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Volumn 93, Issue 6, 2013, Pages 569-588

Why are membrane targets discovered by phenotypic screens and genome sequencing in Mycobacterium tuberculosis?

Author keywords

Antitubercular drugs; Genetic analysis; High throughput screening; Hydrophobic compounds; Membrane targets

Indexed keywords

7 BROMO 2 METHYL 5 NITRO 3 PHENYLQUINOXALINE; ATPE PROTEIN; AU 1235; BEDAQUILINE; BENZIMIDAZOLE; CYCLOSERINE; DAPTOMYCIN; DPRE PROTEIN; ETHAMBUTOL; GLPK PROTEIN; GRAMICIDIN S; GROWTH INHIBITOR; IMIDAZOLE; ISONIAZID; ISONIAZID PLUS RIFAMPICIN; KANAMYCIN; LINEZOLID; LIPID; MEMBRANE PROTEIN; MMPL3 PROTEIN; MOXIFLOXACIN; N (2 ADAMANTYL) N' GERANYLETHYLENEDIAMINE; PKS13 PROTEIN; PYRAZINAMIDE; PYRIMIDINE; QCRB PROTEIN; STREPTOMYCIN; TELAVANCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VI 18469;

EID: 84887406804     PISSN: 14729792     EISSN: 1873281X     Source Type: Journal    
DOI: 10.1016/j.tube.2013.09.003     Document Type: Review
Times cited : (88)

References (193)
  • 3
    • 34547134692 scopus 로고    scopus 로고
    • The evolution of extensively drug resistant tuberculosis (XDR-TB): History, status and issues for global control
    • R.C. Goldman, K.V. Plumley, and B.E. Laughon The evolution of extensively drug resistant tuberculosis (XDR-TB): history, status and issues for global control Infect Disord Drug Targets 7 2007 73 91
    • (2007) Infect Disord Drug Targets , vol.7 , pp. 73-91
    • Goldman, R.C.1    Plumley, K.V.2    Laughon, B.E.3
  • 4
    • 84868704828 scopus 로고    scopus 로고
    • Antimycobacterial drugs currently in Phase II clinical trials and preclinical phase for tuberculosis treatment
    • 10.1517/13543784.2012.724397
    • J. Engohang-Ndong Antimycobacterial drugs currently in Phase II clinical trials and preclinical phase for tuberculosis treatment Expert Opin Investig Drugs 21 2012 1789 1800 10.1517/13543784.2012.724397
    • (2012) Expert Opin Investig Drugs , vol.21 , pp. 1789-1800
    • Engohang-Ndong, J.1
  • 5
    • 79960897912 scopus 로고    scopus 로고
    • HTS promiscuity analyses for accelerating decision making
    • 10.1177/1087057111407763
    • A. Bocker, P.R. Bonneau, and P.J. Edwards HTS promiscuity analyses for accelerating decision making J Biomol Screen 16 2011 765 774 10.1177/1087057111407763
    • (2011) J Biomol Screen , vol.16 , pp. 765-774
    • Bocker, A.1    Bonneau, P.R.2    Edwards, P.J.3
  • 6
    • 34547697192 scopus 로고    scopus 로고
    • Understanding false positives in reporter gene assays: In silico chemogenomics approaches to prioritize cell-based HTS data
    • 10.1021/ci6005504
    • T.J. Crisman, C.N. Parker, J.L. Jenkins, J. Scheiber, M. Thoma, and Z.B. Kang Understanding false positives in reporter gene assays: in silico chemogenomics approaches to prioritize cell-based HTS data J Chem Inf Model 47 2007 1319 1327 10.1021/ci6005504
    • (2007) J Chem Inf Model , vol.47 , pp. 1319-1327
    • Crisman, T.J.1    Parker, C.N.2    Jenkins, J.L.3    Scheiber, J.4    Thoma, M.5    Kang, Z.B.6
  • 7
    • 23844500772 scopus 로고    scopus 로고
    • High-throughput assays for promiscuous inhibitors
    • 10.1038/nchembio718
    • B.Y. Feng, A. Shelat, T.N. Doman, R.K. Guy, and B.K. Shoichet High-throughput assays for promiscuous inhibitors Nat Chem Biol 1 2005 146 148 10.1038/nchembio718
    • (2005) Nat Chem Biol , vol.1 , pp. 146-148
    • Feng, B.Y.1    Shelat, A.2    Doman, T.N.3    Guy, R.K.4    Shoichet, B.K.5
  • 8
    • 74849118854 scopus 로고    scopus 로고
    • Quantitative analyses of aggregation, autofluorescence, and reactivity artifacts in a screen for inhibitors of a thiol protease
    • 10.1021/jm901070c
    • A. Jadhav, R.S. Ferreira, C. Klumpp, B.T. Mott, C.P. Austin, and J. Inglese Quantitative analyses of aggregation, autofluorescence, and reactivity artifacts in a screen for inhibitors of a thiol protease J Med Chem 53 2010 37 51 10.1021/jm901070c
    • (2010) J Med Chem , vol.53 , pp. 37-51
    • Jadhav, A.1    Ferreira, R.S.2    Klumpp, C.3    Mott, B.T.4    Austin, C.P.5    Inglese, J.6
  • 9
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • S.L. McGovern, E. Caselli, N. Grigorieff, and B.K. Shoichet A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening J Med Chem 45 2002 1712 1722
    • (2002) J Med Chem , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 10
    • 33947194049 scopus 로고    scopus 로고
    • Enhancement of chemical rules for predicting compound reactivity towards protein thiol groups
    • 10.1007/s10822-007-9109-z
    • J.T. Metz, J.R. Huth, and P.J. Hajduk Enhancement of chemical rules for predicting compound reactivity towards protein thiol groups J Comput-Aided Mol Des 21 2007 139 144 10.1007/s10822-007-9109-z
    • (2007) J Comput-Aided Mol des , vol.21 , pp. 139-144
    • Metz, J.T.1    Huth, J.R.2    Hajduk, P.J.3
  • 12
    • 33744932217 scopus 로고    scopus 로고
    • Early identification of false positives in high-throughput screening for activators of p53-DNA interaction
    • 10.1177/1087057106286652
    • J. Wolcke, N. Hunt, J. Jungmann, and D. Ullmann Early identification of false positives in high-throughput screening for activators of p53-DNA interaction J Biomol Screen 11 2006 341 350 10.1177/1087057106286652
    • (2006) J Biomol Screen , vol.11 , pp. 341-350
    • Wolcke, J.1    Hunt, N.2    Jungmann, J.3    Ullmann, D.4
  • 13
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • C.A. Lipinski, F. Lombardo, B.W. Dominy, and P.J. Feeney Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv Drug Deliv Rev 46 2001 3 26
    • (2001) Adv Drug Deliv Rev , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 14
  • 15
    • 70350765485 scopus 로고    scopus 로고
    • High-throughput screening for inhibitors of Mycobacterium tuberculosis H37Rv
    • 10.1016/j.tube.2009.05.008
    • S. Ananthan, E.R. Faaleolea, R.C. Goldman, J.V. Hobrath, C.D. Kwong, and B.E. Laughon High-throughput screening for inhibitors of Mycobacterium tuberculosis H37Rv Tuberculosis 89 2009 334 353 10.1016/j.tube.2009.05.008
    • (2009) Tuberculosis , vol.89 , pp. 334-353
    • Ananthan, S.1    Faaleolea, E.R.2    Goldman, R.C.3    Hobrath, J.V.4    Kwong, C.D.5    Laughon, B.E.6
  • 16
    • 78149304433 scopus 로고    scopus 로고
    • High content phenotypic cell-based visual screen identifies Mycobacterium tuberculosis acyltrehalose-containing glycolipids involved in phagosome remodeling
    • 10.1371/journal.ppat.1001100
    • P. Brodin, Y. Poquet, F. Levillain, I. Peguillet, G. Larrouy-Maumus, and M. Gilleron High content phenotypic cell-based visual screen identifies Mycobacterium tuberculosis acyltrehalose-containing glycolipids involved in phagosome remodeling PLoS Pathogens 6 2010 e1001100 10.1371/journal.ppat.1001100
    • (2010) PLoS Pathogens , vol.6 , pp. 1001100
    • Brodin, P.1    Poquet, Y.2    Levillain, F.3    Peguillet, I.4    Larrouy-Maumus, G.5    Gilleron, M.6
  • 17
    • 73649143180 scopus 로고    scopus 로고
    • High content screening identifies decaprenyl-phosphoribose 2' epimerase as a target for intracellular antimycobacterial inhibitors
    • 10.1371/journal.ppat.1000645
    • T. Christophe, M. Jackson, H.K. Jeon, D. Fenistein, M. Contreras-Dominguez, and J. Kim High content screening identifies decaprenyl-phosphoribose 2' epimerase as a target for intracellular antimycobacterial inhibitors PLoS Pathogens 5 2009 e1000645 10.1371/journal. ppat.1000645
    • (2009) PLoS Pathogens , vol.5 , pp. 1000645
    • Christophe, T.1    Jackson, M.2    Jeon, H.K.3    Fenistein, D.4    Contreras-Dominguez, M.5    Kim, J.6
  • 18
    • 84864261321 scopus 로고    scopus 로고
    • Discovery of novel N-phenylphenoxyacetamide derivatives as EthR inhibitors and ethionamide boosters by combining high-throughput screening and synthesis
    • 10.1021/jm300377g
    • M. Flipo, N. Willand, N. Lecat-Guillet, C. Hounsou, M. Desroses, and F. Leroux Discovery of novel N-phenylphenoxyacetamide derivatives as EthR inhibitors and ethionamide boosters by combining high-throughput screening and synthesis J Med Chem 55 2012 6391 6402 10.1021/jm300377g
    • (2012) J Med Chem , vol.55 , pp. 6391-6402
    • Flipo, M.1    Willand, N.2    Lecat-Guillet, N.3    Hounsou, C.4    Desroses, M.5    Leroux, F.6
  • 19
    • 84863088810 scopus 로고    scopus 로고
    • High-throughput screening and sensitized bacteria identify an M tuberculosis dihydrofolate reductase inhibitor with whole cell activity
    • 10.1371/journal.pone.0039961
    • A. Kumar, M. Zhang, L. Zhu, R.P. Liao, C. Mutai, and S. Hafsat High-throughput screening and sensitized bacteria identify an M tuberculosis dihydrofolate reductase inhibitor with whole cell activity PloS One 7 2012 e39961 10.1371/journal.pone.0039961
    • (2012) PloS One , vol.7 , pp. 39961
    • Kumar, A.1    Zhang, M.2    Zhu, L.3    Liao, R.P.4    Mutai, C.5    Hafsat, S.6
  • 20
    • 70449108128 scopus 로고    scopus 로고
    • Antituberculosis activity of the molecular libraries screening center network library
    • 10.1016/j.tube.2009.07.006
    • J.A. Maddry, S. Ananthan, R.C. Goldman, J.V. Hobrath, C.D. Kwong, and C. Maddox Antituberculosis activity of the molecular libraries screening center network library Tuberculosis 89 2009 354 363 10.1016/j.tube.2009.07.006
    • (2009) Tuberculosis , vol.89 , pp. 354-363
    • Maddry, J.A.1    Ananthan, S.2    Goldman, R.C.3    Hobrath, J.V.4    Kwong, C.D.5    Maddox, C.6
  • 21
    • 84856496490 scopus 로고    scopus 로고
    • High throughput screening of a library based on kinase inhibitor scaffolds against Mycobacterium tuberculosis H37Rv
    • 10.1016/j.tube.2011.05.005
    • R.C. Reynolds, S. Ananthan, E. Faaleolea, J.V. Hobrath, C.D. Kwong, and C. Maddox High throughput screening of a library based on kinase inhibitor scaffolds against Mycobacterium tuberculosis H37Rv Tuberculosis 92 2012 72 83 10.1016/j.tube.2011.05.005
    • (2012) Tuberculosis , vol.92 , pp. 72-83
    • Reynolds, R.C.1    Ananthan, S.2    Faaleolea, E.3    Hobrath, J.V.4    Kwong, C.D.5    Maddox, C.6
  • 22
    • 84865253965 scopus 로고    scopus 로고
    • Identification of novel inhibitors of M tuberculosis growth using whole cell based high-throughput screening
    • 10.1021/cb300151m
    • S.A. Stanley, S.S. Grant, T. Kawate, N. Iwase, M. Shimizu, and C. Wivagg Identification of novel inhibitors of M tuberculosis growth using whole cell based high-throughput screening ACS Chem Biol 7 2012 1377 1384 10.1021/cb300151m
    • (2012) ACS Chem Biol , vol.7 , pp. 1377-1384
    • Stanley, S.A.1    Grant, S.S.2    Kawate, T.3    Iwase, N.4    Shimizu, M.5    Wivagg, C.6
  • 23
    • 79251537963 scopus 로고    scopus 로고
    • A chemical genetic screen in Mycobacterium tuberculosis identifies carbon-source-dependent growth inhibitors devoid of in vivo efficacy
    • 10.1038/ncomms1060
    • K. Pethe, P.C. Sequeira, S. Agarwalla, K. Rhee, K. Kuhen, and W.Y. Phong A chemical genetic screen in Mycobacterium tuberculosis identifies carbon-source-dependent growth inhibitors devoid of in vivo efficacy Nat Commun 1 2010 57 10.1038/ncomms1060
    • (2010) Nat Commun , vol.1 , pp. 57
    • Pethe, K.1    Sequeira, P.C.2    Agarwalla, S.3    Rhee, K.4    Kuhen, K.5    Phong, W.Y.6
  • 24
    • 78049483746 scopus 로고    scopus 로고
    • Leads for antitubercular compounds from kinase inhibitor library screens
    • 10.1016/j.tube.2010.09.001
    • S. Magnet, R.C. Hartkoorn, R. Szekely, J. Pato, J.A. Triccas, and P. Schneider Leads for antitubercular compounds from kinase inhibitor library screens Tuberculosis 90 2010 354 360 10.1016/j.tube.2010.09.001
    • (2010) Tuberculosis , vol.90 , pp. 354-360
    • Magnet, S.1    Hartkoorn, R.C.2    Szekely, R.3    Pato, J.4    Triccas, J.A.5    Schneider, P.6
