메뉴 건너뛰기




Volumn 116, Issue 16, 2016, Pages 9162-9236

Plant Natural Products Targeting Bacterial Virulence Factors

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL COMPOUNDS; CHEMOTHERAPY; METABOLITES; MICROORGANISMS;

EID: 84983627549     PISSN: 00092665     EISSN: 15206890     Source Type: Journal    
DOI: 10.1021/acs.chemrev.6b00184     Document Type: Review
Times cited : (359)

References (374)
  • 2
    • 10944272743 scopus 로고    scopus 로고
    • Antibacterial resistance worldwide: Causes, challenges and responses
    • Levy, S. B.; Marshall, B. Antibacterial resistance worldwide: causes, challenges and responses Nat. Med. 2004, 10 (12s) S122-S129 10.1038/nm1145
    • (2004) Nat. Med. , vol.10 , Issue.12 S , pp. S122-S129
    • Levy, S.B.1    Marshall, B.2
  • 6
    • 73849093228 scopus 로고    scopus 로고
    • Safety and pharmacokinetics of urtoxazumab, a humanized monoclonal antibody, against Shiga-like toxin 2 in healthy adults and in pediatric patients infected with Shiga-like toxin-producing Escherichia coli
    • López, E. L.; Contrini, M. M.; Glatstein, E.; González Ayala, S.; Santoro, R.; Allende, D.; Ezcurra, G.; Teplitz, E.; Koyama, T.; Matsumoto, Y. et al. Safety and pharmacokinetics of urtoxazumab, a humanized monoclonal antibody, against shiga-like toxin 2 in healthy adults and in pediatric patients infected with shiga-like toxin-producing Escherichia coli Antimicrob. Agents Chemother. 2010, 54 (1) 239-243 10.1128/AAC.00343-09
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.1 , pp. 239-243
    • López, E.L.1    Contrini, M.M.2    Glatstein, E.3    González Ayala, S.4    Santoro, R.5    Allende, D.6    Ezcurra, G.7    Teplitz, E.8    Koyama, T.9    Matsumoto, Y.10
  • 8
    • 84876002671 scopus 로고    scopus 로고
    • Natural products: A continuing source of novel drug leads
    • Cragg, G. M.; Newman, D. J. Natural products: a continuing source of novel drug leads Biochim. Biophys. Acta, Gen. Subj. 2013, 1830 (6) 3670-3695 10.1016/j.bbagen.2013.02.008
    • (2013) Biochim. Biophys. Acta, Gen. Subj. , vol.1830 , Issue.6 , pp. 3670-3695
    • Cragg, G.M.1    Newman, D.J.2
  • 9
    • 77952495893 scopus 로고    scopus 로고
    • Development of novel drugs from marine surface associated microorganisms
    • Penesyan, A.; Kjelleberg, S.; Egan, S. Development of novel drugs from marine surface associated microorganisms Mar. Drugs 2010, 8 (3) 438-459 10.3390/md8030438
    • (2010) Mar. Drugs , vol.8 , Issue.3 , pp. 438-459
    • Penesyan, A.1    Kjelleberg, S.2    Egan, S.3
  • 10
    • 84858308226 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the 30 years from 1981 to 2010
    • Newman, D. J.; Cragg, G. M. Natural products as sources of new drugs over the 30 years from 1981 to 2010 J. Nat. Prod. 2012, 75 (3) 311-335 10.1021/np200906s
    • (2012) J. Nat. Prod. , vol.75 , Issue.3 , pp. 311-335
    • Newman, D.J.1    Cragg, G.M.2
  • 11
    • 84944174789 scopus 로고    scopus 로고
    • Anti-parasite drugs sweep Nobel prize in medicine 2015
    • Callaway, E.; Cyranoski, D. Anti-parasite drugs sweep Nobel prize in medicine 2015 Nature 2015, 526 (7572) 174-175 10.1038/nature.2015.18507
    • (2015) Nature , vol.526 , Issue.7572 , pp. 174-175
    • Callaway, E.1    Cyranoski, D.2
  • 12
    • 0032765708 scopus 로고    scopus 로고
    • Trade-offs in plant defense against pathogens and herbivores: A field demonstration of chemical elicitors of induced resistance
    • Thaler, J.; Fidantsef, A.; Duffey, S.; Bostock, R. Trade-offs in plant defense against pathogens and herbivores: a field demonstration of chemical elicitors of induced resistance J. Chem. Ecol. 1999, 25 (7) 1597-1609 10.1023/A:1020840900595
    • (1999) J. Chem. Ecol. , vol.25 , Issue.7 , pp. 1597-1609
    • Thaler, J.1    Fidantsef, A.2    Duffey, S.3    Bostock, R.4
  • 13
    • 0035070998 scopus 로고    scopus 로고
    • Quorum sensing as an integral component of gene regulatory networks in Gram-negative bacteria
    • Withers, H.; Swift, S.; Williams, P. Quorum sensing as an integral component of gene regulatory networks in Gram-negative bacteria Curr. Opin. Microbiol. 2001, 4 (2) 186-193 10.1016/S1369-5274(00)00187-9
    • (2001) Curr. Opin. Microbiol. , vol.4 , Issue.2 , pp. 186-193
    • Withers, H.1    Swift, S.2    Williams, P.3
  • 14
    • 37449026650 scopus 로고    scopus 로고
    • Quorum sensing, communication and cross-kingdom signalling in the bacterial world
    • Williams, P. Quorum sensing, communication and cross-kingdom signalling in the bacterial world Microbiology 2007, 153 (12) 3923-3938 10.1099/mic.0.2007/012856-0
    • (2007) Microbiology , vol.153 , Issue.12 , pp. 3923-3938
    • Williams, P.1
  • 15
    • 4644227796 scopus 로고    scopus 로고
    • Quorum sensing and signal interference: Diverse implications
    • Zhang, L.-H.; Dong, Y.-H. Quorum sensing and signal interference: diverse implications Mol. Microbiol. 2004, 53 (6) 1563-1571 10.1111/j.1365-2958.2004.04234.x
    • (2004) Mol. Microbiol. , vol.53 , Issue.6 , pp. 1563-1571
    • Zhang, L.-H.1    Dong, Y.-H.2
  • 17
    • 27944442272 scopus 로고    scopus 로고
    • Quorum Sensing: Cell-to-Cell Communication in Bacteria
    • Waters, C. M.; Bassler, B. L. Quorum Sensing: Cell-to-Cell Communication in Bacteria Annu. Rev. Cell Dev. Biol. 2005, 21 (1) 319-346 10.1146/annurev.cellbio.21.012704.131001
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , Issue.1 , pp. 319-346
    • Waters, C.M.1    Bassler, B.L.2
  • 18
    • 78651408197 scopus 로고    scopus 로고
    • Quorum sensing in Gram-negative bacteria: Small-molecule modulation of AHL and AI-2 quorum sensing pathways
    • Galloway, W. R.; Hodgkinson, J. T.; Bowden, S. D.; Welch, M.; Spring, D. R. Quorum sensing in Gram-negative bacteria: small-molecule modulation of AHL and AI-2 quorum sensing pathways Chem. Rev. 2011, 111 (1) 28-67 10.1021/cr100109t
    • (2011) Chem. Rev. , vol.111 , Issue.1 , pp. 28-67
    • Galloway, W.R.1    Hodgkinson, J.T.2    Bowden, S.D.3    Welch, M.4    Spring, D.R.5
  • 19
    • 84875597802 scopus 로고    scopus 로고
    • Bacterial quorum sensing: Its role in virulence and possibilities for its control
    • Rutherford, S. T.; Bassler, B. L. Bacterial quorum sensing: its role in virulence and possibilities for its control Cold Spring Harbor Perspect. Med. 2012, 2 (11) a012427 10.1101/cshperspect.a012427
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , Issue.11 , pp. a012427
    • Rutherford, S.T.1    Bassler, B.L.2
  • 20
  • 21
    • 45749113796 scopus 로고    scopus 로고
    • Expanding dialogues: From natural autoinducers to non-natural analogues that modulate quorum sensing in Gram-negative bacteria
    • Geske, G. D.; O'Neill, J. C.; Blackwell, H. E. Expanding dialogues: from natural autoinducers to non-natural analogues that modulate quorum sensing in Gram-negative bacteria Chem. Soc. Rev. 2008, 37 (7) 1432-1447 10.1039/b703021p
    • (2008) Chem. Soc. Rev. , vol.37 , Issue.7 , pp. 1432-1447
    • Geske, G.D.1    O'Neill, J.C.2    Blackwell, H.E.3
  • 22
    • 84919711600 scopus 로고    scopus 로고
    • Quorum sensing inhibitors as anti-biofilm agents
    • Brackman, G.; Coenye, T. Quorum sensing inhibitors as anti-biofilm agents Curr. Pharm. Des. 2015, 21 (1) 5-11 10.2174/1381612820666140905114627
    • (2015) Curr. Pharm. Des. , vol.21 , Issue.1 , pp. 5-11
    • Brackman, G.1    Coenye, T.2
  • 23
    • 75749142692 scopus 로고    scopus 로고
    • Can infectious biofilm be controlled by blocking bacterial communication?
