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Volumn 31, Issue , 2016, Pages 98-109

Targeting clinically-relevant metallo-β-lactamases: from high-throughput docking to broad-spectrum inhibitors

Author keywords

Antibiotic resistance; docking; metallo lactamase

Indexed keywords

ANTIINFECTIVE AGENT; BETA LACTAMASE INHIBITOR; CEFOXITIN; METALLO BETA LACTAMASE; METALLO BETA LACTAMASE IMP 1; METALLO BETA LACTAMASE NDM 1; METALLO BETA LACTAMASE VIM 2; N (4 ((2 (7 METHOXY 2 METHYLQUINOLIN 4 YL)HYDRAZONO)METHYL)PHENYL)METHANESULFONAMIDE; NF 1810; UNCLASSIFIED DRUG; BETA LACTAMASE;

EID: 84973885466     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.3109/14756366.2016.1172575     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 39049134890 scopus 로고    scopus 로고
    • Metallo beta lactamases in Pseudomonas aeruginosa and Acinetobacter species
    • Gupta V., Metallo beta lactamases in Pseudomonas aeruginosa and Acinetobacter species. Expert Opin Investig Drugs 2008;17:131–43
    • (2008) Expert Opin Investig Drugs , vol.17 , pp. 131-143
    • Gupta, V.1
  • 2
    • 84903457328 scopus 로고    scopus 로고
    • . Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance
    • King AM, Reid-Yu SA, Wang W, et al. Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance. Nature 2014;510:503–6
    • (2014) Nature , vol.510 , pp. 503-506
    • King, A.M.1    Reid-Yu, S.A.2    Wang, W.3
  • 3
    • 57749107808 scopus 로고    scopus 로고
    • Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America
    • Boucher HW, Talbot GH, Bradley JS, et al. Bad bugs, no drugs:no ESKAPE! An update from the Infectious Diseases Society of America. Clin Infect Dis 2009;48:1–12
    • (2009) Clin Infect Dis , vol.48 , pp. 1-12
    • Boucher, H.W.1    Talbot, G.H.2    Bradley, J.S.3
  • 5
    • 79955006138 scopus 로고    scopus 로고
    • Molecular mechanisms of antibiotic resistance
    • Wright GD., Molecular mechanisms of antibiotic resistance. Chem Commun (Camb) 2011;47:4055–61
    • (2011) Chem Commun (Camb) , vol.47 , pp. 4055-4061
    • Wright, G.D.1
  • 6
    • 77950411087 scopus 로고    scopus 로고
    • Cyclobutanone analogues of beta-lactams revisited: insights into conformational requirements for inhibition of serine- and metallo-beta-lactamases
    • Johnson JW, Gretes M, Goodfellow VJ, et al. Cyclobutanone analogues of beta-lactams revisited:insights into conformational requirements for inhibition of serine- and metallo-beta-lactamases. J Am Chem Soc 2010;132:2558–60
    • (2010) J Am Chem Soc , vol.132 , pp. 2558-2560
    • Johnson, J.W.1    Gretes, M.2    Goodfellow, V.J.3
  • 7
    • 52249094198 scopus 로고    scopus 로고
    • Microbiology. Desperately seeking new antibiotics
    • Payne DJ., Microbiology. Desperately seeking new antibiotics. Science 2008;321:1644–5
    • (2008) Science , vol.321 , pp. 1644-1645
    • Payne, D.J.1
  • 8
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone C., Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 2007;74:1686–701
    • (2007) Biochem Pharmacol , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 9
    • 77951060664 scopus 로고    scopus 로고
    • Current challenges in antimicrobial chemotherapy: focus on ss-lactamase inhibition
    • Bebrone C, Lassaux P, Vercheval L, et al. Current challenges in antimicrobial chemotherapy:focus on ss-lactamase inhibition. Drugs 2010;70:651–79
    • (2010) Drugs , vol.70 , pp. 651-679
    • Bebrone, C.1    Lassaux, P.2    Vercheval, L.3
  • 10
    • 85047699610 scopus 로고    scopus 로고
    • . Aspergillomarasmine A, an inhibitor of bacterial metallo-β-lactamases conferring blaNDM and blaVIM resistance
    • von Nussbaum F, Schiffer G. Aspergillomarasmine A, an inhibitor of bacterial metallo-β-lactamases conferring blaNDM and blaVIM resistance. Angew Chem Int Ed Engl 2014;53:11696–8