  • 25
    • 0027410583 scopus 로고
    • Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator
    • R.T. Voegele, G.D. Sweet, and W. Boos Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator J Bacteriol 175 1993 1087 1094
    • (1993) J Bacteriol , vol.175 , pp. 1087-1094
    • Voegele, R.T.1    Sweet, G.D.2    Boos, W.3
  • 27
    • 19944429772 scopus 로고    scopus 로고
    • A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis
    • 10.1126/science.1106753
    • K. Andries, P. Verhasselt, J. Guillemont, H.W. Gohlmann, J.M. Neefs, and H. Winkler A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis Science 307 2005 223 227 10.1126/science.1106753
    • (2005) Science , vol.307 , pp. 223-227
    • Andries, K.1    Verhasselt, P.2    Guillemont, J.3    Gohlmann, H.W.4    Neefs, J.M.5    Winkler, H.6
  • 28
    • 33746916098 scopus 로고    scopus 로고
    • Genetic basis for natural and acquired resistance to the diarylquinoline R207910 in mycobacteria
    • 10.1128/AAC.00244-06
    • S. Petrella, E. Cambau, A. Chauffour, K. Andries, V. Jarlier, and W. Sougakoff Genetic basis for natural and acquired resistance to the diarylquinoline R207910 in mycobacteria Antimicrobial Agents Chemother 50 2006 2853 2856 10.1128/AAC.00244-06
    • (2006) Antimicrobial Agents Chemother , vol.50 , pp. 2853-2856
    • Petrella, S.1    Cambau, E.2    Chauffour, A.3    Andries, K.4    Jarlier, V.5    Sougakoff, W.6
  • 29
    • 62949223223 scopus 로고    scopus 로고
    • Selectivity of TMC207 towards mycobacterial ATP synthase compared with that towards the eukaryotic homologue
    • 10.1128/AAC.01393-08
    • A.C. Haagsma, R. Abdillahi-Ibrahim, M.J. Wagner, K. Krab, K. Vergauwen, and J. Guillemont Selectivity of TMC207 towards mycobacterial ATP synthase compared with that towards the eukaryotic homologue Antimicrobial Agents Chemother 53 2009 1290 1292 10.1128/AAC.01393-08
    • (2009) Antimicrobial Agents Chemother , vol.53 , pp. 1290-1292
    • Haagsma, A.C.1    Abdillahi-Ibrahim, R.2    Wagner, M.J.3    Krab, K.4    Vergauwen, K.5    Guillemont, J.6
  • 30
    • 80051850771 scopus 로고    scopus 로고
    • Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthase
    • 10.1371/journal.pone.0023575
    • A.C. Haagsma, I. Podasca, A. Koul, K. Andries, J. Guillemont, and H. Lill Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthase PloS One 6 2011 e23575 10.1371/journal.pone.0023575
    • (2011) PloS One , vol.6 , pp. 23575
    • Haagsma, A.C.1    Podasca, I.2    Koul, A.3    Andries, K.4    Guillemont, J.5    Lill, H.6
  • 31
    • 54449084104 scopus 로고    scopus 로고
    • Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis
    • 10.1074/jbc.M803899200
    • A. Koul, L. Vranckx, N. Dendouga, W. Balemans, I. Van den Wyngaert, and K. Vergauwen Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis J Biol Chem 283 2008 25273 25280 10.1074/jbc.M803899200
    • (2008) J Biol Chem , vol.283 , pp. 25273-25280
    • Koul, A.1    Vranckx, L.2    Dendouga, N.3    Balemans, W.4    Van Den Wyngaert, I.5    Vergauwen, K.6
  • 32
    • 78049460213 scopus 로고    scopus 로고
    • Evaluation of the Mycobacterium smegmatis and BCG models for the discovery of Mycobacterium tuberculosis inhibitors
    • 10.1016/j.tube.2010.09.002
    • M. Altaf, C.H. Miller, D.S. Bellows, and R. O'Toole Evaluation of the Mycobacterium smegmatis and BCG models for the discovery of Mycobacterium tuberculosis inhibitors Tuberculosis 90 2010 333 337 10.1016/j.tube.2010.09.002
    • (2010) Tuberculosis , vol.90 , pp. 333-337
    • Altaf, M.1    Miller, C.H.2    Bellows, D.S.3    O'Toole, R.4
  • 33
    • 80053902179 scopus 로고    scopus 로고
    • New tuberculosis drugs on the horizon
    • 10.1016/j.mib.2011.07.022
    • S.T. Cole, and G. Riccardi New tuberculosis drugs on the horizon Curr Opin Microbiol 14 2011 570 576 10.1016/j.mib.2011.07.022
    • (2011) Curr Opin Microbiol , vol.14 , pp. 570-576
    • Cole, S.T.1    Riccardi, G.2
  • 34
    • 77955626451 scopus 로고    scopus 로고
    • Decaprenylphosphoryl-beta-D-ribose 2'-epimerase from Mycobacterium tuberculosis is a magic drug target
    • G. Manina, M.R. Pasca, S. Buroni, E. De Rossi, and G. Riccardi Decaprenylphosphoryl-beta-D-ribose 2'-epimerase from Mycobacterium tuberculosis is a magic drug target Curr Med Chem 17 2010 3099 3108
    • (2010) Curr Med Chem , vol.17 , pp. 3099-3108
    • Manina, G.1    Pasca, M.R.2    Buroni, S.3    De Rossi, E.4    Riccardi, G.5
  • 35
    • 80053459692 scopus 로고    scopus 로고
    • High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism
    • 10.1371/journal.ppat.1002251
    • J.E. Griffin, J.D. Gawronski, M.A. Dejesus, T.R. Ioerger, B.J. Akerley, and C.M. Sassetti High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism PLoS Pathogens 7 2011 e1002251 10.1371/journal.ppat.1002251
    • (2011) PLoS Pathogens , vol.7 , pp. 1002251
    • Griffin, J.E.1    Gawronski, J.D.2    Dejesus, M.A.3    Ioerger, T.R.4    Akerley, B.J.5    Sassetti, C.M.6
  • 36
    • 79951566404 scopus 로고    scopus 로고
    • Decaprenylphosphoryl-beta-D-ribose 2'-epimerase, the target of benzothiazinones and dinitrobenzamides, is an essential enzyme in Mycobacterium smegmatis
    • 10.1371/journal.pone.0016869
    • P.K. Crellin, R. Brammananth, and R.L. Coppel Decaprenylphosphoryl-beta- D-ribose 2'-epimerase, the target of benzothiazinones and dinitrobenzamides, is an essential enzyme in Mycobacterium smegmatis PloS One 6 2011 e16869 10.1371/journal.pone.0016869
    • (2011) PloS One , vol.6 , pp. 16869
    • Crellin, P.K.1    Brammananth, R.2    Coppel, R.L.3
  • 37
    • 82355175801 scopus 로고    scopus 로고
    • Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway
    • 10.1016/j.jprot.2011.08.016
    • G.A. de Souza, N.A. Leversen, H. Malen, and H.G. Wiker Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway J Proteomics 75 2011 502 510 10.1016/j.jprot.2011.08.016
    • (2011) J Proteomics , vol.75 , pp. 502-510
    • De Souza, G.A.1    Leversen, N.A.2    Malen, H.3    Wiker, H.G.4
  • 38
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • 10.1074/mcp.M300060-MCP200
    • S. Gu, J. Chen, K.M. Dobos, E.M. Bradbury, J.T. Belisle, and X. Chen Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain Mol Cell Proteomics: MCP 2 2003 1284 1296 10.1074/mcp.M300060-MCP200
    • (2003) Mol Cell Proteomics: MCP , vol.2 , pp. 1284-1296
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 39
    • 77951518283 scopus 로고    scopus 로고
    • Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv
    • 10.1186/1471-2180-10-132
    • H. Malen, S. Pathak, T. Softeland, G.A. de Souza, and H.G. Wiker Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv BMC Microbiol 10 2010 132 10.1186/1471-2180-10-132
    • (2010) BMC Microbiol , vol.10 , pp. 132
    • Malen, H.1    Pathak, S.2    Softeland, T.3    De Souza, G.A.4    Wiker, H.G.5
  • 40
    • 11144293517 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling
    • 10.1091/mbc.E04-04-0329
    • K.G. Mawuenyega, C.V. Forst, K.M. Dobos, J.T. Belisle, J. Chen, and E.M. Bradbury Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling Mol Biol Cell 16 2005 396 404 10.1091/mbc.E04-04- 0329
    • (2005) Mol Biol Cell , vol.16 , pp. 396-404
    • Mawuenyega, K.G.1    Forst, C.V.2    Dobos, K.M.3    Belisle, J.T.4    Chen, J.5    Bradbury, E.M.6
  • 41
    • 65649096556 scopus 로고    scopus 로고
    • Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis
    • 10.1126/science.1171583
    • V. Makarov, G. Manina, K. Mikusova, U. Mollmann, O. Ryabova, and B. Saint-Joanis Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis Science 324 2009 801 804 10.1126/science.1171583
    • (2009) Science , vol.324 , pp. 801-804
    • Makarov, V.1    Manina, G.2    Mikusova, K.3    Mollmann, U.4    Ryabova, O.5    Saint-Joanis, B.6
  • 42
    • 77956163145 scopus 로고    scopus 로고
    • Biological and structural characterization of the Mycobacterium smegmatis nitroreductase NfnB, and its role in benzothiazinone resistance
    • 10.1111/j.1365-2958.2010.07277.x
    • G. Manina, M. Bellinzoni, M.R. Pasca, J. Neres, A. Milano, and A.L. Ribeiro Biological and structural characterization of the Mycobacterium smegmatis nitroreductase NfnB, and its role in benzothiazinone resistance Mol Microbiol 77 2010 1172 1185 10.1111/j.1365-2958.2010.07277.x
    • (2010) Mol Microbiol , vol.77 , pp. 1172-1185
    • Manina, G.1    Bellinzoni, M.2    Pasca, M.R.3    Neres, J.4    Milano, A.5    Ribeiro, A.L.6
  • 43
    • 80055121178 scopus 로고    scopus 로고
    • Analogous mechanisms of resistance to benzothiazinones and dinitrobenzamides in Mycobacterium smegmatis
    • 10.1371/journal.pone.0026675
    • A.L. Ribeiro, G. Degiacomi, F. Ewann, S. Buroni, M.L. Incandela, and L.R. Chiarelli Analogous mechanisms of resistance to benzothiazinones and dinitrobenzamides in Mycobacterium smegmatis PloS One 6 2011 e26675 10.1371/journal.pone.0026675
    • (2011) PloS One , vol.6 , pp. 26675
    • Ribeiro, A.L.1    Degiacomi, G.2    Ewann, F.3    Buroni, S.4    Incandela, M.L.5    Chiarelli, L.R.6
  • 44
    • 77957310736 scopus 로고    scopus 로고
    • Benzothiazinones: Prodrugs that covalently modify the decaprenylphosphoryl-beta-D-ribose 2'-epimerase DprE1 of Mycobacterium tuberculosis
    • 10.1021/ja106357w
    • C. Trefzer, M. Rengifo-Gonzalez, M.J. Hinner, P. Schneider, V. Makarov, and S.T. Cole Benzothiazinones: prodrugs that covalently modify the decaprenylphosphoryl-beta-D-ribose 2'-epimerase DprE1 of Mycobacterium tuberculosis J Am Chem Soc 132 2010 13663 13665 10.1021/ja106357w
    • (2010) J Am Chem Soc , vol.132 , pp. 13663-13665
    • Trefzer, C.1    Rengifo-Gonzalez, M.2    Hinner, M.J.3    Schneider, P.4    Makarov, V.5    Cole, S.T.6
  • 45
    • 84873098413 scopus 로고    scopus 로고
    • Crystal structure of decaprenylphosphoryl-beta- D-ribose 2'-epimerase from Mycobacterium smegmatis
    • 10.1002/prot.24220
    • H. Li, and G. Jogl Crystal structure of decaprenylphosphoryl-beta- D-ribose 2'-epimerase from Mycobacterium smegmatis Proteins 81 2013 538 543 10.1002/prot.24220
    • (2013) Proteins , vol.81 , pp. 538-543
    • Li, H.1    Jogl, G.2
  • 46
    • 84863919677 scopus 로고    scopus 로고
    • Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors
    • 10.1073/pnas.1205735109
    • S.M. Batt, T. Jabeen, V. Bhowruth, L. Quill, P.A. Lund, and L. Eggeling Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors Proc Natl Acad Sci USA 109 2012 11354 11359 10.1073/pnas.1205735109
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 11354-11359
    • Batt, S.M.1    Jabeen, T.2    Bhowruth, V.3    Quill, L.4    Lund, P.A.5    Eggeling, L.6
  • 47
    • 84865960733 scopus 로고    scopus 로고
    • Structural basis for benzothiazinone-mediated killing of Mycobacterium tuberculosis
    • 10.1126/scitranslmed.3004395 150ra121
    • J. Neres, F. Pojer, E. Molteni, L.R. Chiarelli, N. Dhar, and S. Boy-Rottger Structural basis for benzothiazinone-mediated killing of Mycobacterium tuberculosis Science Transl Med 4 2012 10.1126/scitranslmed. 3004395 150ra121
    • (2012) Science Transl Med , vol.4
    • Neres, J.1    Pojer, F.2    Molteni, E.3    Chiarelli, L.R.4    Dhar, N.5    Boy-Rottger, S.6
  • 48
    • 70350764818 scopus 로고    scopus 로고
    • Discovery and validation of new antitubercular compounds as potential drug leads and probes
    • 10.1016/j.tube.2009.07.007
    • R.C. Goldman, and B.E. Laughon Discovery and validation of new antitubercular compounds as potential drug leads and probes Tuberculosis 89 2009 331 333 10.1016/j.tube.2009.07.007
    • (2009) Tuberculosis , vol.89 , pp. 331-333
    • Goldman, R.C.1    Laughon, B.E.2
  • 49
