38 1999 1463 1468
    • (1999) Biochemistry , vol.38 , pp. 1463-1468
    • Ramjeesingh, M.1    Li, C.2    Garami, E.3    Huan, L.J.4    Galley, K.5    Wang, Y.6    Bear, C.E.7
  • 63
    • 0346725092 scopus 로고    scopus 로고
    • An intrinsic adenylate kinase activity regulates gating of the ABC transporter CFTR
    • C. Randak, and M.J. Welsh An intrinsic adenylate kinase activity regulates gating of the ABC transporter CFTR Cell 115 2003 837 850
    • (2003) Cell , vol.115 , pp. 837-850
    • Randak, C.1    Welsh, M.J.2
  • 65
    • 12244313037 scopus 로고    scopus 로고
    • Normal gating of CFTR requires ATP binding to both nucleotide binding domains and hydrolysis at the second nucleotide binding domain
    • A.L. Berger, M. Ikuma, and M.J. Welsh Normal gating of CFTR requires ATP binding to both nucleotide binding domains and hydrolysis at the second nucleotide binding domain Proc. Natl. Acad. Sci. USA 102 2005 455 460
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 455-460
    • Berger, A.L.1    Ikuma, M.2    Welsh, M.J.3
  • 66
    • 12244251941 scopus 로고    scopus 로고
    • NBD1 might remain nucleotide-bound throughout CFTR channel gating cycle
    • C. Basso, P. Vergani, A.C. Nairn, and D.C. Gadsby NBD1 might remain nucleotide-bound throughout CFTR channel gating cycle Biophys. J. 82 2002 12a
    • (2002) Biophys. J. , vol.82
    • Basso, C.1    Vergani, P.2    Nairn, A.C.3    Gadsby, D.C.4
  • 67
    • 0032954806 scopus 로고    scopus 로고
    • Gating of cysticfibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme
    • S. Zeltwanger, F. Wang, G.T. Wang, K.D. Gillis, and T.C. Hwang Gating of cysticfibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme J. Gen. Physiol. 113 1999 541 554
    • (1999) J. Gen. Physiol. , vol.113 , pp. 541-554
    • Zeltwanger, S.1    Wang, F.2    Wang, G.T.3    Gillis, K.D.4    Hwang, T.C.5
  • 68
    • 0028822992 scopus 로고
    • Structural and functional similarities between the nucleotide-binding domains of CFTR and GFP-binding proteins
    • M.R. Carson, and M.J. Welsh Structural and functional similarities between the nucleotide-binding domains of CFTR and GFP-binding proteins Biophysics 69 1995 2443 2448
    • (1995) Biophysics , vol.69 , pp. 2443-2448
    • Carson, M.R.1    Welsh, M.J.2
  • 69
    • 0036521974 scopus 로고    scopus 로고
    • Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains
    • A.C.J. Powe, L. Al-Nakkash, M. Li, and T.C. Hwang Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains J. Physiol. 539 2002 333 346
    • (2002) J. Physiol. , vol.539 , pp. 333-346
    • Powe, A.C.J.1    Al-Nakkash, L.2    Li, M.3    Hwang, T.C.4
  • 70
    • 0033610840 scopus 로고    scopus 로고
    • Covalent modification of the nucleotide binding domains of cystic fibrosis transmembrane conductance regulator
    • J.F. Cotten, and M.J. Welsh Covalent modification of the nucleotide binding domains of cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 273 1998 31873 31879
    • (1998) J. Biol. Chem. , vol.273 , pp. 31873-31879
    • Cotten, J.F.1    Welsh, M.J.2
  • 72
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • E. Schneider, and S. Hunke ATP-binding cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains FEMS Microbiol. Rev. 22 1998 1 20
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 73
    • 0030611865 scopus 로고    scopus 로고
    • 2+-independent ATP binding of the sulfonylurea receptor SUR1
    • 2+-independent ATP binding of the sulfonylurea receptor SUR1 J. Biol. Chem. 272 1997 22983 22986
    • (1997) J. Biol. Chem. , vol.272 , pp. 22983-22986
    • Ueda, K.1    Inagaki, N.2    Seino, S.3
  • 75
    • 0030609142 scopus 로고    scopus 로고
    • ATP channel activity by diazoxide and MgADP Distinct functions of the two nucleotide binding folds of the sulfonylurea receptor
    • ATP channel activity by diazoxide and MgADP Distinct functions of the two nucleotide binding folds of the sulfonylurea receptor J. Gen. Physiol. 110 1997 643 654
    • (1997) J. Gen. Physiol. , vol.110 , pp. 643-654
    • Shyng, S.L.1    Ferrigni, T.2    Nichols, N.G.3
  • 78
    • 0033601321 scopus 로고    scopus 로고
    • ATP binding properties of the nucleotide-bindings folds of SUR1
    • M. Matsuo, N. Kioka, T. Amachi, and K. Ueda ATP binding properties of the nucleotide-bindings folds of SUR1 J. Biol. Chem. 274 1999 37479 37482
    • (1999) J. Biol. Chem. , vol.274 , pp. 37479-37482
    • Matsuo, M.1    Kioka, N.2    Amachi, T.3    Ueda, K.4
  • 79
    • 0034666295 scopus 로고    scopus 로고
    • Different binding properties and affinities for ATP and ADP among sulfonylurea receptor subtypes, SUR1, SUR2A and SUR2B
    • M. Matsuo, K. Tanabe, N. Kioka, T. Amachi, and K. Ueda Different binding properties and affinities for ATP and ADP among sulfonylurea receptor subtypes, SUR1, SUR2A and SUR2B J. Biol. Chem. 275 2000 28757 28763
    • (2000) J. Biol. Chem. , vol.275 , pp. 28757-28763
    • Matsuo, M.1    Tanabe, K.2    Kioka, N.3    Amachi, T.4    Ueda, K.5
  • 80
    • 0033574068 scopus 로고    scopus 로고
    • Cooperative binding of ATP and MgADP in the sulfonylurea receptor is modulated by glibenclamide
    • K. Ueda, J. Komine, M. Matsuo, S. Seino, and T. Amachi Cooperative binding of ATP and MgADP in the sulfonylurea receptor is modulated by glibenclamide Proc. Natl. Acad. Sci. USA 96 1999 1268 1272
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1268-1272
    • Ueda, K.1    Komine, J.2    Matsuo, M.3    Seino, S.4    Amachi, T.5
  • 91
    • 0034617097 scopus 로고    scopus 로고
    • Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1
    • Y.X. Hou, L. Cui, J.R. Riordan, and X.B. Chang Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1 J. Biol. Chem. 275 2000 20280 20287
    • (2000) J. Biol. Chem. , vol.275 , pp. 20280-20287
    • Hou, Y.X.1    Cui, L.2    Riordan, J.R.3    Chang, X.B.4
  • 94
    • 0035920130 scopus 로고    scopus 로고
    • Cysteines 431 and 1074 are responsible for inhibitory disulfide cross-linking between the two nucleotide-binding sites in human P-glycoprotein
    • I.L. Urbatsch, K. Gimi, S. Wilke-Mounts, N. Lerner-Marmarosh, M.E. Rousseau, P. Gros, and A.E. Senior Cysteines 431 and 1074 are responsible for inhibitory disulfide cross-linking between the two nucleotide-binding sites in human P-glycoprotein J. Biol. Chem. 276 2001 26980 26987
    • (2001) J. Biol. Chem. , vol.276 , pp. 26980-26987
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Lerner-Marmarosh, N.4    Rousseau, M.E.5    Gros, P.6    Senior, A.E.7
  • 95
    • 0034637483 scopus 로고    scopus 로고
    • Conserved Walker a Ser residues in the catalytic sites of P-glycoprotein are critical for catalysis and involved primarily at the transition state step
    • I.L. Urbatsch, K. Gimi, S. Wilke-Mounts, and A.E. Senior Conserved Walker A Ser residues in the catalytic sites of P-glycoprotein are critical for catalysis and involved primarily at the transition state step J. Biol. Chem. 275 2000 25031 25038
    • (2000) J. Biol. Chem. , vol.275 , pp. 25031-25038
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 97
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • J.E. Moody, L. Millen, D. Binns, J.F. Hunt, and P.J. Thomas Cooperative ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters J. Biol. Chem. 277 2002 21111 21114
    • (2002) J. Biol. Chem. , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 100
    • 0037085302 scopus 로고    scopus 로고
    • ATP binding to the first nucleotide binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain
    • Y.X. Hou, L. Cui, J.R. Riordan, and X.B. Chang ATP binding to the first nucleotide binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain J. Biol. Chem. 277 2002 5110 5119
    • (2002) J. Biol. Chem. , vol.277 , pp. 5110-5119
    • Hou, Y.X.1    Cui, L.2    Riordan, J.R.3    Chang, X.B.4
  • 101
    • 0035424958 scopus 로고    scopus 로고
    • Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation
    • L. Cui, Y.X. Hou, J.R. Riordan, and X.B. Chang Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation Arch. Biochem. Biophys. 392 2001 153 161
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 153-161
    • Cui, L.1    Hou, Y.X.2    Riordan, J.R.3    Chang, X.B.4
  • 102
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • I.L. Urbatsch, B. Sankaran, S. Bhagat, and 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
  • 103
    • 0034681959 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity
    • M. Julien, and P. Gros Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity Biochemistry 39 2000 4559 4568