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 11696-11698
    • von Nussbaum, F.1    Schiffer, G.2
  • 11
    • 33750624074 scopus 로고    scopus 로고
    • Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria
    • Crowder MW, Spencer J, Vila AJ., Metallo-beta-lactamases:novel weaponry for antibiotic resistance in bacteria. Acc Chem Res 2006;39:721–8
    • (2006) Acc Chem Res , vol.39 , pp. 721-728
    • Crowder, M.W.1    Spencer, J.2    Vila, A.J.3
  • 12
    • 78049251829 scopus 로고    scopus 로고
    • . Emergence of metallo-β-lactamase NDM-1-producing multidrug-resistant Escherichia coli in Australia
    • Poirel L, Lagrutta E, Taylor P, et al. Emergence of metallo-β-lactamase NDM-1-producing multidrug-resistant Escherichia coli in Australia. Antimicrob Agents Chemother 2010;54:4914–16
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 4914-4916
    • Poirel, L.1    Lagrutta, E.2    Taylor, P.3
  • 13
    • 84916243301 scopus 로고    scopus 로고
    • . Characterization by phenotypic and genotypic methods of metallo-β-lactamase-producing Pseudomonas aeruginosa isolated from patients with cystic fibrosis
    • Li Y, Zhang X, Wang C, et al. Characterization by phenotypic and genotypic methods of metallo-β-lactamase-producing Pseudomonas aeruginosa isolated from patients with cystic fibrosis. Mol Med Rep 2015;11:494–8
    • (2015) Mol Med Rep , vol.11 , pp. 494-498
    • Li, Y.1    Zhang, X.2    Wang, C.3
  • 14
    • 84931830225 scopus 로고    scopus 로고
    • Diaryl-substituted azolylthioacetamides: inhibitor discovery of New Delhi metallo-beta-lactamase-1 (NDM-1)
    • Zhang YL, Yang KW, Zhou YJ, et al. Diaryl-substituted azolylthioacetamides:inhibitor discovery of New Delhi metallo-beta-lactamase-1 (NDM-1). ChemMedChem 2014;9:2445–8
    • (2014) ChemMedChem , vol.9 , pp. 2445-2448
    • Zhang, Y.L.1    Yang, K.W.2    Zhou, Y.J.3
  • 15
    • 84864413500 scopus 로고    scopus 로고
    • Quinolylhydrazones as novel inhibitors of Plasmodium falciparum serine protease PfSUB1
    • Gemma S, Giovani S, Brindisi M, et al. Quinolylhydrazones as novel inhibitors of Plasmodium falciparum serine protease PfSUB1. Bioorg Med Chem Lett 2012;22:5317–21
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 5317-5321
    • Gemma, S.1    Giovani, S.2    Brindisi, M.3
  • 16
    • 39649092493 scopus 로고    scopus 로고
    • Microwave-assisted synthesis of 4-quinolylhydrazines followed by nickel boride reduction: a convenient approach to 4-aminoquinolines and derivatives
    • Gemma S, Kukreja G, Tripaldi P, et al. Microwave-assisted synthesis of 4-quinolylhydrazines followed by nickel boride reduction:a convenient approach to 4-aminoquinolines and derivatives. Tetrahedron Lett 2008;49:2074–7
    • (2008) Tetrahedron Lett , vol.49 , pp. 2074-2077
    • Gemma, S.1    Kukreja, G.2    Tripaldi, P.3
  • 17
    • 68149129505 scopus 로고    scopus 로고
    • Development of antitubercular compounds based on a 4-quinolylhydrazone scaffold. Further structure-activity relationship studies
    • Gemma S, Savini L, Altarelli M, et al. Development of antitubercular compounds based on a 4-quinolylhydrazone scaffold. Further structure-activity relationship studies. Bioorg Med Chem 2009;17:6063–72
    • (2009) Bioorg Med Chem , vol.17 , pp. 6063-6072
    • Gemma, S.1    Savini, L.2    Altarelli, M.3
  • 18
    • 41649097746 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationship studies of 4-quinolinyl- and 9-acrydinylhydrazones as potent antimalarial agents
    • Fattorusso C, Campiani G, Kukreja G, et al. Design, synthesis, and structure-activity relationship studies of 4-quinolinyl- and 9-acrydinylhydrazones as potent antimalarial agents. J Med Chem 2008;51:1333–43
    • (2008) J Med Chem , vol.51 , pp. 1333-1343
    • Fattorusso, C.1    Campiani, G.2    Kukreja, G.3
