메뉴 건너뛰기




Volumn 7, Issue 287, 2015, Pages

Classic reaction kinetics can explain complex patterns of antibiotic action

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC SENSITIVITY; ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL GROWTH; BACTERICIDAL ACTIVITY; BINDING KINETICS; CELL TRANSFORMATION; CHEMICAL BINDING; CHEMICAL REACTION KINETICS; CONCENTRATION RESPONSE; CONTROLLED STUDY; ESCHERICHIA COLI; GROWTH INHIBITION; MATHEMATICAL MODEL; MICROBIAL POPULATION DYNAMICS; NONHUMAN; PRIORITY JOURNAL; THEORETICAL MODEL; TUBERCULOSIS; VIBRIO CHOLERAE; DRUG EFFECTS; KINETICS; MICROBIAL SENSITIVITY TEST;

EID: 84929648835     PISSN: 19466234     EISSN: 19466242     Source Type: Journal    
DOI: 10.1126/scitranslmed.aaa8760     Document Type: Article
Times cited : (56)

References (82)
  • 2
    • 2142760947 scopus 로고    scopus 로고
    • Antimicrobial pharmacodynamics: Critical interactions of "bug and drug"
    • G. L. Drusano, Antimicrobial pharmacodynamics: Critical interactions of "bug and drug". Nat. Rev. Microbiol. 2, 289-300 (2004).
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 289-300
    • Drusano, G.L.1
  • 3
    • 44449148293 scopus 로고    scopus 로고
    • The impact of medication regimen factors on adherence to chronic treatment: A review of literature
    • K. S. Ingersoll, J. Cohen, The impact of medication regimen factors on adherence to chronic treatment: A review of literature. J. Behav. Med. 31, 213-224 (2008).
    • (2008) J. Behav. Med. , vol.31 , pp. 213-224
    • Ingersoll, K.S.1    Cohen, J.2
  • 4
    • 70349634546 scopus 로고    scopus 로고
    • Effect of duration and intermittency of rifampin on tuberculosis treatment outcomes: A systematic review and meta-analysis
    • D. Menzies, A. Benedetti, A. Paydar, I. Martin, S. Royce, M. Pai, A. Vernon, C. Lienhardt, W. Burman, Effect of duration and intermittency of rifampin on tuberculosis treatment outcomes: A systematic review and meta-analysis. PLOS Med. 6, e1000146 (2009).
    • (2009) PLOS Med. , vol.6 , pp. e1000146
    • Menzies, D.1    Benedetti, A.2    Paydar, A.3    Martin, I.4    Royce, S.5    Pai, M.6    Vernon, A.7    Lienhardt, C.8    Burman, W.9
  • 5
    • 80054123332 scopus 로고    scopus 로고
    • Treatment of tuberculosis and optimal dosing schedules
    • K. C. Chang, C. C. Leung, J. Grosset, W. W. Yew, Treatment of tuberculosis and optimal dosing schedules. Thorax 66, 997-1007 (2011).
    • (2011) Thorax , vol.66 , pp. 997-1007
    • Chang, K.C.1    Leung, C.C.2    Grosset, J.3    Yew, W.W.4
  • 6
    • 84903756577 scopus 로고    scopus 로고
    • Intermittent versus daily therapy for treating tuberculosis in children
    • A. Bose, S. Kalita, W. Rose, P. Tharyan, Intermittent versus daily therapy for treating tuberculosis in children. Cochrane Database Syst. Rev. 1, CD007953 (2014).
    • (2014) Cochrane Database Syst. Rev. , vol.1 , pp. CD007953
    • Bose, A.1    Kalita, S.2    Rose, W.3    Tharyan, P.4
  • 7
    • 84862530678 scopus 로고    scopus 로고
    • Malachite green interferes with postantibiotic recovery of mycobacteria
    • E. Gelman, J. D. McKinney, N. Dhar, Malachite green interferes with postantibiotic recovery of mycobacteria. Antimicrob. Agents Chemother. 56, 3610-3614 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 3610-3614
    • Gelman, E.1    McKinney, J.D.2    Dhar, N.3
  • 8
    • 0027236995 scopus 로고
    • Studies on the postantibiotic effect and the postantibiotic sub-MIC effect of meropenem
    • I. Odenholt-Tornqvist, Studies on the postantibiotic effect and the postantibiotic sub-MIC effect of meropenem. J. Antimicrob. Chemother. 31, 881-892 (1993).
    • (1993) J. Antimicrob. Chemother. , vol.31 , pp. 881-892
    • Odenholt-Tornqvist, I.1
  • 9
    • 84877267006 scopus 로고    scopus 로고
    • Advances in the development of new tuberculosis drugs and treatment regimens
    • A. Zumla, P. Nahid, S. T. Cole, Advances in the development of new tuberculosis drugs and treatment regimens. Nat. Rev. Drug Discov. 12, 388-404 (2013).
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 388-404
    • Zumla, A.1    Nahid, P.2    Cole, S.T.3
  • 11
    • 62549089300 scopus 로고    scopus 로고
    • Functional relationship between bacterial cell density and the efficacy of antibiotics
    • K. I. Udekwu, N. Parrish, P. Ankomah, F. Baquero, B. R. Levin, Functional relationship between bacterial cell density and the efficacy of antibiotics. J. Antimicrob. Chemother. 63, 745-757 (2009).
    • (2009) J. Antimicrob. Chemother. , vol.63 , pp. 745-757
    • Udekwu, K.I.1    Parrish, N.2    Ankomah, P.3    Baquero, F.4    Levin, B.R.5
  • 13
    • 0016789374 scopus 로고
    • Effect of inoculum and of beta-lactamase on the anti-staphylococcal activity of thirteen penicillins and cephalosporins
    • L. D. Sabath, C. Garner, C. Wilcox, M. Finland, Effect of inoculum and of beta-lactamase on the anti-staphylococcal activity of thirteen penicillins and cephalosporins. Antimicrob. Agents Chemother. 8, 344-349 (1975).
    • (1975) Antimicrob. Agents Chemother. , vol.8 , pp. 344-349
    • Sabath, L.D.1    Garner, C.2    Wilcox, C.3    Finland, M.4
  • 14
    • 0027285367 scopus 로고
    • Penicillin-binding protein expression at different growth stages determines penicillin efficacy in vitro and in vivo: An explanation for the inoculum effect
    • D. L. Stevens, S. Yan, A. E. Bryant, Penicillin-binding protein expression at different growth stages determines penicillin efficacy in vitro and in vivo: An explanation for the inoculum effect. J. Infect. Dis. 167, 1401-1405 (1993).
    • (1993) J. Infect. Dis. , vol.167 , pp. 1401-1405
    • Stevens, D.L.1    Yan, S.2    Bryant, A.E.3
  • 17
    • 84903279007 scopus 로고    scopus 로고
    • A retrospective analysis of the duration of oral antibiotic therapy for the treatment of acne among adolescents: Investigating practice gaps and potential cost-savings
    • Y. H. Lee, G. Liu, D. M. Thiboutot, D. L. Leslie, J. S. Kirby, A retrospective analysis of the duration of oral antibiotic therapy for the treatment of acne among adolescents: Investigating practice gaps and potential cost-savings. J. Am. Acad. Dermatol. 71, 70-76 (2014).
    • (2014) J. Am. Acad. Dermatol. , vol.71 , pp. 70-76
    • Lee, Y.H.1    Liu, G.2    Thiboutot, D.M.3    Leslie, D.L.4    Kirby, J.S.5
  • 18
    • 84900296078 scopus 로고    scopus 로고
    • Comparing short to standard duration of antibiotic therapy for patients hospitalized with cellulitis (DANCE): Study protocol for a randomized controlled trial
    • D. R. Cranendonk, B. C. Opmeer, J. M. Prins, W. J. Wiersinga, Comparing short to standard duration of antibiotic therapy for patients hospitalized with cellulitis (DANCE): Study protocol for a randomized controlled trial. BMC Infect. Dis. 14, 235 (2014).
    • (2014) BMC Infect. Dis. , vol.14 , pp. 235
    • Cranendonk, D.R.1    Opmeer, B.C.2    Prins, J.M.3    Wiersinga, W.J.4
  • 19
    • 84875895689 scopus 로고    scopus 로고
    • Procalcitoninguided algorithm to reduce length of antibiotic therapy in patients with severe sepsis and septic shock
    • A. Hohn, S. Schroeder, A. Gehrt, K. Bernhardt, B. Bein, K. Wegscheider, M. Hochreiter, Procalcitoninguided algorithm to reduce length of antibiotic therapy in patients with severe sepsis and septic shock. BMC Infect. Dis. 13, 158 (2013).
    • (2013) BMC Infect. Dis. , vol.13 , pp. 158
    • Hohn, A.1    Schroeder, S.2    Gehrt, A.3    Bernhardt, K.4    Bein, B.5    Wegscheider, K.6    Hochreiter, M.7
  • 21
    • 84890257761 scopus 로고    scopus 로고
    • Short-vs long-duration antibiotic regimens for ventilator-associated pneumonia: A systematic review and meta-analysis
    • G. Dimopoulos, G. Poulakou, I. A. Pneumatikos, A. Armaganidis, M. H. Kollef, D. K. Matthaiou, Short-vs long-duration antibiotic regimens for ventilator-associated pneumonia: A systematic review and meta-analysis. Chest 144, 1759-1767 (2013).
    • (2013) Chest , vol.144 , pp. 1759-1767
    • Dimopoulos, G.1    Poulakou, G.2    Pneumatikos, I.A.3    Armaganidis, A.4    Kollef, M.H.5    Matthaiou, D.K.6
  • 22
    • 0032481410 scopus 로고    scopus 로고
    • Low dosage and long treatment duration of β-lactam: Risk factors for carriage of penicillin-resistant Streptococcus pneumoniae
    • D. Guillemot, C. Carbon, B. Balkau, P. Geslin, H. Lecoeur, F. Vauzelle-Kervroëdan, G. Bouvenot, E. Eschwége, Low dosage and long treatment duration of β-lactam: Risk factors for carriage of penicillin-resistant Streptococcus pneumoniae. JAMA 279, 365-370 (1998).
    • (1998) JAMA , vol.279 , pp. 365-370
    • Guillemot, D.1    Carbon, C.2    Balkau, B.3    Geslin, P.4    Lecoeur, H.5    Vauzelle-Kervroëdan, F.6    Bouvenot, G.7    Eschwége, E.8
  • 25
    • 84879072389 scopus 로고    scopus 로고
    • Microbial persistence and the road to drug resistance
    • N. R. Cohen, M. A. Lobritz, J. J. Collins, Microbial persistence and the road to drug resistance. Cell Host Microbe 13, 632-642 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 632-642
    • Cohen, N.R.1    Lobritz, M.A.2    Collins, J.J.3
  • 26
    • 74249107300 scopus 로고    scopus 로고
    • SOS response induces persistence to fluoroquinolones in Escherichia coli
    • T. Dörr, K. Lewis, M. Vulic, SOS response induces persistence to fluoroquinolones in Escherichia coli. PLOS Genet. 5, e1000760 (2009).
    • (2009) PLOS Genet. , vol.5 , pp. e1000760
    • Dörr, T.1    Lewis, K.2    Vulic, M.3
  • 29
    • 84873485631 scopus 로고    scopus 로고
    • Pharmacodynamics, population dynamics, and the evolution of persistence in Staphylococcus aureus
    • P. J. T. Johnson, B. R. Levin, Pharmacodynamics, population dynamics, and the evolution of persistence in Staphylococcus aureus. PLOS Genet. 9, e1003123 (2013).
    • (2013) PLOS Genet. , vol.9 , pp. e1003123
    • Johnson, P.J.T.1    Levin, B.R.2
  • 32
    • 77649174212 scopus 로고    scopus 로고
    • Ciprofloxacin causes persister formation by inducing the TisB toxin in Escherichia coli
    • T. Dörr, M. Vulic, K. Lewis, Ciprofloxacin causes persister formation by inducing the TisB toxin in Escherichia coli. PLOS Biol. 8, e1000317 (2010).
    • (2010) PLOS Biol. , vol.8 , pp. e1000317
    • Dörr, T.1    Vulic, M.2    Lewis, K.3
  • 33
    • 33845607284 scopus 로고    scopus 로고
    • Persister cells, dormancy and infectious disease
    • K. Lewis, Persister cells, dormancy and infectious disease. Nat. Rev. Microbiol. 5, 48-56 (2007).
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 48-56
    • Lewis, K.1
  • 34
    • 84907879368 scopus 로고    scopus 로고
    • Optimization of lag time underlies antibiotic tolerance in evolved bacterial populations
    • O. Fridman, A. Goldberg, I. Ronin, N. Shoresh, N. Q. Balaban, Optimization of lag time underlies antibiotic tolerance in evolved bacterial populations. Nature 513, 418-421 (2014).
    • (2014) Nature , vol.513 , pp. 418-421
    • Fridman, O.1    Goldberg, A.2    Ronin, I.3    Shoresh, N.4    Balaban, N.Q.5
  • 37
    • 78449268845 scopus 로고    scopus 로고
    • Interdependence of cell growth and gene expression: Origins and consequences
    • M. Scott, C. W. Gunderson, E. M. Mateescu, Z. Zhang, T. Hwa, Interdependence of cell growth and gene expression: Origins and consequences. Science 330, 1099-1102 (2010).
    • (2010) Science , vol.330 , pp. 1099-1102
    • Scott, M.1    Gunderson, C.W.2    Mateescu, E.M.3    Zhang, Z.4    Hwa, T.5
  • 39
    • 0021344577 scopus 로고
    • The postantibiotic effect in the treatment of experimental meningitis caused by Streptococcus pneumoniae in rabbits
    • M. G. Täuber, O. Zak, W. M. Scheld, B. Hengstler, M. A. Sande, The postantibiotic effect in the treatment of experimental meningitis caused by Streptococcus pneumoniae in rabbits. J. Infect. Dis. 149, 575-583 (1984).
    • (1984) J. Infect. Dis. , vol.149 , pp. 575-583
    • Täuber, M.G.1    Zak, O.2    Scheld, W.M.3    Hengstler, B.4    Sande, M.A.5
  • 40
    • 0027154004 scopus 로고
    • Post-antibiotic effects in experimental infection models: Relationship to in-vitro phenomena and to treatment of infections in man
    • W. A. Craig, Post-antibiotic effects in experimental infection models: Relationship to in-vitro phenomena and to treatment of infections in man. J. Antimicrob. Chemother. 31(Suppl. D), 149-158 (1993).
    • (1993) J. Antimicrob. Chemother. , vol.31 , pp. 149-158
    • Craig, W.A.1
  • 42
    • 84862765893 scopus 로고    scopus 로고
    • Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells
    • S. Bakshi, A. Siryaporn, M. Goulian, J. C. Weisshaar, Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells. Mol. Microbiol. 85, 21-38 (2012).
    • (2012) Mol. Microbiol. , vol.85 , pp. 21-38
    • Bakshi, S.1    Siryaporn, A.2    Goulian, M.3    Weisshaar, J.C.4
  • 43
    • 0018399333 scopus 로고
    • The curve doses vs survival time in the evaluation of acute toxicity
    • L. Molinengo, The curve doses vs survival time in the evaluation of acute toxicity. J. Pharm. Pharmacol. 31, 343-344 (1979).
    • (1979) J. Pharm. Pharmacol. , vol.31 , pp. 343-344
    • Molinengo, L.1
  • 44
    • 14844348264 scopus 로고    scopus 로고
    • Molecular insights into aminoglycoside action and resistance
    • S. Magnet, J. S. Blanchard, Molecular insights into aminoglycoside action and resistance. Chem. Rev. 105, 477-498 (2005).
    • (2005) Chem. Rev. , vol.105 , pp. 477-498
    • Magnet, S.1    Blanchard, J.S.2
  • 45
    • 0019218755 scopus 로고
    • In vivo interaction of beta-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae
    • R. Williamson, R. Hakenbeck, A. Tomasz, In vivo interaction of beta-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 18, 629-637 (1980).
    • (1980) Antimicrob. Agents Chemother. , vol.18 , pp. 629-637
    • Williamson, R.1    Hakenbeck, R.2    Tomasz, A.3
  • 46
    • 0028305362 scopus 로고
    • Kinetics of penicillin binding to penicillinbinding proteins of Staphylococcus aureus
    • H. F. Chambers, M. J. Sachdeva, C. J. Hackbarth, Kinetics of penicillin binding to penicillinbinding proteins of Staphylococcus aureus. Biochem. J. 301(Pt. 1), 139-144 (1994).
    • (1994) Biochem. J. , vol.301 , pp. 139-144
    • Chambers, H.F.1    Sachdeva, M.J.2    Hackbarth, C.J.3
  • 47
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • T. J. Dougherty, K. Kennedy, R. E. Kessler, M. J. Pucci, Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli. J. Bacteriol. 178, 6110-6115 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 6110-6115
    • Dougherty, T.J.1    Kennedy, K.2    Kessler, R.E.3    Pucci, M.J.4
  • 48
    • 0029817142 scopus 로고    scopus 로고
    • Simultaneous pharmacodynamic analysis of the lag and bactericidal phases exhibited by beta-lactams against Escherichia coli
    • R. C. Li, Simultaneous pharmacodynamic analysis of the lag and bactericidal phases exhibited by beta-lactams against Escherichia coli. Antimicrob. Agents Chemother. 40, 2306-2310 (1996).
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2306-2310
    • Li, R.C.1
  • 49
    • 58149147307 scopus 로고    scopus 로고
    • A simple screen to identify promoters conferring high levels of phenotypic noise
    • N. E. Freed, O. K. Silander, B. Stecher, A. Böhm, W. D. Hardt, M. Ackermann, A simple screen to identify promoters conferring high levels of phenotypic noise. PLOS Genet. 4, e1000307 (2008).
    • (2008) PLOS Genet. , vol.4 , pp. e1000307
    • Freed, N.E.1    Silander, O.K.2    Stecher, B.3    Böhm, A.4    Hardt, W.D.5    Ackermann, M.6
  • 51
    • 0038628994 scopus 로고    scopus 로고
    • Bactericidal and sterilizing activities of antituberculosis drugs during the first 14 days
    • A. Jindani, C. J. Doré, D. A. Mitchison, Bactericidal and sterilizing activities of antituberculosis drugs during the first 14 days. Am. J. Respir. Crit. Care Med. 167, 1348-1354 (2003).
    • (2003) Am. J. Respir. Crit. Care Med. , vol.167 , pp. 1348-1354
    • Jindani, A.1    Doré, C.J.2    Mitchison, D.A.3
  • 52
    • 0036919977 scopus 로고    scopus 로고
    • Rifampicin concentrations in bronchial mucosa, epithelial lining fluid, alveolar macrophages and serum following a single 600 mg oral dose in patients undergoing fibre-optic bronchoscopy
    • H. M. Ziglam, Rifampicin concentrations in bronchial mucosa, epithelial lining fluid, alveolar macrophages and serum following a single 600 mg oral dose in patients undergoing fibre-optic bronchoscopy. J. Antimicrob. Chemother. 50, 1011-1015 (2002).
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 1011-1015
    • Ziglam, H.M.1
  • 55
    • 84899505083 scopus 로고    scopus 로고
    • Molecular mechanisms underlying bacterial persisters
    • E. Maisonneuve, K. Gerdes, Molecular mechanisms underlying bacterial persisters. Cell 157, 539-548 (2014).
    • (2014) Cell , vol.157 , pp. 539-548
    • Maisonneuve, E.1    Gerdes, K.2
  • 57
    • 84920880232 scopus 로고    scopus 로고
    • Stress and host immunity amplify Mycobacterium tuberculosis phenotypic heterogeneity and induce nongrowing metabolically active forms
    • G. Manina, N. Dhar, J. D. McKinney, Stress and host immunity amplify Mycobacterium tuberculosis phenotypic heterogeneity and induce nongrowing metabolically active forms. Cell Host Microbe 17, 32-46 (2015).
    • (2015) Cell Host Microbe , vol.17 , pp. 32-46
    • Manina, G.1    Dhar, N.2    McKinney, J.D.3
  • 58
    • 66249136447 scopus 로고    scopus 로고
    • Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosis
    • S. L. Spencer, S. Gaudet, J. G. Albeck, J. M. Burke, P. K. Sorger, Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosis. Nature 459, 428-432 (2009).