    • (2000) Biochemistry , vol.39 , pp. 4559-4568
    • Julien, M.1    Gros, P.2
  • 104
    • 0242507463 scopus 로고    scopus 로고
    • Analysis of catalytic carboxylate mutants E552Q and E1197Q suggests asymmetric ATP hydrolysis by the two nucleotide binding domains of P-glycoprotein
    • I. Carrier, M. Julien, and P. Gross Analysis of catalytic carboxylate mutants E552Q and E1197Q suggests asymmetric ATP hydrolysis by the two nucleotide binding domains of P-glycoprotein Biochemistry 42 2003 12875 12885
    • (2003) Biochemistry , vol.42 , pp. 12875-12885
    • Carrier, I.1    Julien, M.2    Gross, P.3
  • 105
    • 0037180390 scopus 로고    scopus 로고
    • Importance of the conserved Walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human P-glycoprotein (ABCB1)
    • Z.E. Sauna, M. Müller, X.H. Peng, and S.V. Ambukdar Importance of the conserved Walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human P-glycoprotein (ABCB1) Biochemistry 41 2002 13989 14000
    • (2002) Biochemistry , vol.41 , pp. 13989-14000
    • Sauna, Z.E.1    Müller, M.2    Peng, X.H.3    Ambukdar, S.V.4
  • 106
    • 0034906977 scopus 로고    scopus 로고
    • Domain interactions in the yeast ATP binding cassette transporter Ycf1p: Intragenic suppressor analysis by mutations in the nucleotide binding domains
    • J.M. Falcon-Perez, M. Martinez-Burgos, J. Molano, M.J. Mazon, and P. Eraso Domain interactions in the yeast ATP binding cassette transporter Ycf1p: intragenic suppressor analysis by mutations in the nucleotide binding domains J. Bacteriol. 183 2001 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
  • 107
    • 0025912486 scopus 로고
    • Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide binding domains 1 and 2
    • R.J. Gregory, D.P. Rich, S.H. Cheng, D.W. Souza, S. Paul, P. Manavalan, M.P. Anderson, M.J. Welsh, and A.E. Smith Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide binding domains 1 and 2 Mol. Cell. Biol. 11 1991 3886 3893
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3886-3893
    • Gregory, R.J.1    Rich, D.P.2    Cheng, S.H.3    Souza, D.W.4    Paul, S.5    Manavalan, P.6    Anderson, M.P.7    Welsh, M.J.8    Smith, A.E.9
  • 108
    • 0035095848 scopus 로고    scopus 로고
    • Functional asymmetry of the two nucleotide binding domains in the ABC transporter Ste6
    • C. Proff, and R. Kölling Functional asymmetry of the two nucleotide binding domains in the ABC transporter Ste6 Mol. Gen. Genet. 264 2001 883 893
    • (2001) Mol. Gen. Genet. , vol.264 , pp. 883-893
    • Proff, C.1    Kölling, R.2
  • 109
    • 0036829647 scopus 로고    scopus 로고
    • The "lSGGQ" motif in each nucleotide binding domain of human P-glycoprotein is adjacent to the opposite walker a sequence
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke The "LSGGQ" motif in each nucleotide binding domain of human P-glycoprotein is adjacent to the opposite walker A sequence J. Biol. Chem. 277 2002 41303 41306
    • (2002) J. Biol. Chem. , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 112
    • 2442543305 scopus 로고    scopus 로고
    • The cystic fibrosis mutation G1349D within the signature motif LSHGH of NBD2 abolishes the activation of chloride channels by genistein
    • P. Melin, V. Thoreau, C. Norez, F. Bilan, A. Kitzis, and F. Becq The cystic fibrosis mutation G1349D within the signature motif LSHGH of NBD2 abolishes the activation of chloride channels by genistein Biochem. Pharmacol. 67 2004 2187 2196
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 2187-2196
    • Melin, P.1    Thoreau, V.2    Norez, C.3    Bilan, F.4    Kitzis, A.5    Becq, F.6
  • 113
    • 0032743305 scopus 로고    scopus 로고
    • Defective function of the cystic fibrosis-causing missense mutation G551D is recovered by genistein
    • B. Illek, L. Zhang, N.C. Lewis, R.B. Moss, J.Y. Dong, and H. Fischer Defective function of the cystic fibrosis-causing missense mutation G551D is recovered by genistein Am. J. Physiol. 277 1999 C833 C839
    • (1999) Am. J. Physiol. , vol.277
    • Illek, B.1    Zhang, L.2    Lewis, N.C.3    Moss, R.B.4    Dong, J.Y.5    Fischer, H.6
  • 114
    • 0037102132 scopus 로고    scopus 로고
    • Mutations in the linker domain of NBD2 of SUR inhibits transduction but not nucleotide binding
    • M. Matsuo, M. Dabrowski, K. Ueda, and F.M. Ashcroft Mutations in the linker domain of NBD2 of SUR inhibits transduction but not nucleotide binding EMBO J. 21 2002 4250 4258
    • (2002) EMBO J. , vol.21 , pp. 4250-4258
    • Matsuo, M.1    Dabrowski, M.2    Ueda, K.3    Ashcroft, F.M.4
  • 115
    • 4744347692 scopus 로고    scopus 로고
    • The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers
    • Z. Szentpetery, A. Kern, K. Liliom, B. Sarkadi, A. Varadi, and E. Bakos The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers J. Biol. Chem. 279 2004 41670 41678
    • (2004) J. Biol. Chem. , vol.279 , pp. 41670-41678
    • Szentpetery, Z.1    Kern, A.2    Liliom, K.3    Sarkadi, B.4    Varadi, A.5    Bakos, E.6
  • 116
    • 2442477649 scopus 로고    scopus 로고
    • Functional studies on the MRP1 multidrug transporter: Characterization of ABC-signature mutant variants
    • Z. Szentpetery, B. Sarkadi, E. Bakos, and A. Varadi Functional studies on the MRP1 multidrug transporter: characterization of ABC-signature mutant variants Anticancer Res. 24 2004 449 455
    • (2004) Anticancer Res. , vol.24 , pp. 449-455
    • Szentpetery, Z.1    Sarkadi, B.2    Bakos, E.3    Varadi, A.4
  • 117
    • 0031655970 scopus 로고    scopus 로고
    • Yeast as en expression system for the study of P-glycoprotein and other ABC transporters
    • P. Gros, L. Beaudet, and I.L. Urbatsch Yeast as en expression system for the study of P-glycoprotein and other ABC transporters Acta Physiol. Scand. 163 1998 S219 S225
    • (1998) Acta Physiol. Scand. , vol.163
    • Gros, P.1    Beaudet, L.2    Urbatsch, I.L.3
  • 118
    • 0032130787 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent multidrug transport in P-glycoprotein
    • A.B. Shapiro, and V. Ling The mechanism of ATP-dependent multidrug transport in P-glycoprotein Acta. Physiol. Scand. 163 1998 S227 S234
    • (1998) Acta. Physiol. Scand. , vol.163
    • Shapiro, A.B.1    Ling, V.2
  • 119
    • 0031007555 scopus 로고    scopus 로고
    • Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature regions
    • E. Bakos, I. Klein, E. Welker, K. Szabo, M. Müller, B. Sarkadi, and A. Varadi Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature regions Biochem. J. 323 1997 777 783
    • (1997) Biochem. J. , vol.323 , pp. 777-783
    • Bakos, E.1    Klein, I.2    Welker, E.3    Szabo, K.4    Müller, M.5    Sarkadi, B.6    Varadi, A.7
  • 120
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • S.H. Cheng, R.J. Gregory, J. Marshall, S. Paul, D.W. Souza, G.A. White, C.R. Riordan, and A.E. Smith Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis Cell 63 1990 827 834
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    Riordan, C.R.7    Smith, A.E.8
  • 121
    • 9644259423 scopus 로고    scopus 로고
    • Mistargeted MRPdelta F728 mutant is rescued by intracellular GSH
    • F. Buyse, M. Vandenbranden, and J.M. Ruysschaert Mistargeted MRPdelta F728 mutant is rescued by intracellular GSH FEBS Lett. 578 2004 145 151
    • (2004) FEBS Lett. , vol.578 , pp. 145-151
    • Buyse, F.1    Vandenbranden, M.2    Ruysschaert, J.M.3
  • 123
    • 0035937847 scopus 로고    scopus 로고
    • Conformational and temperature-sensitive stability defects of the Δf508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments
    • M. Sharma, M. Benharouga, W. Hu, and G.L. Lukacs Conformational and temperature-sensitive stability defects of the ΔF508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments J. Biol. Chem. 276 2001 8942 8950
    • (2001) J. Biol. Chem. , vol.276 , pp. 8942-8950
    • Sharma, M.1    Benharouga, M.2    Hu, W.3    Lukacs, G.L.4
  • 124
    • 11444266284 scopus 로고    scopus 로고
    • The Δf508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-transcriptional folding of CFTR
    • K. Du, M. Sharma, and G.L. Lukacs The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-transcriptional folding of CFTR Nat. Struct. Mol. Biol. 26 2005 17 25
    • (2005) Nat. Struct. Mol. Biol. , vol.26 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 125
    • 15544371839 scopus 로고    scopus 로고
    • Assembly of functional CFTR chloride channels
    • J.R. Riordan Assembly of functional CFTR chloride channels Annu. Rev. Physiol. 67 2005 701 718