    • 84858677107 scopus 로고    scopus 로고
    • Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane
    • 10.1038/nchembio.794
    • A.E. Grzegorzewicz, H. Pham, V.A. Gundi, M.S. Scherman, E.J. North, and T. Hess Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane Nat Chem Biol 8 2012 334 341 10.1038/nchembio.794
    • (2012) Nat Chem Biol , vol.8 , pp. 334-341
    • Grzegorzewicz, A.E.1    Pham, H.2    Gundi, V.A.3    Scherman, M.S.4    North, E.J.5    Hess, T.6
  • 51
    • 84860481546 scopus 로고    scopus 로고
    • Screening a library of 1600 adamantyl ureas for anti-Mycobacterium tuberculosis activity in vitro and for better physical chemical properties for bioavailability
    • 10.1016/j.bmc.2012.03.058
    • M.S. Scherman, E.J. North, V. Jones, T.N. Hess, A.E. Grzegorzewicz, and T. Kasagami Screening a library of 1600 adamantyl ureas for anti-Mycobacterium tuberculosis activity in vitro and for better physical chemical properties for bioavailability Bioorg Med Chem 20 2012 3255 3262 10.1016/j.bmc.2012.03.058
    • (2012) Bioorg Med Chem , vol.20 , pp. 3255-3262
    • Scherman, M.S.1    North, E.J.2    Jones, V.3    Hess, T.N.4    Grzegorzewicz, A.E.5    Kasagami, T.6
  • 52
    • 84863404695 scopus 로고    scopus 로고
    • SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis
    • 10.1128/AAC.05708-11
    • K. Tahlan, R. Wilson, D.B. Kastrinsky, K. Arora, V. Nair, and E. Fischer SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis Antimicrobial Agents Chemother 56 2012 1797 1809 10.1128/AAC.05708-11
    • (2012) Antimicrobial Agents Chemother , vol.56 , pp. 1797-1809
    • Tahlan, K.1    Wilson, R.2    Kastrinsky, D.B.3    Arora, K.4    Nair, V.5    Fischer, E.6
  • 53
    • 84860181497 scopus 로고    scopus 로고
    • MmpL genes are associated with mycolic acid metabolism in mycobacteria and corynebacteria
    • 10.1016/j.chembiol.2012.03.006
    • C. Varela, D. Rittmann, A. Singh, K. Krumbach, K. Bhatt, and L. Eggeling MmpL genes are associated with mycolic acid metabolism in mycobacteria and corynebacteria Chem Biol 19 2012 498 506 10.1016/j.chembiol.2012.03.006
    • (2012) Chem Biol , vol.19 , pp. 498-506
    • Varela, C.1    Rittmann, D.2    Singh, A.3    Krumbach, K.4    Bhatt, K.5    Eggeling, L.6
  • 54
    • 0031753303 scopus 로고    scopus 로고
    • Bactericidal activities of the pyrrole derivative BM212 against multidrug-resistant and intramacrophagic Mycobacterium tuberculosis strains
    • D. Deidda, G. Lampis, R. Fioravanti, M. Biava, G.C. Porretta, and S. Zanetti Bactericidal activities of the pyrrole derivative BM212 against multidrug-resistant and intramacrophagic Mycobacterium tuberculosis strains Antimicrobial Agents Chemother 42 1998 3035 3037
    • (1998) Antimicrobial Agents Chemother , vol.42 , pp. 3035-3037
    • Deidda, D.1    Lampis, G.2    Fioravanti, R.3    Biava, M.4    Porretta, G.C.5    Zanetti, S.6
  • 55
    • 19744376797 scopus 로고    scopus 로고
    • Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance
    • 10.1128/IAI.73.6.3492-3501.2005
    • P. Domenech, M.B. Reed, and C.E. Barry III Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance Infect Immun 73 2005 3492 3501 10.1128/IAI.73.6.3492-3501.2005
    • (2005) Infect Immun , vol.73 , pp. 3492-3501
    • Domenech, P.1    Reed, M.B.2    Barry III, C.E.3
  • 56
    • 84874297088 scopus 로고    scopus 로고
    • Improved BM212 MmpL3 inhibitor analogue shows efficacy in acute Murine model of tuberculosis infection
    • 10.1371/journal.pone.0056980
    • G. Poce, R.H. Bates, S. Alfonso, M. Cocozza, G.C. Porretta, and L. Ballell Improved BM212 MmpL3 inhibitor analogue shows efficacy in acute Murine model of tuberculosis infection PloS One 8 2013 e56980 10.1371/journal.pone. 0056980
    • (2013) PloS One , vol.8 , pp. 56980
    • Poce, G.1    Bates, R.H.2    Alfonso, S.3    Cocozza, M.4    Porretta, G.C.5    Ballell, L.6
  • 57
    • 84876129597 scopus 로고    scopus 로고
    • Design, synthesis and anti-tuberculosis activity of 1-adamantyl-3- heteroaryl ureas with improved in vitro pharmacokinetic properties
    • 10.1016/j.bmc.2013.02.028
    • E.J. North, M.S. Scherman, D.F. Bruhn, J.S. Scarborough, M.M. Maddox, and V. Jones Design, synthesis and anti-tuberculosis activity of 1-adamantyl-3-heteroaryl ureas with improved in vitro pharmacokinetic properties Bioorg Med Chem 21 2013 2587 2599 10.1016/j.bmc.2013.02.028
    • (2013) Bioorg Med Chem , vol.21 , pp. 2587-2599
    • North, E.J.1    Scherman, M.S.2    Bruhn, D.F.3    Scarborough, J.S.4    Maddox, M.M.5    Jones, V.6
  • 58
    • 79955637311 scopus 로고    scopus 로고
    • The many faces of the adamantyl group in drug design
    • 10.1016/j.ejmech.2011.01.047
    • J. Liu, D. Obando, V. Liao, T. Lifa, and R. Codd The many faces of the adamantyl group in drug design Eur J Med Chem 46 2011 1949 1963 10.1016/j.ejmech.2011.01.047
    • (2011) Eur J Med Chem , vol.46 , pp. 1949-1963
    • Liu, J.1    Obando, D.2    Liao, V.3    Lifa, T.4    Codd, R.5
  • 59
    • 77955615630 scopus 로고    scopus 로고
    • Use of the adamantane structure in medicinal chemistry
    • G. Lamoureux, and G. Artavia Use of the adamantane structure in medicinal chemistry Curr Med Chem 17 2010 2967 2978
    • (2010) Curr Med Chem , vol.17 , pp. 2967-2978
    • Lamoureux, G.1    Artavia, G.2
  • 60
    • 0034098732 scopus 로고    scopus 로고
    • Characterization of the Mycobacterium tuberculosis iniBAC promoter, a promoter that responds to cell wall biosynthesis inhibition
    • D. Alland, A.J. Steyn, T. Weisbrod, K. Aldrich, and W.R. Jacobs Jr. Characterization of the Mycobacterium tuberculosis iniBAC promoter, a promoter that responds to cell wall biosynthesis inhibition J Bacteriol 182 2000 1802 1811
    • (2000) J Bacteriol , vol.182 , pp. 1802-1811
    • Alland, D.1    Steyn, A.J.2    Weisbrod, T.3    Aldrich, K.4    Jacobs, Jr.W.R.5
  • 61
    • 84876272210 scopus 로고    scopus 로고
    • Tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide and N-benzyl-6',7'-dihydrospiro[piperidine-4,4'-thieno[3,2-c]pyran] analogues with bactericidal efficacy against Mycobacterium tuberculosis targeting MmpL3
    • 10.1371/journal.pone.0060933
    • M.J. Remuinan, E. Perez-Herran, J. Rullas, C. Alemparte, M. Martinez-Hoyos, D.J. Dow L. Ballell, and N. Cammack Tetrahydropyrazolo[1,5-a] pyrimidine-3-carboxamide and N-benzyl-6',7'-dihydrospiro[piperidine-4,4'- thieno[3,2-c]pyran] analogues with bactericidal efficacy against Mycobacterium tuberculosis targeting MmpL3 PloS One 8 2013 e60933 10.1371/journal.pone.0060933
    • (2013) PloS One , vol.8 , pp. 60933
    • Remuinan, M.J.1    Perez-Herran, E.2    Rullas, J.3    Alemparte, C.4    Martinez-Hoyos, M.5    Dow, D.J.6    Ballell, L.7    Cammack, N.8
  • 62
    • 84873811860 scopus 로고    scopus 로고
    • Fueling open-source drug discovery: 177 small-molecule leads against tuberculosis
    • 10.1002/cmdc.201200428
    • L. Ballell, R.H. Bates, R.J. Young, D. Alvarez-Gomez, E. Alvarez-Ruiz, and V. Barroso Fueling open-source drug discovery: 177 small-molecule leads against tuberculosis ChemMedChem 8 2013 313 321 10.1002/cmdc.201200428
    • (2013) ChemMedChem , vol.8 , pp. 313-321
    • Ballell, L.1    Bates, R.H.2    Young, R.J.3    Alvarez-Gomez, D.4    Alvarez-Ruiz, E.5    Barroso, V.6
  • 63
    • 84878098841 scopus 로고    scopus 로고
    • Preliminary structure-activity relationships and biological evaluation of novel antitubercular indolecarboxamide derivatives against drug-susceptible and drug-resistant Mycobacterium tuberculosis strains
    • 10.1021/jm4003878
    • O.K. Onajole, M. Pieroni, S.K. Tipparaju, S. Lun, J. Stec, and G. Chen Preliminary structure-activity relationships and biological evaluation of novel antitubercular indolecarboxamide derivatives against drug-susceptible and drug-resistant Mycobacterium tuberculosis strains J Med Chem 56 2013 4093 4103 10.1021/jm4003878
    • (2013) J Med Chem , vol.56 , pp. 4093-4103
    • Onajole, O.K.1    Pieroni, M.2    Tipparaju, S.K.3    Lun, S.4    Stec, J.5    Chen, G.6
  • 64
    • 84871764621 scopus 로고    scopus 로고
    • Identification of novel imidazo[1,2-a]pyridine inhibitors targeting M tuberculosis QcrB
    • 10.1371/journal.pone.0052951
    • K.A. Abrahams, J.A. Cox, V.L. Spivey, N.J. Loman, M.J. Pallen, and C. Constantinidou Identification of novel imidazo[1,2-a]pyridine inhibitors targeting M tuberculosis QcrB PloS One 7 2012 e52951 10.1371/journal.pone. 0052951
    • (2012) PloS One , vol.7 , pp. 52951
    • Abrahams, K.A.1    Cox, J.A.2    Spivey, V.L.3    Loman, N.J.4    Pallen, M.J.5    Constantinidou, C.6
  • 65
    • 0035940515 scopus 로고    scopus 로고
    • Comprehensive identification of conditionally essential genes in mycobacteria
    • 10.1073/pnas.231275498
    • C.M. Sassetti, D.H. Boyd, and E.J. Rubin Comprehensive identification of conditionally essential genes in mycobacteria Proc Natl Acad Sci USA 98 2001 12712 12717 10.1073/pnas.231275498
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12712-12717
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 66
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • C.M. Sassetti, D.H. Boyd, and E.J. Rubin Genes required for mycobacterial growth defined by high density mutagenesis Mol Microbiol 48 2003 77 84
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 67
    • 84883824094 scopus 로고    scopus 로고
    • Discovery of Q203, a potent clinical candidate for the treatment of tuberculosis
    • 10.1038/nm.3262
    • K. Pethe, P. Bifani, J. Jang, S. Kang, S. Park, and S. Ahn Discovery of Q203, a potent clinical candidate for the treatment of tuberculosis Nat Med 2013 10.1038/nm.3262
    • (2013) Nat Med
    • Pethe, K.1    Bifani, P.2    Jang, J.3    Kang, S.4    Park, S.5    Ahn, S.6
  • 68
    • 0027249653 scopus 로고
    • Roles in inhibitor recognition and quinol oxidation of the amino acid side chains at positions of cyt b providing resistance to Qo-inhibitors of the bc1 complex from Rhodobacter capsulatus
    • M.K. Tokito, and F. Daldal Roles in inhibitor recognition and quinol oxidation of the amino acid side chains at positions of cyt b providing resistance to Qo-inhibitors of the bc1 complex from Rhodobacter capsulatus Mol Microbiol 9 1993 965 978
    • (1993) Mol Microbiol , vol.9 , pp. 965-978
    • Tokito, M.K.1    Daldal, F.2
  • 69
    • 65749100586 scopus 로고    scopus 로고
    • The Pks13/FadD32 crosstalk for the biosynthesis of mycolic acids in Mycobacterium tuberculosis
    • 10.1074/jbc.M109.006940
    • S. Gavalda, M. Leger, B. van der Rest, A. Stella, F. Bardou, and H. Montrozier The Pks13/FadD32 crosstalk for the biosynthesis of mycolic acids in Mycobacterium tuberculosis J Biol Chem 284 2009 19255 19264 10.1074/jbc.M109. 006940
    • (2009) J Biol Chem , vol.284 , pp. 19255-19264
    • Gavalda, S.1    Leger, M.2    Van Der Rest, B.3    Stella, A.4    Bardou, F.5    Montrozier, H.6
  • 70
    • 0347719360 scopus 로고    scopus 로고
    • A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms
    • 10.1073/pnas.0305439101
    • D. Portevin, C. De Sousa-D'Auria, C. Houssin, C. Grimaldi, M. Chami, and M. Daffe A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms Proc Natl Acad Sci USA 101 2004 314 319 10.1073/pnas.0305439101
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 314-319
    • Portevin, D.1    De Sousa-D'Auria, C.2    Houssin, C.3    Grimaldi, C.4    Chami, M.5    Daffe, M.6
  • 71
    • 79961085853 scopus 로고    scopus 로고
    • Identifying vulnerable pathways in Mycobacterium tuberculosis by using a knockdown approach
    • 10.1128/AEM.02880-10
    • P. Carroll, M.C. Faray-Kele, and T. Parish Identifying vulnerable pathways in Mycobacterium tuberculosis by using a knockdown approach Appl Environ Microbiol 77 2011 5040 5043 10.1128/AEM.02880-10
    • (2011) Appl Environ Microbiol , vol.77 , pp. 5040-5043
    • Carroll, P.1    Faray-Kele, M.C.2    Parish, T.3
  • 72
    • 84880924467 scopus 로고    scopus 로고
    • Antituberculosis thiophenes define a requirement for Pks13 in mycolic acid biosynthesis
    • 10.1038/nchembio.1277
    • R. Wilson, P. Kumar, V. Parashar, C. Vilcheze, R. Veyron-Churlet, and J.S. Freundlich Antituberculosis thiophenes define a requirement for Pks13 in mycolic acid biosynthesis Nat Chem Biol 9 2013 499 506 10.1038/nchembio.1277
    • (2013) Nat Chem Biol , vol.9 , pp. 499-506
    • Wilson, R.1    Kumar, P.2    Parashar, V.3    Vilcheze, C.4    Veyron-Churlet, R.5    Freundlich, J.S.6
  • 73
    • 47649098600 scopus 로고    scopus 로고
    • Cooperativity and biological complexity
    • 10.1038/nchembio0808-435
    • A. Whitty Cooperativity and biological complexity Nat Chem Biol 4 2008 435 439 10.1038/nchembio0808-435
    • (2008) Nat Chem Biol , vol.4 , pp. 435-439
    • Whitty, A.1
  • 74
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • A. Rich, N. Davidson, W.H. Freeman and Company London
    • G. Adams, and M. Delbruck Reduction of dimensionality in biological diffusion processes A. Rich, N. Davidson, Structural chemistry and molecular biology San Francisco 1968 W.H. Freeman and Company London 198 215
    • (1968) Structural Chemistry and Molecular Biology San Francisco , pp. 198-215
    • Adams, G.1    Delbruck, M.2
  • 75
    • 0020018758 scopus 로고
    • The interaction of drugs with the sarcoplasmic reticulum
    • 10.1146/annurev.pa.22.040182.002213
    • L. Herbette, F.C. Messineo, and A.M. Katz The interaction of drugs with the sarcoplasmic reticulum Ann Rev Pharmacol Toxicol 22 1982 413 434 10.1146/annurev.pa.22.040182.002213
    • (1982) Ann Rev Pharmacol Toxicol , vol.22 , pp. 413-434
    • Herbette, L.1    Messineo, F.C.2    Katz, A.M.3
  • 76
    • 0021294849 scopus 로고
    • Neutron diffraction and the decomposition of membrane scattering profiles into the scattering profiles of their molecular components
    • J.K. Blasie, J.M. Pachence, and L.G. Herbette Neutron diffraction and the decomposition of membrane scattering profiles into the scattering profiles of their molecular components Basic Life Sci 27 1984 201 210
    • (1984) Basic Life Sci , vol.27 , pp. 201-210
    • Blasie, J.K.1    Pachence, J.M.2    Herbette, L.G.3
  • 77
    • 0021944456 scopus 로고
    • Interaction of amphiphilic molecules with biological membranes. A model for nonspecific and specific drug effects with membranes
    • L. Herbette, C.A. Napolitano, F.C. Messineo, and A.M. Katz Interaction of amphiphilic molecules with biological membranes. A model for nonspecific and specific drug effects with membranes Adv Myocardiol 5 1985 333 346
    • (1985) Adv Myocardiol , vol.5 , pp. 333-346
    • Herbette, L.1    Napolitano, C.A.2    Messineo, F.C.3    Katz, A.M.4
  • 78
    • 0021861363 scopus 로고
    • Kinetics of binding of membrane-active drugs to receptor sites. Diffusion-limited rates for a membrane bilayer approach of 1,4-dihydropyridine calcium channel antagonists to their active site
    • D.G. Rhodes, J.G. Sarmiento, and L.G. Herbette Kinetics of binding of membrane-active drugs to receptor sites. Diffusion-limited rates for a membrane bilayer approach of 1,4-dihydropyridine calcium channel antagonists to their active site Mol Pharmacol 27 1985 612 623
    • (1985) Mol Pharmacol , vol.27 , pp. 612-623
    • Rhodes, D.G.1    Sarmiento, J.G.2    Herbette, L.G.3
  • 79
    • 0023521436 scopus 로고
    • Diffusion of dihydropyridine calcium channel antagonists in cardiac sarcolemmal lipid multibilayers
    • 10.1016/S0006-3495(87)83295-2
    • D.W. Chester, L.G. Herbette, R.P. Mason, A.F. Joslyn, D.J. Triggle, and D.E. Koppel Diffusion of dihydropyridine calcium channel antagonists in cardiac sarcolemmal lipid multibilayers Biophys J 52 1987 1021 1030 10.1016/S0006- 3495(87)83295-2
    • (1987) Biophys J , vol.52 , pp. 1021-1030
    • Chester, D.W.1    Herbette, L.G.2    Mason, R.P.3    Joslyn, A.F.4    Triggle, D.J.5    Koppel, D.E.6
  • 80
    • 0024559362 scopus 로고
    • Interaction of 1,4 dihydropyridine calcium channel antagonists with biological membranes: Lipid bilayer partitioning could occur before drug binding to receptors
    • L.G. Herbette, Y.M. Vant Erve, and D.G. Rhodes Interaction of 1,4 dihydropyridine calcium channel antagonists with biological membranes: lipid bilayer partitioning could occur before drug binding to receptors J Mol Cell Cardiol 21 1989 187 201
    • (1989) J Mol Cell Cardiol , vol.21 , pp. 187-201
    • Herbette, L.G.1    Vant Erve, Y.M.2    Rhodes, D.G.3
  • 81
    • 0024470839 scopus 로고
    • Comparison of location and binding for the positively charged 1,4-dihydropyridine calcium channel antagonist amlodipine with uncharged drugs of this class in cardiac membranes
    • R.P. Mason, S.F. Campbell, S.D. Wang, and L.G. Herbette Comparison of location and binding for the positively charged 1,4-dihydropyridine calcium channel antagonist amlodipine with uncharged drugs of this class in cardiac membranes Mol Pharmacol 36 1989 634 640
    • (1989) Mol Pharmacol , vol.36 , pp. 634-640
    • Mason, R.P.1    Campbell, S.F.2    Wang, S.D.3    Herbette, L.G.4
  • 82
    • 0025881509 scopus 로고
    • New approaches to drug design and delivery based on drug-membrane interactions
    • L.G. Herbette, D.G. Rhodes, and R.P. Mason New approaches to drug design and delivery based on drug-membrane interactions Drug Des Deliv 7 1991 75 118
    • (1991) Drug des Deliv , vol.7 , pp. 75-118
    • Herbette, L.G.1    Rhodes, D.G.2    Mason, R.P.3
  • 83
    • 0022254305 scopus 로고
    • The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffraction
    • L. Herbette, P. DeFoor, S. Fleischer, D. Pascolini, A. Scarpa, and J.K. Blasie The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffraction Biochim et Biophys Acta 817 1985 103 122
    • (1985) Biochim et Biophys Acta , vol.817 , pp. 103-122
    • Herbette, L.1    Defoor, P.2    Fleischer, S.3    Pascolini, D.4    Scarpa, A.5    Blasie, J.K.6
  • 85
    • 0028610108 scopus 로고
    • The molecular basis for lacidipine's unique pharmacokinetics: Optimal hydrophobicity results in membrane interactions that may facilitate the treatment of atherosclerosis
    • L.G. Herbette, P.E. Mason, G. Gaviraghi, T.N. Tulenko, and R.P. Mason The molecular basis for lacidipine's unique pharmacokinetics: optimal hydrophobicity results in membrane interactions that may facilitate the treatment of atherosclerosis J Cardiovasc Pharmacol 23 Suppl. 5 1994 S16 S25
    • (1994) J Cardiovasc Pharmacol , vol.23 , Issue.SUPPL. 5
    • Herbette, L.G.1    Mason, P.E.2    Gaviraghi, G.3    Tulenko, T.N.4    Mason, R.P.5
  • 86
    • 0028205555 scopus 로고
    • Favorable amphiphilicity of nimodipine facilitates its interactions with brain membranes
    • L.G. Herbette, P.E. Mason, K.R. Sweeney, M.W. Trumbore, and R.P. Mason Favorable amphiphilicity of nimodipine facilitates its interactions with brain membranes Neuropharmacology 33 1994 241 249
    • (1994) Neuropharmacology , vol.33 , pp. 241-249
    • Herbette, L.G.1    Mason, P.E.2    Sweeney, K.R.3    Trumbore, M.W.4    Mason, R.P.5
  • 87
    • 0023772307 scopus 로고
    • Possible molecular basis for the pharmacokinetics and pharmacodynamics of three membrane-active drugs: Propranolol, nimodipine and amiodarone
    • L.G. Herbette, M. Trumbore, D.W. Chester, and A.M. Katz Possible molecular basis for the pharmacokinetics and pharmacodynamics of three membrane-active drugs: propranolol, nimodipine and amiodarone J Mol Cell Cardiol 20 1988 373 378
    • (1988) J Mol Cell Cardiol , vol.20 , pp. 373-378
    • Herbette, L.G.1    Trumbore, M.2    Chester, D.W.3    Katz, A.M.4
  • 88
    • 0344867043 scopus 로고    scopus 로고
    • Nonspecific membrane effects of CH-103: Hydrophobicity, surface activity and membrane fluidity studies in comparison with propranolol and practolol
    • E. Varga, J. Szollosi, K. Antal, P. Kovacs, and J.Z. Szabo Nonspecific membrane effects of CH-103: hydrophobicity, surface activity and membrane fluidity studies in comparison with propranolol and practolol Die Pharmazie 54 1999 380 384
    • (1999) Die Pharmazie , vol.54 , pp. 380-384
    • Varga, E.1    Szollosi, J.2    Antal, K.3    Kovacs, P.4    Szabo, J.Z.5
  • 89
    • 33845763471 scopus 로고    scopus 로고
    • Molecular modeling approaches for the prediction of the nonspecific binding of drugs to hepatic microsomes
    • 10.1021/ci600221h
    • M.J. Sykes, M.J. Sorich, and J.O. Miners Molecular modeling approaches for the prediction of the nonspecific binding of drugs to hepatic microsomes J Chem Inform Model 46 2006 2661 2673 10.1021/ci600221h
    • (2006) J Chem Inform Model , vol.46 , pp. 2661-2673
    • Sykes, M.J.1    Sorich, M.J.2    Miners, J.O.3
  • 90
    • 2042479407 scopus 로고    scopus 로고
    • Effects of lipid chain length on molecular interactions between paclitaxel and phospholipid within model biomembranes
    • 10.1016/j.jcis.2003.12.009
    • L. Zhao, and S.S. Feng Effects of lipid chain length on molecular interactions between paclitaxel and phospholipid within model biomembranes J Colloid Interface Sci 274 2004 55 68 10.1016/j.jcis.2003.12.009
    • (2004) J Colloid Interface Sci , vol.274 , pp. 55-68
    • Zhao, L.1    Feng, S.S.2
  • 91
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • 10.1016/j.bbamem.2010.12.008
    • L. Adamian, H. Naveed, and J. Liang Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis Biochim et Biophys Acta 1808 2011 1092 1102 10.1016/j.bbamem.2010.12.008
    • (2011) Biochim et Biophys Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 92
    • 26644444070 scopus 로고    scopus 로고
    • How lipids and proteins interact in a membrane: A molecular approach
    • 10.1039/b504527d
    • A.G. Lee How lipids and proteins interact in a membrane: a molecular approach Mol BioSystems 1 2005 203 212 10.1039/b504527d
    • (2005) Mol BioSystems , vol.1 , pp. 203-212
    • Lee, A.G.1
  • 93
    • 33847292794 scopus 로고    scopus 로고
    • Beta-Barrel membrane bacterial proteins: Structure, function, assembly and interaction with lipids
    • S. Galdiero, M. Galdiero, and C. Pedone beta-Barrel membrane bacterial proteins: structure, function, assembly and interaction with lipids Curr Protein Pept Sci 8 2007 63 82
    • (2007) Curr Protein Pept Sci , vol.8 , pp. 63-82
    • Galdiero, S.1    Galdiero, M.2    Pedone, C.3
  • 94
    • 33646125196 scopus 로고    scopus 로고
    • Stoichiometry of lipid interactions with transmembrane proteins-Deduced from the 3D structures
    • 10.1110/ps.052021406
    • T. Pali, D. Bashtovyy, and D. Marsh Stoichiometry of lipid interactions with transmembrane proteins-Deduced from the 3D structures Protein Sci Pub Protein Soc 15 2006 1153 1161 10.1110/ps.052021406
    • (2006) Protein Sci Pub Protein Soc , vol.15 , pp. 1153-1161
    • Pali, T.1    Bashtovyy, D.2    Marsh, D.3
  • 95
    • 84872189670 scopus 로고    scopus 로고
    • Amphipathic antenna of an inward rectifier K+ channel responds to changes in the inner membrane leaflet
    • 10.1073/pnas.1217323110
    • M. Iwamoto, and S. Oiki Amphipathic antenna of an inward rectifier K+ channel responds to changes in the inner membrane leaflet Proc Natl Acad Sci USA 110 2013 749 754 10.1073/pnas.1217323110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 749-754
    • Iwamoto, M.1    Oiki, S.2
  • 96
    • 79955912551 scopus 로고    scopus 로고
    • The potassium channel KcsA: A model protein in studying membrane protein oligomerization and stability of oligomeric assembly?
    • 10.1016/j.abb.2011.03.010
    • M. Raja The potassium channel KcsA: a model protein in studying membrane protein oligomerization and stability of oligomeric assembly? Arch Biochem Biophys 510 2011 1 10 10.1016/j.abb.2011.03.010
    • (2011) Arch Biochem Biophys , vol.510 , pp. 1-10
    • Raja, M.1
  • 98
    • 10044244661 scopus 로고    scopus 로고
    • Lipid-protein interactions of integral membrane proteins: A comparative simulation study
    • 10.1529/biophysj.104.048397
    • S.S. Deol, P.J. Bond, C. Domene, and M.S. Sansom Lipid-protein interactions of integral membrane proteins: a comparative simulation study Biophys J 87 2004 3737 3749 10.1529/biophysj.104.048397
    • (2004) Biophys J , vol.87 , pp. 3737-3749
    • Deol, S.S.1    Bond, P.J.2    Domene, C.3    Sansom, M.S.4
  • 99
    • 27844535720 scopus 로고    scopus 로고
    • Molecular simulations and lipid-protein interactions: Potassium channels and other membrane proteins
    • 10.1042/BST20050916
    • M.S. Sansom, P.J. Bond, S.S. Deol, A. Grottesi, S. Haider, and Z.A. Sands Molecular simulations and lipid-protein interactions: potassium channels and other membrane proteins Biochem Soc Trans 33 2005 916 920 10.1042/BST20050916
    • (2005) Biochem Soc Trans , vol.33 , pp. 916-920
    • Sansom, M.S.1    Bond, P.J.2    Deol, S.S.3    Grottesi, A.4    Haider, S.5    Sands, Z.A.6
  • 100
    • 0041828861 scopus 로고    scopus 로고
    • The potassium channel KcsA and its interaction with the lipid bilayer
    • 10.1007/s00018-003-3172-y
    • I.M. Williamson, S.J. Alvis, J.M. East, and A.G. Lee The potassium channel KcsA and its interaction with the lipid bilayer Cell Mol Life Sci CMLS 60 2003 1581 1590 10.1007/s00018-003-3172-y
    • (2003) Cell Mol Life Sci CMLS , vol.60 , pp. 1581-1590
    • Williamson, I.M.1    Alvis, S.J.2    East, J.M.3    Lee, A.G.4
  • 101
    • 27844504698 scopus 로고    scopus 로고
    • Lipid interactions with bacterial channels: Fluorescence studies
    • 10.1042/BST20050905
    • A.M. Powl, J. Carney, P. Marius, J.M. East, and A.G. Lee Lipid interactions with bacterial channels: fluorescence studies Biochem Soc Trans 33 2005 905 909 10.1042/BST20050905
    • (2005) Biochem Soc Trans , vol.33 , pp. 905-909
    • Powl, A.M.1    Carney, J.2    Marius, P.3    East, J.M.4    Lee, A.G.5
  • 102
    • 17144372582 scopus 로고    scopus 로고
    • Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: Hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation
    • 10.1021/bi047439e
    • A.M. Powl, J.M. East, and A.G. Lee Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation Biochemistry 44 2005 5873 5883 10.1021/bi047439e
    • (2005) Biochemistry , vol.44 , pp. 5873-5883
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 103
    • 34247849390 scopus 로고    scopus 로고
    • Penetration of lipid chains into transmembrane surfaces of membrane proteins: Studies with MscL
    • 10.1529/biophysj.106.102210
    • J. Carney, J.M. East, and A.G. Lee Penetration of lipid chains into transmembrane surfaces of membrane proteins: studies with MscL Biophys J 92 2007 3556 3563 10.1529/biophysj.106.102210
    • (2007) Biophys J , vol.92 , pp. 3556-3563
    • Carney, J.1    East, J.M.2    Lee, A.G.3
  • 104
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • E.J. Prenner, R.N. Lewis, and R.N. McElhaney The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes Biochim et Biophys Acta 1462 1999 201 221
    • (1999) Biochim et Biophys Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.2    McElhaney, R.N.3
  • 105
    • 0019390764 scopus 로고
    • Changes in the structural state of boundary lipids in bacterial membrane under effect of the membranotropic antibiotic gramicidin S
    • A.D. Dergunov, A.S. Kaprel'iants, and D.N. Ostrovskii Changes in the structural state of boundary lipids in bacterial membrane under effect of the membranotropic antibiotic gramicidin S Biokhimiia 46 1981 1499 1509
    • (1981) Biokhimiia , vol.46 , pp. 1499-1509
    • Dergunov, A.D.1    Kaprel'Iants, A.S.2    Ostrovskii, D.N.3
  • 106
    • 4544239063 scopus 로고    scopus 로고
    • The macrolide-bacterium interaction and its biological basis
    • R.C. Goldman, and F. Scaglione The macrolide-bacterium interaction and its biological basis Curr Drug Targets Infect Disord 4 2004 241 260
    • (2004) Curr Drug Targets Infect Disord , vol.4 , pp. 241-260
    • Goldman, R.C.1    Scaglione, F.2
  • 107
    • 0027326490 scopus 로고
    • Anti-Candida activity of cispentacin: The active transport by amino acid permeases and possible mechanisms of action
    • 10.1006/bbrc.1993.1153
    • J.O. Capobianco, D. Zakula, M.L. Coen, and R.C. Goldman Anti-Candida activity of cispentacin: the active transport by amino acid permeases and possible mechanisms of action Biochem Biophys Res Commun 190 1993 1037 1044 10.1006/bbrc.1993.1153
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 1037-1044
    • Capobianco, J.O.1    Zakula, D.2    Coen, M.L.3    Goldman, R.C.4
  • 108
    • 0031670205 scopus 로고    scopus 로고
    • Mechanism of isoniazid uptake in Mycobacterium tuberculosis
    • F. Bardou, C. Raynaud, C. Ramos, M.A. Laneelle, and G. Laneelle Mechanism of isoniazid uptake in Mycobacterium tuberculosis Microbiology 144 Pt 9 1998 2539 2544
    • (1998) Microbiology , vol.144 , Issue.PART 9 , pp. 2539-2544
    • Bardou, F.1    Raynaud, C.2    Ramos, C.3    Laneelle, M.A.4    Laneelle, G.5
  • 109
    • 0033952249 scopus 로고    scopus 로고
    • Accumulation of rifampicin by Mycobacterium aurum, Mycobacterium smegmatis and Mycobacterium tuberculosis
    • L.J. Piddock, K.J. Williams, and V. Ricci Accumulation of rifampicin by Mycobacterium aurum, Mycobacterium smegmatis and Mycobacterium tuberculosis J Antimicrobial Chemother 45 2000 159 165
    • (2000) J Antimicrobial Chemother , vol.45 , pp. 159-165
    • Piddock, L.J.1    Williams, K.J.2    Ricci, V.3
  • 110
    • 0031762557 scopus 로고    scopus 로고
    • Accumulation of rifampicin by Escherichia coli and Staphylococcus aureus
    • K.J. Williams, and L.J. Piddock Accumulation of rifampicin by Escherichia coli and Staphylococcus aureus J Antimicrobial Chemother 42 1998 597 603
    • (1998) J Antimicrobial Chemother , vol.42 , pp. 597-603
    • Williams, K.J.1    Piddock, L.J.2
  • 111
    • 0031968179 scopus 로고    scopus 로고
    • Accumulation of norfloxacin by Mycobacterium aurum and Mycobacterium smegmatis
    • K.J. Williams, G.A. Chung, and L.J. Piddock Accumulation of norfloxacin by Mycobacterium aurum and Mycobacterium smegmatis Antimicrobial Agents Chemother 42 1998 795 800
    • (1998) Antimicrobial Agents Chemother , vol.42 , pp. 795-800
    • Williams, K.J.1    Chung, G.A.2    Piddock, L.J.3
  • 112
    • 0028849122 scopus 로고
    • Intracellular accumulation of norfloxacin in Mycobacterium smegmatis
    • S. Corti, J. Chevalier, and A. Cremieux Intracellular accumulation of norfloxacin in Mycobacterium smegmatis Antimicrobial Agents Chemother 39 1995 2466 2471
    • (1995) Antimicrobial Agents Chemother , vol.39 , pp. 2466-2471
    • Corti, S.1    Chevalier, J.2    Cremieux, A.3
  • 113
    • 0015432390 scopus 로고
    • Uptake and binding of 14C-ethambutol by tubercle bacilli and the relation of binding to growth inhibition
    • W.H. Beggs, and N.E. Auran Uptake and binding of 14C-ethambutol by tubercle bacilli and the relation of binding to growth inhibition Antimicrobial Agents Chemother 2 1972 390 394
    • (1972) Antimicrobial Agents Chemother , vol.2 , pp. 390-394
    • Beggs, W.H.1    Auran, N.E.2
  • 114
    • 0014854531 scopus 로고
    • Mechanism of D-cycloserine action: Transport systems for D-alanine, D-cycloserine, L-alanine, and glycine
    • R.J. Wargel, C.A. Shadur, and F.C. Neuhaus Mechanism of D-cycloserine action: transport systems for D-alanine, D-cycloserine, L-alanine, and glycine J Bacteriol 103 1970 778 788
    • (1970) J Bacteriol , vol.103 , pp. 778-788
    • Wargel, R.J.1    Shadur, C.A.2    Neuhaus, F.C.3
  • 115
    • 0023615466 scopus 로고
    • Mechanism of bactericidal action of aminoglycosides
    • B.D. Davis Mechanism of bactericidal action of aminoglycosides Microbiol Rev 51 1987 341 350
    • (1987) Microbiol Rev , vol.51 , pp. 341-350
    • Davis, B.D.1
  • 116
    • 0003830516 scopus 로고
    • Misread protein creates membrane channels: An essential step in the bactericidal action of aminoglycosides
    • B.D. Davis, L.L. Chen, and P.C. Tai Misread protein creates membrane channels: an essential step in the bactericidal action of aminoglycosides Proc Natl Acad Sci USA 83 1986 6164 6168
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6164-6168
    • Davis, B.D.1    Chen, L.L.2    Tai, P.C.3
  • 117
    • 70349342842 scopus 로고    scopus 로고
    • The arabinosyltransferase EmbC is inhibited by ethambutol in Mycobacterium tuberculosis
    • 10.1128/AAC.00162-09
    • R. Goude, A.G. Amin, D. Chatterjee, and T. Parish The arabinosyltransferase EmbC is inhibited by ethambutol in Mycobacterium tuberculosis Antimicrobial Agents Chemother 53 2009 4138 4146 10.1128/AAC.00162-09
    • (2009) Antimicrobial Agents Chemother , vol.53 , pp. 4138-4146
    • Goude, R.1    Amin, A.G.2    Chatterjee, D.3    Parish, T.4
  • 118
    • 77954184916 scopus 로고    scopus 로고
    • EmbCAB sequence variation among ethambutol-resistant Mycobacterium tuberculosis isolates without embB306 mutation
    • 10.1093/jac/dkq120
    • C. Plinke, H.S. Cox, N. Zarkua, H.A. Karimovich, K. Braker, and R. Diel embCAB sequence variation among ethambutol-resistant Mycobacterium tuberculosis isolates without embB306 mutation J Antimicrobial Chemother 65 2010 1359 1367 10.1093/jac/dkq120
    • (2010) J Antimicrobial Chemother , vol.65 , pp. 1359-1367
    • Plinke, C.1    Cox, H.S.2    Zarkua, N.3    Karimovich, H.A.4    Braker, K.5    Diel, R.6
  • 119
    • 79956320527 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis embB codon 306 mutations confer moderately increased resistance to ethambutol in vitro and in vivo
    • 10.1128/AAC.00007-10
    • C. Plinke, K. Walter, S. Aly, S. Ehlers, and S. Niemann Mycobacterium tuberculosis embB codon 306 mutations confer moderately increased resistance to ethambutol in vitro and in vivo Antimicrobial Agents Chemother 55 2011 2891 2896 10.1128/AAC.00007-10
    • (2011) Antimicrobial Agents Chemother , vol.55 , pp. 2891-2896
    • Plinke, C.1    Walter, K.2    Aly, S.3    Ehlers, S.4    Niemann, S.5
  • 120
    • 0043284551 scopus 로고    scopus 로고
    • Mechanisms of pyrazinamide resistance in mycobacteria: Importance of lack of uptake in addition to lack of pyrazinamidase activity
    • C. Raynaud, M.A. Laneelle, R.H. Senaratne, P. Draper, G. Laneelle, and M. Daffe Mechanisms of pyrazinamide resistance in mycobacteria: importance of lack of uptake in addition to lack of pyrazinamidase activity Microbiology 145 Pt 6 1999 1359 1367
    • (1999) Microbiology , vol.145 , Issue.PART 6 , pp. 1359-1367
    • Raynaud, C.1    Laneelle, M.A.2    Senaratne, R.H.3    Draper, P.4    Laneelle, G.5    Daffe, M.6
  • 121
    • 0036207006 scopus 로고    scopus 로고
    • Effects of pyrazinamide on fatty acid synthesis by whole mycobacterial cells and purified fatty acid synthase i
    • H.I. Boshoff, V. Mizrahi, and C.E. Barry III Effects of pyrazinamide on fatty acid synthesis by whole mycobacterial cells and purified fatty acid synthase I J Bacteriol 184 2002 2167 2172
    • (2002) J Bacteriol , vol.184 , pp. 2167-2172
    • Boshoff, H.I.1    Mizrahi, V.2    Barry III, C.E.3
  • 122
    • 0024349349 scopus 로고
    • Does pyrazinoic acid as an active moiety of pyrazinamide have specific activity against Mycobacterium tuberculosis?
    • L.B. Heifets, M.A. Flory, and P.J. Lindholm-Levy Does pyrazinoic acid as an active moiety of pyrazinamide have specific activity against Mycobacterium tuberculosis? Antimicrobial Agents Chemother 33 1989 1252 1254
    • (1989) Antimicrobial Agents Chemother , vol.33 , pp. 1252-1254
    • Heifets, L.B.1    Flory, M.A.2    Lindholm-Levy, P.J.3
  • 123
    • 80054681349 scopus 로고    scopus 로고
    • Pyrazinoic acid decreases the proton motive force, respiratory ATP synthesis activity, and cellular ATP levels
    • 10.1128/AAC.00507-11
    • P. Lu, A.C. Haagsma, H. Pham, J.J. Maaskant, S. Mol, and H. Lill Pyrazinoic acid decreases the proton motive force, respiratory ATP synthesis activity, and cellular ATP levels Antimicrobial Agents Chemother 55 2011 5354 5357 10.1128/AAC.00507-11
    • (2011) Antimicrobial Agents Chemother , vol.55 , pp. 5354-5357
    • Lu, P.1    Haagsma, A.C.2    Pham, H.3    Maaskant, J.J.4    Mol, S.5    Lill, H.6
  • 124
    • 34447258829 scopus 로고    scopus 로고
    • Inhibition of isolated Mycobacterium tuberculosis fatty acid synthase i by pyrazinamide analogs
    • 10.1128/AAC.01458-06
    • S.C. Ngo, O. Zimhony, W.J. Chung, H. Sayahi, W.R. Jacobs Jr., and J.T. Welch Inhibition of isolated Mycobacterium tuberculosis fatty acid synthase I by pyrazinamide analogs Antimicrobial Agents Chemother 51 2007 2430 2435 10.1128/AAC.01458-06
    • (2007) Antimicrobial Agents Chemother , vol.51 , pp. 2430-2435
    • Ngo, S.C.1    Zimhony, O.2    Chung, W.J.3    Sayahi, H.4    Jacobs, Jr.W.R.5    Welch, J.T.6
  • 125
    • 81155160151 scopus 로고    scopus 로고
    • Pyrazinamide inhibits trans-translation in Mycobacterium tuberculosis
    • 10.1126/science.1208813
    • W. Shi, X. Zhang, X. Jiang, H. Yuan, J.S. Lee, and C.E. Barry III Pyrazinamide inhibits trans-translation in Mycobacterium tuberculosis Science 333 2011 1630 1632 10.1126/science.1208813
    • (2011) Science , vol.333 , pp. 1630-1632
    • Shi, W.1    Zhang, X.2    Jiang, X.3    Yuan, H.4    Lee, J.S.5    Barry III, C.E.6
  • 126
    • 0029069432 scopus 로고
    • Activity of n-propyl pyrazinoate against pyrazinamide-resistant Mycobacterium tuberculosis: Investigations into mechanism of action of and mechanism of resistance to pyrazinamide
    • R.J. Speirs, J.T. Welch, and M.H. Cynamon Activity of n-propyl pyrazinoate against pyrazinamide-resistant Mycobacterium tuberculosis: investigations into mechanism of action of and mechanism of resistance to pyrazinamide Antimicrobial Agents Chemother 39 1995 1269 1271
    • (1995) Antimicrobial Agents Chemother , vol.39 , pp. 1269-1271
    • Speirs, R.J.1    Welch, J.T.2    Cynamon, M.H.3
  • 127
    • 33846605483 scopus 로고    scopus 로고
    • Pyrazinoic acid and its n-propyl ester inhibit fatty acid synthase type i in replicating tubercle bacilli
    • 10.1128/AAC.01369-06
    • O. Zimhony, C. Vilcheze, M. Arai, J.T. Welch, and W.R. Jacobs Jr. Pyrazinoic acid and its n-propyl ester inhibit fatty acid synthase type I in replicating tubercle bacilli Antimicrobial Agents Chemother 51 2007 752 754 10.1128/AAC.01369-06
    • (2007) Antimicrobial Agents Chemother , vol.51 , pp. 752-754
    • Zimhony, O.1    Vilcheze, C.2    Arai, M.3    Welch, J.T.4    Jacobs, Jr.W.R.5
  • 128
    • 0016591187 scopus 로고
    • The effect of p-aminosalicyclic acid on iron transport and assimilation in mycobacteria
    • K.A. Brown, and C. Ratledge The effect of p-aminosalicyclic acid on iron transport and assimilation in mycobacteria Biochim et Biophys Acta 385 1975 207 220
    • (1975) Biochim et Biophys Acta , vol.385 , pp. 207-220
    • Brown, K.A.1    Ratledge, C.2
  • 129
    • 84871927537 scopus 로고    scopus 로고
    • Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis
    • 10.1126/science.1228980
    • S. Chakraborty, T. Gruber, C.E. Barry III, H.I. Boshoff, and K.Y. Rhee Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis Science 339 2013 88 91 10.1126/science.1228980
    • (2013) Science , vol.339 , pp. 88-91
    • Chakraborty, S.1    Gruber, T.2    Barry III, C.E.3    Boshoff, H.I.4    Rhee, K.Y.5
  • 130
    • 84868090447 scopus 로고    scopus 로고
    • Targeting the mycobacterial envelope for tuberculosis drug development
    • 10.1586/eri.12.91
    • L. Favrot, and D.R. Ronning Targeting the mycobacterial envelope for tuberculosis drug development Expert Rev Anti-Infect Ther 10 2012 1023 1036 10.1586/eri.12.91
    • (2012) Expert Rev Anti-Infect Ther , vol.10 , pp. 1023-1036
    • Favrot, L.1    Ronning, D.R.2
  • 132
    • 0029061399 scopus 로고
    • The envelope of mycobacteria
    • 10.1146/annurev.bi.64.070195.000333
    • P.J. Brennan, and H. Nikaido The envelope of mycobacteria Ann Rev Biochem 64 1995 29 63 10.1146/annurev.bi.64.070195.000333
    • (1995) Ann Rev Biochem , vol.64 , pp. 29-63
    • Brennan, P.J.1    Nikaido, H.2
  • 133
    • 0032718515 scopus 로고    scopus 로고
    • Porins in the cell wall of Mycobacterium tuberculosis
    • B. Kartmann, S. Stenger, and M. Niederweis Porins in the cell wall of Mycobacterium tuberculosis J Bacteriol 181 1999 6543 6546
    • (1999) J Bacteriol , vol.181 , pp. 6543-6546
    • Kartmann, B.1    Stenger, S.2    Niederweis, M.3
  • 134
    • 0141677886 scopus 로고    scopus 로고
    • Mycobacterial porins-new channel proteins in unique outer membranes
    • M. Niederweis Mycobacterial porins-new channel proteins in unique outer membranes Mol Microbiol 49 2003 1167 1177
    • (2003) Mol Microbiol , vol.49 , pp. 1167-1177
    • Niederweis, M.1
  • 135
    • 42949135614 scopus 로고    scopus 로고
    • Nutrient acquisition by mycobacteria
    • 10.1099/mic.0.2007/012872-0
    • M. Niederweis Nutrient acquisition by mycobacteria Microbiology 154 2008 679 692 10.1099/mic.0.2007/012872-0
    • (2008) Microbiology , vol.154 , pp. 679-692
    • Niederweis, M.1
  • 137
    • 77955411450 scopus 로고    scopus 로고
    • Outer membrane pore protein prediction in mycobacteria using genomic comparison
    • 10.1099/mic.0.040089-0
    • N. Mah, C. Perez-Iratxeta, and M.A. Andrade-Navarro Outer membrane pore protein prediction in mycobacteria using genomic comparison Microbiology 156 2010 2506 2515 10.1099/mic.0.040089-0
    • (2010) Microbiology , vol.156 , pp. 2506-2515
    • Mah, N.1    Perez-Iratxeta, C.2    Andrade-Navarro, M.A.3
  • 139
    • 41949110521 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis CYP130: Crystal structure, biophysical characterization, and interactions with antifungal azole drugs
    • 10.1074/jbc.M708734200
    • H. Ouellet, L.M. Podust, and P.R. de Montellano Mycobacterium tuberculosis CYP130: crystal structure, biophysical characterization, and interactions with antifungal azole drugs J Biol Chem 283 2008 5069 5080 10.1074/jbc.M708734200
    • (2008) J Biol Chem , vol.283 , pp. 5069-5080
    • Ouellet, H.1    Podust, L.M.2    De Montellano, P.R.3
  • 140
    • 69949136444 scopus 로고    scopus 로고
    • Interaction of Mycobacterium tuberculosis CYP130 with heterocyclic arylamines
    • 10.1074/jbc.M109.017632
    • L.M. Podust, H. Ouellet, J.P. von Kries, and P.R. de Montellano Interaction of Mycobacterium tuberculosis CYP130 with heterocyclic arylamines J Biol Chem 284 2009 25211 25219 10.1074/jbc.M109.017632
    • (2009) J Biol Chem , vol.284 , pp. 25211-25219
    • Podust, L.M.1    Ouellet, H.2    Von Kries, J.P.3    De Montellano, P.R.4
  • 141
    • 33846015513 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode
    • 10.1074/jbc.M607665200
    • H.E. Seward, A. Roujeinikova, K.J. McLean, A.W. Munro, and D. Leys Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode J Biol Chem 281 2006 39437 39443 10.1074/jbc.M607665200
    • (2006) J Biol Chem , vol.281 , pp. 39437-39443
    • Seward, H.E.1    Roujeinikova, A.2    McLean, K.J.3    Munro, A.W.4    Leys, D.5
  • 142
    • 84867868400 scopus 로고    scopus 로고
    • Design and synthesis of 1H-1,2,3-triazoles derived from econazole as antitubercular agents
    • 10.1016/j.bmcl.2012.09.041
    • S. Kim, S.N. Cho, T. Oh, and P. Kim Design and synthesis of 1H-1,2,3-triazoles derived from econazole as antitubercular agents Bioorg Med Chem Lett 22 2012 6844 6847 10.1016/j.bmcl.2012.09.041
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 6844-6847
    • Kim, S.1    Cho, S.N.2    Oh, T.3    Kim, P.4
  • 143
    • 79951723342 scopus 로고    scopus 로고
    • Synthesis and antitubercular activity of monocyclic nitroimidazoles: Insights from econazole
    • 10.1016/j.bmcl.2010.12.128
    • S.H. Lee, S. Kim, M.H. Yun, Y.S. Lee, S.N. Cho, and T. Oh Synthesis and antitubercular activity of monocyclic nitroimidazoles: insights from econazole Bioorg Med Chem Lett 21 2011 1515 1518 10.1016/j.bmcl.2010.12.128
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 1515-1518
    • Lee, S.H.1    Kim, S.2    Yun, M.H.3    Lee, Y.S.4    Cho, S.N.5    Oh, T.6
  • 144
    • 84866604365 scopus 로고    scopus 로고
    • Click chemistry approach for bis-chromenyl triazole hybrids and their antitubercular activity
    • 10.1111/j.1747-0285.2012.01441.x
    • R.J. Naik, M.V. Kulkarni, K. Sreedhara Ranganath Pai, and P.G. Nayak Click chemistry approach for bis-chromenyl triazole hybrids and their antitubercular activity Chem Biol Drug Des 80 2012 516 523 10.1111/j.1747-0285. 2012.01441.x
    • (2012) Chem Biol Drug des , vol.80 , pp. 516-523
    • Naik, R.J.1    Kulkarni, M.V.2    Sreedhara Ranganath Pai, K.3    Nayak, P.G.4
  • 145
    • 34547912161 scopus 로고    scopus 로고
    • Activity of ketoconazole against Mycobacterium tuberculosis in vitro and in the mouse model
    • 10.1099/jmm.0.47058-0
    • S.T. Byrne, S.M. Denkin, P. Gu, E. Nuermberger, and Y. Zhang Activity of ketoconazole against Mycobacterium tuberculosis in vitro and in the mouse model J Med Microbiol 56 2007 1047 1051 10.1099/jmm.0.47058-0
    • (2007) J Med Microbiol , vol.56 , pp. 1047-1051
    • Byrne, S.T.1    Denkin, S.M.2    Gu, P.3    Nuermberger, E.4    Zhang, Y.5
  • 147
    • 24144473033 scopus 로고    scopus 로고
    • Genomic approach to identifying the putative target of and mechanisms of resistance to mefloquine in mycobacteria
    • 10.1128/AAC.49.9.3707-3714.2005
    • L. Danelishvili, M. Wu, L.S. Young, and L.E. Bermudez Genomic approach to identifying the putative target of and mechanisms of resistance to mefloquine in mycobacteria Antimicrobial Agents Chemother 49 2005 3707 3714 10.1128/AAC.49.9.3707-3714.2005
    • (2005) Antimicrobial Agents Chemother , vol.49 , pp. 3707-3714
    • Danelishvili, L.1    Wu, M.2    Young, L.S.3    Bermudez, L.E.4
  • 148
    • 69049098197 scopus 로고    scopus 로고
    • Resistant mutants of Mycobacterium tuberculosis selected in vitro do not reflect the in vivo mechanism of isoniazid resistance
    • 10.1093/jac/dkp237
    • I.L. Bergval, A.R. Schuitema, P.R. Klatser, and R.M. Anthony Resistant mutants of Mycobacterium tuberculosis selected in vitro do not reflect the in vivo mechanism of isoniazid resistance J Antimicrobial Chemother 64 2009 515 523 10.1093/jac/dkp237
    • (2009) J Antimicrobial Chemother , vol.64 , pp. 515-523
    • Bergval, I.L.1    Schuitema, A.R.2    Klatser, P.R.3    Anthony, R.M.4
  • 149
    • 0034702247 scopus 로고    scopus 로고
    • A small-molecule nitroimidazopyran drug candidate for the treatment of tuberculosis
    • 10.1038/35016103
    • C.K. Stover, P. Warrener, D.R. VanDevanter, D.R. Sherman, T.M. Arain, and M.H. Langhorne A small-molecule nitroimidazopyran drug candidate for the treatment of tuberculosis Nature 405 2000 962 966 10.1038/35016103
    • (2000) Nature , vol.405 , pp. 962-966
    • Stover, C.K.1    Warrener, P.2    Vandevanter, D.R.3    Sherman, D.R.4    Arain, T.M.5    Langhorne, M.H.6
  • 150
    • 77952326917 scopus 로고    scopus 로고
    • A collaborative database and computational models for tuberculosis drug discovery
    • 10.1039/b917766c
    • S. Ekins, J. Bradford, K. Dole, A. Spektor, K. Gregory, and D. Blondeau A collaborative database and computational models for tuberculosis drug discovery Mol BioSystems 6 2010 840 851 10.1039/b917766c
    • (2010) Mol BioSystems , vol.6 , pp. 840-851
    • Ekins, S.1    Bradford, J.2    Dole, K.3    Spektor, A.4    Gregory, K.5    Blondeau, D.6
  • 151
    • 77957680455 scopus 로고    scopus 로고
    • Analysis and hit filtering of a very large library of compounds screened against Mycobacterium tuberculosis
    • 10.1039/c0mb00104j
    • S. Ekins, T. Kaneko, C.A. Lipinski, J. Bradford, K. Dole, and A. Spektor Analysis and hit filtering of a very large library of compounds screened against Mycobacterium tuberculosis Mol BioSystems 6 2010 2316 2324 10.1039/c0mb00104j
    • (2010) Mol BioSystems , vol.6 , pp. 2316-2324
    • Ekins, S.1    Kaneko, T.2    Lipinski, C.A.3    Bradford, J.4    Dole, K.5    Spektor, A.6
  • 152
    • 37549071045 scopus 로고    scopus 로고
    • Drug discovery beyond the 'rule-of-five'
    • 10.1016/j.copbio.2007.10.005
    • M.Q. Zhang, and B. Wilkinson Drug discovery beyond the 'rule-of-five' Curr Opin Biotechnol 18 2007 478 488 10.1016/j.copbio.2007.10.005
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 478-488
    • Zhang, M.Q.1    Wilkinson, B.2
  • 154
    • 0037208308 scopus 로고    scopus 로고
    • Property distributions: Differences between drugs, natural products, and molecules from combinatorial chemistry
    • 10.1021/ci0200467
    • M. Feher, and J.M. Schmidt Property distributions: differences between drugs, natural products, and molecules from combinatorial chemistry J Chem Inform Comput Sci 43 2003 218 227 10.1021/ci0200467
    • (2003) J Chem Inform Comput Sci , vol.43 , pp. 218-227
    • Feher, M.1    Schmidt, J.M.2
  • 155
    • 0035347869 scopus 로고    scopus 로고
    • Scaffold architecture and pharmacophoric properties of natural products and trade drugs: Application in the design of natural product-based combinatorial libraries
    • M.L. Lee, and G. Schneider Scaffold architecture and pharmacophoric properties of natural products and trade drugs: application in the design of natural product-based combinatorial libraries J Comb Chem 3 2001 284 289
    • (2001) J Comb Chem , vol.3 , pp. 284-289
    • Lee, M.L.1    Schneider, G.2
  • 156
    • 66149148225 scopus 로고    scopus 로고
    • Chemoinformatic analysis of combinatorial libraries, drugs, natural products, and molecular libraries small molecule repository
    • 10.1021/ci800426u
    • N. Singh, R. Guha, M.A. Giulianotti, C. Pinilla, R.A. Houghten, and J.L. Medina-Franco Chemoinformatic analysis of combinatorial libraries, drugs, natural products, and molecular libraries small molecule repository J Chem Inf Model 49 2009 1010 1024 10.1021/ci800426u
    • (2009) J Chem Inf Model , vol.49 , pp. 1010-1024
    • Singh, N.1    Guha, R.2    Giulianotti, M.A.3    Pinilla, C.4    Houghten, R.A.5    Medina-Franco, J.L.6
  • 157
    • 0037292994 scopus 로고    scopus 로고
    • A structure-permeability study of small drug-like molecules
    • T. Fichert, M. Yazdanian, and J.R. Proudfoot A structure-permeability study of small drug-like molecules Bioorg Med Chem Lett 13 2003 719 722
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 719-722
    • Fichert, T.1    Yazdanian, M.2    Proudfoot, J.R.3
  • 158
    • 33746071900 scopus 로고    scopus 로고
    • A practical view of 'druggability'
    • 10.1016/j.cbpa.2006.06.014
    • T.H. Keller, A. Pichota, and Z. Yin A practical view of 'druggability' Curr Opin Chem Biol 10 2006 357 361 10.1016/j.cbpa.2006.06.014
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 357-361
    • Keller, T.H.1    Pichota, A.2    Yin, Z.3
  • 160
    • 0037404468 scopus 로고    scopus 로고
    • Selection criteria for drug-like compounds
    • 10.1002/med.10041
    • I. Muegge Selection criteria for drug-like compounds Med Res Rev 23 2003 302 321 10.1002/med.10041
    • (2003) Med Res Rev , vol.23 , pp. 302-321
    • Muegge, I.1
  • 161
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • D.F. Veber, S.R. Johnson, H.Y. Cheng, B.R. Smith, K.W. Ward, and K.D. Kopple Molecular properties that influence the oral bioavailability of drug candidates J Med Chem 45 2002 2615 2623
    • (2002) J Med Chem , vol.45 , pp. 2615-2623
    • Veber, D.F.1    Johnson, S.R.2    Cheng, H.Y.3    Smith, B.R.4    Ward, K.W.5    Kopple, K.D.6
  • 162
    • 0037468884 scopus 로고    scopus 로고
    • A comparison of physiochemical property profiles of development and marketed oral drugs
    • 10.1021/jm021053p
    • M.C. Wenlock, R.P. Austin, P. Barton, A.M. Davis, and P.D. Leeson A comparison of physiochemical property profiles of development and marketed oral drugs J Med Chem 46 2003 1250 1256 10.1021/jm021053p
    • (2003) J Med Chem , vol.46 , pp. 1250-1256
    • Wenlock, M.C.1    Austin, R.P.2    Barton, P.3    Davis, A.M.4    Leeson, P.D.5
  • 163
    • 84856405594 scopus 로고    scopus 로고
    • Going further than Lipinski's rule in drug design
    • 10.1517/17460441.2012.648612
    • W.P. Walters Going further than Lipinski's rule in drug design Expert Opin Drug Discov 7 2012 99 107 10.1517/17460441.2012.648612
    • (2012) Expert Opin Drug Discov , vol.7 , pp. 99-107
    • Walters, W.P.1
  • 164
    • 79958851565 scopus 로고    scopus 로고
    • Ligand efficiency indices (LEIs): More than a Simple efficiency Yardstick
    • C. Abad-Zapatero, and D. Blasie Ligand efficiency indices (LEIs): more than a Simple efficiency Yardstick Mol Inform 30 2011 122 132
    • (2011) Mol Inform , vol.30 , pp. 122-132
    • Abad-Zapatero, C.1    Blasie, D.2
  • 165
    • 77957682613 scopus 로고    scopus 로고
    • Ligand efficiency indices for an effective mapping of chemico-biological space: The concept of an atlas-like representation
    • 10.1016/j.drudis.2010.08.004
    • C. Abad-Zapatero, O. Perisic, J. Wass, A.P. Bento, J. Overington, and B. Al-Lazikani Ligand efficiency indices for an effective mapping of chemico-biological space: the concept of an atlas-like representation Drug Discov Today 15 2010 804 811 10.1016/j.drudis.2010.08.004
    • (2010) Drug Discov Today , vol.15 , pp. 804-811
    • Abad-Zapatero, C.1    Perisic, O.2    Wass, J.3    Bento, A.P.4    Overington, J.5    Al-Lazikani, B.6
  • 166
    • 84869506185 scopus 로고    scopus 로고
    • AtlasCBS: A web server to map and explore chemico-biological space
    • 10.1007/s10822-012-9587-5
    • A. Cortes-Cabrera, A. Morreale, F. Gago, and C. Abad-Zapatero AtlasCBS: a web server to map and explore chemico-biological space J Comput-Aided Mol Des 26 2012 995 1003 10.1007/s10822-012-9587-5
    • (2012) J Comput-Aided Mol des , vol.26 , pp. 995-1003
    • Cortes-Cabrera, A.1    Morreale, A.2    Gago, F.3    Abad-Zapatero, C.4
  • 167
    • 36549024945 scopus 로고    scopus 로고
    • A sorcerer's apprentice and the Rule of Five: From rule-of-thumb to commandment and beyond
    • 10.1016/j.drudis.2007.10.022
    • C. Abad-Zapatero A sorcerer's apprentice and the Rule of Five: from rule-of-thumb to commandment and beyond Drug Discov Today 12 2007 995 997 10.1016/j.drudis.2007.10.022
    • (2007) Drug Discov Today , vol.12 , pp. 995-997
    • Abad-Zapatero, C.1
  • 168
    • 6144253216 scopus 로고
    • Strong Inference: Certain systematic methods of scientific thinking may produce much more rapid progress than others
    • 10.1126/science.146.3642.347
    • J.R. Platt Strong Inference: certain systematic methods of scientific thinking may produce much more rapid progress than others Science 146 1964 347 353 10.1126/science.146.3642.347
    • (1964) Science , vol.146 , pp. 347-353
    • Platt, J.R.1
  • 169
    • 84886414806 scopus 로고    scopus 로고
    • Ask the experts: Past, present and future of the rule of five
    • 10.4155/fmc.13.61
    • J. Baell, M. Congreve, P. Leeson, and C. Abad-Zapatero Ask the experts: past, present and future of the rule of five Future Med Chem 5 2013 745 752 10.4155/fmc.13.61
    • (2013) Future Med Chem , vol.5 , pp. 745-752
    • Baell, J.1    Congreve, M.2    Leeson, P.3    Abad-Zapatero, C.4
  • 170
    • 84870813551 scopus 로고    scopus 로고
    • Chris Lipinski. Interview by Peter Kirkpatrick
    • 10.1038/nrd3895
    • C. Lipinski Chris Lipinski. Interview by Peter Kirkpatrick Nat Rev Drug Discov 11 2012 900 901 10.1038/nrd3895
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 900-901
    • Lipinski, C.1
  • 171
    • 0037252194 scopus 로고    scopus 로고
    • Chris Lipinski discusses life and chemistry after the Rule of Five
    • C.A. Lipinski Chris Lipinski discusses life and chemistry after the Rule of Five Drug Discov Today 8 2003 12 16