    • Macedo, A. J.; Abraham, W. R. Can infectious biofilm be controlled by blocking bacterial communication? Med. Chem. 2009, 5 (6) 517-528 10.2174/157340609790170515
    • (2009) Med. Chem. , vol.5 , Issue.6 , pp. 517-528
    • Macedo, A.J.1    Abraham, W.R.2
  • 24
    • 84857124144 scopus 로고    scopus 로고
    • Quorum quenching quandary: Resistance to antivirulence compounds
    • Maeda, T.; Garcia-Contreras, R.; Pu, M.; Sheng, L.; Garcia, L. R.; Tomas, M.; Wood, T. K. Quorum quenching quandary: resistance to antivirulence compounds ISME J. 2012, 6 (3) 493-501 10.1038/ismej.2011.122
    • (2012) ISME J. , vol.6 , Issue.3 , pp. 493-501
    • Maeda, T.1    Garcia-Contreras, R.2    Pu, M.3    Sheng, L.4    Garcia, L.R.5    Tomas, M.6    Wood, T.K.7
  • 25
    • 84923311364 scopus 로고    scopus 로고
    • Quorum sensing enhancement of the stress response promotes resistance to quorum quenching and prevents social cheating
    • Garcia-Contreras, R.; Nunez-Lopez, L.; Jasso-Chavez, R.; Kwan, B. W.; Belmont, J. A.; Rangel-Vega, A.; Maeda, T.; Wood, T. K. Quorum sensing enhancement of the stress response promotes resistance to quorum quenching and prevents social cheating ISME J. 2015, 9 (1) 115-125 10.1038/ismej.2014.98
    • (2015) ISME J. , vol.9 , Issue.1 , pp. 115-125
    • Garcia-Contreras, R.1    Nunez-Lopez, L.2    Jasso-Chavez, R.3    Kwan, B.W.4    Belmont, J.A.5    Rangel-Vega, A.6    Maeda, T.7    Wood, T.K.8
  • 26
    • 84879100114 scopus 로고    scopus 로고
    • Microbiology: Plan B for quorum sensing
    • Dandekar, A. A.; Greenberg, E. P. Microbiology: plan B for quorum sensing Nat. Chem. Biol. 2013, 9 (5) 292-293 10.1038/nchembio.1233
    • (2013) Nat. Chem. Biol. , vol.9 , Issue.5 , pp. 292-293
    • Dandekar, A.A.1    Greenberg, E.P.2
  • 29
    • 84928724752 scopus 로고    scopus 로고
    • Antimicrobial activity of selected phytochemicals against Escherichia coli and Staphylococcus aureus and their biofilms
    • Monte, J.; Abreu, A.; Borges, A.; Simões, L.; Simões, M. Antimicrobial activity of selected phytochemicals against Escherichia coli and Staphylococcus aureus and their biofilms Pathogens 2014, 3 (2) 473-498 10.3390/pathogens3020473
    • (2014) Pathogens , vol.3 , Issue.2 , pp. 473-498
    • Monte, J.1    Abreu, A.2    Borges, A.3    Simões, L.4    Simões, M.5
  • 30
    • 84877318511 scopus 로고    scopus 로고
    • Caffeine as a potential quorum sensing inhibitor
    • Norizan, S.; Yin, W.-F.; Chan, K.-G. Caffeine as a potential quorum sensing inhibitor Sensors 2013, 13 (4) 5117-5129 10.3390/s130405117
    • (2013) Sensors , vol.13 , Issue.4 , pp. 5117-5129
    • Norizan, S.1    Yin, W.-F.2    Chan, K.-G.3
  • 31
    • 84929352915 scopus 로고    scopus 로고
    • Trigonella foenum-graceum (Seed) extract interferes with quorum sensing regulated traits and biofilm formation in the strains of Pseudomonas aeruginosa and Aeromonas hydrophila
    • Husain, F. M.; Ahmad, I.; Khan, M. S.; Al-Shabib, N. A. Trigonella foenum-graceum (Seed) extract interferes with quorum sensing regulated traits and biofilm formation in the strains of Pseudomonas aeruginosa and Aeromonas hydrophila Evid Based Complement Alternat Med. 2015, 2015, 1-10 10.1155/2015/879540
    • (2015) Evid Based Complement Alternat Med. , vol.2015 , pp. 1-10
    • Husain, F.M.1    Ahmad, I.2    Khan, M.S.3    Al-Shabib, N.A.4
  • 32
    • 84856973352 scopus 로고    scopus 로고
    • Tomatidine acts in synergy with aminoglycoside antibiotics against multiresistant Staphylococcus aureus and prevents virulence gene expression
    • Mitchell, G.; Lafrance, M.; Boulanger, S.; Seguin, D. L.; Guay, I.; Gattuso, M.; Marsault, E.; Bouarab, K.; Malouin, F. Tomatidine acts in synergy with aminoglycoside antibiotics against multiresistant Staphylococcus aureus and prevents virulence gene expression J. Antimicrob. Chemother. 2012, 67 (3) 559-568 10.1093/jac/dkr510
    • (2012) J. Antimicrob. Chemother. , vol.67 , Issue.3 , pp. 559-568
    • Mitchell, G.1    Lafrance, M.2    Boulanger, S.3    Seguin, D.L.4    Guay, I.5    Gattuso, M.6    Marsault, E.7    Bouarab, K.8    Malouin, F.9
  • 33
    • 0029558610 scopus 로고
    • Cell density control of staphylococcal virulence mediated by an octapeptide pheromone
    • Ji, G.; Beavis, R. C.; Novick, R. P. Cell density control of staphylococcal virulence mediated by an octapeptide pheromone Proc. Natl. Acad. Sci. U. S. A. 1995, 92 (26) 12055-12059 10.1073/pnas.92.26.12055
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , Issue.26 , pp. 12055-12059
    • Ji, G.1    Beavis, R.C.2    Novick, R.P.3
  • 34
    • 84863232908 scopus 로고    scopus 로고
    • Capsaicin protects mice from community-associated methicillin-resistant Staphylococcus aureus pneumonia
    • Qiu, J.; Niu, X.; Wang, J.; Xing, Y.; Leng, B.; Dong, J.; Li, H.; Luo, M.; Zhang, Y.; Dai, X. et al. Capsaicin protects mice from community-associated methicillin-resistant Staphylococcus aureus pneumonia PLoS One 2012, 7 (3) e33032 10.1371/journal.pone.0033032
    • (2012) PLoS One , vol.7 , Issue.3 , pp. e33032
    • Qiu, J.1    Niu, X.2    Wang, J.3    Xing, Y.4    Leng, B.5    Dong, J.6    Li, H.7    Luo, M.8    Zhang, Y.9    Dai, X.10
  • 35
    • 84892998000 scopus 로고    scopus 로고
    • Evaluation of the effects of selected phytochemicals on quorum sensing inhibition and in vitro cytotoxicity
    • Borges, A.; Serra, S.; Cristina Abreu, A.; Saavedra, M. J.; Salgado, A.; Simões, M. Evaluation of the effects of selected phytochemicals on quorum sensing inhibition and in vitro cytotoxicity Biofouling 2014, 30 (2) 183-195 10.1080/08927014.2013.852542
    • (2014) Biofouling , vol.30 , Issue.2 , pp. 183-195
    • Borges, A.1    Serra, S.2    Cristina Abreu, A.3    Saavedra, M.J.4    Salgado, A.5    Simões, M.6
  • 39
    • 84871813251 scopus 로고    scopus 로고
    • Sulforaphane and erucin, natural isothiocyanates from broccoli, inhibit bacterial quorum sensing
    • Ganin, H.; Rayo, J.; Amara, N.; Levy, N.; Krief, P.; Meijler, M. M. Sulforaphane and erucin, natural isothiocyanates from broccoli, inhibit bacterial quorum sensing MedChemComm 2013, 4 (1) 175-179 10.1039/C2MD20196H
    • (2013) MedChemComm , vol.4 , Issue.1 , pp. 175-179
    • Ganin, H.1    Rayo, J.2    Amara, N.3    Levy, N.4    Krief, P.5    Meijler, M.M.6
  • 40
    • 79251538367 scopus 로고    scopus 로고
    • Structure-activity relationship of cinnamaldehyde analogs as inhibitors of AI-2 based quorum sensing and their effect on virulence of Vibrio spp
    • Brackman, G.; Celen, S.; Hillaert, U.; Van Calenbergh, S.; Cos, P.; Maes, L.; Nelis, H. J.; Coenye, T. Structure-activity relationship of cinnamaldehyde analogs as inhibitors of AI-2 based quorum sensing and their effect on virulence of Vibrio spp PLoS One 2011, 6 (1) e16084 10.1371/journal.pone.0016084
    • (2011) PLoS One , vol.6 , Issue.1 , pp. e16084
    • Brackman, G.1    Celen, S.2    Hillaert, U.3    Van Calenbergh, S.4    Cos, P.5    Maes, L.6    Nelis, H.J.7    Coenye, T.8
  • 41
    • 84916215147 scopus 로고    scopus 로고
    • The impact of plant vo|atiles on bacterial quorum sensyng
    • Ahmad, A.; Vyljoen, A. M.; Chenia, H. Y. The0impact of plant volatiles on basterial quorum sensing Lett. App|. Microbiol. 2015, 60 (1) 8-19 10.1111/lam.12343
    • (2015) Lett. Appl. Microbio|. , vol.60 , Issue.1 , pp. 8-19
    • Qhmad, A.1    Viljoen, A.M.2    Chenia, H.Y.3
  • 42
    • 84907083345 scopus 로고    scopus 로고
    • Inhibitory effects of 4-hydroxy-2,5-dimethyl-3(2X)-furanone (HDMF) on acyl-homosurine lactone-mediated virulence0factor production and biofilm formation in Pseudomonas aeruginosa PAO1
    • Choi, S. C.; Zhang, C.; Moon, S.; Oh, Y. S. Inhibitory effects of 4-hydroxy-2,5-dimethyl-3(2H)-furanonu (HDMF) on acyl-homoserine lactne-mediated virulence factor production and biofilm formation in Pseudomonas aeruginosa PAO1 J.0Microbiol. 2014, 52 (9) 734-742010.1007/s12275-014-4060-x
    • (2014) J. Microbiol. , vol.52 , Issue.9 , pp. 734-742
    • Choi, S.C.1    Zhang, C.2    Moon, S.3    Oh, Y.S.4
  • 43
    • 84922569045 scopus 로고    scopus 로고
    • Quorum0quenching activity of Syzygium sumini (L.) Skeels and its anthosyanin malvidin against Klebsiel|a pneumoniae
    • Gopu, V.; Kothandapani, S.; Shetty, P.0H. Quorum quenching activity of0Syzygium cumini (L.) Skeels and0its anthocyanin malvidin against Klebsiella pneumoniae Microb. Pathog. 2015, 79, 61-69 10.1016/z.micpath.2015.01.010.
    • (2015) Microb. Pathog. , vol.79 , pp. 61-69
    • Gopu, V.1    Kothandapai, S.2    Shetty, P.H.3
  • 44
    • 84925484723 scopus 로고    scopus 로고
    • Deciphering the role of coumarin as a novel quorum sensing inhibitor suppressing virulence phenotypes in bacterial pathogens
    • Gutierrez-Barranquero, J. A.; Reen, F. J.; McCarthy, R. R.; O'Gara, F. Deciphering the role of coumarin as a novel quorum sensing inhibitor suppressing virulence phenotypes in bacterial pathogens Appl. Microbiol. Biotechnol. 2015, 99 (7) 3303-3316 10.1007/s00253-015-6436-1
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , Issue.7 , pp. 3303-3316
    • Gutierrez-Barranquero, J.A.1    Reen, F.J.2    McCarthy, R.R.3    O'Gara, F.4
  • 45
    • 0034018438 scopus 로고    scopus 로고
    • The pseudomonas quinolone signal regulates rhl quorum sensing in Pseudomonas aeruginosa
    • McKnight, S. L.; Iglewski, B. H.; Pesci, E. C. The pseudomonas quinolone signal regulates rhl quorum sensing in Pseudomonas aeruginosa J. Bacteriol. 2000, 182 (10) 2702-2708 10.1128/JB.182.10.2702-2708.2000
    • (2000) J. Bacteriol. , vol.182 , Issue.10 , pp. 2702-2708
    • McKnight, S.L.1    Iglewski, B.H.2    Pesci, E.C.3
  • 46
    • 33846446695 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa 4-quinolone signal molecules HHQ and PQS play multifunctional roles in quorum sensing and iron entrapment