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 701-718
    • Riordan, J.R.1
  • 126
    • 0030773897 scopus 로고    scopus 로고
    • Genistein potentiates wild-type and delta F508-CFTR channel activity
    • T.C. Hwang, F. Wang, C.H. Yang, and W.W. Reenstra Genistein potentiates wild-type and delta F508-CFTR channel activity Am. J. Physiol. 273 1997 C988 C998
    • (1997) Am. J. Physiol. , vol.273
    • Hwang, T.C.1    Wang, F.2    Yang, C.H.3    Reenstra, W.W.4
  • 127
    • 27144481548 scopus 로고    scopus 로고
    • Rescue of DeltaF508 and other misprocessed CFTR mutants by a novel quinazoline compound
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke Rescue of DeltaF508 and other misprocessed CFTR mutants by a novel quinazoline compound Mol. Pharm. 2 2005 407 413
    • (2005) Mol. Pharm. , vol.2 , pp. 407-413
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 128
    • 0036896021 scopus 로고    scopus 로고
    • Rescuing protein conformation: Prospects for pharmacological therapy of cystic fibrosis
    • M. Gelman, and R. Kopito Rescuing protein conformation: prospects for pharmacological therapy of cystic fibrosis J. Clin. Invest. 110 2002 1591 1597
    • (2002) J. Clin. Invest. , vol.110 , pp. 1591-1597
    • Gelman, M.1    Kopito, R.2
  • 130
    • 0033536032 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator: Solution structures of peptides based on the Phe508 region, the most common site of disease-causing Δf508 mutation
    • M. Massiah, Y. Ko, P. Pedersen, and A. Mildvan Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing ΔF508 mutation Biochemistry 38 1999 7453 7461
    • (1999) Biochemistry , vol.38 , pp. 7453-7461
    • Massiah, M.1    Ko, Y.2    Pedersen, P.3    Mildvan, A.4
  • 131
    • 0034192547 scopus 로고    scopus 로고
    • Deletion of phenylalanine 508 causes attenuated phosphorylation-dependent activation of CFTR chloride channels
    • F. Wang, S. Zeltwanger, S. Hu, and T.C. Hwang Deletion of phenylalanine 508 causes attenuated phosphorylation-dependent activation of CFTR chloride channels J. Physiol. 524 2000 637 648
    • (2000) J. Physiol. , vol.524 , pp. 637-648
    • Wang, F.1    Zeltwanger, S.2    Hu, S.3    Hwang, T.C.4
  • 132
    • 20344393911 scopus 로고    scopus 로고
    • Identification of molecular determinants that modulate trafficking of DeltaF508 CFTR, the mutant ABC transporter associated with cystic fibrosis
    • I. Tsigelny, M. Hotchko, J.X. Yuan, and S.H. Keller Identification of molecular determinants that modulate trafficking of DeltaF508 CFTR, the mutant ABC transporter associated with cystic fibrosis Cell Biochem. Biophys. 42 2005 41 53
    • (2005) Cell Biochem. Biophys. , vol.42 , pp. 41-53
    • Tsigelny, I.1    Hotchko, M.2    Yuan, J.X.3    Keller, S.H.4
  • 133
    • 0035956875 scopus 로고    scopus 로고
    • ATP channels caused by a sulfonylurea receptor 1 mutation associated with persisten thyperinsulinemic hypoglycemia of infancy
    • ATP channels caused by a sulfonylurea receptor 1 mutation associated with persisten thyperinsulinemic hypoglycemia of infancy Proc. Natl. Acad. Sci. USA 98 2001 2882 2887
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2882-2887
    • Cartier, E.A.1    Conti, L.R.2    Vandenberg, C.A.3    Shyng, S.L.4
  • 134
    • 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, and B. Tummler 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    Tummler, B.5
  • 135
    • 0031021804 scopus 로고    scopus 로고
    • Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators
    • T.W. Loo, and D.M. Clarke Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators J. Biol. Chem. 272 1997 709 712
    • (1997) J. Biol. Chem. , vol.272 , pp. 709-712
    • Loo, T.W.1    Clarke, D.M.2
  • 136
    • 0032915873 scopus 로고    scopus 로고
    • Mutational disruption of plasma membrane trafficking of Saccharomyces cerevisiae Yor1p, a homologue of mammalian multidrug resistance protein
    • D.J. Katzmann, E.A. Epping, and W.S. Moye-Rowley Mutational disruption of plasma membrane trafficking of Saccharomyces cerevisiae Yor1p, a homologue of mammalian multidrug resistance protein Mol. Cell. Biol. 19 1999 2998 3009
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2998-3009
    • Katzmann, D.J.1    Epping, E.A.2    Moye-Rowley, W.S.3
  • 138
    • 0037127222 scopus 로고    scopus 로고
    • Mutations that change the position of the putative γ-phosphate linker in the nucleotide binding domains of CFTR alter channel gating
    • A.L. Berger, M. Ikuma, J.F. Hunt, P.J. Thomas, and M.J. Welsh Mutations that change the position of the putative γ-phosphate linker in the nucleotide binding domains of CFTR alter channel gating J. Biol. Chem. 277 2002 2125 2131
    • (2002) J. Biol. Chem. , vol.277 , pp. 2125-2131
    • Berger, A.L.1    Ikuma, M.2    Hunt, J.F.3    Thomas, P.J.4    Welsh, M.J.5
  • 139
    • 0028929909 scopus 로고
    • Mechanism of dysfunction of two nucleotide binding domain mutations in cystic fibrosis transmembrane conductance regulator that are associated with pancreatic sufficiency
    • D.N. Sheppard, L.S. Ostedgaard, M.C. Winter, and M.J. Welsh Mechanism of dysfunction of two nucleotide binding domain mutations in cystic fibrosis transmembrane conductance regulator that are associated with pancreatic sufficiency EMBO J. 14 1995 876 883
    • (1995) EMBO J. , vol.14 , pp. 876-883
    • Sheppard, D.N.1    Ostedgaard, L.S.2    Winter, M.C.3    Welsh, M.J.4
  • 140
    • 0036198469 scopus 로고    scopus 로고
    • Cysteine residues in the nucleotide binding domains regulate the conductance state of CFTR channels
    • M.A. Harrington, and R.R. Kopito Cysteine residues in the nucleotide binding domains regulate the conductance state of CFTR channels Biophys. J. 82 2002 1278 1292
    • (2002) Biophys. J. , vol.82 , pp. 1278-1292
    • Harrington, M.A.1    Kopito, R.R.2
  • 144
    • 9444282152 scopus 로고    scopus 로고
    • Identification of a functionally important negatively charged residue within the second catalytic site of the SUR1 nucleotide binding domains
    • J.D. Campbell, P. Proks, J.D. Lippiat, M.S. Sansom, and F.M. Ashcroft Identification of a functionally important negatively charged residue within the second catalytic site of the SUR1 nucleotide binding domains Diabetes 53 2004 S123 S127
    • (2004) Diabetes , vol.53
    • Campbell, J.D.1    Proks, P.2    Lippiat, J.D.3    Sansom, M.S.4    Ashcroft, F.M.5
  • 145
    • 4844227861 scopus 로고    scopus 로고
    • + channels: Implication for dimerization of nucleotide-binding domains to induce channel opening
    • + channels: implication for dimerization of nucleotide-binding domains to induce channel opening Mol. Pharmacol. 66 2004 807 816
    • (2004) Mol. Pharmacol. , vol.66 , pp. 807-816
    • Yamada, M.1    Ishii, M.2    Hibino, H.3    Kurachi, Y.4
  • 146
    • 10344236531 scopus 로고    scopus 로고
    • Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1
    • Q. Zhao, and X.B. Chang Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1 J. Biol. Chem. 279 2004 48505 48512
    • (2004) J. Biol. Chem. , vol.279 , pp. 48505-48512
    • Zhao, Q.1    Chang, X.B.2
  • 147
    • 0036830243 scopus 로고    scopus 로고
    • Trafficking defect and functional defect by mutations of the ATP-binding domains in the multidrug resistance protein 2 in patients with Dubin-Johnson syndrome
    • K. Hashimoto, T. Uchiumi, T. Konno, T. Ebihara, T. Nakamura, M. Wada, S. Sakisaka, F. Maniwa, T. Amachi, K. Ueda, and M. Kuwano Trafficking defect and functional defect by mutations of the ATP-binding domains in the multidrug resistance protein 2 in patients with Dubin-Johnson syndrome Hepatology 36 2002 1236 1245
    • (2002) Hepatology , vol.36 , pp. 1236-1245
    • Hashimoto, K.1    Uchiumi, T.2    Konno, T.3    Ebihara, T.4    Nakamura, T.5    Wada, M.6    Sakisaka, S.7    Maniwa, F.8    Amachi, T.9    Ueda, K.10    Kuwano, M.11
  • 148
    • 0032560635 scopus 로고    scopus 로고
    • Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphate activity
    • L. Beaudet, I.L. Urbatsch, and P. Gross Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphate activity Biochemistry 37 1998 9073 9082
    • (1998) Biochemistry , vol.37 , pp. 9073-9082
    • Beaudet, L.1    Urbatsch, I.L.2    Gross, P.3
  • 150
    • 0038143251 scopus 로고    scopus 로고
    • A region within the lumenal loop of Saccharomyces cerevisiae Ycf1p directs proteolytic processing and substrate specificity
    • D.L. Mason, M.P. Mallampalli, G. Huyer, and S. Michaelis A region within the lumenal loop of Saccharomyces cerevisiae Ycf1p directs proteolytic processing and substrate specificity Eukaryot. Cell 2 2003 588 598
