-
1
-
-
64649096369
-
Mechanisms of RND multidrug efflux pumps
-
Nikaido H, Takatsuka Y (2009) Mechanisms of RND multidrug efflux pumps. Biochim Biophys Acta 1794:769-781.
-
(2009)
Biochim Biophys Acta
, vol.1794
, pp. 769-781
-
-
Nikaido, H.1
Takatsuka, Y.2
-
2
-
-
0036889033
-
Substrate specificity of the RND-type multidrug efflux pumps AcrB and AcrD of Escherichia coli is determined predominately by two large periplasmic loops
-
DOI 10.1128/JB.184.23.6490-6499.2002
-
Elkins CA, Nikaido H (2002) Substrate specificity of the RND-type multidrug efflux pumps AcrB and AcrD of Escherichia coli is determined predominantly by two large periplasmic loops. J Bacteriol 184:6490-6498. (Pubitemid 35332552)
-
(2002)
Journal of Bacteriology
, vol.184
, Issue.23
, pp. 6490-6498
-
-
Elkins, C.A.1
Nikaido, H.2
-
3
-
-
0028926676
-
Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
-
Ma D, et al. (1995) Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol Microbiol 16:45-55.
-
(1995)
Mol Microbiol
, vol.16
, pp. 45-55
-
-
Ma, D.1
-
4
-
-
0029796966
-
Evidence that TolC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli
-
Fralick JA (1996) Evidence that TolC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli. J Bacteriol 178:5803-5805.
-
(1996)
J Bacteriol
, vol.178
, pp. 5803-5805
-
-
Fralick, J.A.1
-
5
-
-
66349137043
-
The assembled structure of a complete tripartite bacterial multidrug efflux pump
-
Symmons MF, Bokma E, Koronakis E, Hughes C, Koronakis V (2009) The assembled structure of a complete tripartite bacterial multidrug efflux pump. Proc Natl Acad Sci USA 106:7173-7178.
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 7173-7178
-
-
Symmons, M.F.1
Bokma, E.2
Koronakis, E.3
Hughes, C.4
Koronakis, V.5
-
6
-
-
0037057652
-
Crystal structure of bacterial multidrug efflux transporter AcrB
-
Murakami S, Nakashima R, Yamashita E, Yamaguchi A (2002) Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419:587-593.
-
(2002)
Nature
, vol.419
, pp. 587-593
-
-
Murakami, S.1
Nakashima, R.2
Yamashita, E.3
Yamaguchi, A.4
-
7
-
-
33749632749
-
Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway
-
Su CC, et al. (2006) Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway. J Bacteriol 188:7290-7296.
-
(2006)
J Bacteriol
, vol.188
, pp. 7290-7296
-
-
Su, C.C.1
-
8
-
-
80053598150
-
Vestibules are part of the substrate path in the multidrug efflux transporter AcrB of Escherichia coli
-
Husain F, Bikhchandani M, Nikaido H (2011) Vestibules are part of the substrate path in the multidrug efflux transporter AcrB of Escherichia coli. J Bacteriol 193:5847-5849.
-
(2011)
J Bacteriol
, vol.193
, pp. 5847-5849
-
-
Husain, F.1
Bikhchandani, M.2
Nikaido, H.3
-
9
-
-
67649583295
-
Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: Evidence from site-directed mutagenesis and carbodiimide labeling
-
Seeger MA, von Ballmoos C, Verrey F, Pos KM (2009) Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: Evidence from site-directed mutagenesis and carbodiimide labeling. Biochemistry 48:5801-5812.
-
(2009)
Biochemistry
, vol.48
, pp. 5801-5812
-
-
Seeger, M.A.1
Von Ballmoos, C.2
Verrey, F.3
Pos, K.M.4
-
10
-
-
33748670458
-
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
-
DOI 10.1038/nature05076, PII NATURE05076
-
Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A (2006) Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443:173-179. (Pubitemid 44387601)
-
(2006)
Nature
, vol.443
, Issue.7108
, pp. 173-179
-
-
Murakami, S.1
Nakashima, R.2
Yamashita, E.3
Matsumoto, T.4
Yamaguchi, A.5
-
11
-
-
33748310520
-
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
-
DOI 10.1126/science.1131542
-
Seeger MA, et al. (2006) Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313:1295-1298. (Pubitemid 44330954)
-
(2006)
Science
, vol.313
, Issue.5791
, pp. 1295-1298
-
-
Seeger, M.A.1
Schiefner, A.2
Eicher, T.3
Verrey, F.4
Diederichs, K.5
Pos, K.M.6
-
12
-
-
33846363597
-
Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors
-
Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grütter MG (2007) Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol 5:e7.
