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Volumn 23, Issue 6, 2016, Pages 487-493

Mechanistic diversity in ATP-binding cassette (ABC) transporters

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; MULTIDRUG RESISTANCE PROTEIN; POTASSIUM CHANNEL; TRACE ELEMENT; ADENOSINE TRIPHOSPHATE; PROTEIN BINDING;

EID: 84976500356     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3216     Document Type: Review
Times cited : (599)

References (100)
  • 1
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L., Dassa, E., Orelle, C.&Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72, 317-364 (2008).
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 2
    • 84856291637 scopus 로고    scopus 로고
    • ABC solute importers in bacteria
    • Cui, J.&Davidson, A. L. ABC solute importers in bacteria. Essays Biochem. 50, 85-99 (2011).
    • (2011) Essays Biochem. , vol.50 , pp. 85-99
    • Cui, J.1    Davidson, A.L.2
  • 4
    • 84947246951 scopus 로고    scopus 로고
    • The substrate-binding protein in bacterial ABC transporters: Dissecting roles in the evolution of substrate specificity
    • Maqbool, A. et al. The substrate-binding protein in bacterial ABC transporters: dissecting roles in the evolution of substrate specificity. Biochem. Soc. Trans. 43, 1011-1017 (2015).
    • (2015) Biochem. Soc. Trans. , vol.43 , pp. 1011-1017
    • Maqbool, A.1
  • 6
    • 77958007497 scopus 로고    scopus 로고
    • ABC transporters involved in export of cell surface glycoconjugates
    • Cuthbertson, L., Kos, V.&Whitfield, C. ABC transporters involved in export of cell surface glycoconjugates. Microbiol. Mol. Biol. Rev. 74, 341-362 (2010).
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 341-362
    • Cuthbertson, L.1    Kos, V.2    Whitfield, C.3
  • 7
    • 44449176988 scopus 로고    scopus 로고
    • Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Ruiz, N., Gronenberg, L. S., Kahne, D.&Silhavy, T. J. Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 105, 5537-5542 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5537-5542
    • Ruiz, N.1    Gronenberg, L.S.2    Kahne, D.3    Silhavy, T.J.4
  • 9
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • Seeger, M. A.&van Veen, H. W. Molecular basis of multidrug transport by ABC transporters. Biochim. Biophys. Acta. 1794, 725-737 (2009).
    • (2009) Biochim. Biophys. Acta. , vol.1794 , pp. 725-737
    • Seeger, M.A.1    Van Veen, H.W.2
  • 10
    • 84856275069 scopus 로고    scopus 로고
    • ABC transporters involved in drug resistance in human parasites
    • Leprohon, P., Légaré, D.&Ouellette, M. ABC transporters involved in drug resistance in human parasites. Essays Biochem. 50, 121-144 (2011).
    • (2011) Essays Biochem. , vol.50 , pp. 121-144
    • Leprohon, P.1    Légaré, D.2    Ouellette, M.3
  • 11
    • 34248222428 scopus 로고    scopus 로고
    • Plant ATP-binding cassette transporters
    • Rea, P. A. Plant ATP-binding cassette transporters. Annu. Rev. Plant Biol. 58, 347-375 (2007).
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 347-375
    • Rea, P.A.1
  • 12
    • 0036943710 scopus 로고    scopus 로고
    • Multifunctionality of plant ABC transporters: More than just detoxifiers
    • Martinoia, E. et al. Multifunctionality of plant ABC transporters: more than just detoxifiers. Planta 214, 345-355 (2002).
    • (2002) Planta , vol.214 , pp. 345-355
    • Martinoia, E.1
  • 13
    • 78651376221 scopus 로고    scopus 로고
    • Evolution of ABC transporters by gene duplication and their role in human disease
    • Moitra, K.&Dean, M. Evolution of ABC transporters by gene duplication and their role in human disease. Biol. Chem. 392, 29-37 (2011).