    • Diggle, S. P.; Matthijs, S.; Wright, V. J.; Fletcher, M. P.; Chhabra, S. R.; Lamont, I. L.; Kong, X.; Hider, R. C.; Cornelis, P.; Camara, M. et al. The Pseudomonas aeruginosa 4-quinolone signal molecules HHQ and PQS play multifunctional roles in quorum sensing and iron entrapment Chem. Biol. 2007, 14 (1) 87-96 10.1016/j.chembiol.2006.11.014
    • (2007) Chem. Biol. , vol.14 , Issue.1 , pp. 87-96
    • Diggle, S.P.1    Matthijs, S.2    Wright, V.J.3    Fletcher, M.P.4    Chhabra, S.R.5    Lamont, I.L.6    Kong, X.7    Hider, R.C.8    Cornelis, P.9    Camara, M.10
  • 47
    • 80055066978 scopus 로고    scopus 로고
    • Food phytochemicals act as Quorum Sensing inhibitors reducing production and/or degrading autoinducers of Yersinia enterocolitica and Erwinia carotovora
    • Truchado, P.; Tomás-Barberán, F. A.; Larrosa, M.; Allende, A. Food phytochemicals act as Quorum Sensing inhibitors reducing production and/or degrading autoinducers of Yersinia enterocolitica and Erwinia carotovora Food Control 2012, 24 (1-2) 78-85 10.1016/j.foodcont.2011.09.006
    • (2012) Food Control , vol.24 , Issue.1-2 , pp. 78-85
    • Truchado, P.1    Tomás-Barberán, F.A.2    Larrosa, M.3    Allende, A.4
  • 51
    • 74049118359 scopus 로고    scopus 로고
    • Subinhibitory concentrations of licochalcone A decrease alpha-toxin production in both methicillin-sensitive and methicillin-resistant Staphylococcus aureus isolates
    • Qiu, J.; Jiang, Y.; Xia, L.; Xiang, H.; Feng, H.; Pu, S.; Huang, N.; Yu, L.; Deng, X. Subinhibitory concentrations of licochalcone A decrease alpha-toxin production in both methicillin-sensitive and methicillin-resistant Staphylococcus aureus isolates Lett. Appl. Microbiol. 2010, 50 (2) 223-229 10.1111/j.1472-765X.2009.02783.x
    • (2010) Lett. Appl. Microbiol. , vol.50 , Issue.2 , pp. 223-229
    • Qiu, J.1    Jiang, Y.2    Xia, L.3    Xiang, H.4    Feng, H.5    Pu, S.6    Huang, N.7    Yu, L.8    Deng, X.9
  • 52
    • 84861307787 scopus 로고    scopus 로고
    • Antimicrobial activity of licochalcone e against Staphylococcus aureus and its impact on the production of staphylococcal alpha-toxin
    • Zhou, T.; Deng, X.; Qiu, J. Antimicrobial activity of licochalcone E against Staphylococcus aureus and its impact on the production of staphylococcal alpha-toxin J. Microbiol. Biotechnol. 2012, 22 (6) 800-805 10.4014/jmb.1112.12020
    • (2012) J. Microbiol. Biotechnol. , vol.22 , Issue.6 , pp. 800-805
    • Zhou, T.1    Deng, X.2    Qiu, J.3
  • 53
    • 76149099273 scopus 로고    scopus 로고
    • Identification of catechin as one of the flavonoids from Combretum albiflorum bark extract that reduces the production of quorum-sensing-controlled virulence factors in Pseudomonas aeruginosa PAO1
    • Vandeputte, O. M.; Kiendrebeogo, M.; Rajaonson, S.; Diallo, B.; Mol, A.; El Jaziri, M.; Baucher, M. Identification of catechin as one of the flavonoids from Combretum albiflorum bark extract that reduces the production of quorum-sensing-controlled virulence factors in Pseudomonas aeruginosa PAO1 Appl. Environ. Microbiol. 2010, 76 (1) 243-253 10.1128/AEM.01059-09
    • (2010) Appl. Environ. Microbiol. , vol.76 , Issue.1 , pp. 243-253
    • Vandeputte, O.M.1    Kiendrebeogo, M.2    Rajaonson, S.3    Diallo, B.4    Mol, A.5    El Jaziri, M.6    Baucher, M.7
  • 54
    • 84918822792 scopus 로고    scopus 로고
    • 2(5H)-Furanone, epigallocatechin gallate, and a citric-based disinfectant disturb quorum-sensing activity and reduce motility and biofilm formation of Campylobacter jejuni
    • Castillo, S.; Heredia, N.; Garcia, S. 2(5H)-Furanone, epigallocatechin gallate, and a citric-based disinfectant disturb quorum-sensing activity and reduce motility and biofilm formation of Campylobacter jejuni Folia Microbiol. (Dordrecht, Neth.) 2015, 60 (1) 89-95 10.1007/s12223-014-0344-0
    • (2015) Folia Microbiol. (Dordrecht, Neth.) , vol.60 , Issue.1 , pp. 89-95
    • Castillo, S.1    Heredia, N.2    Garcia, S.3
  • 55
    • 0346336785 scopus 로고    scopus 로고
    • Influence of polyphenols on bacterial biofilm formation and quorum-sensing
    • Huber, B.; Eberl, L.; Feucht, W.; Polster, J. Influence of polyphenols on bacterial biofilm formation and quorum-sensing Z. Naturforsch., C: J. Biosci. 2003, 58 (11-12) 879-884 10.1515/znc-2003-11-1224
    • (2003) Z. Naturforsch., C: J. Biosci. , vol.58 , Issue.11-12 , pp. 879-884
    • Huber, B.1    Eberl, L.2    Feucht, W.3    Polster, J.4
  • 56
    • 77954514638 scopus 로고    scopus 로고
    • Suppression of bacterial cell-cell signalling, biofilm formation and type III secretion system by citrus flavonoids
    • Vikram, A.; Jayaprakasha, G. K.; Jesudhasan, P. R.; Pillai, S. D.; Patil, B. S. Suppression of bacterial cell-cell signalling, biofilm formation and type III secretion system by citrus flavonoids J. Appl. Microbiol. 2010, 109 (2) 515-527 10.1111/j.1365-2672.2010.04677.x
    • (2010) J. Appl. Microbiol. , vol.109 , Issue.2 , pp. 515-527
    • Vikram, A.1    Jayaprakasha, G.K.2    Jesudhasan, P.R.3    Pillai, S.D.4    Patil, B.S.5
  • 59
    • 84873059749 scopus 로고    scopus 로고
    • Silibinin in vitro protects A549 cells from Staphylococcus aureus-mediated injury and in vivo alleviates the lung injury of staphylococcal pneumonia
    • Wang, X.; Dong, J.; Dai, X.; Zhang, Y.; Wang, J.; Li, H.; Lu, C.; Tan, W.; Gao, X.; Deng, X. et al. Silibinin in vitro protects A549 cells from Staphylococcus aureus-mediated injury and in vivo alleviates the lung injury of staphylococcal pneumonia Planta Med. 2013, 79 (2) 110-115 10.1055/s-0032-1328068
    • (2013) Planta Med. , vol.79 , Issue.2 , pp. 110-115
    • Wang, X.1    Dong, J.2    Dai, X.3    Zhang, Y.4    Wang, J.5    Li, H.6    Lu, C.7    Tan, W.8    Gao, X.9    Deng, X.10
  • 60
    • 84905192740 scopus 로고    scopus 로고
    • Puerarin protects against Staphylococcus aureus-induced injury of human alveolar epithelial A549 cells via downregulating alpha-hemolysin secretion
    • Tang, F.; Li, W. H.; Zhou, X.; Liu, Y. H.; Li, Z.; Tang, Y. S.; Kou, X.; Wang, S. D.; Bao, M.; Qu, L. D. et al. Puerarin protects against Staphylococcus aureus-induced injury of human alveolar epithelial A549 cells via downregulating alpha-hemolysin secretion Microb. Drug Resist. 2014, 20 (4) 357-363 10.1089/mdr.2013.0104
    • (2014) Microb. Drug Resist. , vol.20 , Issue.4 , pp. 357-363
    • Tang, F.1    Li, W.H.2    Zhou, X.3    Liu, Y.H.4    Li, Z.5    Tang, Y.S.6    Kou, X.7    Wang, S.D.8    Bao, M.9    Qu, L.D.10
  • 61
    • 84876346880 scopus 로고    scopus 로고
    • Inhibition of alpha-toxin production by subinhibitory concentrations of naringenin controls Staphylococcus aureus pneumonia
    • Zhang, Y.; Wang, J. F.; Dong, J.; Wei, J. Y.; Wang, Y. N.; Dai, X. H.; Wang, X.; Luo, M. J.; Tan, W.; Deng, X. M. et al. Inhibition of alpha-toxin production by subinhibitory concentrations of naringenin controls Staphylococcus aureus pneumonia Fitoterapia 2013, 86, 92-99 10.1016/j.fitote.2013.02.001
    • (2013) Fitoterapia , vol.86 , pp. 92-99
    • Zhang, Y.1    Wang, J.F.2    Dong, J.3    Wei, J.Y.4    Wang, Y.N.5    Dai, X.H.6    Wang, X.7    Luo, M.J.8    Tan, W.9    Deng, X.M.10
  • 62
    • 84871712999 scopus 로고    scopus 로고
    • Apigenin alleviates the symptoms of Staphylococcus aureus pneumonia by inhibiting the production of alpha-hemolysin
    • Dong, J.; Qiu, J.; Wang, J.; Li, H.; Dai, X.; Zhang, Y.; Wang, X.; Tan, W.; Niu, X.; Deng, X. et al. Apigenin alleviates the symptoms of Staphylococcus aureus pneumonia by inhibiting the production of alpha-hemolysin FEMS Microbiol. Lett. 2013, 338 (2) 124-131 10.1111/1574-6968.12040
    • (2013) FEMS Microbiol. Lett. , vol.338 , Issue.2 , pp. 124-131
    • Dong, J.1    Qiu, J.2    Wang, J.3    Li, H.4    Dai, X.5    Zhang, Y.6    Wang, X.7    Tan, W.8    Niu, X.9    Deng, X.10
  • 63
    • 84879125795 scopus 로고    scopus 로고
    • Subinhibitory concentrations of pinocembrin exert anti-Staphylococcus aureus activity by reducing alpha-toxin expression
    • Soromou, L. W.; Zhang, Y.; Cui, Y.; Wei, M.; Chen, N.; Yang, X.; Huo, M.; Balde, A.; Guan, S.; Deng, X. et al. Subinhibitory concentrations of pinocembrin exert anti-Staphylococcus aureus activity by reducing alpha-toxin expression J. Appl. Microbiol. 2013, 115 (1) 41-49 10.1111/jam.12221
    • (2013) J. Appl. Microbiol. , vol.115 , Issue.1 , pp. 41-49
    • Soromou, L.W.1    Zhang, Y.2    Cui, Y.3    Wei, M.4    Chen, N.5    Yang, X.6    Huo, M.7    Balde, A.8    Guan, S.9    Deng, X.10
  • 64
    • 84877686083 scopus 로고    scopus 로고
    • Liquiritigenin prevents Staphylococcus aureus-mediated lung cell injury via inhibiting the production of alpha-hemolysin
    • Dai, X. H.; Li, H. E.; Lu, C. J.; Wang, J. F.; Dong, J.; Wei, J. Y.; Zhang, Y.; Wang, X.; Tan, W.; Deng, X. M. et al. Liquiritigenin prevents Staphylococcus aureus-mediated lung cell injury via inhibiting the production of alpha-hemolysin J. Asian Nat. Prod. Res. 2013, 15 (4) 390-399 10.1080/10286020.2013.771344
    • (2013) J. Asian Nat. Prod. Res. , vol.15 , Issue.4 , pp. 390-399
    • Dai, X.H.1    Li, H.E.2    Lu, C.J.3    Wang, J.F.4    Dong, J.5    Wei, J.Y.6    Zhang, Y.7    Wang, X.8    Tan, W.9    Deng, X.M.10
  • 65
    • 79960140545 scopus 로고    scopus 로고
    • Impact of luteolin on the production of alpha-toxin by Staphylococcus aureus
    • Qiu, J.; Li, H.; Meng, H.; Hu, C.; Li, J.; Luo, M.; Dong, J.; Wang, X.; Wang, J.; Deng, Y. et al. Impact of luteolin on the production of alpha-toxin by Staphylococcus aureus Lett. Appl. Microbiol. 2011, 53 (2) 238-243 10.1111/j.1472-765X.2011.03098.x
    • (2011) Lett. Appl. Microbiol. , vol.53 , Issue.2 , pp. 238-243
    • Qiu, J.1    Li, H.2    Meng, H.3    Hu, C.4    Li, J.5    Luo, M.6    Dong, J.7    Wang, X.8    Wang, J.9    Deng, Y.10
  • 66
    • 78651463685 scopus 로고    scopus 로고
    • Subinhibitory concentrations of farrerol reduce α-toxin expression in Staphylococcus aureus