  • 20
    • 20444433125 scopus 로고    scopus 로고
    • . New 3- and 4-hydroxyfuranones as anti-oxidants and anti-inflammatory agents
    • Weber V, Rubat C, Duroux E, et al. New 3- and 4-hydroxyfuranones as anti-oxidants and anti-inflammatory agents. Bioorg Med Chem 2005;13:4552–64
    • (2005) Bioorg Med Chem , vol.13 , pp. 4552-4564
    • Weber, V.1    Rubat, C.2    Duroux, E.3
  • 21
    • 72049122106 scopus 로고    scopus 로고
    • Discovery of 2-arylthieno[3,2-d]pyrimidines containing 8-oxa-3-azabi-cyclo[3.2.1]octane in the 4-position as potent inhibitors of mTOR with selectivity over PI3K
    • Verheijen JC, Yu K, Toral-Barza L, et al. Discovery of 2-arylthieno[3,2-d]pyrimidines containing 8-oxa-3-azabi-cyclo[3.2.1]octane in the 4-position as potent inhibitors of mTOR with selectivity over PI3K. Bioorg Med Chem Lett 2010;20:375–9
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 375-379
    • Verheijen, J.C.1    Yu, K.2    Toral-Barza, L.3
  • 22
    • 84886563976 scopus 로고    scopus 로고
    • Discovery of a novel series of potent non-nucleoside inhibitors of hepatitis C virus NS5B
    • Schoenfeld RC, Bourdet DL, Brameld KA, et al. Discovery of a novel series of potent non-nucleoside inhibitors of hepatitis C virus NS5B. J Med Chem 2013;56:8163–82
    • (2013) J Med Chem , vol.56 , pp. 8163-8182
    • Schoenfeld, R.C.1    Bourdet, D.L.2    Brameld, K.A.3
  • 23
    • 51549121525 scopus 로고    scopus 로고
    • Convenient synthesis of primary sulfonamides
    • Greenfield A, Grosanu C., Convenient synthesis of primary sulfonamides. Tetrahedron Lett 2008;49:6300–3
    • (2008) Tetrahedron Lett , vol.49 , pp. 6300-6303
    • Greenfield, A.1    Grosanu, C.2
  • 24
    • 0035966877 scopus 로고    scopus 로고
    • Cardioselective K(ATP) channel blockers derived from a new series of m-anisamidoethylbenzenesulfonylthioureas
    • Englert HC, Gerlach U, Goegelein H, et al. Cardioselective K(ATP) channel blockers derived from a new series of m-anisamidoethylbenzenesulfonylthioureas. J Med Chem 2001;44:1085–98
    • (2001) J Med Chem , vol.44 , pp. 1085-1098
    • Englert, H.C.1    Gerlach, U.2    Goegelein, H.3
  • 25
    • 37349001297 scopus 로고    scopus 로고
    • Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor
    • Yamaguchi Y, Jin W, Matsunaga K, et al. Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor. J Med Chem 2007;50:6647–53
    • (2007) J Med Chem , vol.50 , pp. 6647-6653
    • Yamaguchi, Y.1    Jin, W.2    Matsunaga, K.3
  • 26
    • 37349007671 scopus 로고    scopus 로고
    • The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
    • Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O., The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J Mol Biol 2008;375:604–11
    • (2008) J Mol Biol , vol.375 , pp. 604-611
    • Garcia-Saez, I.1    Docquier, J.D.2    Rossolini, G.M.3    Dideberg, O.4
  • 27
    • 79957618735 scopus 로고    scopus 로고
    • . Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
    • Zhang H, Hao Q. Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism. FASEB J 2011;25:2574–82
    • (2011) FASEB J , vol.25 , pp. 2574-2582
    • Zhang, H.1    Hao, Q.2
  • 28
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor
    • Concha NO, Janson CA, Rowling P, et al. Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor:binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 2000;39:4288–98
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3
  • 29
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, TiradoRives J., Development and testing of the OPLS all atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 1996;118:11225–36
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    TiradoRives, J.3
  • 30
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still WC, Tempczyk A, Hawley RC, Hendrickson T., Semianalytical treatment of solvation for molecular mechanics and dynamics. J Am Chem Soc 1990;112:6127–9
    • (1990) J Am Chem Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 31
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, et al. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997;267:727–48
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 32
    • 84913554344 scopus 로고    scopus 로고
    • Targeting dopamine D and serotonin 5-HT and 5-HT receptors for developing effective antipsychotics: synthesis, biological characterization, and behavioral studies
    • Brindisi M, Butini S, Franceschini S, et al. Targeting dopamine D and serotonin 5-HT and 5-HT receptors for developing effective antipsychotics:synthesis, biological characterization, and behavioral studies. J Med Chem 2014;26:9575–97
    • (2014) J Med Chem , vol.26 , pp. 9575-9597
    • Brindisi, M.1    Butini, S.2    Franceschini, S.3
  • 33
    • 84902481986 scopus 로고    scopus 로고
    • . Disease-modifying anti-Alzheimer's drugs: inhibitors of human cholinesterases interfering with β-amyloid aggregation
    • Brogi S, Butini S, Maramai S, et al. Disease-modifying anti-Alzheimer's drugs:inhibitors of human cholinesterases interfering with β-amyloid aggregation. CNS Neurosci Ther 2014;20:624–32
    • (2014) CNS Neurosci Ther , vol.20 , pp. 624-632
    • Brogi, S.1    Butini, S.2    Maramai, S.3
  • 34
    • 84903957340 scopus 로고    scopus 로고
    • Rational design of the first difluorostatone-based PfSUB1 inhibitors
    • Giovani S, Penzo M, Brogi S, et al. Rational design of the first difluorostatone-based PfSUB1 inhibitors. Bioorg Med Chem Lett 2014;24:3582–6
    • (2014) Bioorg Med Chem Lett , vol.24 , pp. 3582-3586
    • Giovani, S.1    Penzo, M.2    Brogi, S.3
  • 35
    • 0032925064 scopus 로고    scopus 로고
    • Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli
    • Laraki N, Franceschini N, Rossolini GM, et al. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli. Antimicrob Agents Chemother 1999;43:902–6
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 902-906
    • Laraki, N.1    Franceschini, N.2    Rossolini, G.M.3
  • 36
    • 0038335754 scopus 로고    scopus 로고
    • IMP-12, a new plasmid-encoded metallo-beta-lactamase from a Pseudomonas putida clinical isolate
    • Docquier JD, Riccio ML, Mugnaioli C, et al. IMP-12, a new plasmid-encoded metallo-beta-lactamase from a Pseudomonas putida clinical isolate. Antimicrob Agents Chemother 2003;47:1522–8
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1522-1528
    • Docquier, J.D.1    Riccio, M.L.2    Mugnaioli, C.3
  • 37
    • 78650648960 scopus 로고    scopus 로고
    • Genetic context and biochemical characterization of the IMP-18 metallo-beta-lactamase identified in a Pseudomonas aeruginosa isolate from the United States
    • Borgianni L, Prandi S, Salden L, et al. Genetic context and biochemical characterization of the IMP-18 metallo-beta-lactamase identified in a Pseudomonas aeruginosa isolate from the United States. Antimicrob Agents Chemother 2011;55:140–5
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 140-145
    • Borgianni, L.1    Prandi, S.2    Salden, L.3
  • 38
    • 0037329156 scopus 로고    scopus 로고
    • On functional and structural heterogeneity of VIM-type metallo-beta-lactamases
    • Docquier JD, Lamotte-Brasseur J, Galleni M, et al. On functional and structural heterogeneity of VIM-type metallo-beta-lactamases. J Antimicrob Chemother 2003;51:257–66
    • (2003) J Antimicrob Chemother , vol.51 , pp. 257-266
    • Docquier, J.D.1    Lamotte-Brasseur, J.2    Galleni, M.3
  • 39
    • 77955383826 scopus 로고    scopus 로고
    • Mutational analysis of VIM-2 reveals an essential determinant for metallo-beta-lactamase stability and folding