    • (2011) Biol. Chem. , vol.392 , pp. 29-37
    • Moitra, K.1    Dean, M.2
  • 14
    • 33846658399 scopus 로고    scopus 로고
    • ABCC8 and ABCC9: ABC transporters that regulate K+ channels
    • Bryan, J. et al. ABCC8 and ABCC9: ABC transporters that regulate K+ channels. Pflugers Arch. 453, 703-718 (2007).
    • (2007) Pflugers Arch. , vol.453 , pp. 703-718
    • Bryan, J.1
  • 15
    • 61449365340 scopus 로고    scopus 로고
    • SUR1: A unique ATP-binding cassette protein that functions as an ion channel regulator
    • Aittoniemi, J. et al. SUR1: A unique ATP-binding cassette protein that functions as an ion channel regulator. Phil. Trans. R. Soc. Lond. B 364, 257-267 (2009).
    • (2009) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 257-267
    • Aittoniemi, J.1
  • 16
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan, J. R. CFTR function and prospects for therapy. Annu. Rev. Biochem. 77, 701-726 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 17
    • 84856236848 scopus 로고    scopus 로고
    • The TAP translocation machinery in adaptive immunity and viral escape mechanisms
    • Abele, R.&Tampé, R. The TAP translocation machinery in adaptive immunity and viral escape mechanisms. Essays Biochem. 50, 249-264 (2011).
    • (2011) Essays Biochem. , vol.50 , pp. 249-264
    • Abele, R.1    Tampé, R.2
  • 18
    • 84938910744 scopus 로고    scopus 로고
    • The transporter associated with antigen processing: A key player in adaptive immunity
    • Eggensperger, S.&Tampé, R. The transporter associated with antigen processing: A key player in adaptive immunity. Biol. Chem. 396, 1059-1072 (2015).
    • (2015) Biol. Chem. , vol.396 , pp. 1059-1072
    • Eggensperger, S.1    Tampé, R.2
  • 19
    • 33749488939 scopus 로고    scopus 로고
    • Human multidrug resistance ABCB and ABCG transporters: Participation in a chemoimmunity defense system
    • Sarkadi, B., Homolya, L., Szakács, G.&Váradi, A. Human multidrug resistance ABCB and ABCG transporters: participation in a chemoimmunity defense system. Physiol. Rev. 86, 1179-1236 (2006).
    • (2006) Physiol. Rev. , vol.86 , pp. 1179-1236
    • Sarkadi, B.1    Homolya, L.2    Szakács, G.3    Váradi, A.4
  • 20
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • Gottesman, M. M., Fojo, T.&Bates, S. E. Multidrug resistance in cancer: role of ATP-dependent transporters. Nat. Rev. Cancer 2, 48-58 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 21
    • 84856271899 scopus 로고    scopus 로고
    • The P-glycoprotein multidrug transporter
    • Sharom, F. J. The P-glycoprotein multidrug transporter. Essays Biochem. 50, 161-178 (2011).
    • (2011) Essays Biochem. , vol.50 , pp. 161-178
    • Sharom, F.J.1
  • 22
    • 79953799375 scopus 로고    scopus 로고
    • Advances in the molecular detection of ABC transporters involved in multidrug resistance in cancer
    • Gillet, J. P.&Gottesman, M. M. Advances in the molecular detection of ABC transporters involved in multidrug resistance in cancer. Curr. Pharm. Biotechnol. 12, 686-692 (2011).
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 686-692
    • Gillet, J.P.1    Gottesman, M.M.2
  • 23
    • 84455171488 scopus 로고    scopus 로고
    • In vitro inhibition of the bile salt export pump correlates with risk of cholestatic drug-induced liver injury in humans
    • Dawson, S., Stahl, S., Paul, N., Barber, J.&Kenna, J. G. In vitro inhibition of the bile salt export pump correlates with risk of cholestatic drug-induced liver injury in humans. Drug Metab. Dispos. 40, 130-138 (2012).
    • (2012) Drug Metab. Dispos. , vol.40 , pp. 130-138
    • Dawson, S.1    Stahl, S.2    Paul, N.3    Barber, J.4    Kenna, J.G.5
  • 24
    • 84935882341 scopus 로고    scopus 로고
    • Molecular mechanisms for biliary phospholipid and drug efflux mediated by ABCB4 and bile salts
    • Morita, S. Y.&Terada, T. Molecular mechanisms for biliary phospholipid and drug efflux mediated by ABCB4 and bile salts. BioMed Res. Int. 2014, 954781 (2014).