    • Qiu, J.; Xiang, H.; Hu, C.; Wang, Q.; Dong, J.; Li, H.; Luo, M.; Wang, J.; Deng, X. Subinhibitory concentrations of farrerol reduce α-toxin expression in Staphylococcus aureus FEMS Microbiol. Lett. 2011, 315 (2) 129-133 10.1111/j.1574-6968.2010.02183.x
    • (2011) FEMS Microbiol. Lett. , vol.315 , Issue.2 , pp. 129-133
    • Qiu, J.1    Xiang, H.2    Hu, C.3    Wang, Q.4    Dong, J.5    Li, H.6    Luo, M.7    Wang, J.8    Deng, X.9
  • 68
    • 84899945637 scopus 로고    scopus 로고
    • Anti-quorum sensing activity of Psidium guajava L. Flavonoids against Chromobacterium violaceum and Pseudomonas aeruginosa PAO1
    • Vasavi, H. S.; Arun, A. B.; Rekha, P. D. Anti-quorum sensing activity of Psidium guajava L. flavonoids against Chromobacterium violaceum and Pseudomonas aeruginosa PAO1 Microbiol. Immunol. 2014, 58 (5) 286-293 10.1111/1348-0421.12150
    • (2014) Microbiol. Immunol. , vol.58 , Issue.5 , pp. 286-293
    • Vasavi, H.S.1    Arun, A.B.2    Rekha, P.D.3
  • 69
    • 68149158717 scopus 로고    scopus 로고
    • Inhibition of quorum sensing mechanism and Aeromonas hydrophila biofilm formation by vanillin
    • Ponnusamy, K.; Paul, D.; Kweon, J. H. Inhibition of quorum sensing mechanism and Aeromonas hydrophila biofilm formation by vanillin Environ. Eng. Sci. 2009, 26 (8) 1359-1363 10.1089/ees.2008.0415
    • (2009) Environ. Eng. Sci. , vol.26 , Issue.8 , pp. 1359-1363
    • Ponnusamy, K.1    Paul, D.2    Kweon, J.H.3
  • 70
    • 33750592622 scopus 로고    scopus 로고
    • Salicylic acid reduces the production of several potential virulence factors of Pseudomonas aeruginosa associated with microbial keratitis
    • Bandara, M. B. K.; Zhu, H.; Sankaridurg, P. R.; Willcox, M. D. P. Salicylic acid reduces the production of several potential virulence factors of Pseudomonas aeruginosa associated with microbial keratitis Invest. Ophthalmol. Visual Sci. 2006, 47 (10) 4453-4460 10.1167/iovs.06-0288
    • (2006) Invest. Ophthalmol. Visual Sci. , vol.47 , Issue.10 , pp. 4453-4460
    • Bandara, M.B.K.1    Zhu, H.2    Sankaridurg, P.R.3    Willcox, M.D.P.4
  • 71
    • 84922647023 scopus 로고    scopus 로고
    • Non-antibiotic quorum sensing inhibitors acting against N-acyl homoserine lactone synthase as druggable target
    • Chang, C.-Y.; Krishnan, T.; Wang, H.; Chen, Y.; Yin, W.-F.; Chong, Y.-M.; Tan, L. Y.; Chong, T. M.; Chan, K.-G. Non-antibiotic quorum sensing inhibitors acting against N-acyl homoserine lactone synthase as druggable target Sci. Rep. 2014, 4, 7245 10.1038/srep07245
    • (2014) Sci. Rep. , vol.4 , pp. 7245
    • Chang, C.-Y.1    Krishnan, T.2    Wang, H.3    Chen, Y.4    Yin, W.-F.5    Chong, Y.-M.6    Tan, L.Y.7    Chong, T.M.8    Chan, K.-G.9
  • 73
    • 52749086338 scopus 로고    scopus 로고
    • Cinnamaldehyde and cinnamaldehyde derivatives reduce virulence in Vibrio spp. by decreasing the DNA-binding activity of the quorum sensing response regulator LuxR
    • Brackman, G.; Defoirdt, T.; Miyamoto, C.; Bossier, P.; Van Calenbergh, S.; Nelis, H.; Coenye, T. Cinnamaldehyde and cinnamaldehyde derivatives reduce virulence in Vibrio spp. by decreasing the DNA-binding activity of the quorum sensing response regulator LuxR BMC Microbiol. 2008, 8, 149 10.1186/1471-2180-8-149
    • (2008) BMC Microbiol. , vol.8 , pp. 149
    • Brackman, G.1    Defoirdt, T.2    Miyamoto, C.3    Bossier, P.4    Van Calenbergh, S.5    Nelis, H.6    Coenye, T.7
  • 74
    • 84920067990 scopus 로고    scopus 로고
    • Cinnamon bark oil and its components inhibit biofilm formation and toxin production
    • Kim, Y.-G.; Lee, J.-H.; Kim, S.-I.; Baek, K.-H.; Lee, J. Cinnamon bark oil and its components inhibit biofilm formation and toxin production Int. J. Food Microbiol. 2015, 195 (0) 30-39 10.1016/j.ijfoodmicro.2014.11.028
    • (2015) Int. J. Food Microbiol. , vol.195 , pp. 30-39
    • Kim, Y.-G.1    Lee, J.-H.2    Kim, S.-I.3    Baek, K.-H.4    Lee, J.5
  • 75
    • 84874805377 scopus 로고    scopus 로고
    • Eugenol inhibits quorum sensing at sub-inhibitory concentrations
    • Zhou, L.; Zheng, H.; Tang, Y.; Yu, W.; Gong, Q. Eugenol inhibits quorum sensing at sub-inhibitory concentrations Biotechnol. Lett. 2013, 35 (4) 631-637 10.1007/s10529-012-1126-x
    • (2013) Biotechnol. Lett. , vol.35 , Issue.4 , pp. 631-637
    • Zhou, L.1    Zheng, H.2    Tang, Y.3    Yu, W.4    Gong, Q.5
  • 76
    • 77956590595 scopus 로고    scopus 로고
    • Eugenol reduces the expression of virulence-related exoproteins in Staphylococcus aureus
    • Qiu, J.; Feng, H.; Lu, J.; Xiang, H.; Wang, D.; Dong, J.; Wang, J.; Wang, X.; Liu, J.; Deng, X. Eugenol reduces the expression of virulence-related exoproteins in Staphylococcus aureus Appl. Environ. Microbiol. 2010, 76 (17) 5846-5851 10.1128/AEM.00704-10
    • (2010) Appl. Environ. Microbiol. , vol.76 , Issue.17 , pp. 5846-5851
    • Qiu, J.1    Feng, H.2    Lu, J.3    Xiang, H.4    Wang, D.5    Dong, J.6    Wang, J.7    Wang, X.8    Liu, J.9    Deng, X.10
  • 77
    • 84925497000 scopus 로고    scopus 로고
    • Anti-virulence potential of eugenyl acetate against pathogenic bacteria of medical importance
    • Musthafa, K. S.; Voravuthikunchai, S. P. Anti-virulence potential of eugenyl acetate against pathogenic bacteria of medical importance Antonie van Leeuwenhoek 2015, 107 (3) 703-710 10.1007/s10482-014-0364-4
    • (2015) Antonie van Leeuwenhoek , vol.107 , Issue.3 , pp. 703-710
    • Musthafa, K.S.1    Voravuthikunchai, S.P.2
  • 78
    • 80755184768 scopus 로고    scopus 로고
    • Antibiofilm and quorum sensing inhibitory potential of Cuminum cyminum and its secondary metabolite methyl eugenol against Gram negative bacterial pathogens
    • Packiavathy, I. A. S. V.; Agilandeswari, P.; Musthafa, K. S.; Pandian, S. K.; Ravi, A. V. Antibiofilm and quorum sensing inhibitory potential of Cuminum cyminum and its secondary metabolite methyl eugenol against Gram negative bacterial pathogens Food Res. Int. 2012, 45 (1) 85-92 10.1016/j.foodres.2011.10.022
    • (2012) Food Res. Int. , vol.45 , Issue.1 , pp. 85-92
    • Packiavathy, I.A.S.V.1    Agilandeswari, P.2    Musthafa, K.S.3    Pandian, S.K.4    Ravi, A.V.5
  • 79
    • 84898062269 scopus 로고    scopus 로고
    • Synthesis and quorum sensing inhibitory activity of key phenolic compounds of ginger and their derivatives
    • Kumar, N. V.; Murthy, P. S.; Manjunatha, J. R.; Bettadaiah, B. K. Synthesis and quorum sensing inhibitory activity of key phenolic compounds of ginger and their derivatives Food Chem. 2014, 159, 451-457 10.1016/j.foodchem.2014.03.039
    • (2014) Food Chem. , vol.159 , pp. 451-457
    • Kumar, N.V.1    Murthy, P.S.2    Manjunatha, J.R.3    Bettadaiah, B.K.4
  • 80
    • 84923928617 scopus 로고    scopus 로고
    • Zingerone silences quorum sensing and attenuates virulence of Pseudomonas aeruginosa
    • Kumar, L.; Chhibber, S.; Kumar, R.; Kumar, M.; Harjai, K. Zingerone silences quorum sensing and attenuates virulence of Pseudomonas aeruginosa Fitoterapia 2015, 102 (0) 84-95 10.1016/j.fitote.2015.02.002
    • (2015) Fitoterapia , vol.102 , pp. 84-95
    • Kumar, L.1    Chhibber, S.2    Kumar, R.3    Kumar, M.4    Harjai, K.5
  • 81
    • 84923882008 scopus 로고    scopus 로고
    • 6-Gingerol reduces Pseudomonas aeruginosa biofilm formation and virulence via quorum sensing inhibition
    • Kim, H.-S.; Lee, S.-H.; Byun, Y.; Park, H.-D. 6-Gingerol reduces Pseudomonas aeruginosa biofilm formation and virulence via quorum sensing inhibition Sci. Rep. 2015, 5, 8656 10.1038/srep08656
    • (2015) Sci. Rep. , vol.5 , pp. 8656
    • Kim, H.-S.1    Lee, S.-H.2    Byun, Y.3    Park, H.-D.4
  • 82
    • 41849114939 scopus 로고    scopus 로고
    • Curcumin, a known phenolic from Curcuma longa, attenuates the virulence of Pseudomonas aeruginosa PAO1 in whole plant and animal pathogenicity models
    • Rudrappa, T.; Bais, H. P. Curcumin, a known phenolic from Curcuma longa, attenuates the virulence of Pseudomonas aeruginosa PAO1 in whole plant and animal pathogenicity models J. Agric. Food Chem. 2008, 56 (6) 1955-1962 10.1021/jf072591j
    • (2008) J. Agric. Food Chem. , vol.56 , Issue.6 , pp. 1955-1962
    • Rudrappa, T.1    Bais, H.P.2
  • 83
    • 84888204500 scopus 로고    scopus 로고
    • Prevention of quorum-sensing-mediated biofilm development and virulence factors production in Vibrio spp. by curcumin
    • Packiavathy, I. A. S. V.; Sasikumar, P.; Pandian, S. K.; Veera Ravi, A. Prevention of quorum-sensing-mediated biofilm development and virulence factors production in Vibrio spp. by curcumin Appl. Microbiol. Biotechnol. 2013, 97 (23) 10177-10187 10.1007/s00253-013-4704-5
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , Issue.23 , pp. 10177-10187
    • Packiavathy, I.A.S.V.1    Sasikumar, P.2    Pandian, S.K.3    Veera Ravi, A.4
  • 84
    • 84888303148 scopus 로고    scopus 로고
    • Inhibition of biofilm development of uropathogens by curcumin - An anti-quorum sensing agent from Curcuma longa
    • Packiavathy, I. A. S. V.; Priya, S.; Pandian, S. K.; Ravi, A. V. Inhibition of biofilm development of uropathogens by curcumin-An anti-quorum sensing agent from Curcuma longa Food Chem. 2014, 148 (0) 453-460 10.1016/j.foodchem.2012.08.002
    • (2014) Food Chem. , vol.148 , pp. 453-460
    • Packiavathy, I.A.S.V.1    Priya, S.2    Pandian, S.K.3    Ravi, A.V.4
  • 85
    • 70350011882 scopus 로고    scopus 로고
    • Quorum sensing inhibition activity of garlic extract and p-coumaric acid
    • Bodini, S. F.; Manfredini, S.; Epp, M.; Valentini, S.; Santori, F. Quorum sensing inhibition activity of garlic extract and p-coumaric acid Lett. Appl. Microbiol. 2009, 49 (5) 551-555 10.1111/j.1472-765X.2009.02704.x
    • (2009) Lett. Appl. Microbiol. , vol.49 , Issue.5 , pp. 551-555
    • Bodini, S.F.1    Manfredini, S.2    Epp, M.3    Valentini, S.4    Santori, F.5
  • 86