    • Borgianni L, Vandenameele J, Matagne A, et al. Mutational analysis of VIM-2 reveals an essential determinant for metallo-beta-lactamase stability and folding. Antimicrob Agents Chemother 2010;54:3197–204
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 3197-3204
    • Borgianni, L.1    Vandenameele, J.2    Matagne, A.3
  • 40
    • 84997592591 scopus 로고    scopus 로고
    • Clinical Laboratory Standard Institute. Performance standards for antimicrobial disk susceptibility tests; approved standard—Twelfth Edition (M02-A12). Wayne, PA, USA; 2015
    • (2015)
  • 41
    • 43049135206 scopus 로고    scopus 로고
    • Tetrafluoroboric acid adsorbed on silica gel as a reusable heterogeneous dual-purpose catalyst for conversion of aldehydes/ketones into acetals/ketals and back again
    • Kumar D, Kumar R, Chakraborti AK., Tetrafluoroboric acid adsorbed on silica gel as a reusable heterogeneous dual-purpose catalyst for conversion of aldehydes/ketones into acetals/ketals and back again. Synthesis 2008;1249–56
    • (2008) Synthesis , pp. 1249-1256
    • Kumar, D.1    Kumar, R.2    Chakraborti, A.K.3
  • 42
    • 84929000082 scopus 로고    scopus 로고
    • Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking
    • Brindisi M, Brogi S, Relitti N, et al. Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking. Scientific Rep 2015;5
    • (2015) Scientific Rep , vol.5
    • Brindisi, M.1    Brogi, S.2    Relitti, N.3
  • 43
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC., Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J Mol Biol 1995;245:43–53
    • (1995) J Mol Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 44
    • 3042631515 scopus 로고    scopus 로고
    • Update of the standard numbering scheme for class B beta-lactamases
    • Garau G, Garcia-Saez I, Bebrone C, et al. Update of the standard numbering scheme for class B beta-lactamases. Antimicrob Agents Chemother 2004;48:2347–9
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2347-2349
    • Garau, G.1    Garcia-Saez, I.2    Bebrone, C.3
  • 45
    • 0036024720 scopus 로고    scopus 로고
    • Acridine derivatives as chemotherapeutic agents
    • Denny WA., Acridine derivatives as chemotherapeutic agents. Curr Med Chem 2002;9:1655–65
    • (2002) Curr Med Chem , vol.9 , pp. 1655-1665
    • Denny, W.A.1
  • 46
    • 84861189060 scopus 로고    scopus 로고
    • Synthesis and cytotoxic activity of new acridine-thiazolidine derivatives
    • Barros FW, Silva TG, da Rocha Pitta MG, et al. Synthesis and cytotoxic activity of new acridine-thiazolidine derivatives. Bioorg Med Chem 2012;20:3533–9
    • (2012) Bioorg Med Chem , vol.20 , pp. 3533-3539
    • Barros, F.W.1    Silva, T.G.2    da Rocha Pitta, M.G.3
  • 47
    • 84890458088 scopus 로고    scopus 로고
    • Multifunctional cholinesterase and amyloid beta fibrillization modulators. Synthesis and biological investigation
    • Butini S, Brindisi M, Brogi S, et al. Multifunctional cholinesterase and amyloid beta fibrillization modulators. Synthesis and biological investigation. ACS Med Chem Lett 2013;4:1178–82
    • (2013) ACS Med Chem Lett , vol.4 , pp. 1178-1182
    • Butini, S.1    Brindisi, M.2    Brogi, S.3
  • 48
    • 84916602272 scopus 로고    scopus 로고
    • Novel tetrahydroacridine derivatives inhibit human lung adenocarcinoma cell growth by inducing G1 phase cell cycle arrest and apoptosis
    • Olszewska P, Mikiciuk-Olasik E, Blaszczak-Swiatkiewicz K, et al. Novel tetrahydroacridine derivatives inhibit human lung adenocarcinoma cell growth by inducing G1 phase cell cycle arrest and apoptosis. Biomed Pharmacother 2014;68:959–67
    • (2014) Biomed Pharmacother , vol.68 , pp. 959-967
    • Olszewska, P.1    Mikiciuk-Olasik, E.2    Blaszczak-Swiatkiewicz, K.3


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