    • (2014) BioMed Res. Int. , vol.2014 , pp. 954781
    • Morita, S.Y.1    Terada, T.2
  • 25
    • 82755163760 scopus 로고    scopus 로고
    • Canalicular ABC transporters and liver disease
    • Nicolaou, M. et al. Canalicular ABC transporters and liver disease. J. Pathol. 226, 300-315 (2012).
    • (2012) J. Pathol. , vol.226 , pp. 300-315
    • Nicolaou, M.1
  • 26
    • 84947220788 scopus 로고    scopus 로고
    • Lipid flopping in the liver
    • Linton, K. J. Lipid flopping in the liver. Biochem. Soc. Trans. 43, 1003-1010 (2015).
    • (2015) Biochem. Soc. Trans. , vol.43 , pp. 1003-1010
    • Linton, K.J.1
  • 27
    • 77954374158 scopus 로고    scopus 로고
    • Role of the bile salt export pump, BSEP, in acquired forms of cholestasis
    • Stieger, B. Role of the bile salt export pump, BSEP, in acquired forms of cholestasis. Drug Metab. Rev. 42, 437-445 (2010).
    • (2010) Drug Metab. Rev. , vol.42 , pp. 437-445
    • Stieger, B.1
  • 28
    • 84856282091 scopus 로고    scopus 로고
    • The controversial role of ABC transporters in clinical oncology
    • Tamaki, A., Ierano, C., Szakacs, G., Robey, R. W.&Bates, S. E. The controversial role of ABC transporters in clinical oncology. Essays Biochem. 50, 209-232 (2011).
    • (2011) Essays Biochem. , vol.50 , pp. 209-232
    • Tamaki, A.1    Ierano, C.2    Szakacs, G.3    Robey, R.W.4    Bates, S.E.5
  • 29
    • 84887898959 scopus 로고    scopus 로고
    • A multifactorial approach to hepatobiliary transporter assessment enables improved therapeutic compound development
    • Morgan, R. E. et al. A multifactorial approach to hepatobiliary transporter assessment enables improved therapeutic compound development. Toxicol. Sci. 136, 216-241 (2013).
    • (2013) Toxicol. Sci. , vol.136 , pp. 216-241
    • Morgan, R.E.1
  • 30
    • 84896373130 scopus 로고    scopus 로고
    • Overview of experimental models of the blood-brain barrier in CNS drug discovery
    • Palmer, A. M.&Alavijeh, M. S. Overview of experimental models of the blood-brain barrier in CNS drug discovery. Curr Protoc Pharmacol. 62, 7. 15 (2013).
    • (2013) Curr Protoc Pharmacol. , vol.62 , pp. 715
    • Palmer, A.M.1    Alavijeh, M.S.2
  • 31
    • 84937628052 scopus 로고    scopus 로고
    • Prediction of drug-ABC-transporter interaction: Recent advances and future challenges
    • Montanari, F.&Ecker, G. F. Prediction of drug-ABC-transporter interaction: recent advances and future challenges. Adv. Drug Deliv. Rev. 86, 17-26 (2015).
    • (2015) Adv. Drug Deliv. Rev. , vol.86 , pp. 17-26
    • Montanari, F.1    Ecker, G.F.2
  • 32
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • Gerber, S., Comellas-Bigler, M., Goetz, B. A.&Locher, K. P. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321, 246-250 (2008).
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 33
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. Coli methionine ABC transporter: Structure and allosteric regulation
    • Kadaba, N. S., Kaiser, J. T., Johnson, E., Lee, A.&Rees, D. C. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321, 250-253 (2008).
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 34
    • 84882338908 scopus 로고    scopus 로고
    • Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain
    • Ward, A. B. et al. Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. Proc. Natl. Acad. Sci. USA 110, 13386-13391 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 13386-13391
    • Ward, A.B.1
  • 35
    • 34447311648 scopus 로고    scopus 로고
    • Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism
    • Dawson, R. J. P., Hollenstein, K.&Locher, K. P. Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism. Mol. Microbiol. 65, 250-257 (2007).