    • (2003) Eukaryot. Cell , vol.2 , pp. 588-598
    • Mason, D.L.1    Mallampalli, M.P.2    Huyer, G.3    Michaelis, S.4
  • 151
    • 0026681083 scopus 로고
    • Phosphorylation of the cystic fibrosis transmembrane conductance regulator
    • M.R. Picciotto, J.A. Cohn, G. Bertuzzi, P. Greengard, and A.C. Nairn Phosphorylation of the cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 267 1992 12742 12752
    • (1992) J. Biol. Chem. , vol.267 , pp. 12742-12752
    • Picciotto, M.R.1    Cohn, J.A.2    Bertuzzi, G.3    Greengard, P.4    Nairn, A.C.5
  • 152
    • 0030667705 scopus 로고    scopus 로고
    • Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry
    • D.C. Neville, C.R. Rozanas, E.M. Price, D.B. Gruis, A.S. Verkman, and R.R. Townsend Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry Protein Sci. 6 1997 2436 2445
    • (1997) Protein Sci. , vol.6 , pp. 2436-2445
    • Neville, D.C.1    Rozanas, C.R.2    Price, E.M.3    Gruis, D.B.4    Verkman, A.S.5    Townsend, R.R.6
  • 153
    • 20844457435 scopus 로고    scopus 로고
    • Preferential phosphorylation of R-domain Ser768 dampens activation of CFTR channels by PKA
    • L. Csanady, D. Seto-Young, K.W. Chan, C. Cenciarelli, B.B. Angel, J. Qin, D.T. McLachlin, A.N. Krutchinsky, B.T. Chait, A.C. Nairn, and D.C. Gadsby Preferential phosphorylation of R-domain Ser768 dampens activation of CFTR channels by PKA J. Gen. Physiol. 125 2005 171 186
    • (2005) J. Gen. Physiol. , vol.125 , pp. 171-186
    • Csanady, L.1    Seto-Young, D.2    Chan, K.W.3    Cenciarelli, C.4    Angel, B.B.5    Qin, J.6
  • 154
    • 0028891373 scopus 로고
    • Mutation of potential phosphorylation sites in the recombinant R domain of the cystic fibrosis transmembrane conductance regulator has significant effects on domain conformation
    • A.M. Dulhanty, X.B. Chang, and J.R. Riordan Mutation of potential phosphorylation sites in the recombinant R domain of the cystic fibrosis transmembrane conductance regulator has significant effects on domain conformation Biochem. Biophys. Res. Commun. 206 1995 207 214
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 207-214
    • Dulhanty, A.M.1    Chang, X.B.2    Riordan, J.R.3
  • 155
    • 0032562143 scopus 로고    scopus 로고
    • Expression and characterization of the NBD1-R domain region of CFTR: Evidence for subunit-subunit interactions
    • D.C. Neville, C.R. Rozanas, B.M. Tulk, R.R. Townsend, and A.S. Verkman Expression and characterization of the NBD1-R domain region of CFTR: evidence for subunit-subunit interactions Biochemistry 37 1998 2401 2409
    • (1998) Biochemistry , vol.37 , pp. 2401-2409
    • Neville, D.C.1    Rozanas, C.R.2    Tulk, B.M.3    Townsend, R.R.4    Verkman, A.S.5
  • 157
    • 0037383783 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C sites in NBD1 and the R domain control CFTR channel activation by PKA
    • V. Chappe, D.A. Hinkson, T. Zhu, X.B. Chang, R.J. Riordan, and J.W. Hanrahan Phosphorylation of protein kinase C sites in NBD1 and the R domain control CFTR channel activation by PKA J. Physiol. 548 2003 39 52
    • (2003) J. Physiol. , vol.548 , pp. 39-52
    • Chappe, V.1    Hinkson, D.A.2    Zhu, T.3    Chang, X.B.4    Riordan, R.J.5    Hanrahan, J.W.6
  • 159
    • 6044274620 scopus 로고    scopus 로고
    • Potentiation of effect of PKA stimulation of Xenopus CFTR by activation of PKC: Role of NBD2
    • Y. Chen, B. Button, G.A. Altenberg, and L. Reuss Potentiation of effect of PKA stimulation of Xenopus CFTR by activation of PKC: role of NBD2 Am. J. Physiol. Cell Physiol. 287 2004 1426 1444
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287 , pp. 1426-1444
    • Chen, Y.1    Button, B.2    Altenberg, G.A.3    Reuss, L.4
  • 160
    • 0031689866 scopus 로고    scopus 로고
    • Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator
    • A. Vankeerberghen, L. Wei, M. Jaspers, J.J. Cassiman, B. Nilius, and H. Cuppens Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator Hum. Mol. Genet. 7 1998 1761 1769
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1761-1769
    • Vankeerberghen, A.1    Wei, L.2    Jaspers, M.3    Cassiman, J.J.4    Nilius, B.5    Cuppens, H.6
  • 161
    • 0033610809 scopus 로고    scopus 로고
    • A conserved region of the R domain of cystic fibrosis transmembrane conductance regulator is important in processing and function
    • E.A. Pasyk, X.K. Morin, P. Zeman, E. Garami, K. Galley, L.J. Huan, Y. Wang, and C.E. Bear A conserved region of the R domain of cystic fibrosis transmembrane conductance regulator is important in processing and function J. Biol. Chem. 273 1998 31759 31764
    • (1998) J. Biol. Chem. , vol.273 , pp. 31759-31764
    • Pasyk, E.A.1    Morin, X.K.2    Zeman, P.3    Garami, E.4    Galley, K.5    Huan, L.J.6    Wang, Y.7    Bear, C.E.8
  • 162
    • 0742272647 scopus 로고    scopus 로고
    • Intermolecular interaction between R domain of cystic fibrosis transmembrane conductance regulator
    • S. Gupta, J. Xie, J. Ma, and P.B. Davis Intermolecular interaction between R domain of cystic fibrosis transmembrane conductance regulator Am. J. Respir. Cell. Mol. Biol. 30 2004 242 248
    • (2004) Am. J. Respir. Cell. Mol. Biol. , vol.30 , pp. 242-248
    • Gupta, S.1    Xie, J.2    Ma, J.3    Davis, P.B.4
  • 163
    • 0037151094 scopus 로고    scopus 로고
    • A short segment of the R domain of cystic fibrosis transmembrane conductance regulator contains channel stimulatory and inhibitory activities that are separable by sequence modification
    • J. Xie, L.M. Adams, J. Zhao, T.A. Gerken, P.B. Davis, and J. Ma A short segment of the R domain of cystic fibrosis transmembrane conductance regulator contains channel stimulatory and inhibitory activities that are separable by sequence modification J. Biol. Chem. 277 2002 23019 23027
    • (2002) J. Biol. Chem. , vol.277 , pp. 23019-23027
    • Xie, J.1    Adams, L.M.2    Zhao, J.3    Gerken, T.A.4    Davis, P.B.5    Ma, J.6
  • 164
    • 0030774895 scopus 로고    scopus 로고
    • Covalent modification of the regulatory domain irreversibly stimulates cystic fibrosis transmembrane conductance regulator
    • J.F. Cotten, and M.J. Welsh Covalent modification of the regulatory domain irreversibly stimulates cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 272 1997 25617 25622
    • (1997) J. Biol. Chem. , vol.272 , pp. 25617-25622
    • Cotten, J.F.1    Welsh, M.J.2
  • 165
    • 0032515182 scopus 로고    scopus 로고
    • Phosphorylation site independent single R-domain mutations affect CFTR channel activity
    • L. Wei, A. Vankeerberghen, H. Cuppens, G. Droogmans, J.J. Cassiman, and B. Nilus Phosphorylation site independent single R-domain mutations affect CFTR channel activity FEBS Lett. 439 1998 121 126
    • (1998) FEBS Lett. , vol.439 , pp. 121-126
    • Wei, L.1    Vankeerberghen, A.2    Cuppens, H.3    Droogmans, G.4    Cassiman, J.J.5    Nilus, B.6
  • 166
    • 0035886655 scopus 로고    scopus 로고
    • A cluster of negative charges at the amino terminal tail of CFTR regulates ATP-dependent channel gating
    • J. Fu, H.L. Ji, A.P. Naren, and K.L. Kirk A cluster of negative charges at the amino terminal tail of CFTR regulates ATP-dependent channel gating J. Physiol. 536 2001 459 470
    • (2001) J. Physiol. , vol.536 , pp. 459-470
    • Fu, J.1    Ji, H.L.2    Naren, A.P.3    Kirk, K.L.4
  • 167
    • 0035929683 scopus 로고    scopus 로고
    • Cysteine substitutions reveal dual functions of the animo-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating
    • J. Fu, and K.L. Kirk Cysteine substitutions reveal dual functions of the animo-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating J. Biol. Chem. 276 2001 35660 35668
    • (2001) J. Biol. Chem. , vol.276 , pp. 35660-35668
    • Fu, J.1    Kirk, K.L.2
  • 168
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion selectivity filter of the cystic transmembrane conductance regulator (CFTR). chloride channel
    • M. Cheung, and M.H. Akabas Locating the anion selectivity filter of the cystic transmembrane conductance regulator (CFTR). chloride channel J. Gen. Physiol. 109 1997 289 299
    • (1997) J. Gen. Physiol. , vol.109 , pp. 289-299
    • Cheung, M.1    Akabas, M.H.2
  • 169
    • 0030931382 scopus 로고    scopus 로고
    • Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator
    • X. Xiong, A. Bragin, J.H. Widdicombe, J. Cohn, and W.R. Skach Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator J. Clin. Invest. 100 1997 1079 1088
    • (1997) J. Clin. Invest. , vol.100 , pp. 1079-1088
    • Xiong, X.1    Bragin, A.2    Widdicombe, J.H.3    Cohn, J.4    Skach, W.R.5
  • 170
    • 15844397666 scopus 로고    scopus 로고
    • Contribution of proline residues in the membrane-spanning domains of CFTR to chloride channel function
    • D.N. Sheppard, S.M. Travis, H. Ishihara, and M.J. Welsh Contribution of proline residues in the membrane-spanning domains of CFTR to chloride channel function J. Biol. Chem. 271 1996 14995 15001
    • (1996) J. Biol. Chem. , vol.271 , pp. 14995-15001
    • Sheppard, D.N.1    Travis, S.M.2    Ishihara, H.3    Welsh, M.J.4
  • 172
    • 0030775639 scopus 로고    scopus 로고
    • Disease-associated mutations in the cytosolic loops 1 and 2 of cystic fibrosis transmembrane conductance regulator impede processing or opening of the channel
    • F.S. Seibert, Y. Jia, C.J. Mathews, J.W. Hanrahan, J.R. Riordan, T.W. Loo, and D.M. Clarke Disease-associated mutations in the cytosolic loops 1 and 2 of cystic fibrosis transmembrane conductance regulator impede processing or opening of the channel Biochemistry 36 1997 11966 11974
    • (1997) Biochemistry , vol.36 , pp. 11966-11974
    • Seibert, F.S.1    Jia, Y.2    Mathews, C.J.3    Hanrahan, J.W.4    Riordan, J.R.5    Loo, T.W.6    Clarke, D.M.7
  • 173
    • 0037133518 scopus 로고    scopus 로고
    • Polar residues in membrane domains of proteins: Molecular basis for helix-helix association in a mutant CFTR transmembrane segment
    • A.W. Partridge, R.A. Melnyk, and C.M. Deber Polar residues in membrane domains of proteins: molecular basis for helix-helix association in a mutant CFTR transmembrane segment Biochemistry 41 2002 3647 3653
    • (2002) Biochemistry , vol.41 , pp. 3647-3653
    • Partridge, A.W.1    Melnyk, R.A.2    Deber, C.M.3
  • 174
    • 0036206202 scopus 로고    scopus 로고
    • Intracellular cysteines of the cystic fibrosis transmembrane conductance regulator (CFTR) modulate channel gating
    • C.J. Ketchum, H. Yue, K.A. Alessi, S. Devidas, W.B. Guggino, and P.C. Maloney Intracellular cysteines of the cystic fibrosis transmembrane conductance regulator (CFTR) modulate channel gating Cell Physiol. Biochem. 12 2002 1 8
    • (2002) Cell Physiol. Biochem. , vol.12 , pp. 1-8
    • Ketchum, C.J.1    Yue, H.2    Alessi, K.A.3    Devidas, S.4    Guggino, W.B.5    Maloney, P.C.6
  • 175
    • 0033931302 scopus 로고    scopus 로고
    • Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator
    • Z.R. Zhang, S.I. McDonough, and N.A. McCarty Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator Biophys. J. 79 2000 298 313
    • (2000) Biophys. J. , vol.79 , pp. 298-313
    • Zhang, Z.R.1    McDonough, S.I.2    McCarty, N.A.3
  • 177
    • 0033898228 scopus 로고    scopus 로고
    • Permeation through the CFTR chloride channel
    • N.A. McCarty Permeation through the CFTR chloride channel J. Exp. Biol. 203 2000 1947 1962
    • (2000) J. Exp. Biol. , vol.203 , pp. 1947-1962
    • McCarty, N.A.1
  • 178
    • 0035811064 scopus 로고    scopus 로고
    • Asymmetric structure of the cystic fibrosis transmembrane conductance regulator chloride channel pore suggested by mutagenesis of the twelfth transmembrane region
    • J. Gupta, A. Evagelidis, J.W. Hanrahan, and P. Linsdell Asymmetric structure of the cystic fibrosis transmembrane conductance regulator chloride channel pore suggested by mutagenesis of the twelfth transmembrane region Biochemistry 40 2001 6620 6627
    • (2001) Biochemistry , vol.40 , pp. 6620-6627
    • Gupta, J.1    Evagelidis, A.2    Hanrahan, J.W.3    Linsdell, P.4
  • 179
    • 0036129622 scopus 로고    scopus 로고
    • Point mutations in the pore region directly or indirectly affect glibenclamide block of the CFTR chloride channel
    • J. Gupta, and P. Linsdell Point mutations in the pore region directly or indirectly affect glibenclamide block of the CFTR chloride channel Eur. J. Physiol. 443 2002 739 747
    • (2002) Eur. J. Physiol. , vol.443 , pp. 739-747
    • Gupta, J.1    Linsdell, P.2
  • 181
    • 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, and 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
  • 182
    • 0030731950 scopus 로고    scopus 로고
    • Cystic fibrosis phenotype associated with pancreatic insufficiency does not always reflect the cAMP-dependent chloride conductive pathway defect
    • P. Fanen, R. Labarthe, F. Garnier, M. Benharouga, M. Goosens, and A. Edelman Cystic fibrosis phenotype associated with pancreatic insufficiency does not always reflect the cAMP-dependent chloride conductive pathway defect J. Biol. Chem. 272 1997 30563 30566
    • (1997) J. Biol. Chem. , vol.272 , pp. 30563-30566
    • Fanen, P.1    Labarthe, R.2    Garnier, F.3    Benharouga, M.4    Goosens, M.5    Edelman, A.6
  • 184
    • 0035868361 scopus 로고    scopus 로고
    • Multiple endocytic signals in the C-terminal tail of the cystic fibrosis transmembrane conductance regulator
    • W. Hu, M. Howard, and G.L. Lukacs Multiple endocytic signals in the C-terminal tail of the cystic fibrosis transmembrane conductance regulator Biochem. J. 354 2001 561 572
    • (2001) Biochem. J. , vol.354 , pp. 561-572
    • Hu, W.1    Howard, M.2    Lukacs, G.L.3
  • 185
    • 0037147151 scopus 로고    scopus 로고
    • Ablation of internalization signals in the carboxy-terminal tail of the cystic fibrosis transmembrane conductance regulator enhances cell surface expression
    • K. Peter, K. Varga, Z. Bebok, C.M. McNicholas-Bevensee, L. Schwiebert, E.J. Sorscher, E.M. Schwiebert, and J.F. Collawn Ablation of internalization signals in the carboxy-terminal tail of the cystic fibrosis transmembrane conductance regulator enhances cell surface expression J. Biol. Chem. 277 2002 49952 49957
    • (2002) J. Biol. Chem. , vol.277 , pp. 49952-49957
    • Peter, K.1    Varga, K.2    Bebok, Z.3    McNicholas-Bevensee, C.M.4    Schwiebert, L.5    Sorscher, E.J.6    Schwiebert, E.M.7    Collawn, J.F.8
  • 188
    • 0033608961 scopus 로고    scopus 로고
    • Arg 352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel
    • R. Guinamard, and M.H. Akabas Arg 352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel Biochemistry 38 1999 5528 5537
    • (1999) Biochemistry , vol.38 , pp. 5528-5537
    • Guinamard, R.1    Akabas, M.H.2
  • 189
    • 0034084793 scopus 로고    scopus 로고
    • Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • P. Linsdell, A. Evagelidis, and J.W. Hanrahan Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore Biophys. J. 78 2000 2973 2982
    • (2000) Biophys. J. , vol.78 , pp. 2973-2982
    • Linsdell, P.1    Evagelidis, A.2    Hanrahan, J.W.3
  • 190
    • 0035865354 scopus 로고    scopus 로고
    • Relationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • P. Linsdell Relationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel pore J. Physiol. 531 2001 51 66
    • (2001) J. Physiol. , vol.531 , pp. 51-66
    • Linsdell, P.1
  • 192
    • 0034774836 scopus 로고    scopus 로고
    • CFTR: Covalent and non-covalent modification suggests a role for fixed charges in anion conduction
    • S.S. Smith, X. Liu, Z.R. Zhang, F. Sun, T.E. Kriewall, N.A. McCarty, and D.C. Dawson CFTR: covalent and non-covalent modification suggests a role for fixed charges in anion conduction J. Gen. Physiol. 118 2001 407 431
    • (2001) J. Gen. Physiol. , vol.118 , pp. 407-431
    • Smith, S.S.1    Liu, X.2    Zhang, Z.R.3    Sun, F.4    Kriewall, T.E.5    McCarty, N.A.6    Dawson, D.C.7
  • 193
    • 0344304517 scopus 로고    scopus 로고
    • Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore
    • X. Gong, and P. Linsdell Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore J. Gen. Physiol. 122 2003 673 687
    • (2003) J. Gen. Physiol. , vol.122 , pp. 673-687
    • Gong, X.1    Linsdell, P.2
  • 194
    • 0035853675 scopus 로고    scopus 로고
    • Perturbation of the pore of the cystic fibrosis transmembrane conductance regulator (CFTR) inhibits its ATPase activity
    • I. Kogan, M. Ramjeesingh, L.J. Huan, Y. Wang, and C.E. Bear Perturbation of the pore of the cystic fibrosis transmembrane conductance regulator (CFTR) inhibits its ATPase activity J. Biol. Chem. 276 2001 11575 11581
    • (2001) J. Biol. Chem. , vol.276 , pp. 11575-11581
    • Kogan, I.1    Ramjeesingh, M.2    Huan, L.J.3    Wang, Y.4    Bear, C.E.5
  • 195
    • 0037266979 scopus 로고    scopus 로고
    • Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore
    • J. Gupta, and P. Linsdell Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore Mol. Membr. Biol. 20 2003 45 52
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 45-52
    • Gupta, J.1    Linsdell, P.2
  • 196
    • 0038120974 scopus 로고    scopus 로고
    • Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore
    • X. Gong, and P. Linsdell Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore J. Physiol. 549 2003 387 397
    • (2003) J. Physiol. , vol.549 , pp. 387-397
    • Gong, X.1    Linsdell, P.2
  • 197
    • 2042437156 scopus 로고    scopus 로고
    • Interaction of channel blockers with R347D-CFTR
    • P. Linsdell, and J.W. Hanrahan Interaction of channel blockers with R347D-CFTR Ped. Pulmonol. Suppl. 14 1997 215
    • (1997) Ped. Pulmonol. Suppl. , vol.14 , pp. 215
    • Linsdell, P.1    Hanrahan, J.W.2
  • 198
    • 10044283304 scopus 로고    scopus 로고
    • CFTR: A cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore
    • X. Liu, Z.R. Zhang, M.D. Fuller, J. Billingsley, N.A. McCarty, and D.C. Dawson CFTR: a cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore Biophys. J. 87 2004 3826 3841
    • (2004) Biophys. J. , vol.87 , pp. 3826-3841
    • Liu, X.1    Zhang, Z.R.2    Fuller, M.D.3    Billingsley, J.4    McCarty, N.A.5    Dawson, D.C.6
  • 199
    • 14244262456 scopus 로고    scopus 로고
    • Destabilization of the transmembrane domain induces misfolding in a phenotypic mutant of cystic fibrosis transmembrane conductance regulator
    • M.Y. Choi, A.W. Partridge, C. Daniels, K. Du, G.L. Lukacs, and C.M. Deber Destabilization of the transmembrane domain induces misfolding in a phenotypic mutant of cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 280 2005 4968 4974
    • (2005) J. Biol. Chem. , vol.280 , pp. 4968-4974
    • Choi, M.Y.1    Partridge, A.W.2    Daniels, C.3    Du, K.4    Lukacs, G.L.5    Deber, C.M.6
  • 200
    • 0033605158 scopus 로고    scopus 로고
    • Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge
    • J.F. Cotten, and M.J. Welsh Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge J. Biol. Chem. 274 1999 5429 5435
    • (1999) J. Biol. Chem. , vol.274 , pp. 5429-5435
    • Cotten, J.F.1    Welsh, M.J.2
  • 201
    • 0035937749 scopus 로고    scopus 로고
    • Two mild cystic fibrosis-associated mutations result in severe cystic fibrosis when combined in cis and reveal a residue important for cystic fibrosis transmembrane conductance regulator processing and function
    • J. Clain, J. Fritsch, J. Lehmann-Che, M. Bali, N. Arous, M. Goosens, A. Edelman, and P. Fanen Two mild cystic fibrosis-associated mutations result in severe cystic fibrosis when combined in cis and reveal a residue important for cystic fibrosis transmembrane conductance regulator processing and function J. Biol. Chem. 276 2001 9045 9049
    • (2001) J. Biol. Chem. , vol.276 , pp. 9045-9049
    • Clain, J.1    Fritsch, J.2    Lehmann-Che, J.3    Bali, M.4    Arous, N.5    Goosens, M.6    Edelman, A.7    Fanen, P.8
  • 203
    • 0037067720 scopus 로고    scopus 로고
    • Membrane targeting of ATP-sensitive potassium channel
    • L.R. Conti, C.M. Radeke, and C.A. Vanderberg Membrane targeting of ATP-sensitive potassium channel J. Biol. Chem. 277 2002 25416 25422
    • (2002) J. Biol. Chem. , vol.277 , pp. 25416-25422
    • Conti, L.R.1    Radeke, C.M.2    Vanderberg, C.A.3
  • 204
    • 0031799545 scopus 로고    scopus 로고
    • Functional analyses of novel mutations in the sulfonylurea receptor 1 associated with persistent hyperinsulinemic hypoglycemia of infancy
    • S.L. Shyng, T. Ferrigni, J.B. Shepard, A. Nestorowizc, B. Glaser, M.A. Permutt, and C.G. Nichols Functional analyses of novel mutations in the sulfonylurea receptor 1 associated with persistent hyperinsulinemic hypoglycemia of infancy Diabetes 47 1998 1145 1151
    • (1998) Diabetes , vol.47 , pp. 1145-1151
    • Shyng, S.L.1    Ferrigni, T.2    Shepard, J.B.3    Nestorowizc, A.4    Glaser, B.5    Permutt, M.A.6    Nichols, C.G.7
  • 205
    • 0035929661 scopus 로고    scopus 로고
    • Identification and pharmalogical correction of a membrane trafficking defect associated with a mutation in the sulfonylurea receptor causing familial hyperinsulinism
    • C.J. Partridge, D.J. Beech, and A. Sivaprasadarao Identification and pharmalogical correction of a membrane trafficking defect associated with a mutation in the sulfonylurea receptor causing familial hyperinsulinism J. Biol. Chem. 276 2001 35947 35952
    • (2001) J. Biol. Chem. , vol.276 , pp. 35947-35952
    • Partridge, C.J.1    Beech, D.J.2    Sivaprasadarao, A.3
  • 210
    • 0034948401 scopus 로고    scopus 로고
    • Characterization of a mutant sulfonylurea receptor SUR2B with high affinity for sulfonylureas and openers: Differences in the coupling to Kir6.x subtypes
    • A. Hambrock, C. Loffler-Walz, U. Russ, U. Lange, and U. Quast Characterization of a mutant sulfonylurea receptor SUR2B with high affinity for sulfonylureas and openers: differences in the coupling to Kir6.x subtypes Mol. Pharmacol. 60 2001 190 199
    • (2001) Mol. Pharmacol. , vol.60 , pp. 190-199
    • Hambrock, A.1    Loffler-Walz, C.2    Russ, U.3    Lange, U.4    Quast, U.5
  • 211
    • 0036024235 scopus 로고    scopus 로고
    • Glibenclamide binding to sulfonylurea receptor subtypes: Dependence on adenine nucleotides
    • A. Hambrock, C. Loffler-Walz, and U. Quast Glibenclamide binding to sulfonylurea receptor subtypes: dependence on adenine nucleotides Br. J. Pharmacol. 136 2002 995 1004
    • (2002) Br. J. Pharmacol. , vol.136 , pp. 995-1004
    • Hambrock, A.1    Loffler-Walz, C.2    Quast, U.3
  • 212
    • 17844382965 scopus 로고    scopus 로고
    • The mutation Y1206S increases the affinity of the sulfonylurea receptor SUR2A for glibenclamide and enhances the effects of coexpression with Kir6.2
    • D. Stephan, E. Stauss, U. Lange, H. Felsch, C. Loffer-Walz, A. Hambrock, U. Russ, and U. Quast The mutation Y1206S increases the affinity of the sulfonylurea receptor SUR2A for glibenclamide and enhances the effects of coexpression with Kir6.2 Br. J. Pharmacol. 144 2005 1078 1088
    • (2005) Br. J. Pharmacol. , vol.144 , pp. 1078-1088
    • Stephan, D.1    Stauss, E.2    Lange, U.3    Felsch, H.4    Loffer-Walz, C.5    Hambrock, A.6    Russ, U.7    Quast, U.8
  • 215
    • 1642565240 scopus 로고    scopus 로고
    • Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor
    • F. Yan, C.W. Lin, E. Weisiger, E.A. Cartier, G. Taschenberger, and S.L. Shyng Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor J. Biol. Chem. 279 2004 11096 11105
    • (2004) J. Biol. Chem. , vol.279 , pp. 11096-11105
    • Yan, F.1    Lin, C.W.2    Weisiger, E.3    Cartier, E.A.4    Taschenberger, G.5    Shyng, S.L.6
  • 218
    • 0037036427 scopus 로고    scopus 로고
    • Determinants for substrate specifity of multidrug resistance protein 1
    • D.W. Zhang, S.P.C. Cole, and R.G. Deeley Determinants for substrate specifity of multidrug resistance protein 1 J. Biol. Chem. 277 2002 20934 20941
    • (2002) J. Biol. Chem. , vol.277 , pp. 20934-20941
    • Zhang, D.W.1    Cole, S.P.C.2    Deeley, R.G.3
  • 220
    • 0035851106 scopus 로고    scopus 로고
    • Mutation of Trp 1254 in the multispecific organic anion transporter, multidrug resistance protein 2 (MRP2) (ABCC2) alters substrate specificity and results in loss of methotrexate transport activity
    • L. Ito, C.J. Oleschuk, C. Westlake, M.Z. Vasa, R.G. Deeley, and S.P.C. Cole Mutation of Trp 1254 in the multispecific organic anion transporter, multidrug resistance protein 2 (MRP2) (ABCC2) alters substrate specificity and results in loss of methotrexate transport activity J. Biol. Chem. 276 2001 38108 38114
    • (2001) J. Biol. Chem. , vol.276 , pp. 38108-38114
    • Ito, L.1    Oleschuk, C.J.2    Westlake, C.3    Vasa, M.Z.4    Deeley, R.G.5    Cole, S.P.C.6
  • 221
    • 0042473136 scopus 로고    scopus 로고
    • Characterization of the role of polar amino acid residues within predicted transmembrane helix 17 in determining the substrate specificity of multidrug resistance protein 3
    • D.W. Zhang, H.M. Gu, M. Vasa, M. Muredda, S.P.C Cole, and R.G. Deeley Characterization of the role of polar amino acid residues within predicted transmembrane helix 17 in determining the substrate specificity of multidrug resistance protein 3 Biochemistry 42 2003 9989 10000
    • (2003) Biochemistry , vol.42 , pp. 9989-10000
    • Zhang, D.W.1    Gu, H.M.2    Vasa, M.3    Muredda, M.4    Cole, P.C.5    Deeley, R.G.6
  • 223
    • 0042009288 scopus 로고    scopus 로고
    • Mutation of proline residues in the NH2-terminal region of the multidrug resistance protein MRP1 (ABCC1): Effects on protein expression, membrane localization and transport function