    • (2003) Drug Discov Today , vol.8 , pp. 12-16
    • Lipinski, C.A.1
  • 172
    • 0029379551 scopus 로고
    • Let's get specific: The relationship between specificity and affinity
    • B.E. Eaton, L. Gold, and D.A. Zichi Let's get specific: the relationship between specificity and affinity Chem Biol 2 1995 633 638
    • (1995) Chem Biol , vol.2 , pp. 633-638
    • Eaton, B.E.1    Gold, L.2    Zichi, D.A.3
  • 173
    • 0033965502 scopus 로고    scopus 로고
    • Chlorobiphenyl-desleucyl-vancomycin inhibits the transglycosylation process required for peptidoglycan synthesis in bacteria in the absence of dipeptide binding
    • R.C. Goldman, E.R. Baizman, C.B. Longley, and A.A. Branstrom Chlorobiphenyl-desleucyl-vancomycin inhibits the transglycosylation process required for peptidoglycan synthesis in bacteria in the absence of dipeptide binding FEMS Microbiol Lett 183 2000 209 214
    • (2000) FEMS Microbiol Lett , vol.183 , pp. 209-214
    • Goldman, R.C.1    Baizman, E.R.2    Longley, C.B.3    Branstrom, A.A.4
  • 174
    • 0034987305 scopus 로고    scopus 로고
    • Synthesis of hydrophobic N'-mono and N', N-double alkylated eremomycins inhibiting the transglycosylation stage of bacterial cell wall biosynthesis
    • A.Y. Pavlov, O.V. Miroshnikova, S.S. Printsevskaya, E.N. Olsufyeva, M.N. Preobrazhenskaya, and R.C. Goldman Synthesis of hydrophobic N'-mono and N', N-double alkylated eremomycins inhibiting the transglycosylation stage of bacterial cell wall biosynthesis J Antibiot 54 2001 455 459
    • (2001) J Antibiot , vol.54 , pp. 455-459
    • Pavlov, A.Y.1    Miroshnikova, O.V.2    Printsevskaya, S.S.3    Olsufyeva, E.N.4    Preobrazhenskaya, M.N.5    Goldman, R.C.6
  • 175
    • 0037075809 scopus 로고    scopus 로고
    • Synthesis and mode of action of hydrophobic derivatives of the glycopeptide antibiotic eremomycin and des-(N-methyl-D-leucyl)eremomycin against glycopeptide-sensitive and -resistant bacteria
    • S.S. Printsevskaya, A.Y. Pavlov, E.N. Olsufyeva, E.P. Mirchink, E.B. Isakova, and M.I. Reznikova Synthesis and mode of action of hydrophobic derivatives of the glycopeptide antibiotic eremomycin and des-(N-methyl-D- leucyl)eremomycin against glycopeptide-sensitive and -resistant bacteria J Med Chem 45 2002 1340 1347
    • (2002) J Med Chem , vol.45 , pp. 1340-1347
    • Printsevskaya, S.S.1    Pavlov, A.Y.2    Olsufyeva, E.N.3    Mirchink, E.P.4    Isakova, E.B.5    Reznikova, M.I.6
  • 176
    • 0035850868 scopus 로고    scopus 로고
    • Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin
    • 10.1126/science.1063611
    • U.S. Eggert, N. Ruiz, B.V. Falcone, A.A. Branstrom, R.C. Goldman, and T.J. Silhavy Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin Science 294 2001 361 364 10.1126/science.1063611
    • (2001) Science , vol.294 , pp. 361-364
    • Eggert, U.S.1    Ruiz, N.2    Falcone, B.V.3    Branstrom, A.A.4    Goldman, R.C.5    Silhavy, T.J.6
  • 177
    • 58149475508 scopus 로고    scopus 로고
    • Backbone structure of a small helical integral membrane protein: A unique structural characterization
    • 10.1002/pro.24
    • R.C. Page, S. Lee, J.D. Moore, S.J. Opella, and T.A. Cross Backbone structure of a small helical integral membrane protein: a unique structural characterization Protein Sci Pub Protein Soc 18 2009 134 146 10.1002/pro.24
    • (2009) Protein Sci Pub Protein Soc , vol.18 , pp. 134-146
    • Page, R.C.1    Lee, S.2    Moore, J.D.3    Opella, S.J.4    Cross, T.A.5
  • 178
    • 67650173033 scopus 로고    scopus 로고
    • Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis
    • 10.1074/jbc.M901581200
    • J. Hu, M. Sharma, H. Qin, F.P. Gao, and T.A. Cross Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis J Biol Chem 284 2009 15619 15628 10.1074/jbc.M901581200
    • (2009) J Biol Chem , vol.284 , pp. 15619-15628
    • Hu, J.1    Sharma, M.2    Qin, H.3    Gao, F.P.4    Cross, T.A.5
  • 179
    • 44449145917 scopus 로고    scopus 로고
    • Construction of a series of vectors for high throughput cloning and expression screening of membrane proteins from Mycobacterium tuberculosis
    • 10.1186/1472-6750-8-51
    • H. Qin, J. Hu, Y. Hua, S.V. Challa, T.A. Cross, and F.P. Gao Construction of a series of vectors for high throughput cloning and expression screening of membrane proteins from Mycobacterium tuberculosis BMC Biotechnol 8 2008 51 10.1186/1472-6750-8-51
    • (2008) BMC Biotechnol , vol.8 , pp. 51
    • Qin, H.1    Hu, J.2    Hua, Y.3    Challa, S.V.4    Cross, T.A.5    Gao, F.P.6
  • 180
    • 69149100344 scopus 로고    scopus 로고
    • 1H, 15N and 13C backbone resonance assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis
    • 10.1007/s12104-008-9081-0
    • H.B. Nguyen, and T.A. Cross 1H, 15N and 13C backbone resonance assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis Biomol NMR Assign 2 2008 47 49 10.1007/s12104-008-9081-0
    • (2008) Biomol NMR Assign , vol.2 , pp. 47-49
    • Nguyen, H.B.1    Cross, T.A.2
  • 181
    • 34247844400 scopus 로고    scopus 로고
    • Uniformly aligned full-length membrane proteins in liquid crystalline bilayers for structural characterization
    • 10.1021/ja068402f
    • C. Li, P. Gao, H. Qin, R. Chase, P.L. Gor'kov, and W.W. Brey Uniformly aligned full-length membrane proteins in liquid crystalline bilayers for structural characterization J Am Chem Soc 129 2007 5304 5305 10.1021/ja068402f
    • (2007) J Am Chem Soc , vol.129 , pp. 5304-5305
    • Li, C.1    Gao, P.2    Qin, H.3    Chase, R.4    Gor'Kov, P.L.5    Brey, W.W.6
  • 182
    • 33847145336 scopus 로고    scopus 로고
    • Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein
    • 10.1016/j.pep.2006.11.022
    • A. Korepanova, J.D. Moore, H.B. Nguyen, Y. Hua, T.A. Cross, and F. Gao Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein Protein Expr Purif 53 2007 24 30 10.1016/j.pep.2006.11.022
    • (2007) Protein Expr Purif , vol.53 , pp. 24-30
    • Korepanova, A.1    Moore, J.D.2    Nguyen, H.B.3    Hua, Y.4    Cross, T.A.5    Gao, F.6
  • 183
    • 34748899645 scopus 로고    scopus 로고
    • Structural biology of transmembrane domains: Efficient production and characterization of transmembrane peptides by NMR
    • 10.1110/ps.072996707
    • J. Hu, H. Qin, C. Li, M. Sharma, T.A. Cross, and F.P. Gao Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR Protein Sci Pub Protein Soc 16 2007 2153 2165 10.1110/ps.072996707
    • (2007) Protein Sci Pub Protein Soc , vol.16 , pp. 2153-2165
    • Hu, J.1    Qin, H.2    Li, C.3    Sharma, M.4    Cross, T.A.5    Gao, F.P.6
  • 184
    • 20844432340 scopus 로고    scopus 로고
    • Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry
    • 10.1021/pr0500049
    • Y. Xiong, M.J. Chalmers, F.P. Gao, T.A. Cross, and A.G. Marshall Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry J Proteome Res 4 2005 855 861 10.1021/pr0500049
    • (2005) J Proteome Res , vol.4 , pp. 855-861
    • Xiong, Y.1    Chalmers, M.J.2    Gao, F.P.3    Cross, T.A.4    Marshall, A.G.5
  • 185
    • 11144234979 scopus 로고    scopus 로고
    • Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli
    • 10.1110/ps.041022305
    • A. Korepanova, F.P. Gao, Y. Hua, H. Qin, R.K. Nakamoto, and T.A. Cross Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli Protein Sci Pub Protein Soc 14 2005 148 158 10.1110/ps.041022305
    • (2005) Protein Sci Pub Protein Soc , vol.14 , pp. 148-158
    • Korepanova, A.1    Gao, F.P.2    Hua, Y.3    Qin, H.4    Nakamoto, R.K.5    Cross, T.A.6
  • 186
    • 84857770864 scopus 로고    scopus 로고
    • Daptomycin: A review of properties, clinical use, drug delivery and resistance
    • C. Vilhena, and A. Bettencourt Daptomycin: a review of properties, clinical use, drug delivery and resistance Mini Rev Med Chem 12 2012 202 209
    • (2012) Mini Rev Med Chem , vol.12 , pp. 202-209
    • Vilhena, C.1    Bettencourt, A.2
  • 188
    • 78149493797 scopus 로고    scopus 로고
    • Amphotericin B membrane action: Role for two types of ion channels in eliciting cell survival and lethal effects
    • 10.1007/s00232-010-9313-y
    • B.E. Cohen Amphotericin B membrane action: role for two types of ion channels in eliciting cell survival and lethal effects J Membr Biol 238 2010 1 20 10.1007/s00232-010-9313-y
    • (2010) J Membr Biol , vol.238 , pp. 1-20
    • Cohen, B.E.1
  • 189
    • 44449116133 scopus 로고    scopus 로고
    • Cellular pharmacokinetics of telavancin, a novel lipoglycopeptide antibiotic, and analysis of lysosomal changes in cultured eukaryotic cells (J774 mouse macrophages and rat embryonic fibroblasts)
    • 10.1093/jac/dkn120
    • M. Barcia-Macay, F. Mouaden, M.P. Mingeot-Leclercq, P.M. Tulkens, and F. Van Bambeke Cellular pharmacokinetics of telavancin, a novel lipoglycopeptide antibiotic, and analysis of lysosomal changes in cultured eukaryotic cells (J774 mouse macrophages and rat embryonic fibroblasts) J Antimicrobial Chemother 61 2008 1288 1294 10.1093/jac/dkn120
    • (2008) J Antimicrobial Chemother , vol.61 , pp. 1288-1294
    • Barcia-Macay, M.1    Mouaden, F.2    Mingeot-Leclercq, M.P.3    Tulkens, P.M.4    Van Bambeke, F.5
  • 190
    • 18244402385 scopus 로고    scopus 로고
    • Mixed-lipid storage disorder induced in macrophages and fibroblasts by oritavancin (LY333328), a new glycopeptide antibiotic with exceptional cellular accumulation
    • 10.1128/AAC.49.5.1695-1700.2005
    • F. Van Bambeke, J. Saffran, M.P. Mingeot-Leclercq, and P.M. Tulkens Mixed-lipid storage disorder induced in macrophages and fibroblasts by oritavancin (LY333328), a new glycopeptide antibiotic with exceptional cellular accumulation Antimicrobial Agents Chemother 49 2005 1695 1700 10.1128/AAC.49.5.1695-1700.2005
    • (2005) Antimicrobial Agents Chemother , vol.49 , pp. 1695-1700
    • Van Bambeke, F.1    Saffran, J.2    Mingeot-Leclercq, M.P.3    Tulkens, P.M.4
  • 191
    • 55449112796 scopus 로고    scopus 로고
    • Pre-clinical experience with daptomycin
    • 10.1093/jac/dkn367
    • P.M. Hawkey Pre-clinical experience with daptomycin J Antimicrobial Chemother 62 Suppl. 3 2008 iii7 14 10.1093/jac/dkn367
    • (2008) J Antimicrobial Chemother , vol.62 , Issue.SUPPL. 3 , pp. 7-14
    • Hawkey, P.M.1


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