    • (2009) Nature , vol.459 , pp. 428-432
    • Spencer, S.L.1    Gaudet, S.2    Albeck, J.G.3    Burke, J.M.4    Sorger, P.K.5
  • 59
    • 33745189789 scopus 로고    scopus 로고
    • Non-inherited antibiotic resistance
    • B. R. Levin, D. E. Rozen, Non-inherited antibiotic resistance. Nat. Rev. Microbiol. 4, 556-562 (2006).
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 556-562
    • Levin, B.R.1    Rozen, D.E.2
  • 62
    • 33846814925 scopus 로고    scopus 로고
    • Intracellular growth and drug susceptibility of Mycobacterium tuberculosis in macrophages
    • S. Chanwong, N. Maneekarn, L. Makonkawkeyoon, S. Makonkawkeyoon, Intracellular growth and drug susceptibility of Mycobacterium tuberculosis in macrophages. Tuberculosis 87, 130-133 (2007).
    • (2007) Tuberculosis , vol.87 , pp. 130-133
    • Chanwong, S.1    Maneekarn, N.2    Makonkawkeyoon, L.3    Makonkawkeyoon, S.4
  • 63
    • 77956197501 scopus 로고    scopus 로고
    • Isonicotinic acid hydrazide conversion to isonicotinyl-NAD by catalase-peroxidases
    • B. Wiseman, X. Carpena, M. Feliz, L. J. Donald, M. Pons, I. Fita, P. C. Loewen, Isonicotinic acid hydrazide conversion to isonicotinyl-NAD by catalase-peroxidases. J. Biol. Chem. 285, 26662-26673 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 26662-26673
    • Wiseman, B.1    Carpena, X.2    Feliz, M.3    Donald, L.J.4    Pons, M.5    Fita, I.6    Loewen, P.C.7
  • 64
    • 18344417541 scopus 로고    scopus 로고
    • Use of flow field-flow fractionation for the rapid quantitation of ribosome and ribosomal subunits in Escherichia coli at different protein production conditions
    • M. Nilsson, L. Bülow, K. G. Wahlund, Use of flow field-flow fractionation for the rapid quantitation of ribosome and ribosomal subunits in Escherichia coli at different protein production conditions. Biotechnol. Bioeng. 54, 461-467 (1997).
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 461-467
    • Nilsson, M.1    Bülow, L.2    Wahlund, K.G.3
  • 66
    • 0021298678 scopus 로고
    • The binding of 6-demethylchlortetracycline to 70S, 50S and 30S ribosomal particles: A quantitative study by fluorescence anisotropy
    • B. Epe, P. Woolley, The binding of 6-demethylchlortetracycline to 70S, 50S and 30S ribosomal particles: A quantitative study by fluorescence anisotropy. EMBO J. 3, 121-126 (1984).
    • (1984) EMBO J. , vol.3 , pp. 121-126
    • Epe, B.1    Woolley, P.2
  • 67
    • 42149157706 scopus 로고    scopus 로고
    • Chemical biology of tetracycline antibiotics
    • B. Zakeri, G. D. Wright, Chemical biology of tetracycline antibiotics. Biochem. Cell Biol. 86, 124-136 (2008).
    • (2008) Biochem. Cell Biol. , vol.86 , pp. 124-136
    • Zakeri, B.1    Wright, G.D.2
  • 69
    • 0017671181 scopus 로고
    • Ribosome-tetracycline interactions
    • T. R. Tritton, Ribosome-tetracycline interactions. Biochemistry 16, 4133-4138 (1977).
    • (1977) Biochemistry , vol.16 , pp. 4133-4138
    • Tritton, T.R.1
  • 70
    • 0021992123 scopus 로고
    • Mechanism of action of gentamicin components. Characteristics of their binding to Escherichia coli ribosomes
    • F. Tangy, M. Moukkadem, E. Vindimian, M. L. Capmau, F. Le Goffic, Mechanism of action of gentamicin components. Characteristics of their binding to Escherichia coli ribosomes. Eur. J. Biochem. 147, 381-386 (1985).
    • (1985) Eur. J. Biochem. , vol.147 , pp. 381-386
    • Tangy, F.1    Moukkadem, M.2    Vindimian, E.3    Capmau, M.L.4    Le Goffic, F.5
  • 71
    • 67651002917 scopus 로고    scopus 로고
    • Fluorescently labeled ribosomes as a tool for analyzing antibiotic binding
    • B. Llano-Sotelo, R. P. Hickerson, L. Lancaster, H. F. Noller, A. S. Mankin, Fluorescently labeled ribosomes as a tool for analyzing antibiotic binding. RNA 15, 1597-1604 (2009).
    • (2009) RNA , vol.15 , pp. 1597-1604
    • Llano-Sotelo, B.1    Hickerson, R.P.2    Lancaster, L.3    Noller, H.F.4    Mankin, A.S.5
  • 72
    • 0015417692 scopus 로고
    • Binding of dihydrostreptomycin to Escherichia coli ribosomes: Kinetics of the reaction
    • F. N. Chang, J. G. Flaks, Binding of dihydrostreptomycin to Escherichia coli ribosomes: Kinetics of the reaction. Antimicrob. Agents Chemother. 2, 308-319 (1972).
    • (1972) Antimicrob. Agents Chemother. , vol.2 , pp. 308-319
    • Chang, F.N.1    Flaks, J.G.2
  • 73
    • 0017188238 scopus 로고
    • Paromomycin and dihydrostreptomycin binding to Escherichia coli ribosomes
    • D. Lando, M. A. Cousin, T. Ojasoo, J. P. Raymond, Paromomycin and dihydrostreptomycin binding to Escherichia coli ribosomes. Eur. J. Biochem. 66, 597-606 (1976).
    • (1976) Eur. J. Biochem. , vol.66 , pp. 597-606
    • Lando, D.1    Cousin, M.A.2    Ojasoo, T.3    Raymond, J.P.4
  • 74
    • 0013096299 scopus 로고
    • Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12
    • B. G. Spratt, Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U. S. A. 72, 2999-3003 (1975).
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 2999-3003
    • Spratt, B.G.1
  • 75
  • 77
    • 68449102172 scopus 로고    scopus 로고
    • Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
    • J. Malmström, M. Beck, A. Schmidt, V. Lange, E. W. Deutsch, R. Aebersold, Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans. Nature 460, 762-765 (2009).
    • (2009) Nature , vol.460 , pp. 762-765
    • Malmström, J.1    Beck, M.2    Schmidt, A.3    Lange, V.4    Deutsch, E.W.5    Aebersold, R.6
  • 78
    • 0017663729 scopus 로고
    • Kinetic studies of the interaction between rifampicin and DNA-dependent RNA polymerase of Escherichia coli
    • W. Wehrli, Kinetic studies of the interaction between rifampicin and DNA-dependent RNA polymerase of Escherichia coli. Eur. J. Biochem. 80, 325-330 (1977).
    • (1977) Eur. J. Biochem. , vol.80 , pp. 325-330
    • Wehrli, W.1
  • 80
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E.coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Y. Taniguchi, P. J. Choi, G. W. Li, H. Chen, M. Babu, J. Hearn, A. Emili, X. S. Xie, Quantifying E.coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 329, 533-538 (2010).
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4    Babu, M.5    Hearn, J.6    Emili, A.7    Xie, X.S.8
  • 81
    • 0033520469 scopus 로고    scopus 로고
    • Spontaneous formation of the bioactive form of the tuberculosis drug isoniazid
    • M. Wilming, K. Johnsson, Spontaneous formation of the bioactive form of the tuberculosis drug isoniazid. Angew. Chem. Int. Ed. Engl. 38, 2588-2590 (1999).
    • (1999) Angew. Chem. Int. Ed. Engl. , vol.38 , pp. 2588-2590
    • Wilming, M.1    Johnsson, K.2
  • 82
    • 0345133299 scopus 로고    scopus 로고
    • The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance
    • R. Rawat, A. Whitty, P. J. Tonge, The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance. Proc. Natl. Acad. Sci. U. S. A. 100, 13881-13886 (2003).
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13881-13886
    • Rawat, R.1    Whitty, A.2    Tonge, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.