-
(2007)
PLoS Biol
, vol.5
-
-
Sennhauser, G.1
Amstutz, P.2
Briand, C.3
Storchenegger, O.4
Grütter, M.G.5
-
13
-
-
79959981732
-
Analysis of AcrB and AcrB/DARPin ligand complexes by LILBID MS
-
Brandstätter L, et al. (2011) Analysis of AcrB and AcrB/DARPin ligand complexes by LILBID MS. Biochim Biophys Acta 1808:2189-2196.
-
(2011)
Biochim Biophys Acta
, vol.1808
, pp. 2189-2196
-
-
Brandstätter, L.1
-
14
-
-
0031008228
-
The ATP synthase-a splendid molecular machine
-
Boyer PD (1997) The ATP synthase-a splendid molecular machine. Annu Rev Biochem 66:717-749.
-
(1997)
Annu Rev Biochem
, vol.66
, pp. 717-749
-
-
Boyer, P.D.1
-
15
-
-
64649100965
-
Drug transport mechanism of the AcrB efflux pump
-
Pos KM (2009) Drug transport mechanism of the AcrB efflux pump. Biochim Biophys Acta 1794:782-793.
-
(2009)
Biochim Biophys Acta
, vol.1794
, pp. 782-793
-
-
Pos, K.M.1
-
16
-
-
52449109122
-
The AcrB efflux pump: Conformational cycling and peristalsis lead to multidrug resistance
-
Seeger MA, et al. (2008) The AcrB efflux pump: Conformational cycling and peristalsis lead to multidrug resistance. Curr Drug Targets 9:729-749.
-
(2008)
Curr Drug Targets
, vol.9
, pp. 729-749
-
-
Seeger, M.A.1
-
17
-
-
77951221725
-
Kinetic parameters of efflux of penicillins by the multidrug efflux transporter AcrAB-TolC of Escherichia coli
-
Lim SP, Nikaido H (2010) Kinetic parameters of efflux of penicillins by the multidrug efflux transporter AcrAB-TolC of Escherichia coli. Antimicrob Agents Chemother 54: 1800-1806.
-
(2010)
Antimicrob Agents Chemother
, vol.54
, pp. 1800-1806
-
-
Lim, S.P.1
Nikaido, H.2
-
18
-
-
65249172043
-
Kinetic behavior of the major multidrug efflux pump AcrB of Escherichia coli
-
Nagano K, Nikaido H (2009) Kinetic behavior of the major multidrug efflux pump AcrB of Escherichia coli. Proc Natl Acad Sci USA 106:5854-5858.
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 5854-5858
-
-
Nagano, K.1
Nikaido, H.2
-
19
-
-
63049131979
-
Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism
-
Takatsuka Y, Nikaido H (2009) Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism. J Bacteriol 191: 1729-1737.
-
(2009)
J Bacteriol
, vol.191
, pp. 1729-1737
-
-
Takatsuka, Y.1
Nikaido, H.2
-
20
-
-
36749045119
-
Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli
-
DOI 10.1128/JB.01127-07
-
Takatsuka Y, Nikaido H (2007) Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli. J Bacteriol 189:8677-8684. (Pubitemid 350210038)
-
(2007)
Journal of Bacteriology
, vol.189
, Issue.23
, pp. 8677-8684
-
-
Takatsuka, Y.1
Nikaido, H.2
-
21
-
-
38849185972
-
Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB
-
DOI 10.1038/nsmb.1379, PII NSMB1379
-
Seeger MA, et al. (2008) Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB. Nat Struct Mol Biol 15:199-205. (Pubitemid 351207515)
-
(2008)
Nature Structural and Molecular Biology
, vol.15
, Issue.2
, pp. 199-205
-
-
Seeger, M.A.1
Von Ballmoos, C.2
Eicher, T.3
Brandstatter, L.4
Verrey, F.5
Diederichs, K.6
Pos, K.M.7
-
22
-
-
77957141422
-
Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport
-
Long F, et al. (2010) Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature 467:484-488.