    • K.I. Ito, K.E. Weigl, R.G. Deeley, and S.P.C. Cole Mutation of proline residues in the NH2-terminal region of the multidrug resistance protein MRP1 (ABCC1): effects on protein expression, membrane localization and transport function Biochim. Biophys. Acta 1615 2003 103 114
    • (2003) Biochim. Biophys. Acta , vol.1615 , pp. 103-114
    • Ito, K.I.1    Weigl, K.E.2    Deeley, R.G.3    Cole, S.P.C.4
  • 226
    • 18244399574 scopus 로고    scopus 로고
    • Role of the NH2-terminal membrane spanning domain of MRP1/ABCC1 in protein processing and trafficking
    • C.J. Westlake, S.P.C. Cole, and R.G. Deeley Role of the NH2-terminal membrane spanning domain of MRP1/ABCC1 in protein processing and trafficking Mol. Biol. Cell 16 2005 2483 2492
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2483-2492
    • Westlake, C.J.1    Cole, S.P.C.2    Deeley, R.G.3
  • 228
    • 2442660256 scopus 로고    scopus 로고
    • Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1(ABCC1)
    • A. Haimeur, G. Conseil, R.G. Deeley, and S.P.C. Cole Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1(ABCC1) Mol. Pharmacol. 65 2004 1375 1385
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1375-1385
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.C.4
  • 229
    • 1242267914 scopus 로고    scopus 로고
    • Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity and nucleotide interactions
    • K. Koike, G. Conseil, E.M. Leslie, R.G. Deeley, and S.P.C. Cole Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity and nucleotide interactions J. Biol. Chem. 279 2004 12325 12336
    • (2004) J. Biol. Chem. , vol.279 , pp. 12325-12336
    • Koike, K.1    Conseil, G.2    Leslie, E.M.3    Deeley, R.G.4    Cole, S.P.C.5
  • 230
    • 0035958862 scopus 로고    scopus 로고
    • Transport of the β-O-glucuronide conjugate of the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by the multidrug resistance protein 1 (MRP1/ABCC1): Requirement for glutathione or a non-sulfur-containing analog
    • E.M. Leslie, K. Ito, P. Upadhyaya, S.S. Hecht, R.G. Deeley, and S.P.C. Cole Transport of the β-O-glucuronide conjugate of the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by the multidrug resistance protein 1 (MRP1/ABCC1): requirement for glutathione or a non-sulfur-containing analog J. Biol. Chem. 276 2001 27846 27854
    • (2001) J. Biol. Chem. , vol.276 , pp. 27846-27854
    • Leslie, E.M.1    Ito, K.2    Upadhyaya, P.3    Hecht, S.S.4    Deeley, R.G.5    Cole, S.P.C.6
  • 231
    • 0036016317 scopus 로고    scopus 로고
    • A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistance
    • S. Conrad, H.M. Kauffmann, K.I. Ito, E.M. Leslie, R.G. Deeley, D. Schrenk, and S.P.C. Cole A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistance Pharmacogenetics 12 2002 321 330
    • (2002) Pharmacogenetics , vol.12 , pp. 321-330
    • Conrad, S.1    Kauffmann, H.M.2    Ito, K.I.3    Leslie, E.M.4    Deeley, R.G.5    Schrenk, D.6    Cole, S.P.C.7
  • 233
    • 4644278479 scopus 로고    scopus 로고
    • Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): Glutamate 1204 is important for both the expression and catalytic activity of the transporter
    • D. Situ, A. Haimeur, G. Conseil, K.E. Sparks, D. Zhang, R.G. Deeley, and S.P.C. Cole Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter J. Biol. Chem. 279 2004 38871 38880
    • (2004) J. Biol. Chem. , vol.279 , pp. 38871-38880
    • Situ, D.1    Haimeur, A.2    Conseil, G.3    Sparks, K.E.4    Zhang, D.5    Deeley, R.G.6    Cole, S.P.C.7
  • 234
    • 0242412511 scopus 로고    scopus 로고
    • Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): Identification of an aspartate residue critical for conversion from a high to a low affinity substrate binding state
    • D.W. Zhang, H.M. Gu, D. Situ, A. Haimeur, S.P.C. Cole, and R.G. Deeley Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to a low affinity substrate binding state J. Biol. Chem. 278 2003 46052 46063
    • (2003) J. Biol. Chem. , vol.278 , pp. 46052-46063
    • Zhang, D.W.1    Gu, H.M.2    Situ, D.3    Haimeur, A.4    Cole, S.P.C.5    Deeley, R.G.6
  • 235
    • 0035918322 scopus 로고    scopus 로고
    • Identification of an amino acid residue in multidrug resistance protein (MRP) 1 critical for conferring resistance to anthracyclines
    • D.W. Zhang, S.P.C. Cole, and R.G. Deeley Identification of an amino acid residue in multidrug resistance protein (MRP) 1 critical for conferring resistance to anthracyclines J. Biol. Chem. 276 2001 13231 13239
    • (2001) J. Biol. Chem. , vol.276 , pp. 13231-13239
    • Zhang, D.W.1    Cole, S.P.C.2    Deeley, R.G.3
  • 236
    • 0035103009 scopus 로고    scopus 로고
    • Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects
    • S. Ito, I. Ieiri, M. Tanabe, A. Suzuki, S. Higuchi, and K. Otsubo Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects Pharmacogenetics 11 2001 175 184
    • (2001) Pharmacogenetics , vol.11 , pp. 175-184
    • Ito, S.1    Ieiri, I.2    Tanabe, M.3    Suzuki, A.4    Higuchi, S.5    Otsubo, K.6
  • 237
    • 11144231983 scopus 로고    scopus 로고
    • Identification and characterization of functionally important elements of the multidrug resistance protein 1 COOH-terminal region
    • C.J. Westlake, L. Payen, M. Gao, S.P.C. Cole, and R.G. Deeley Identification and characterization of functionally important elements of the multidrug resistance protein 1 COOH-terminal region J. Biol. Chem. 279 2004 53571 53583
    • (2004) J. Biol. Chem. , vol.279 , pp. 53571-53583
    • Westlake, C.J.1    Payen, L.2    Gao, M.3    Cole, S.P.C.4    Deeley, R.G.5
  • 238
    • 0034671544 scopus 로고    scopus 로고
    • Identification of basic residues involved in drug export function of human multidrug resistance-associated protein 2
    • S. Ryu, T. Kawabe, S. Nada, and A. Yamaguchi Identification of basic residues involved in drug export function of human multidrug resistance-associated protein 2 J. Biol. Chem. 275 2000 39617 39624
    • (2000) J. Biol. Chem. , vol.275 , pp. 39617-39624
    • Ryu, S.1    Kawabe, T.2    Nada, S.3    Yamaguchi, A.4
  • 239
    • 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
    • S.B. Fernandez, Z. Hollo, A. Kern, E. Bakos, P.A. Fischer, P. Borst, and R. Evers 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 2002 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
  • 240
    • 0142024010 scopus 로고    scopus 로고
    • Homozygous mutation Arg768Trp in the ABC-transporter encoding gene MRP2/cMOAT/ABCC2 causes Dubin-Johnson syndrome in a Caucasian patient
    • V. Materna, and H. Lage Homozygous mutation Arg768Trp in the ABC-transporter encoding gene MRP2/cMOAT/ABCC2 causes Dubin-Johnson syndrome in a Caucasian patient J. Hum. Genet. 48 2003 484 486
    • (2003) J. Hum. Genet. , vol.48 , pp. 484-486
    • Materna, V.1    Lage, H.2
  • 243
    • 0027512768 scopus 로고
    • Functional consequences of proline mutations in the predicted transmembrane domain of P-glycoprotein
    • T.W. Loo, and D.M. Clarke Functional consequences of proline mutations in the predicted transmembrane domain of P-glycoprotein J. Biol. Chem. 268 1993 3143 3149
    • (1993) J. Biol. Chem. , vol.268 , pp. 3143-3149
    • Loo, T.W.1    Clarke, D.M.2
  • 244
    • 0033580634 scopus 로고    scopus 로고
    • A single amino acid residue contributes to distinct mechanisms of inhibition of the human multidrug transporter by stereoisomers of the dopamine receptor antagonist flupentixol
    • S. Dey, P. Haftemeyer, I. Pastan, and M.M. Gottesman A single amino acid residue contributes to distinct mechanisms of inhibition of the human multidrug transporter by stereoisomers of the dopamine receptor antagonist flupentixol Biochemistry 38 1999 6630 6639
    • (1999) Biochemistry , vol.38 , pp. 6630-6639
    • Dey, S.1    Haftemeyer, P.2    Pastan, I.3    Gottesman, M.M.4
  • 245
    • 0028245416 scopus 로고
    • Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein
    • T.W. Loo, and 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
  • 246
    • 1842538878 scopus 로고    scopus 로고
    • Improved energy coupling of human P-glycoprotein by the glycine 185 to valine mutation
    • H. Omote, R.A. Figler, M.K. Polar, and M.K. Al-Shawi Improved energy coupling of human P-glycoprotein by the glycine 185 to valine mutation Biochemistry 43 2004 3917 3928
    • (2004) Biochemistry , vol.43 , pp. 3917-3928
    • Omote, H.1    Figler, R.A.2    Polar, M.K.3    Al-Shawi, M.K.4
  • 247
    • 0031156390 scopus 로고    scopus 로고
    • How does P-glycoprotein recognize its substrates?