    • 81355153643 scopus 로고    scopus 로고
    • Screening for novel quorum-sensing inhibitors to interfere with the formation of Pseudomonas aeruginosa biofilm
    • Ding, X.; Yin, B.; Qian, L.; Zeng, Z.; Yang, Z.; Li, H.; Lu, Y.; Zhou, S. Screening for novel quorum-sensing inhibitors to interfere with the formation of Pseudomonas aeruginosa biofilm J. Med. Microbiol. 2011, 60 (12) 1827-1834 10.1099/jmm.0.024166-0
    • (2011) J. Med. Microbiol. , vol.60 , Issue.12 , pp. 1827-1834
    • Ding, X.1    Yin, B.2    Qian, L.3    Zeng, Z.4    Yang, Z.5    Li, H.6    Lu, Y.7    Zhou, S.8
  • 87
    • 84866672762 scopus 로고    scopus 로고
    • 10′(Z),13′(E)-heptadecadienylhydroquinone inhibits swarming and virulence factors and increases polymyxin B susceptibility in Proteus mirabilis
    • Liu, M. C.; Lin, S. B.; Chien, H. F.; Wang, W. B.; Yuan, Y. H.; Hsueh, P. R.; Liaw, S. J. 10′(Z),13′(E)-heptadecadienylhydroquinone inhibits swarming and virulence factors and increases polymyxin B susceptibility in Proteus mirabilis PLoS One 2012, 7 (9) e45563 10.1371/journal.pone.0045563
    • (2012) PLoS One , vol.7 , Issue.9 , pp. e45563
    • Liu, M.C.1    Lin, S.B.2    Chien, H.F.3    Wang, W.B.4    Yuan, Y.H.5    Hsueh, P.R.6    Liaw, S.J.7
  • 88
    • 84865158481 scopus 로고    scopus 로고
    • Antiquorum sensing and antimicrobial activity of natural agents with potential use in food
    • Alvarez, M. V.; Moreira, M. R.; Ponce, A. Antiquorum sensing and antimicrobial activity of natural agents with potential use in food J. Food Saf. 2012, 32 (3) 379-387 10.1111/j.1745-4565.2012.00390.x
    • (2012) J. Food Saf. , vol.32 , Issue.3 , pp. 379-387
    • Alvarez, M.V.1    Moreira, M.R.2    Ponce, A.3
  • 89
    • 33750457654 scopus 로고    scopus 로고
    • Inhibition of swarming and virulence factor expression in Proteus mirabilis by resveratrol
    • Wang, W. B.; Lai, H. C.; Hsueh, P. R.; Chiou, R. Y.; Lin, S. B.; Liaw, S. J. Inhibition of swarming and virulence factor expression in Proteus mirabilis by resveratrol J. Med. Microbiol. 2006, 55 (10) 1313-1321 10.1099/jmm.0.46661-0
    • (2006) J. Med. Microbiol. , vol.55 , Issue.10 , pp. 1313-1321
    • Wang, W.B.1    Lai, H.C.2    Hsueh, P.R.3    Chiou, R.Y.4    Lin, S.B.5    Liaw, S.J.6
  • 90
    • 0031785679 scopus 로고    scopus 로고
    • Characterization of Proteus mirabilis precocious swarming mutants: Identification of rsbA, encoding a regulator of swarming behavior
    • Belas, R.; Schneider, R.; Melch, M. Characterization of Proteus mirabilis precocious swarming mutants: identification of rsbA, encoding a regulator of swarming behavior J. Bacteriol. 1998, 180 (23) 6126-6139
    • (1998) J. Bacteriol. , vol.180 , Issue.23 , pp. 6126-6139
    • Belas, R.1    Schneider, R.2    Melch, M.3
  • 91
    • 84973412496 scopus 로고    scopus 로고
    • Interference of quorum sensing in urinary pathogen Serratia marcescens by Anethum graveolens
    • Salini, R.; Pandian, S. K. Interference of quorum sensing in urinary pathogen Serratia marcescens by Anethum graveolens Pathog. Dis. 2015, 73 (6) ftv038 10.1093/femspd/ftv038
    • (2015) Pathog. Dis. , vol.73 , Issue.6 , pp. ftv038
    • Salini, R.1    Pandian, S.K.2
  • 93
    • 67651235397 scopus 로고    scopus 로고
    • Use of quorum sensing antagonists to deter the formation of crystalline Proteus mirabilis biofilms
    • Jones, S. M.; Dang, T. T.; Martinuzzi, R. Use of quorum sensing antagonists to deter the formation of crystalline Proteus mirabilis biofilms Int. J. Antimicrob. Agents 2009, 34 (4) 360-364 10.1016/j.ijantimicag.2009.06.011
    • (2009) Int. J. Antimicrob. Agents , vol.34 , Issue.4 , pp. 360-364
    • Jones, S.M.1    Dang, T.T.2    Martinuzzi, R.3
  • 94
    • 84907031382 scopus 로고    scopus 로고
    • Punicalagin inhibits salmonella virulence factors and has anti-quorum-sensing potential
    • Li, G.; Yan, C.; Xu, Y.; Feng, Y.; Wu, Q.; Lv, X.; Yang, B.; Wang, X.; Xia, X. Punicalagin inhibits salmonella virulence factors and has anti-quorum-sensing potential Appl. Environ. Microbiol. 2014, 80 (19) 6204-6211 10.1128/AEM.01458-14
    • (2014) Appl. Environ. Microbiol. , vol.80 , Issue.19 , pp. 6204-6211
    • Li, G.1    Yan, C.2    Xu, Y.3    Feng, Y.4    Wu, Q.5    Lv, X.6    Yang, B.7    Wang, X.8    Xia, X.9
  • 95
    • 84907360531 scopus 로고    scopus 로고
    • Mangostanaxanthones i and II, new xanthones from the pericarp of Garcinia mangostana
    • Mohamed, G. A.; Ibrahim, S. R. M.; Shaaban, M. I. A.; Ross, S. A. Mangostanaxanthones I and II, new xanthones from the pericarp of Garcinia mangostana Fitoterapia 2014, 98 (0) 215-221 10.1016/j.fitote.2014.08.014
    • (2014) Fitoterapia , vol.98 , pp. 215-221
    • Mohamed, G.A.1    Ibrahim, S.R.M.2    Shaaban, M.I.A.3    Ross, S.A.4
  • 96
    • 84898603171 scopus 로고    scopus 로고
    • The natural antimicrobial carvacrol inhibits quorum sensing in Chromobacterium violaceum and reduces bacterial biofilm formation at sub-lethal concentrations
    • Burt, S. A.; Ojo-Fakunle, V. T. A.; Woertman, J.; Veldhuizen, E. J. A. The natural antimicrobial carvacrol inhibits quorum sensing in Chromobacterium violaceum and reduces bacterial biofilm formation at sub-lethal concentrations PLoS One 2014, 9 (4) e93414 10.1371/journal.pone.0093414
    • (2014) PLoS One , vol.9 , Issue.4 , pp. e93414
    • Burt, S.A.1    Ojo-Fakunle, V.T.A.2    Woertman, J.3    Veldhuizen, E.J.A.4
  • 97
    • 84884979643 scopus 로고    scopus 로고
    • Anti-biofilm forming and anti-quorum sensing activity of selected essential oils and their main components on food-related micro-organisms
    • Kerekes, E. B.; Deák, é.; Takó, M.; Tserennadmid, R.; Petkovits, T.; Vágvölgyi, C.; Krisch, J. Anti-biofilm forming and anti-quorum sensing activity of selected essential oils and their main components on food-related micro-organisms J. Appl. Microbiol. 2013, 115 (4) 933-942 10.1111/jam.12289
    • (2013) J. Appl. Microbiol. , vol.115 , Issue.4 , pp. 933-942
    • Kerekes, E.B.1    Deák, É.2    Takó, M.3    Tserennadmid, R.4    Petkovits, T.5    Vágvölgyi, C.6    Krisch, J.7
  • 98
    • 79954779965 scopus 로고    scopus 로고
    • Menthol diminishes Staphylococcus aureus virulence-associated extracellular proteins expression
    • Qiu, J.; Luo, M.; Dong, J.; Wang, J.; Li, H.; Wang, X.; Deng, Y.; Feng, H.; Deng, X. Menthol diminishes Staphylococcus aureus virulence-associated extracellular proteins expression Appl. Microbiol. Biotechnol. 2011, 90 (2) 705-712 10.1007/s00253-011-3122-9
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , Issue.2 , pp. 705-712
    • Qiu, J.1    Luo, M.2    Dong, J.3    Wang, J.4    Li, H.5    Wang, X.6    Deng, Y.7    Feng, H.8    Deng, X.9
  • 99
    • 78651453769 scopus 로고    scopus 로고
    • Subinhibitory concentrations of thymol reduce enterotoxins A and B and alpha-hemolysin production in Staphylococcus aureus isolates
    • Qiu, J.; Wang, D.; Xiang, H.; Feng, H.; Jiang, Y.; Xia, L.; Dong, J.; Lu, J.; Yu, L.; Deng, X. Subinhibitory concentrations of thymol reduce enterotoxins A and B and alpha-hemolysin production in Staphylococcus aureus isolates PLoS One 2010, 5 (3) e9736 10.1371/journal.pone.0009736
    • (2010) PLoS One , vol.5 , Issue.3 , pp. e9736
    • Qiu, J.1    Wang, D.2    Xiang, H.3    Feng, H.4    Jiang, Y.5    Xia, L.6    Dong, J.7    Lu, J.8    Yu, L.9    Deng, X.10
  • 100
    • 84931264445 scopus 로고    scopus 로고
    • L. Sub-MICs of Mentha piperita essential oil and menthol inhibits AHL mediated quorum sensing and biofilm of Gram negative bacteria
    • Husain, F. M.; Ahmad, I.; Khan, M. S.; Ahmad, E.; Khan, M. S.; Tahseen, Q.; Alshabib, N. A. l. Sub-MICs of Mentha piperita essential oil and menthol inhibits AHL mediated quorum sensing and biofilm of Gram negative bacteria Front. Microbiol. 2015, 10.3389/fmicb.2015.00420
    • (2015) Front. Microbiol.
    • Husain, F.M.1    Ahmad, I.2    Khan, M.S.3    Ahmad, E.4    Khan, M.S.5    Tahseen, Q.6    Alshabib, N.A.7
  • 101
    • 34547697812 scopus 로고    scopus 로고
    • Farnesol, a common sesquiterpene, inhibits PQS production in Pseudomonas aeruginosa
    • Cugini, C.; Calfee, M. W.; Farrow, J. M., 3rd; Morales, D. K.; Pesci, E. C.; Hogan, D. A. Farnesol, a common sesquiterpene, inhibits PQS production in Pseudomonas aeruginosa Mol. Microbiol. 2007, 65 (4) 896-906 10.1111/j.1365-2958.2007.05840.x
    • (2007) Mol. Microbiol. , vol.65 , Issue.4 , pp. 896-906
    • Cugini, C.1    Calfee, M.W.2    Farrow, J.M.3    Morales, D.K.4    Pesci, E.C.5    Hogan, D.A.6
  • 102
    • 84866732685 scopus 로고    scopus 로고
    • Inhibition of quorum sensing in Pseudomonas aeruginosa by sesquiterpene lactones
    • Amaya, S.; Pereira, J. A.; Borkosky, S. A.; Valdez, J. C.; Bardón, A.; Arena, M. E. Inhibition of quorum sensing in Pseudomonas aeruginosa by sesquiterpene lactones Phytomedicine 2012, 19 (13) 1173-1177 10.1016/j.phymed.2012.07.003
    • (2012) Phytomedicine , vol.19 , Issue.13 , pp. 1173-1177
    • Amaya, S.1    Pereira, J.A.2    Borkosky, S.A.3    Valdez, J.C.4    Bardón, A.5    Arena, M.E.6
  • 104
    • 84863994185 scopus 로고    scopus 로고
    • α-Cyperone alleviates lung cell injury caused by Staphylococcus aureus via attenuation of alpha-hemolysin expression
    • Luo, M.; Qiu, J.; Zhang, Y.; Wang, J.; Dong, J.; Li, H.; Leng, B.; Zhang, Q.; Dai, X.; Niu, X. et al. α-Cyperone alleviates lung cell injury caused by Staphylococcus aureus via attenuation of alpha-hemolysin expression J. Microbiol. Biotechnol. 2012, 22 (8) 1170-1176 10.4014/jmb.1202.02017
    • (2012) J. Microbiol. Biotechnol. , vol.22 , Issue.8 , pp. 1170-1176
    • Luo, M.1    Qiu, J.2    Zhang, Y.3    Wang, J.4    Dong, J.5    Li, H.6    Leng, B.7    Zhang, Q.8    Dai, X.9    Niu, X.10
  • 106
    • 84885005029 scopus 로고    scopus 로고
    • Applying insights from biofilm biology to drug development - Can a new approach be developed?