-
(2010)
Nature
, vol.467
, pp. 484-488
-
-
Long, F.1
-
23
-
-
34248572735
-
Crystal structure of the multidrug efflux transporter AcrB at 3.1 A resolution reveals the N-terminal region with conserved amino acids
-
DOI 10.1016/j.jsb.2006.12.004, PII S1047847706003881
-
Das D, et al. (2007) Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids. J Struct Biol 158: 494-502. (Pubitemid 46764563)
-
(2007)
Journal of Structural Biology
, vol.158
, Issue.3
, pp. 494-502
-
-
Das, D.1
Xu, Q.S.2
Lee, J.Y.3
Ankoudinova, I.4
Huang, C.5
Lou, Y.6
DeGiovanni, A.7
Kim, R.8
Kim, S.-H.9
-
24
-
-
57049135864
-
The structure of the efflux pump AcrB in complex with bile acid
-
Drew D, et al. (2008) The structure of the efflux pump AcrB in complex with bile acid. Mol Membr Biol 25:677-682.
-
(2008)
Mol Membr Biol
, vol.25
, pp. 677-682
-
-
Drew, D.1
-
25
-
-
36749071555
-
Crystal Structure of AcrB in Complex with a Single Transmembrane Subunit Reveals Another Twist
-
DOI 10.1016/j.str.2007.09.023, PII S0969212607004133
-
Törnroth-Horsefield S, et al. (2007) Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist. Structure 15:1663-1673. (Pubitemid 350213410)
-
(2007)
Structure
, vol.15
, Issue.12
, pp. 1663-1673
-
-
Tornroth-Horsefield, S.1
Gourdon, P.2
Horsefield, R.3
Brive, L.4
Yamamoto, N.5
Mori, H.6
Snijder, A.7
Neutze, R.8
-
26
-
-
0038670226
-
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
-
DOI 10.1126/science.1083137
-
Yu EW, McDermott G, Zgurskaya HI, Nikaido H, Koshland DE, Jr. (2003) Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300:976-980. (Pubitemid 36548884)
-
(2003)
Science
, vol.300
, Issue.5621
, pp. 976-980
-
-
Yu, E.W.1
McDermott, G.2
Zgurskaya, H.I.3
Nikaido, H.4
Koshland Jr., D.E.5
-
27
-
-
25144504245
-
A periplasmic drug-binding site of the AcrB multidrug efflux pump: A crystallographic and site-directed mutagenesis study
-
DOI 10.1128/JB.187.19.6804-6815.2005
-
Yu EW, Aires JR, McDermott G, Nikaido H (2005) A periplasmic drug-binding site of the AcrB multidrug efflux pump: A crystallographic and site-directed mutagenesis study. J Bacteriol 187:6804-6815. (Pubitemid 41356254)
-
(2005)
Journal of Bacteriology
, vol.187
, Issue.19
, pp. 6804-6815
-
-
Yu, E.W.1
Aires, J.R.2
McDermott, G.3
Nikaido, H.4
-
28
-
-
78649344142
-
Substrate path in the AcrB multidrug efflux pump of Escherichia coli
-
Husain F, Nikaido H (2010) Substrate path in the AcrB multidrug efflux pump of Escherichia coli. Mol Microbiol 78:320-330.
-
(2010)
Mol Microbiol
, vol.78
, pp. 320-330
-
-
Husain, F.1
Nikaido, H.2
-
29
-
-
59749093160
-
Site-directed mutagenesis reveals amino acid residues in the Escherichia coli RND efflux pump AcrB that confer macrolide resistance
-
Wehmeier C, Schuster S, Fähnrich E, Kern WV, Bohnert JA (2009) Site-directed mutagenesis reveals amino acid residues in the Escherichia coli RND efflux pump AcrB that confer macrolide resistance. Antimicrob Agents Chemother 53:329-330.
-
(2009)
Antimicrob Agents Chemother
, vol.53
, pp. 329-330
-
-
Wehmeier, C.1
Schuster, S.2
Fähnrich, E.3
Kern, W.V.4
Bohnert, J.A.5
-
30
-
-
57349135305
-
Site-directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB
-
Bohnert JA, et al. (2008) Site-directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB. J Bacteriol 190:8225-8229.
-
(2008)
J Bacteriol
, vol.190
, pp. 8225-8229
-
-
Bohnert, J.A.1
-
31
-
-
78650046142
-
Drug export and allosteric coupling in a multidrug transporter revealed by molecular simulations
-
Yao XQ, Kenzaki H, Murakami S, Takada S (2010) Drug export and allosteric coupling in a multidrug transporter revealed by molecular simulations. Nat Commun 1:117.
-
(2010)
Nat Commun
, vol.1
, pp. 117
-
-
Yao, X.Q.1
Kenzaki, H.2
Murakami, S.3
Takada, S.4
-
32
-
-
84355166442
-
Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
-
Nakashima R, Sakurai K, Yamasaki S, Nishino K, Yamaguchi A (2011) Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket. Nature 480:565-569.
-
(2011)
Nature
, vol.480
, pp. 565-569
-
-
Nakashima, R.1
Sakurai, K.2
Yamasaki, S.3
Nishino, K.4
Yamaguchi, A.5
-
33
-
-
0021249685
-
Self-association of doxorubicin and related compounds in aqueous solution
-
Menozzi M, Valentini L, Vannini E, Arcamone F (1984) Self-association of doxorubicin and related compounds in aqueous solution. J Pharm Sci 73:766-770. (Pubitemid 14122790)
-
(1984)
Journal of Pharmaceutical Sciences
, vol.73
, Issue.6
, pp. 766-770
-
-
Menozzi, M.1
Valentini, L.2
Vannini, E.3
Arcamone, F.4
-
34
-
-
0030593468
-
Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
-
DOI 10.1006/jmbi.1996.0399
-
Miroux B, Walker JE (1996) Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J Mol Biol 260:289-298. (Pubitemid 26254109)
-
(1996)
Journal of Molecular Biology
, vol.260
, Issue.3
, pp. 289-298
-
-
Miroux, B.1
Walker, J.E.2
-
35
-
-
0036794301
-
Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein
-
Pos KM, Diederichs K (2002) Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein. Acta Crystallogr Biol Crystallogr D58(Pt 10 Pt 2):1865-1867.
-
(2002)
Acta Crystallogr Biol Crystallogr
, vol.D58
, Issue.PART 10 PART 2
, pp. 1865-1867
-
-
Pos, K.M.1
Diederichs, K.2
-
37
-
-
0345832205
-
Role of a Conserved Membrane-Embedded Acidic Residue in the Multidrug Transporter MdfA
-
DOI 10.1021/bi035485t
-
Adler J, Lewinson O, Bibi E (2004) Role of a conserved membrane-embedded acidic residue in the multidrug transporter MdfA. Biochemistry 43:518-525. (Pubitemid 38082575)
-
(2004)
Biochemistry
, vol.43
, Issue.2
, pp. 518-525
-
-
Adler, J.1
Lewinson, O.2
Bibi, E.3
-
38
-
-
76449106188
-
Integration, scaling, space-group assignment and post-refinement
-
Kabsch W (2010) Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr D Biol Crystallogr 66:133-144.
-
(2010)
Acta Crystallogr D Biol Crystallogr
, vol.66
, pp. 133-144
-
-
Kabsch, W.1
-
39
-
-
0000560808
-
MOLREP: An automated program for molecular replacement
-
Vagin AA, Teplyakov A (1997) MOLREP: An automated program for molecular replacement. J Appl Cryst 30:1022-1025.
-
(1997)
J Appl Cryst
, vol.30
, pp. 1022-1025
-
-
Vagin, A.A.1
Teplyakov, A.2
-
41
-
-
76449098262
-
PHENIX: A comprehensive Python-based system for macromolecular structure solution
-
Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66:213-221.
-
(2010)
Acta Crystallogr D Biol Crystallogr
, vol.66
, pp. 213-221
-
-
Adams, P.D.1
-
42
-
-
13244281317
-
Coot: Model-building tools for molecular graphics
-
Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr Bio Crystallogr 60(Pt 12 Pt 1):2126-2132.
-
(2004)
Acta Crystallogr Bio Crystallogr
, vol.60
, Issue.PART 12 PART 1
, pp. 2126-2132
-
-
Emsley, P.1
Cowtan, K.2
-
43
-
-
13444307044
-
Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
-
Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60 (Pt 12 Pt 1):2256-2268.
-
(2004)
Acta Crystallogr D Biol Crystallogr
, vol.60
, Issue.PART 12 PART 1
, pp. 2256-2268
-
-
Krissinel, E.1
Henrick, K.2
|