    • K. Ueda, Y. Taguchi, and M. Morishima How does P-glycoprotein recognize its substrates? Semin. Cancer Biol. 8 1997 151 159
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 151-159
    • Ueda, K.1    Taguchi, Y.2    Morishima, M.3
  • 248
    • 0032601621 scopus 로고    scopus 로고
    • Merck Frosst Award Lecture 1998. Molecular dissection of the human multidrug resistance P-glycoprotein
    • T.W. Loo, and D.M. Clarke Merck Frosst Award Lecture 1998. Molecular dissection of the human multidrug resistance P-glycoprotein Biochem. Cell Biol. 77 1999 11 23
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 11-23
    • Loo, T.W.1    Clarke, D.M.2
  • 249
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • T.W. Loo, and D.M. Clarke Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein J. Biol. Chem. 277 2002 44332 44338
    • (2002) J. Biol. Chem. , vol.277 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 250
    • 0032541975 scopus 로고    scopus 로고
    • Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein
    • P. Hafkemeyer, S. Dey, S.V. Ambudkar, C.A. Hrycyna, I. Pastan, and M.M. Gottesman Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein Biochemistry 37 1998 16400 16409
    • (1998) Biochemistry , vol.37 , pp. 16400-16409
    • Hafkemeyer, P.1    Dey, S.2    Ambudkar, S.V.3    Hrycyna, C.A.4    Pastan, I.5    Gottesman, M.M.6
  • 251
    • 0035805573 scopus 로고    scopus 로고
    • Defining the drug-binding site of the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil
    • T.W. Loo, and D.M. Clarke Defining the drug-binding site of the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil J. Biol. Chem. 276 2001 14972 14979
    • (2001) J. Biol. Chem. , vol.276 , pp. 14972-14979
    • Loo, T.W.1    Clarke, D.M.2
  • 252
    • 21844451868 scopus 로고    scopus 로고
    • The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment
    • A. Rothnie, J. Storm, R. McMahon, A. Taylor, I.D. Kerr, and R. Callaghan The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment FEBS Lett. 579 2005 3984 3990
    • (2005) FEBS Lett. , vol.579 , pp. 3984-3990
    • Rothnie, A.1    Storm, J.2    McMahon, R.3    Taylor, A.4    Kerr, I.D.5    Callaghan, R.6
  • 253
    • 0034765599 scopus 로고    scopus 로고
    • Further characterization of the sixth transmembrane domain of Pgp1 by site-directed mutagenesis
    • J. Song, and P.W. Melera Further characterization of the sixth transmembrane domain of Pgp1 by site-directed mutagenesis Cancer Chemother. Pharmacol. 48 2001 339 346
    • (2001) Cancer Chemother. Pharmacol. , vol.48 , pp. 339-346
    • Song, J.1    Melera, P.W.2
  • 254
    • 0034920965 scopus 로고    scopus 로고
    • 125I] iodoarylazidoprazosin labeling
    • 125I] iodoarylazidoprazosin labeling Mol. Pharmacol. 60 2001 254 261
    • (2001) Mol. Pharmacol. , vol.60 , pp. 254-261
    • Song, J.1    Melera, P.W.2
  • 255
    • 23044503311 scopus 로고    scopus 로고
    • ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein Biochemistry 44 2005 10250 10258
    • (2005) Biochemistry , vol.44 , pp. 10250-10258
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 256
    • 4544254316 scopus 로고    scopus 로고
    • Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains J. Biol. Chem. 279 2004 38395 38401
    • (2004) J. Biol. Chem. , vol.279 , pp. 38395-38401
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 258
    • 0040700700 scopus 로고    scopus 로고
    • Mutations in the sixth transmembrane domain of P-glycoprotein that alter the pattern of cross-resistance also alter sensitivity to cyclosporine a reversal
    • J.F. Ma, G. Grant, and P.W. Melera Mutations in the sixth transmembrane domain of P-glycoprotein that alter the pattern of cross-resistance also alter sensitivity to cyclosporine A reversal Mol. Pharmacol. 51 1997 922 930
    • (1997) Mol. Pharmacol. , vol.51 , pp. 922-930
    • Ma, J.F.1    Grant, G.2    Melera, P.W.3
  • 259
    • 13244265753 scopus 로고    scopus 로고
    • The dileucine motif at the COOH terminus of human multidrug resistance P-glycoprotein is important for folding but not for activity
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke The dileucine motif at the COOH terminus of human multidrug resistance P-glycoprotein is important for folding but not for activity J. Biol. Chem. 280 2005 2522 2528
    • (2005) J. Biol. Chem. , vol.280 , pp. 2522-2528
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 260
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • A.L. Davidson, and J. Chen ATP-binding cassette transporters in bacteria Annu. Rev. Biochem. 73 2004 241 268
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 261
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • K.P. Locher, A.T. Lee, and D.C. Rees The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism Science 296 2002 1091 1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 262
    • 0242405509 scopus 로고    scopus 로고
    • The structures of BtuCD and MscS and their implications for transporter and channel function
    • R.B. Bass, K.P. Locher, E. Borths, Y. Poon, P. Strop, A. Lee, and D.C. Rees The structures of BtuCD and MscS and their implications for transporter and channel function FEBS Lett. 555 2003 111 115
    • (2003) FEBS Lett. , vol.555 , pp. 111-115
    • Bass, R.B.1    Locher, K.P.2    Borths, E.3    Poon, Y.4    Strop, P.5    Lee, A.6    Rees, D.C.7
  • 263
    • 1942532335 scopus 로고    scopus 로고
    • ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF
    • K.P. Locher, and E. Borths ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF FEBS Lett. 564 2004 264 268
    • (2004) FEBS Lett. , vol.564 , pp. 264-268
    • Locher, K.P.1    Borths, E.2
  • 264
    • 28944442871 scopus 로고    scopus 로고
    • In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B(12) uptake
    • E.L. Borths, B. Poolman, R.N. Hvorup, K.P. Locher, and D.C. Rees In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B(12) uptake Biochemistry 44 2005 16301 16309
    • (2005) Biochemistry , vol.44 , pp. 16301-16309
    • Borths, E.L.1    Poolman, B.2    Hvorup, R.N.3    Locher, K.P.4    Rees, D.C.5
  • 265
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • G. Chang, and C.B. Roth Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters Science 293 2001 1793 1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 266
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1). Crystallization and single particle analysis
    • M.F. Rosenberg, Q. Mao, A. Holzenburg, R.C. Ford, R.G. Deeley, and S.P. Cole The structure of the multidrug resistance protein 1 (MRP1/ABCC1). Crystallization and single particle analysis J. Biol. Chem. 276 2001 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
  • 267
    • 0037424343 scopus 로고    scopus 로고
    • Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding
    • M.F. Rosenberg, A.B. Kamis, R. Callaghan, C.F. Higgins, and R.C. Ford Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding J. Biol. Chem. 278 2003 8294 8299
    • (2003) J. Biol. Chem. , vol.278 , pp. 8294-8299
    • Rosenberg, M.F.1    Kamis, A.B.2    Callaghan, R.3    Higgins, C.F.4    Ford, R.C.5
  • 268
    • 27844520938 scopus 로고    scopus 로고
    • Crystallographic and single-particle analyses of native- and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein
    • N.H. Awayn, M.F. Rosenberg, A.B. Kamis, L.A. Aleksandrov, J.R. Riordan, and R.C. Ford Crystallographic and single-particle analyses of native- and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein Biochem. Soc. Trans. 33 2005 996 999
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 996-999
    • Awayn, N.H.1    Rosenberg, M.F.2    Kamis, A.B.3    Aleksandrov, L.A.4    Riordan, J.R.5    Ford, R.C.6
  • 270
    • 13244292479 scopus 로고    scopus 로고
    • Three dimensional structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • M.F. Rosenberg, R. Callaghan, S. Modok, C.F. Higgins, and R.C. Ford Three dimensional structure of P-glycoprotein: the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state J. Biol. Chem. 280 2005 2857 2862
    • (2005) J. Biol. Chem. , vol.280 , pp. 2857-2862
    • Rosenberg, M.F.1    Callaghan, R.2    Modok, S.3    Higgins, C.F.4    Ford, R.C.5
  • 271
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • C.F. Higgins, and K.J. Linton The ATP switch model for ABC transporters Nat. Struct. Mol. Biol. 11 2004 918 926
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.