    • Bjarnsholt, T.; Ciofu, O.; Molin, S.; Givskov, M.; Hoiby, N. Applying insights from biofilm biology to drug development-can a new approach be developed? Nat. Rev. Drug Discovery 2013, 12 (10) 791-808 10.1038/nrd4000
    • (2013) Nat. Rev. Drug Discovery , vol.12 , Issue.10 , pp. 791-808
    • Bjarnsholt, T.1    Ciofu, O.2    Molin, S.3    Givskov, M.4    Hoiby, N.5
  • 108
    • 0034443286 scopus 로고    scopus 로고
    • A. Microbial biofilms: From ecology to molecular genetics
    • Davey, M. E.; O'Toole, G. A. Microbial biofilms: from ecology to molecular genetics Microbiol Mol. Biol. Rev. 2000, 64 (4) 847-867 10.1128/MMBR.64.4.847-867.2000
    • (2000) Microbiol Mol. Biol. Rev. , vol.64 , Issue.4 , pp. 847-867
    • Davey, M.E.1    O'Toole, G.2
  • 109
    • 33947181889 scopus 로고    scopus 로고
    • Interrelationships between colonies, biofilms, and planktonic cells of Pseudomonas aeruginosa
    • Mikkelsen, H.; Duck, Z.; Lilley, K. S.; Welch, M. Interrelationships between colonies, biofilms, and planktonic cells of Pseudomonas aeruginosa J. Bacteriol. 2007, 189 (6) 2411-2416 10.1128/JB.01687-06
    • (2007) J. Bacteriol. , vol.189 , Issue.6 , pp. 2411-2416
    • Mikkelsen, H.1    Duck, Z.2    Lilley, K.S.3    Welch, M.4
  • 111
    • 0035859467 scopus 로고    scopus 로고
    • Antibiotic resistance of bacteria in biofilms
    • Stewart, P. S.; Costerton, J. W. Antibiotic resistance of bacteria in biofilms Lancet 2001, 358 (9276) 135-138 10.1016/S0140-6736(01)05321-1
    • (2001) Lancet , vol.358 , Issue.9276 , pp. 135-138
    • Stewart, P.S.1    Costerton, J.W.2
  • 112
    • 34447554517 scopus 로고    scopus 로고
    • The challenge of treating biofilm-associated bacterial infections
    • del Pozo, J. L.; Patel, R. The challenge of treating biofilm-associated bacterial infections Clin. Pharmacol. Ther. 2007, 82 (2) 204-209 10.1038/sj.clpt.6100247
    • (2007) Clin. Pharmacol. Ther. , vol.82 , Issue.2 , pp. 204-209
    • Del Pozo, J.L.1    Patel, R.2
  • 113
    • 0035029378 scopus 로고    scopus 로고
    • Biofilms and device-associated infections
    • Donlan, R. M. Biofilms and device-associated infections Emerging Infect. Dis. 2001, 7 (2) 277-281 10.3201/eid0702.010226
    • (2001) Emerging Infect. Dis. , vol.7 , Issue.2 , pp. 277-281
    • Donlan, R.M.1
  • 114
    • 0036228505 scopus 로고    scopus 로고
    • Biofilms: Survival mechanisms of clinically relevant microorganisms
    • Donlan, R. M.; Costerton, J. W. Biofilms: survival mechanisms of clinically relevant microorganisms Clin. Microbiol. Rev. 2002, 15 (2) 167-193 10.1128/CMR.15.2.167-193.2002
    • (2002) Clin. Microbiol. Rev. , vol.15 , Issue.2 , pp. 167-193
    • Donlan, R.M.1    Costerton, J.W.2
  • 115
    • 45549084273 scopus 로고    scopus 로고
    • Staphylococcal biofilms
    • Otto, M. Staphylococcal biofilms Curr. Top. Microbiol. Immunol. 2008, 322, 207-228 10.1007/978-3-540-75418-3-10
    • (2008) Curr. Top. Microbiol. Immunol. , vol.322 , pp. 207-228
    • Otto, M.1
  • 116
    • 38549128203 scopus 로고    scopus 로고
    • Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis
    • Jacobsen, S. M.; Stickler, D. J.; Mobley, H. L. T.; Shirtliff, M. E. Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis Clin Microbiol Rev. 2008, 21 (1) 26-59 10.1128/CMR.00019-07
    • (2008) Clin Microbiol Rev. , vol.21 , Issue.1 , pp. 26-59
    • Jacobsen, S.M.1    Stickler, D.J.2    Mobley, H.L.T.3    Shirtliff, M.E.4
  • 117
    • 0037129218 scopus 로고    scopus 로고
    • Pseudomonas biofilm formation and antibiotic resistance are linked to phenotypic variation
    • Drenkard, E.; Ausubel, F. M. Pseudomonas biofilm formation and antibiotic resistance are linked to phenotypic variation Nature 2002, 416 (6882) 740-743 10.1038/416740a
    • (2002) Nature , vol.416 , Issue.6882 , pp. 740-743
    • Drenkard, E.1    Ausubel, F.M.2
  • 118
    • 56349140707 scopus 로고    scopus 로고
    • Biofilms in the food industry: Problems and potential solutions
    • Brooks, J. D.; Flint, S. H. Biofilms in the food industry: problems and potential solutions Int. J. Food Sci. Technol. 2008, 43 (12) 2163-2176 10.1111/j.1365-2621.2008.01839.x
    • (2008) Int. J. Food Sci. Technol. , vol.43 , Issue.12 , pp. 2163-2176
    • Brooks, J.D.1    Flint, S.H.2
  • 119
    • 77956938332 scopus 로고    scopus 로고
    • Biofilm formation and the food industry, a focus on the bacterial outer surface
    • Van Houdt, R.; Michiels, C. W. Biofilm formation and the food industry, a focus on the bacterial outer surface J. Appl. Microbiol. 2010, 109 (4) 1117-1131 10.1111/j.1365-2672.2010.04756.x
    • (2010) J. Appl. Microbiol. , vol.109 , Issue.4 , pp. 1117-1131
    • Van Houdt, R.1    Michiels, C.W.2
  • 120
    • 69249230962 scopus 로고    scopus 로고
    • Biofilm formation and food safety in food industries
    • Shi, X.; Zhu, X. Biofilm formation and food safety in food industries Trends Food Sci. Technol. 2009, 20 (9) 407-413 10.1016/j.tifs.2009.01.054
    • (2009) Trends Food Sci. Technol. , vol.20 , Issue.9 , pp. 407-413
    • Shi, X.1    Zhu, X.2
  • 122
    • 34247237888 scopus 로고    scopus 로고
    • Dental plaque as a biofilm and a microbial community - Implications for health and disease
    • Marsh, P. D. Dental plaque as a biofilm and a microbial community-implications for health and disease BMC Oral Health 2006, 6, S14 10.1186/1472-6831-6-S1-S14
    • (2006) BMC Oral Health , vol.6 , pp. S14
    • Marsh, P.D.1
  • 124
    • 0024160452 scopus 로고
    • Infections from biomaterials and implants: A race for the surface
    • Gristina, A. G.; Naylor, P.; Myrvik, Q. Infections from biomaterials and implants: A race for the surface Med. Prog. Technol. 1988, 14 (3-4) 205-224
    • (1988) Med. Prog. Technol. , vol.14 , Issue.3-4 , pp. 205-224
    • Gristina, A.G.1    Naylor, P.2    Myrvik, Q.3
  • 125
    • 85027934799 scopus 로고    scopus 로고
    • Efficient surface modification of biomaterial to prevent biofilm formation and the attachment of microorganisms
    • Bazaka, K.; Jacob, M. V.; Crawford, R. J.; Ivanova, E. P. Efficient surface modification of biomaterial to prevent biofilm formation and the attachment of microorganisms Appl. Microbiol. Biotechnol. 2012, 95 (2) 299-311 10.1007/s00253-012-4144-7
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , Issue.2 , pp. 299-311
    • Bazaka, K.1    Jacob, M.V.2    Crawford, R.J.3    Ivanova, E.P.4
  • 126
    • 84882870530 scopus 로고    scopus 로고
    • A review of the biomaterials technologies for infection-resistant surfaces
    • Campoccia, D.; Montanaro, L.; Arciola, C. R. A review of the biomaterials technologies for infection-resistant surfaces Biomaterials 2013, 34 (34) 8533-8554 10.1016/j.biomaterials.2013.07.089
    • (2013) Biomaterials , vol.34 , Issue.34 , pp. 8533-8554
    • Campoccia, D.1    Montanaro, L.2    Arciola, C.R.3
  • 127
    • 84949604075 scopus 로고    scopus 로고
    • Influence of oxynitrided surface in the production of a less susceptible titanium surface to skin-borne bacterial adhesion
    • Aires, M. d. M.; Treter, J.; Braz, D. C.; Krug, C.; Macedo, A. J.; Alves Júnior, C. Influence of oxynitrided surface in the production of a less susceptible titanium surface to skin-borne bacterial adhesion Artif. Organs 2016, 40 (5) 521-526 10.1111/aor.12581
    • (2016) Artif. Organs , vol.40 , Issue.5 , pp. 521-526
    • Aires, M.D.M.1    Treter, J.2    Braz, D.C.3    Krug, C.4    Macedo, A.J.5    Alves Júnior, C.6
  • 129
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge, R. Principles of c-di-GMP signalling in bacteria Nat. Rev. Microbiol. 2009, 7 (4) 263-273 10.1038/nrmicro2109
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.4 , pp. 263-273
    • Hengge, R.1
  • 130
    • 84953645695 scopus 로고    scopus 로고
    • C-di-GMP and its effects on biofilm formation and dispersion: A Pseudomonas aeruginosa review
    • MB-0003-2014
    • Ha, D. G.; O'Toole, G. A. c-di-GMP and its effects on biofilm formation and dispersion: a Pseudomonas aeruginosa review Microbiol. Spectrum 2015, 3 (2) MB-0003-2014 10.1128/microbiolspec.MB-0003-2014
    • (2015) Microbiol. Spectrum , vol.3 , Issue.2
    • Ha, D.G.1    O'Toole, G.A.2
  • 131
    • 70549098563 scopus 로고    scopus 로고
    • Therapeutic potential of biofilm-dispersing enzymes
    • Kaplan, J. B. Therapeutic potential of biofilm-dispersing enzymes Int. J. Artif. Organs 2009, 32 (9) 545-554
    • (2009) Int. J. Artif. Organs , vol.32 , Issue.9 , pp. 545-554
    • Kaplan, J.B.1
  • 132
    • 79952078501 scopus 로고    scopus 로고
    • Engineering a novel c-di-GMP-binding protein for biofilm dispersal
    • Ma, Q.; Yang, Z.; Pu, M.; Peti, W.; Wood, T. K. Engineering a novel c-di-GMP-binding protein for biofilm dispersal Environ. Microbiol. 2011, 13 (3) 631-642 10.1111/j.1462-2920.2010.02368.x
    • (2011) Environ. Microbiol. , vol.13 , Issue.3 , pp. 631-642
    • Ma, Q.1    Yang, Z.2    Pu, M.3    Peti, W.4    Wood, T.K.5
  • 133
    • 33751245559 scopus 로고    scopus 로고
    • Proteins with GGDEF and EAL domains regulate Pseudomonas putida biofilm formation and dispersal
    • Gjermansen, M.; Ragas, P.; Tolker-Nielsen, T. Proteins with GGDEF and EAL domains regulate Pseudomonas putida biofilm formation and dispersal FEMS Microbiol. Lett. 2006, 265 (2) 215-224 10.1111/j.1574-6968.2006.00493.x
    • (2006) FEMS Microbiol. Lett. , vol.265 , Issue.2 , pp. 215-224
    • Gjermansen, M.1    Ragas, P.2    Tolker-Nielsen, T.3
  • 134
    • 78650772918 scopus 로고    scopus 로고
    • 3-Indolylacetonitrile decreases Escherichia coli O157:H7 biofilm formation and Pseudomonas aeruginosa virulence
    • Lee, J.-H.; Cho, M. H.; Lee, J. 3-Indolylacetonitrile decreases Escherichia coli O157:H7 biofilm formation and Pseudomonas aeruginosa virulence Environ. Microbiol. 2011, 13 (1) 62-73 10.1111/j.1462-2920.2010.02308.x
    • (2011) Environ. Microbiol. , vol.13 , Issue.1 , pp. 62-73
    • Lee, J.-H.1    Cho, M.H.2    Lee, J.3
  • 135
    • 84862806555 scopus 로고    scopus 로고
    • 7-fluoroindole as an antivirulence compound against Pseudomonas aeruginosa
    • Lee, J. H.; Kim, Y. G.; Cho, M. H.; Kim, J. A.; Lee, J. 7-fluoroindole as an antivirulence compound against Pseudomonas aeruginosa FEMS Microbiol. Lett. 2012, 329 (1) 36-44 10.1111/j.1574-6968.2012.02500.x
    • (2012) FEMS Microbiol. Lett. , vol.329 , Issue.1 , pp. 36-44
    • Lee, J.H.1    Kim, Y.G.2    Cho, M.H.3    Kim, J.A.4    Lee, J.5
  • 137
    • 84898729748 scopus 로고    scopus 로고
    • Inhibition of major virulence pathways of Streptococcus mutans by quercitrin and deoxynojirimycin: A synergistic approach of infection control
    • Hasan, S.; Singh, K.; Danisuddin, M.; Verma, P. K.; Khan, A. U. Inhibition of major virulence pathways of Streptococcus mutans by quercitrin and deoxynojirimycin: a synergistic approach of infection control PLoS One 2014, 9 (3) e91736 10.1371/journal.pone.0091736
    • (2014) PLoS One , vol.9 , Issue.3 , pp. e91736
    • Hasan, S.1    Singh, K.2    Danisuddin, M.3    Verma, P.K.4    Khan, A.U.5
  • 138
    • 52949142423 scopus 로고    scopus 로고
    • Novel anti-adherence activity of mulberry leaves: Inhibition of Streptococcus mutans biofilm by 1-deoxynojirimycin isolated from Morus alba
    • Islam, B.; Khan, S. N.; Haque, I.; Alam, M.; Mushfiq, M.; Khan, A. U. Novel anti-adherence activity of mulberry leaves: inhibition of Streptococcus mutans biofilm by 1-deoxynojirimycin isolated from Morus alba J. Antimicrob. Chemother. 2008, 62 (4) 751-757 10.1093/jac/dkn253
    • (2008) J. Antimicrob. Chemother. , vol.62 , Issue.4 , pp. 751-757
    • Islam, B.1    Khan, S.N.2    Haque, I.3    Alam, M.4    Mushfiq, M.5    Khan, A.U.6
  • 139
    • 70350217494 scopus 로고    scopus 로고
    • Berberine inhibits Staphylococcus epidermidis adhesion and biofilm formation on the surface of titanium alloy
    • Wang, X.; Qiu, S.; Yao, X.; Tang, T.; Dai, K.; Zhu, Z. a. Berberine inhibits Staphylococcus epidermidis adhesion and biofilm formation on the surface of titanium alloy J. Orthop. Res. 2009, 27 (11) 1487-1492 10.1002/jor.20917
    • (2009) J. Orthop. Res. , vol.27 , Issue.11 , pp. 1487-1492
    • Wang, X.1    Qiu, S.2    Yao, X.3    Tang, T.4    Dai, K.5    Zhu, Z.A.6
  • 141
    • 84884164218 scopus 로고    scopus 로고
    • Identification of natural compounds which inhibit biofilm formation in clinical isolates of Klebsiella pneumoniae
    • Magesh, H.; Kumar, A.; Alam, A.; Priyam; Sekar, U.; Sumantran, V. N.; Vaidyanathan, R. Identification of natural compounds which inhibit biofilm formation in clinical isolates of Klebsiella pneumoniae Indian J. Exp. Biol. 2013, 51 (9) 764-772
    • (2013) Indian J. Exp. Biol. , vol.51 , Issue.9 , pp. 764-772
    • Magesh, H.1    Kumar, A.2    Alam, A.3    Priyam4    Sekar, U.5    Sumantran, V.N.6    Vaidyanathan, R.7
  • 143
    • 51349120653 scopus 로고    scopus 로고
    • Impact of oleic acid (cis-9-octadecenoic acid) on bacterial viability and biofilm production in Staphylococcus aureus
    • Stenz, L.; François, P.; Fischer, A.; Huyghe, A.; Tangomo, M.; Hernandez, D.; Cassat, J.; Linder, P.; Schrenzel, J. Impact of oleic acid (cis-9-octadecenoic acid) on bacterial viability and biofilm production in Staphylococcus aureus FEMS Microbiol. Lett. 2008, 287 (2) 149-155 10.1111/j.1574-6968.2008.01316.x
    • (2008) FEMS Microbiol. Lett. , vol.287 , Issue.2 , pp. 149-155
    • Stenz, L.1    François, P.2    Fischer, A.3    Huyghe, A.4    Tangomo, M.5    Hernandez, D.6    Cassat, J.7    Linder, P.8    Schrenzel, J.9
  • 144
    • 84937640687 scopus 로고    scopus 로고
    • Identification of anti-biofilm components in Withania somnifera and their effect on virulence of Streptococcus mutans biofilms
    • Pandit, S.; Cai, J. N.; Song, K. Y.; Jeon, J. G. Identification of anti-biofilm components in Withania somnifera and their effect on virulence of Streptococcus mutans biofilms J. Appl. Microbiol. 2015, 119 (2) 571-581 10.1111/jam.12851
    • (2015) J. Appl. Microbiol. , vol.119 , Issue.2 , pp. 571-581
    • Pandit, S.1    Cai, J.N.2    Song, K.Y.3    Jeon, J.G.4
  • 145
    • 84906047022 scopus 로고    scopus 로고
    • Identification of linoleic acid, a main component of the n-hexane fraction from Dryopteris crassirhizoma, as an anti-Streptococcus mutans biofilm agent
    • Jung, J. E.; Pandit, S.; Jeon, J. G. Identification of linoleic acid, a main component of the n-hexane fraction from Dryopteris crassirhizoma, as an anti-Streptococcus mutans biofilm agent Biofouling 2014, 30 (7) 789-798 10.1080/08927014.2014.930446
    • (2014) Biofouling , vol.30 , Issue.7 , pp. 789-798
    • Jung, J.E.1    Pandit, S.2    Jeon, J.G.3
  • 146
    • 84887095611 scopus 로고    scopus 로고
    • The action of selected isothiocyanates on bacterial biofilm prevention and control
    • Borges, A.; Simões, L. C.; Saavedra, M. J.; Simões, M. The action of selected isothiocyanates on bacterial biofilm prevention and control Int. Biodeterior. Biodegrad. 2014, 86, 25-33 10.1016/j.ibiod.2013.01.015
    • (2014) Int. Biodeterior. Biodegrad. , vol.86 , pp. 25-33
    • Borges, A.1    Simões, L.C.2    Saavedra, M.J.3    Simões, M.4
  • 147
    • 84942526213 scopus 로고    scopus 로고
    • Analyzing the antibacterial effects of food ingredients: Model experiments with allicin and garlic extracts on biofilm formation and viability of Staphylococcus epidermidis
    • Wu, X.; Santos, R. R.; Fink-Gremmels, J. Analyzing the antibacterial effects of food ingredients: model experiments with allicin and garlic extracts on biofilm formation and viability of Staphylococcus epidermidis Food Sci. Nutr. 2015, 3 (2) 158-168 10.1002/fsn3.199
    • (2015) Food Sci. Nutr. , vol.3 , Issue.2 , pp. 158-168
    • Wu, X.1    Santos, R.R.2    Fink-Gremmels, J.3
  • 148
    • 17144464125 scopus 로고    scopus 로고
    • In vitro activity of allicin against Staphylococcus epidermidis and influence of subinhibitory concentrations on biofilm formation
    • Perez-Giraldo, C.; Cruz-Villalon, G.; Sanchez-Silos, R.; Martinez-Rubio, R.; Blanco, M. T.; Gomez-Garcia, A. C. In vitro activity of allicin against Staphylococcus epidermidis and influence of subinhibitory concentrations on biofilm formation J. Appl. Microbiol. 2003, 95 (4) 709-711 10.1046/j.1365-2672.2003.02030.x
    • (2003) J. Appl. Microbiol. , vol.95 , Issue.4 , pp. 709-711
    • Perez-Giraldo, C.1    Cruz-Villalon, G.2    Sanchez-Silos, R.3    Martinez-Rubio, R.4    Blanco, M.T.5    Gomez-Garcia, A.C.6
  • 151
    • 78449248788 scopus 로고    scopus 로고
    • Novel compound from Trachyspermum ammi (Ajowan caraway) seeds with antibiofilm and antiadherence activities against Streptococcus mutans: A potential chemotherapeutic agent against dental caries
    • Khan, R.; Zakir, M.; Khanam, Z.; Shakil, S.; Khan, A. U. Novel compound from Trachyspermum ammi (Ajowan caraway) seeds with antibiofilm and antiadherence activities against Streptococcus mutans: a potential chemotherapeutic agent against dental caries J. Appl. Microbiol. 2010, 109 (6) 2151-2159 10.1111/j.1365-2672.2010.04847.x
    • (2010) J. Appl. Microbiol. , vol.109 , Issue.6 , pp. 2151-2159
    • Khan, R.1    Zakir, M.2    Khanam, Z.3    Shakil, S.4    Khan, A.U.5
  • 152
    • 84885834052 scopus 로고    scopus 로고
    • Spectroscopic identification and anti-biofilm properties of polar metabolites from the medicinal plant Helichrysum italicum against Pseudomonas aeruginosa
    • D'Abrosca, B.; Buommino, E.; D'Angelo, G.; Coretti, L.; Scognamiglio, M.; Severino, V.; Pacifico, S.; Donnarumma, G.; Fiorentino, A. Spectroscopic identification and anti-biofilm properties of polar metabolites from the medicinal plant Helichrysum italicum against Pseudomonas aeruginosa Bioorg. Med. Chem. 2013, 21 (22) 7038-7046 10.1016/j.bmc.2013.09.019
    • (2013) Bioorg. Med. Chem. , vol.21 , Issue.22 , pp. 7038-7046
    • D'Abrosca, B.1    Buommino, E.2    D'Angelo, G.3    Coretti, L.4    Scognamiglio, M.5    Severino, V.6    Pacifico, S.7    Donnarumma, G.8    Fiorentino, A.9
  • 153
    • 84902013261 scopus 로고    scopus 로고
    • Coumarins reduce biofilm formation and the virulence of Escherichia coli O157:H7
    • Lee, J.-H.; Kim, Y.-G.; Cho, H. S.; Ryu, S. Y.; Cho, M. H.; Lee, J. Coumarins reduce biofilm formation and the virulence of Escherichia coli O157:H7 Phytomedicine 2014, 21 (8-9) 1037-1042 10.1016/j.phymed.2014.04.008
    • (2014) Phytomedicine , vol.21 , Issue.8-9 , pp. 1037-1042
    • Lee, J.-H.1    Kim, Y.-G.2    Cho, H.S.3    Ryu, S.Y.4    Cho, M.H.5    Lee, J.6
  • 154
    • 42149131438 scopus 로고    scopus 로고
    • Virtual screening for novel quorum sensing inhibitors to eradicate biofilm formation of Pseudomonas aeruginosa
    • Zeng, Z.; Qian, L.; Cao, L.; Tan, H.; Huang, Y.; Xue, X.; Shen, Y.; Zhou, S. Virtual screening for novel quorum sensing inhibitors to eradicate biofilm formation of Pseudomonas aeruginosa Appl. Microbiol. Biotechnol. 2008, 79 (1) 119-126 10.1007/s00253-008-1406-5
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , Issue.1 , pp. 119-126
    • Zeng, Z.1    Qian, L.2    Cao, L.3    Tan, H.4    Huang, Y.5    Xue, X.6    Shen, Y.7    Zhou, S.8
  • 155
    • 84882516618 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli O157:H7 motility and biofilm by β-sitosterol glucoside
    • Vikram, A.; Jayaprakasha, G. K.; Uckoo, R. M.; Patil, B. S. Inhibition of Escherichia coli O157:H7 motility and biofilm by β-sitosterol glucoside Biochim. Biophys. Acta, Gen. Subj. 2013, 1830 (11) 5219-5228 10.1016/j.bbagen.2013.07.022
    • (2013) Biochim. Biophys. Acta, Gen. Subj. , vol.1830 , Issue.11 , pp. 5219-5228
    • Vikram, A.1    Jayaprakasha, G.K.2    Uckoo, R.M.3    Patil, B.S.4
  • 156
    • 84934897261 scopus 로고    scopus 로고
    • Molecular basis of Streptococcus mutans sortase A inhibition by the flavonoid natural product trans-chalcone
    • Wallock-Richards, D. J.; Marles-Wright, J.; Clarke, D. J.; Maitra, A.; Dodds, M.; Hanley, B.; Campopiano, D. J. Molecular basis of Streptococcus mutans sortase A inhibition by the flavonoid natural product trans-chalcone Chem. Commun. 2015, 51 (52) 10483-10485 10.1039/C5CC01816A
    • (2015) Chem. Commun. , vol.51 , Issue.52 , pp. 10483-10485
    • Wallock-Richards, D.J.1    Marles-Wright, J.2    Clarke, D.J.3    Maitra, A.4    Dodds, M.5    Hanley, B.6    Campopiano, D.J.7
  • 157
    • 84884894197 scopus 로고    scopus 로고
    • Systematic exploration of natural and synthetic flavonoids for the inhibition of Staphylococcus aureus biofilms
    • Manner, S.; Skogman, M.; Goeres, D.; Vuorela, P.; Fallarero, A. Systematic exploration of natural and synthetic flavonoids for the inhibition of Staphylococcus aureus biofilms Int. J. Mol. Sci. 2013, 14 (10) 19434-19451 10.3390/ijms141019434
    • (2013) Int. J. Mol. Sci. , vol.14 , Issue.10 , pp. 19434-19451
    • Manner, S.1    Skogman, M.2    Goeres, D.3    Vuorela, P.4    Fallarero, A.5
  • 159
    • 84862908776 scopus 로고    scopus 로고
    • Apple flavonoid phloretin inhibits Escherichia coli O157:H7 biofilm formation and ameliorates colon inflammation in rats
    • Lee, J.-H.; Regmi, S. C.; Kim, J.-A.; Cho, M. H.; Yun, H.; Lee, C.-S.; Lee, J. Apple flavonoid phloretin inhibits Escherichia coli O157:H7 biofilm formation and ameliorates colon inflammation in rats Infect. Immun. 2011, 79 (12) 4819-4827 10.1128/IAI.05580-11
    • (2011) Infect. Immun. , vol.79 , Issue.12 , pp. 4819-4827
    • Lee, J.-H.1    Regmi, S.C.2    Kim, J.-A.3    Cho, M.H.4    Yun, H.5    Lee, C.-S.6    Lee, J.7
  • 160
    • 60549108400 scopus 로고    scopus 로고
    • Effects of phenol and natural phenolic compounds on biofilm formation by Pseudomonas aeruginosa
    • Jagani, S.; Chelikani, R.; Kim, D. S. Effects of phenol and natural phenolic compounds on biofilm formation by Pseudomonas aeruginosa Biofouling 2009, 25 (4) 321-324 10.1080/08927010802660854
    • (2009) Biofouling , vol.25 , Issue.4 , pp. 321-324
    • Jagani, S.1    Chelikani, R.2    Kim, D.S.3
  • 161
    • 25844527749 scopus 로고    scopus 로고
    • Epigallocatechin gallate inhibits biofilm formation by ocular staphylococcal isolates
    • Blanco, A. R.; Sudano-Roccaro, A.; Spoto, G. C.; Nostro, A.; Rusciano, D. Epigallocatechin gallate inhibits biofilm formation by ocular staphylococcal isolates Antimicrob. Agents Chemother. 2005, 49 (10) 4339-4343 10.1128/AAC.49.10.4339-4343.2005
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.10 , pp. 4339-4343
    • Blanco, A.R.1    Sudano-Roccaro, A.2    Spoto, G.C.3    Nostro, A.4    Rusciano, D.5
  • 162
    • 79952339749 scopus 로고    scopus 로고
    • The tea catechin epigallocatechin gallate suppresses cariogenic virulence factors of Streptococcus mutans
    • Xu, X.; Zhou, X. D.; Wu, C. D. The tea catechin epigallocatechin gallate suppresses cariogenic virulence factors of Streptococcus mutans Antimicrob. Agents Chemother. 2011, 55 (3) 1229-1236 10.1128/AAC.01016-10
    • (2011) Antimicrob. Agents Chemother. , vol.55 , Issue.3 , pp. 1229-1236
    • Xu, X.1    Zhou, X.D.2    Wu, C.D.3
  • 163
    • 84860228056 scopus 로고    scopus 로고
    • Tea catechin epigallocatechin gallate inhibits Streptococcus mutans biofilm formation by suppressing gtf genes
    • Xu, X.; Zhou, X. D.; Wu, C. D. Tea catechin epigallocatechin gallate inhibits Streptococcus mutans biofilm formation by suppressing gtf genes Arch. Oral Biol. 2012, 57 (6) 678-683 10.1016/j.archoralbio.2011.10.021
    • (2012) Arch. Oral Biol. , vol.57 , Issue.6 , pp. 678-683
    • Xu, X.1    Zhou, X.D.2    Wu, C.D.3
  • 164
  • 166
    • 84919699057 scopus 로고    scopus 로고
    • Effects of epigallocatechin gallate against Enterococcus faecalis biofilm and virulence
    • Lee, P.; Tan, K. S. Effects of epigallocatechin gallate against Enterococcus faecalis biofilm and virulence Arch. Oral Biol. 2015, 60 (3) 393-399 10.1016/j.archoralbio.2014.11.014
    • (2015) Arch. Oral Biol. , vol.60 , Issue.3 , pp. 393-399
    • Lee, P.1    Tan, K.S.2
  • 167
    • 84908394498 scopus 로고    scopus 로고
    • Neuraminidase inhibitory activities of quaternary isoquinoline alkaloids from Corydalis turtschaninovii rhizome
    • Kim, J. H.; Ryu, Y. B.; Lee, W. S.; Kim, Y. H. Neuraminidase inhibitory activities of quaternary isoquinoline alkaloids from Corydalis turtschaninovii rhizome Bioorg. Med. Chem. 2014, 22 (21) 6047-6052 10.1016/j.bmc.2014.09.004
    • (2014) Bioorg. Med. Chem. , vol.22 , Issue.21 , pp. 6047-6052
    • Kim, J.H.1    Ryu, Y.B.2    Lee, W.S.3    Kim, Y.H.4
  • 168
    • 84934966493 scopus 로고    scopus 로고
    • Interconverting flavonostilbenes with antibacterial activity from Sophora alopecuroides
    • Wan, C. X.; Luo, J. G.; Ren, X. P.; Kong, L. Y. Interconverting flavonostilbenes with antibacterial activity from Sophora alopecuroides Phytochemistry 2015, 116, 290-297 10.1016/j.phytochem.2015.02.022
    • (2015) Phytochemistry , vol.116 , pp. 290-297
    • Wan, C.X.1    Luo, J.G.2    Ren, X.P.3    Kong, L.Y.4
  • 170
    • 84922155260 scopus 로고    scopus 로고
    • Red wines and flavonoids diminish Staphylococcus aureus virulence with anti-biofilm and anti-hemolytic activities
    • Cho, H. S.; Lee, J. H.; Cho, M. H.; Lee, J. Red wines and flavonoids diminish Staphylococcus aureus virulence with anti-biofilm and anti-hemolytic activities Biofouling 2015, 31 (1) 1-11 10.1080/08927014.2014.991319
    • (2015) Biofouling , vol.31 , Issue.1 , pp. 1-11
    • Cho, H.S.1    Lee, J.H.2    Cho, M.H.3    Lee, J.4
  • 171
    • 84915770383 scopus 로고    scopus 로고
    • Non-toxic plant metabolites regulate staphylococcus viability and biofilm formation: A natural therapeutic strategy useful in the treatment and prevention of skin infections
    • Moran, A.; Gutierrez, S.; Martinez-Blanco, H.; Ferrero, M. A.; Monteagudo-Mera, A.; Rodriguez-Aparicio, L. B. Non-toxic plant metabolites regulate staphylococcus viability and biofilm formation: a natural therapeutic strategy useful in the treatment and prevention of skin infections Biofouling 2014, 30 (10) 1175-1182 10.1080/08927014.2014.976207
    • (2014) Biofouling , vol.30 , Issue.10 , pp. 1175-1182
    • Moran, A.1    Gutierrez, S.2    Martinez-Blanco, H.3    Ferrero, M.A.4    Monteagudo-Mera, A.5    Rodriguez-Aparicio, L.B.6
  • 172
    • 84907314485 scopus 로고    scopus 로고
    • Luteolin decreases the attachment, invasion and cytotoxicity of UPEC in bladder epithelial cells and inhibits UPEC biofilm formation
    • Shen, X.-f.; Ren, L.-b.; Teng, Y.; Zheng, S.; Yang, X.-l.; Guo, X.-j.; Wang, X.-y.; Sha, K.-h.; Li, N.; Xu, G.-y. et al. Luteolin decreases the attachment, invasion and cytotoxicity of UPEC in bladder epithelial cells and inhibits UPEC biofilm formation Food Chem. Toxicol. 2014, 72 (0) 204-211 10.1016/j.fct.2014.07.019
    • (2014) Food Chem. Toxicol. , vol.72 , pp. 204-211
    • Shen, X.-F.1    Ren, L.-B.2    Teng, Y.3    Zheng, S.4    Yang, X.-L.5    Guo, X.-J.6    Wang, X.-Y.7    Sha, K.-H.8    Li, N.9    Xu, G.-Y.10
  • 173
    • 84921661514 scopus 로고    scopus 로고
    • Teucrium polium phenylethanol and iridoid glycoside characterization and flavonoid inhibition of biofilm-forming Staphylococcus aureus
    • Elmasri, W. A.; Yang, T.; Tran, P.; Hegazy, M. E.; Hamood, A. N.; Mechref, Y.; Pare, P. W. Teucrium polium phenylethanol and iridoid glycoside characterization and flavonoid inhibition of biofilm-forming Staphylococcus aureus J. Nat. Prod. 2015, 78 (1) 2-9 10.1021/np5004092
    • (2015) J. Nat. Prod. , vol.78 , Issue.1 , pp. 2-9
    • Elmasri, W.A.1    Yang, T.2    Tran, P.3    Hegazy, M.E.4    Hamood, A.N.5    Mechref, Y.6    Pare, P.W.7
  • 175
    • 84858076522 scopus 로고    scopus 로고
    • Eradication of Propionibacterium acnes biofilms by plant extracts and putative identification of icariin, resveratrol and salidroside as active compounds
    • Coenye, T.; Brackman, G.; Rigole, P.; De Witte, E.; Honraet, K.; Rossel, B.; Nelis, H. J. Eradication of Propionibacterium acnes biofilms by plant extracts and putative identification of icariin, resveratrol and salidroside as active compounds Phytomedicine 2012, 19 (5) 409-412 10.1016/j.phymed.2011.10.005
    • (2012) Phytomedicine , vol.19 , Issue.5 , pp. 409-412
    • Coenye, T.1    Brackman, G.2    Rigole, P.3    De Witte, E.4    Honraet, K.5    Rossel, B.6    Nelis, H.J.7
  • 176
    • 84878550765 scopus 로고    scopus 로고
    • Anti-biofilm activities of quercetin and tannic acid against Staphylococcus aureus
    • Lee, J.-H.; Park, J.-H.; Cho, H. S.; Joo, S. W.; Cho, M. H.; Lee, J. Anti-biofilm activities of quercetin and tannic acid against Staphylococcus aureus Biofouling 2013, 29 (5) 491-499 10.1080/08927014.2013.788692
    • (2013) Biofouling , vol.29 , Issue.5 , pp. 491-499
    • Lee, J.-H.1    Park, J.-H.2    Cho, H.S.3    Joo, S.W.4    Cho, M.H.5    Lee, J.6
  • 177
    • 84871315208 scopus 로고    scopus 로고
    • Flavone reduces the production of virulence factors, staphyloxanthin and alpha-hemolysin, in Staphylococcus aureus
    • Lee, J. H.; Park, J. H.; Cho, M. H.; Lee, J. Flavone reduces the production of virulence factors, staphyloxanthin and alpha-hemolysin, in Staphylococcus aureus Curr. Microbiol. 2012, 65 (6) 726-732 10.1007/s00284-012-0229-x
    • (2012) Curr. Microbiol. , vol.65 , Issue.6 , pp. 726-732
    • Lee, J.H.1    Park, J.H.2    Cho, M.H.3    Lee, J.4
  • 178
    • 33745933320 scopus 로고    scopus 로고
    • Guaijaverin - A plant flavonoid as potential antiplaque agent against Streptococcus mutans
    • Prabu, G. R.; Gnanamani, A.; Sadulla, S. Guaijaverin-a plant flavonoid as potential antiplaque agent against Streptococcus mutans J. Appl. Microbiol. 2006, 101 (2) 487-495 10.1111/j.1365-2672.2006.02912.x
    • (2006) J. Appl. Microbiol. , vol.101 , Issue.2 , pp. 487-495
    • Prabu, G.R.1    Gnanamani, A.2    Sadulla, S.3
  • 179
    • 79952528409 scopus 로고    scopus 로고
    • The anti-biofouling effect of polyphenols against Streptococcus mutans
    • Sendamangalam, V.; Choi, O. K.; Kim, D.; Seo, Y. The anti-biofouling effect of polyphenols against Streptococcus mutans Biofouling 2011, 27 (1) 13-19 10.1080/08927014.2010.535897
    • (2011) Biofouling , vol.27 , Issue.1 , pp. 13-19
    • Sendamangalam, V.1    Choi, O.K.2    Kim, D.3    Seo, Y.4
  • 180
  • 181
    • 84920170415 scopus 로고    scopus 로고
    • Novel strategy for biofilm inhibition by using small molecules targeting molecular chaperone DnaK
    • Arita-Morioka, K.-i.; Yamanaka, K.; Mizunoe, Y.; Ogura, T.; Sugimoto, S. Novel strategy for biofilm inhibition by using small molecules targeting molecular chaperone DnaK Antimicrob. Agents Chemother. 2015, 59 (1) 633-641 10.1128/AAC.04465-14
    • (2015) Antimicrob. Agents Chemother. , vol.59 , Issue.1 , pp. 633-641
    • Arita-Morioka, K.-I.1    Yamanaka, K.2    Mizunoe, Y.3    Ogura, T.4    Sugimoto, S.5
  • 182
    • 84893682189 scopus 로고    scopus 로고
    • