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Volumn 496, Issue 7444, 2013, Pages 247-251

Author Correction: Structural basis for the drug extrusion mechanism by a MATE multidrug transporter (Nature, (2013), 496, 7444, (247-251), 10.1038/nature12014);Structural basis for the drug extrusion mechanism by a MATE multidrug transporter

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CYCLOPEPTIDE; MACROCYCLIC COMPOUND; MULTIDRUG AND TOXIC COMPOUND EXTRUSION TRANSPORTER PROTEIN; NORFLOXACIN; SULFIDE; UNCLASSIFIED DRUG;

EID: 84876297961     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/s41586-019-1762-6     Document Type: Erratum
Times cited : (205)

References (42)
  • 1
    • 0032949426 scopus 로고    scopus 로고
    • The multidrug efflux protein NorM is a prototype of a new family of transporters
    • Brown, M. H., Paulsen, I. T. & Skurray, R. A. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol. Microbiol. 31, 394-395 (1999).
    • (1999) Mol. Microbiol. , vol.31 , pp. 394-395
    • Brown, M.H.1    Paulsen, I.T.2    Skurray, R.A.3
  • 2
    • 0346991732 scopus 로고    scopus 로고
    • 1-coupled multidrug efflux pump, PmpM, a member of the MATE family of transporters, from Pseudomonas aeruginosa
    • 1-coupled multidrug efflux pump, PmpM, a member of the MATE family of transporters, from Pseudomonas aeruginosa. J. Bacteriol. 186, 262-265 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 262-265
    • He, G.X.1
  • 3
    • 18244388696 scopus 로고    scopus 로고
    • Multidrug resistance in Staphylococcus aureus due to overexpression of a novel multidrug and toxin extrusion (MATE) transport protein
    • Kaatz, G. W., McAleese, F. & Seo, S. M. Multidrug resistance in Staphylococcus aureus due to overexpression of a novel multidrug and toxin extrusion (MATE) transport protein. Antimicrob. Agents Chemother. 49, 1857-1864 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1857-1864
    • Kaatz, G.W.1    McAleese, F.2    Seo, S.M.3
  • 4
    • 18244403495 scopus 로고    scopus 로고
    • A novel MATE family efflux pump contributes to the reduced susceptibility of laboratory-derived Staphylococcus aureus mutants to tigecycline
    • McAleese, F. et al. A novel MATE family efflux pump contributes to the reduced susceptibility of laboratory-derived Staphylococcus aureus mutants to tigecycline. Antimicrob. Agents Chemother. 49, 1865-1871 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1865-1871
    • McAleese, F.1
  • 5
    • 33846854920 scopus 로고    scopus 로고
    • 1/organic cation antiporter MATE1
    • 1/organic cation antiporter MATE1. Am. J. Physiol. 292, F593-F598 (2007).
    • (2007) Am. J. Physiol. , vol.292
    • Tsuda, M.1
  • 6
    • 62749133967 scopus 로고    scopus 로고
    • Genetic variation in the multidrug and toxin extrusion 1 transporter protein influences the glucose-lowering effect ofmetformininpatients with diabetes: A preliminary study
    • Becker, M. L. et al. Genetic variation in the multidrug and toxin extrusion 1 transporter protein influences the glucose-lowering effect ofmetformininpatients with diabetes: a preliminary study. Diabetes 58, 745-749 (2009).
    • (2009) Diabetes , vol.58 , pp. 745-749
    • Becker, M.L.1
  • 7
    • 79955092770 scopus 로고    scopus 로고
    • Interactions of tyrosine kinase inhibitors with organic cation transporters and multidrug and toxic compound extrusion proteins
    • Minematsu, T. & Giacomini, K. M. Interactions of tyrosine kinase inhibitors with organic cation transporters and multidrug and toxic compound extrusion proteins. Mol. Cancer Ther. 10, 531-539 (2011).
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 531-539
    • Minematsu, T.1    Giacomini, K.M.2
  • 8
    • 77949675459 scopus 로고    scopus 로고
    • Potent and specific inhibition of mMate1-mediated efflux of type i organic cations in the liver and kidney by pyrimethamine
    • Ito, S. et al. Potent and specific inhibition of mMate1-mediated efflux of type I organic cations in the liver and kidney by pyrimethamine. J. Pharmacol. Exp. Ther. 333, 341-350 (2010).
    • (2010) J. Pharmacol. Exp. Ther. , vol.333 , pp. 341-350
    • Ito, S.1
  • 9
    • 79956333806 scopus 로고    scopus 로고
    • Effects of a MATE protein inhibitor, pyrimethamine, on the renal elimination of metformin at oral microdose and at therapeutic dose in healthy subjects
    • Kusuhara, H. et al. Effects of a MATE protein inhibitor, pyrimethamine, on the renal elimination of metformin at oral microdose and at therapeutic dose in healthy subjects. Clin. Pharmacol. Ther. 89, 837-844 (2011).
    • (2011) Clin. Pharmacol. Ther. , vol.89 , pp. 837-844
    • Kusuhara, H.1
  • 10
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. & 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.1    Locher, K.P.2
  • 11
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami, S., Nakashima, R., Yamashita, E., Matsumoto, T. & Yamaguchi, A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443, 173-179 (2006).
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 13
    • 0031836031 scopus 로고    scopus 로고
    • NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus andits homologinEscherichia coli
    • Morita, Y. et al. NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus andits homologinEscherichia coli. Antimicrob. Agents Chemother. 42, 1778-1782 (1998).
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1778-1782
    • Morita, Y.1
  • 15
    • 14244266607 scopus 로고    scopus 로고
    • 1/multidrug antiporter in Vibrio parahaemolyticus
    • 1/multidrug antiporter in Vibrio parahaemolyticus. J. Bacteriol. 187, 1552-1558 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 1552-1558
    • Otsuka, M.1
  • 16
    • 77958596325 scopus 로고    scopus 로고
    • Structure of a cation-bound multidrug and toxic compound extrusion transporter
    • He, X. et al. Structure of a cation-bound multidrug and toxic compound extrusion transporter. Nature 467, 991-994 (2010).
    • (2010) Nature , vol.467 , pp. 991-994
    • He, X.1
  • 17
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law, C. J., Maloney, P. C. & Wang, D. N. Ins and outs of major facilitator superfamily antiporters. Annu. Rev. Microbiol. 62, 289-305 (2008).
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 18
    • 80052089906 scopus 로고    scopus 로고
    • Lipidic cubic phase technologies for membrane protein structural studies
    • Cherezov, V. Lipidic cubic phase technologies for membrane protein structural studies. Curr. Opin. Struct. Biol. 21, 559-566 (2011).
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 559-566
    • Cherezov, V.1
  • 19
    • 84859627442 scopus 로고    scopus 로고
    • Ribosomal production and in vitro selection of natural product-like peptidomimetics: The FIT and RaPID systems
    • Hipolito, C. J. & Suga, H. Ribosomal production and in vitro selection of natural product-like peptidomimetics: the FIT and RaPID systems. Curr. Opin. Chem. Biol. 16, 196-203 (2012).
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 196-203
    • Hipolito, C.J.1    Suga, H.2
  • 20
    • 84858657128 scopus 로고    scopus 로고
    • In vitro selection of anti-Akt2 thioether-macrocyclic peptides leading to isoform-selective inhibitors
    • Hayashi, Y., Morimoto, J. & Suga, H. In vitro selection of anti-Akt2 thioether-macrocyclic peptides leading to isoform-selective inhibitors. ACS Chem. Biol. 7, 607-613 (2012).
    • (2012) ACS Chem. Biol. , vol.7 , pp. 607-613
    • Hayashi, Y.1    Morimoto, J.2    Suga, H.3
  • 21
    • 84555190565 scopus 로고    scopus 로고
    • Natural product-like macrocyclic N-methyl-peptide inhibitors against a ubiquitin ligase uncovered from a ribosome-expressed de novo library
    • Yamagishi, Y. et al. Natural product-like macrocyclic N-methyl-peptide inhibitors against a ubiquitin ligase uncovered from a ribosome-expressed de novo library. Chem. Biol. 18, 1562-1570 (2011).
    • (2011) Chem. Biol. , vol.18 , pp. 1562-1570
    • Yamagishi, Y.1
  • 22
    • 84859239807 scopus 로고    scopus 로고
    • Discoveryof macrocyclic peptides armed with a mechanism-based warhead: Isoform-selective inhibition of human deacetylase SIRT2
    • Morimoto, J., Hayashi, Y. & Suga, H. Discoveryof macrocyclic peptides armed with a mechanism-based warhead: isoform-selective inhibition of human deacetylase SIRT2. Angew. Chem. Int. Ed. 51, 3423-3427 (2012).
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 3423-3427
    • Morimoto, J.1    Hayashi, Y.2    Suga, H.3
  • 23
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • Altschul, S. F. et al. Protein database searches using compositionally adjusted substitution matrices. FEBS J. 272, 5101-5109 (2005).
    • (2005) FEBS J. , vol.272 , pp. 5101-5109
    • Altschul, S.F.1
  • 24
    • 0019252702 scopus 로고
    • Structure-activity relationships of antibacterial 6, 7-and 7, 8-disubstituted 1-alkyl-1, 4-dihydro-4-oxoquinoline-3-carboxylic acids
    • Koga, H., Itoh, A., Murayama, S., Suzue, S. & Irikura, T. Structure-activity relationships of antibacterial 6, 7-and 7, 8-disubstituted 1-alkyl-1, 4-dihydro-4-oxoquinoline-3-carboxylic acids. J. Med. Chem. 23, 1358-1363 (1980).
    • (1980) J. Med. Chem. , vol.23 , pp. 1358-1363
    • Koga, H.1    Itoh, A.2    Murayama, S.3    Suzue, S.4    Irikura, T.5
  • 25
    • 84873431135 scopus 로고    scopus 로고
    • 1-coupled, substrate-bound MATE multidrug transporter
    • 1-coupled, substrate-bound MATE multidrug transporter. Proc. Natl Acad. Sci. USA 110, 2099-2104 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 2099-2104
    • Lu, M.1
  • 26
    • 73449131843 scopus 로고    scopus 로고
    • The ID23-2 structural biology microfocus beamline at the ESRF
    • Flot, D. et al. The ID23-2 structural biology microfocus beamline at the ESRF. J. Synchrotron Radiat. 17, 107-118 (2010).
    • (2010) J. Synchrotron Radiat. , vol.17 , pp. 107-118
    • Flot, D.1
  • 27
    • 0024300293 scopus 로고
    • Intracellular pHofhalobacteria can be determined by the fluorescent dye 29, 79-bis (carboxyethyl)-5 (6)-carboxyfluorescein
    • Tsujimoto, K., Semadeni, M., Huflejt, M. & Packer, L. Intracellular pHofhalobacteria can be determined by the fluorescent dye 29, 79-bis (carboxyethyl)-5 (6)-carboxyfluorescein. Biochem. Biophys. Res. Commun. 155, 123-129 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 123-129
    • Tsujimoto, K.1    Semadeni, M.2    Huflejt, M.3    Packer, L.4
  • 28
    • 12244293832 scopus 로고    scopus 로고
    • Contributions of MexAB-OprM and an EmrE homolog to intrinsic resistance of Pseudomonas aeruginosa to aminoglycosides and dyes
    • Li, X. Z., Poole, K. & Nikaido, H. Contributions of MexAB-OprM and an EmrE homolog to intrinsic resistance of Pseudomonas aeruginosa to aminoglycosides and dyes. Antimicrob. Agents Chemother. 47, 27-33 (2003).
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 27-33
    • Li, X.Z.1    Poole, K.2    Nikaido, H.3
  • 30
    • 43749121852 scopus 로고    scopus 로고
    • SnB version 2.3: Triplet sieve phasing for centrosymmetric structures
    • Xu, H., Smith, A. B., Sahinidis, N. V. & Weeks, C. M. SnB version 2. 3: triplet sieve phasing for centrosymmetric structures. J. Appl. Cryst. 41, 644-646 (2008).
    • (2008) J. Appl. Cryst. , vol.41 , pp. 644-646
    • Xu, H.1    Smith, A.B.2    Sahinidis, N.V.3    Weeks, C.M.4
  • 32
    • 48849113878 scopus 로고    scopus 로고
    • Comparative protein structure modeling using MODELLER
    • Eswar, N. et al. Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. 2, 2. 9. 1-2. 9. 31 (2007).
    • (2007) Curr. Protoc. Protein Sci. , vol.2 , pp. 291-2931
    • Eswar, N.1
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 35
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 36
    • 84860287260 scopus 로고    scopus 로고
    • Exploiting structure similarityin refinement: Automated NCS and target-structure restraints in BUSTER
    • Smart, O. S. et al. Exploiting structure similarityin refinement: automated NCS and target-structure restraints in BUSTER. Acta Crystallogr. D 68, 368-380 (2012).
    • (2012) Acta Crystallogr. D , vol.68 , pp. 368-380
    • Smart, O.S.1
  • 37
    • 74549178560 scopus 로고    scopus 로고
    • Mol Probity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. Mol Probity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 38
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 39
    • 49649085631 scopus 로고    scopus 로고
    • Automated structure solution with the PHENIX suite
    • Zwart, P. H. et al. Automated structure solution with the PHENIX suite. Methods Mol. Biol. 426, 419-435 (2008).
    • (2008) Methods Mol. Biol. , vol.426 , pp. 419-435
    • Zwart, P.H.1
  • 40
    • 0029975504 scopus 로고    scopus 로고
    • Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: TRNA-protein mimicry hypothesis
    • Ito, K., Ebihara, K., Uno, M. & Nakamura, Y. Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc. Natl Acad. Sci. USA 93, 5443-5448 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5443-5448
    • Ito, K.1    Ebihara, K.2    Uno, M.3    Nakamura, Y.4


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