    • (2007) Mol. Microbiol. , vol.65 , pp. 250-257
    • Dawson, R.J.P.1    Hollenstein, K.2    Locher, K.P.3
  • 37
    • 75149135645 scopus 로고    scopus 로고
    • Multidrug efflux pumps: The structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues
    • Kerr, I. D., Jones, P. M.&George, A. M. Multidrug efflux pumps: The structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues. FEBS J. 277, 550-563 (2010).
    • (2010) FEBS J. , vol.277 , pp. 550-563
    • Kerr, I.D.1    Jones, P.M.2    George, A.M.3
  • 38
    • 84864564117 scopus 로고    scopus 로고
    • Perspectives on the structure-function of ABC transporters: The Switch and Constant Contact models
    • George, A. M.&Jones, P. M. Perspectives on the structure-function of ABC transporters: The Switch and Constant Contact models. Prog. Biophys. Mol. Biol. 109, 95-107 (2012).
    • (2012) Prog. Biophys. Mol. Biol. , vol.109 , pp. 95-107
    • George, A.M.1    Jones, P.M.2
  • 39
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen, J., Sharma, S., Quiocho, F. A.&Davidson, A. L. Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. USA 98, 1525-1530 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 40
    • 84947029309 scopus 로고    scopus 로고
    • Structure of a bacterial ABC transporter involved in the import of an acidic polysaccharide alginate
    • Maruyama, Y. et al. Structure of a bacterial ABC transporter involved in the import of an acidic polysaccharide alginate. Structure 23, 1643-1654 (2015).
    • (2015) Structure , vol.23 , pp. 1643-1654
    • Maruyama, Y.1
  • 41
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein, K., Frei, D. C.&Locher, K. P. Structure of an ABC transporter in complex with its binding protein. Nature 446, 213-216 (2007).
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 42
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L.&Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521 (2007).
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 43
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • Patzlaff, J. S., van der Heide, T.&Poolman, B. The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. J. Biol. Chem. 278, 29546-29551 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 44
    • 84926432107 scopus 로고    scopus 로고
    • The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter
    • Yang, J. G.&Rees, D. C. The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter. J. Biol. Chem. 290, 9135-9140 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 9135-9140
    • Yang, J.G.1    Rees, D.C.2
  • 45
    • 84880511070 scopus 로고    scopus 로고
    • Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography
    • Chen, S., Oldham, M. L., Davidson, A. L.&Chen, J. Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography. Nature 499, 364-368 (2013).
    • (2013) Nature , vol.499 , pp. 364-368
    • Chen, S.1    Oldham, M.L.2    Davidson, A.L.3    Chen, J.4
  • 46
    • 79953302147 scopus 로고    scopus 로고
    • Recent insights into iron import by bacteria
    • Braun, V.&Hantke, K. Recent insights into iron import by bacteria. Curr. Opin. Chem. Biol. 15, 328-334 (2011).
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 328-334
    • Braun, V.1    Hantke, K.2
  • 47
    • 0343395846 scopus 로고    scopus 로고
    • ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12
    • Köster, W. ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12. Res. Microbiol. 152, 291-301 (2001).
    • (2001) Res. Microbiol. , vol.152 , pp. 291-301
    • Köster, W.1
  • 48
    • 84867670628 scopus 로고    scopus 로고
    • Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F
    • Korkhov, V. M., Mireku, S. A.&Locher, K. P. Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F. Nature 490, 367-372 (2012).
    • (2012) Nature , vol.490 , pp. 367-372
    • Korkhov, V.M.1    Mireku, S.A.2    Locher, K.P.3
  • 49
    • 84923799962 scopus 로고    scopus 로고
    • Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F
    • Korkhov, V. M., Mireku, S. A., Veprintsev, D. B.&Locher, K. P. Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F. Nat. Struct. Mol. Biol. 21, 1097-1099 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 1097-1099
    • Korkhov, V.M.1    Mireku, S.A.2    Veprintsev, D.B.3    Locher, K.P.4
  • 50
    • 58149512047 scopus 로고    scopus 로고
    • Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking
    • Goetz, B. A., Perozo, E.&Locher, K. P. Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking. FEBS Lett. 583, 266-270 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 266-270
    • Goetz, B.A.1    Perozo, E.2    Locher, K.P.3
  • 51
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup, R. N. et al. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317, 1387-1390 (2007).
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1
  • 52
    • 81755171418 scopus 로고    scopus 로고
    • Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle
    • Joseph, B., Jeschke, G., Goetz, B. A., Locher, K. P.&Bordignon, E. Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle. J. Biol. Chem. 286, 41008-41017 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 41008-41017
    • Joseph, B.1    Jeschke, G.2    Goetz, B.A.3    Locher, K.P.4    Bordignon, E.5
  • 53
    • 0037052565 scopus 로고    scopus 로고
    • The E. Coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T.&Rees, D. C. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 296, 1091-1098 (2002).
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 54
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. P.&Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 55
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • Hohl, M., Briand, C., Grütter, M. G.&Seeger, M. A. Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nat. Struct. Mol. Biol. 19, 395-402 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 395-402
    • Hohl, M.1    Briand, C.2    Grütter, M.G.3    Seeger, M.A.4
  • 56
    • 84905040016 scopus 로고    scopus 로고
    • Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter
    • Hohl, M. et al. Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter. Proc. Natl. Acad. Sci. USA 111, 11025-11030 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 11025-11030
    • Hohl, M.1
  • 57
    • 84937844507 scopus 로고    scopus 로고
    • Crystal structures of a polypeptide processing and secretion transporter
    • Lin, D. Y. W., Huang, S.&Chen, J. Crystal structures of a polypeptide processing and secretion transporter. Nature 523, 425-430 (2015).
    • (2015) Nature , vol.523 , pp. 425-430
    • Lin, D.Y.W.1    Huang, S.2    Chen, J.3
  • 58
    • 84879002569 scopus 로고    scopus 로고
    • Structures of ABCB10, a human ATP-binding cassette transporter in apo-and nucleotide-bound states
    • Shintre, C. A. et al. Structures of ABCB10, a human ATP-binding cassette transporter in apo-and nucleotide-bound states. Proc. Natl. Acad. Sci. USA 110, 9710-9715 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 9710-9715
    • Shintre, C.A.1
  • 59
    • 47049101437 scopus 로고    scopus 로고
    • Mutational analysis of ABC proteins
    • Loo, T. W.&Clarke, D. M. Mutational analysis of ABC proteins. Arch. Biochem. Biophys. 476, 51-64 (2008).
    • (2008) Arch. Biochem. Biophys. , vol.476 , pp. 51-64
    • Loo, T.W.1    Clarke, D.M.2
  • 60
    • 84891912095 scopus 로고    scopus 로고
    • Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1)
    • Chufan, E. E. et al. Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1). PLoS One 8, e82463 (2013).
    • (2013) PLoS One , vol.8 , pp. e82463
    • Chufan, E.E.1
  • 61
    • 84937605067 scopus 로고    scopus 로고
    • Multiple drug transport pathways through human P-glycoprotein
    • McCormick, J. W., Vogel, P. D.&Wise, J. G. Multiple drug transport pathways through human P-glycoprotein. Biochemistry 54, 4374-4390 (2015).
    • (2015) Biochemistry , vol.54 , pp. 4374-4390
    • McCormick, J.W.1    Vogel, P.D.2    Wise, J.G.3
  • 62
    • 79952167215 scopus 로고    scopus 로고
    • Conformation of peptides bound to the transporter associated with antigen processing (TAP)
    • Herget, M. et al. Conformation of peptides bound to the transporter associated with antigen processing (TAP). Proc. Natl. Acad. Sci. USA 108, 1349-1354 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1349-1354
    • Herget, M.1
  • 63
    • 84903478669 scopus 로고    scopus 로고
    • Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state
    • Choudhury, H. G. et al. Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state. Proc. Natl. Acad. Sci. USA 111, 9145-9150 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 9145-9150
    • Choudhury, H.G.1
  • 64
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R. J. P.&Locher, K. P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581, 935-938 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.P.1    Locher, K.P.2
  • 65
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra, M. et al. Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 37, 5010-5019 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1
  • 66
    • 84940550346 scopus 로고    scopus 로고
    • Structure and mechanism of an active lipid-linked oligosaccharide flippase
    • Perez, C. et al. Structure and mechanism of an active lipid-linked oligosaccharide flippase. Nature 524, 433-438 (2015).
    • (2015) Nature , vol.524 , pp. 433-438
    • Perez, C.1
  • 67
    • 84922645558 scopus 로고    scopus 로고
    • Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter
    • Kim, J. et al. Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter. Nature 517, 396-400 (2015).
    • (2015) Nature , vol.517 , pp. 396-400
    • Kim, J.1
  • 68
    • 84956641350 scopus 로고    scopus 로고
    • A mechanism of viral immune evasion revealed by cryo-EM analysis of the TAP transporter
    • Oldham, M. L. et al. A mechanism of viral immune evasion revealed by cryo-EM analysis of the TAP transporter. Nature 529, 537-540 (2016).
    • (2016) Nature , vol.529 , pp. 537-540
    • Oldham, M.L.1
  • 69
    • 84900860340 scopus 로고    scopus 로고
    • Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter
    • Mishra, S. et al. Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter. eLife 3, e02740 (2014).
    • (2014) ELife , vol.3 , pp. e02740
    • Mishra, S.1
  • 70
    • 79953183043 scopus 로고    scopus 로고
    • Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus
    • Zutz, A. et al. Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus. J. Biol. Chem. 286, 7104-7115 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 7104-7115
    • Zutz, A.1
  • 71
    • 84862012971 scopus 로고    scopus 로고
    • Asymmetry in the homodimeric ABC transporter MsbA recognized by a DARPin
    • Mittal, A., Böhm, S., Grütter, M. G., Bordignon, E.&Seeger, M. A. Asymmetry in the homodimeric ABC transporter MsbA recognized by a DARPin. J. Biol. Chem. 287, 20395-20406 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 20395-20406
    • Mittal, A.1    Böhm, S.2    Grütter, M.G.3    Bordignon, E.4    Seeger, M.A.5
  • 72
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • Zaitseva, J. et al. A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 25, 3432-3443 (2006).
    • (2006) EMBO J , vol.25 , pp. 3432-3443
    • Zaitseva, J.1
  • 73
    • 61449361477 scopus 로고    scopus 로고
    • ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator
    • Muallem, D.&Vergani, P. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator. Phil. Trans. R. Soc. Lond. B 364, 247-255 (2009).
    • (2009) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 247-255
    • Muallem, D.1    Vergani, P.2
  • 74
    • 84921028041 scopus 로고    scopus 로고
    • Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter
    • Grossmann, N. et al. Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter. Nat. Commun. 5, 5419 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 5419
    • Grossmann, N.1
  • 75
    • 84915827775 scopus 로고    scopus 로고
    • A reciprocating twin-channel model for ABC transporters
    • Jones, P. M.&George, A. M. A reciprocating twin-channel model for ABC transporters. Q. Rev. Biophys. 47, 189-220 (2014).
    • (2014) Q. Rev. Biophys. , vol.47 , pp. 189-220
    • Jones, P.M.1    George, A.M.2
  • 76
    • 70349646681 scopus 로고    scopus 로고
    • Membrane porters of ATP-binding cassette transport systems are polyphyletic
    • Wang, B., Dukarevich, M., Sun, E. I., Yen, M. R.&Saier, M. H. Jr. Membrane porters of ATP-binding cassette transport systems are polyphyletic. J. Membr. Biol. 231, 1-10 (2009).
    • (2009) J. Membr. Biol. , vol.231 , pp. 1-10
    • Wang, B.1    Dukarevich, M.2    Sun, E.I.3    Yen, M.R.4    Saier, M.H.5
  • 77
    • 84877038330 scopus 로고    scopus 로고
    • Evolutionary relationships of ATP-binding cassette (ABC) uptake porters
    • Zheng, W. H. et al. Evolutionary relationships of ATP-binding cassette (ABC) uptake porters. BMC Microbiol. 13, 98 (2013).
    • (2013) BMC Microbiol. , vol.13 , pp. 98
    • Zheng, W.H.1
  • 78
    • 84947205644 scopus 로고    scopus 로고
    • Watching conformational dynamics of ABC transporters with single-molecule tools
    • Husada, F. et al. Watching conformational dynamics of ABC transporters with single-molecule tools. Biochem. Soc. Trans. 43, 1041-1047 (2015).
    • (2015) Biochem. Soc. Trans. , vol.43 , pp. 1041-1047
    • Husada, F.1
  • 79
    • 84899982879 scopus 로고    scopus 로고
    • The central cavity of ABCB1 undergoes alternating access during ATP hydrolysis
    • van Wonderen, J. H. et al. The central cavity of ABCB1 undergoes alternating access during ATP hydrolysis. FEBS J. 281, 2190-2201 (2014).
    • (2014) FEBS J. , vol.281 , pp. 2190-2201
    • Van Wonderen, J.H.1
  • 80
    • 84947223826 scopus 로고    scopus 로고
    • Investigating the dynamic nature of the ABC transporters: ABCB1 and MsbA as examples for the potential synergies of MD theory and EPR applications
    • Stockner, T., Mullen, A.&MacMillan, F. Investigating the dynamic nature of the ABC transporters: ABCB1 and MsbA as examples for the potential synergies of MD theory and EPR applications. Biochem. Soc. Trans. 43, 1023-1032 (2015).
    • (2015) Biochem. Soc. Trans. , vol.43 , pp. 1023-1032
    • Stockner, T.1    Mullen, A.2    MacMillan, F.3
  • 81
    • 84942598594 scopus 로고    scopus 로고
    • Conformational changes of the antibacterial peptide ATP binding cassette transporter McjD revealed by molecular dynamics simulations
    • Gu, R. X. et al. Conformational changes of the antibacterial peptide ATP binding cassette transporter McjD revealed by molecular dynamics simulations. Biochemistry 54, 5989-5998 (2015).
    • (2015) Biochemistry , vol.54 , pp. 5989-5998
    • Gu, R.X.1
  • 82
    • 84888089116 scopus 로고    scopus 로고
    • Mechanistic picture for conformational transition of a membrane transporter at atomic resolution
    • Moradi, M.&Tajkhorshid, E. Mechanistic picture for conformational transition of a membrane transporter at atomic resolution. Proc. Natl. Acad. Sci. USA 110, 18916-18921 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 18916-18921
    • Moradi, M.1    Tajkhorshid, E.2
  • 83
    • 84885019160 scopus 로고    scopus 로고
    • Structure, biosynthesis, and function of bacterial capsular polysaccharides synthesized by ABC transporter-dependent pathways
    • Willis, L. M.&Whitfield, C. Structure, biosynthesis, and function of bacterial capsular polysaccharides synthesized by ABC transporter-dependent pathways. Carbohydr. Res. 378, 35-44 (2013).
    • (2013) Carbohydr. Res. , vol.378 , pp. 35-44
    • Willis, L.M.1    Whitfield, C.2
  • 84
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway
    • Holland, I. B., Schmitt, L.&Young, J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway. Mol. Membr. Biol. 22, 29-39 (2005).
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 85
    • 84897000286 scopus 로고    scopus 로고
    • The resolution revolution
    • Kühlbrandt, W. The resolution revolution. Science 343, 1443-1444 (2014).
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kühlbrandt, W.1
  • 87
    • 84877756304 scopus 로고    scopus 로고
    • Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis
    • Xu, K. et al. Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis. Nature 497, 268-271 (2013).
    • (2013) Nature , vol.497 , pp. 268-271
    • Xu, K.1
  • 88
    • 70349333637 scopus 로고    scopus 로고
    • The mechanism of ABC transporters: General lessons from structural and functional studies of an antigenic peptide transporter
    • Procko, E., O'Mara, M. L., Bennett, W. F. D., Tieleman, D. P.&Gaudet, R. The mechanism of ABC transporters: general lessons from structural and functional studies of an antigenic peptide transporter. FASEB J. 23, 1287-1302 (2009).
    • (2009) FASEB J. , vol.23 , pp. 1287-1302
    • Procko, E.1    O'Mara, M.L.2    Bennett, W.F.D.3    Tieleman, D.P.4    Gaudet, R.5
  • 89
    • 84922342044 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Wilkens, S. Structure and mechanism of ABC transporters. F1000Prime Rep. 7, 14 (2015).
    • (2015) F1000Prime Rep. , vol.7 , pp. 14
    • Wilkens, S.1
  • 91
    • 84888874764 scopus 로고    scopus 로고
    • Structure and mechanism of energy-coupling factor transporters
    • Zhang, P. Structure and mechanism of energy-coupling factor transporters. Trends Microbiol. 21, 652-659 (2013).
    • (2013) Trends Microbiol. , vol.21 , pp. 652-659
    • Zhang, P.1
  • 92
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from
    • Jin, M. S., Oldham, M. L., Zhang, Q. J.&Chen, J. Crystal structure of the multidrug transporter P-glycoprotein from. Caenorhabditis elegans. Nature 490, 566-569 (2012).
    • (2012) Caenorhabditis Elegans. Nature , vol.490 , pp. 566-569
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.J.3    Chen, J.4
  • 93
    • 84896512558 scopus 로고    scopus 로고
    • Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog
    • Kodan, A. et al. Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Proc. Natl. Acad. Sci. USA 111, 4049-4054 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 4049-4054
    • Kodan, A.1
  • 94
    • 84896803955 scopus 로고    scopus 로고
    • Structural basis for heavy metal detoxification by an Atm1-type ABC exporter
    • Lee, J. Y., Yang, J. G., Zhitnitsky, D., Lewinson, O.&Rees, D. C. Structural basis for heavy metal detoxification by an Atm1-type ABC exporter. Science 343, 1133-1136 (2014).
    • (2014) Science , vol.343 , pp. 1133-1136
    • Lee, J.Y.1    Yang, J.G.2    Zhitnitsky, D.3    Lewinson, O.4    Rees, D.C.5
  • 95
    • 84900449189 scopus 로고    scopus 로고
    • Refined structures of mouse P-glycoprotein
    • Li, J., Jaimes, K. F.&Aller, S. G. Refined structures of mouse P-glycoprotein. Protein Sci. 23, 34-46 (2014).
    • (2014) Protein Sci. , vol.23 , pp. 34-46
    • Li, J.1    Jaimes, K.F.2    Aller, S.G.3
  • 96
    • 84896800834 scopus 로고    scopus 로고
    • Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1
    • Srinivasan, V., Pierik, A. J.&Lill, R. Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1. Science 343, 1137-1140 (2014).
    • (2014) Science , vol.343 , pp. 1137-1140
    • Srinivasan, V.1    Pierik, A.J.2    Lill, R.3
  • 97
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B.&Chang, G. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc. Natl. Acad. Sci. USA 104, 19005-19010 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 98
    • 61449341855 scopus 로고    scopus 로고
    • Structure and mechanism of ATP-binding cassette transporters
    • Locher, K. P. Structure and mechanism of ATP-binding cassette transporters. Phil. Trans. R. Soc. Lond. B 364, 239-245 (2009).
    • (2009) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 99
    • 38449119773 scopus 로고    scopus 로고
    • Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis
    • Borbat, P. P. et al. Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis. PLoS Biol. 5, e271 (2007).
    • (2007) PLoS Biol. , vol.5 , pp. e271
    • Borbat, P.P.1
  • 100
    • 77951877993 scopus 로고    scopus 로고
    • Human P-glycoprotein is active when the two halves are clamped together in the closed conformation
    • Loo, T. W., Bartlett, M. C.&Clarke, D. M. Human P-glycoprotein is active when the two halves are clamped together in the closed conformation. Biochem. Biophys. Res. Commun. 395, 436-440 (2010).
    • (2010) Biochem. Biophys. Res. Commun. , vol.395 , pp. 436-440
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3


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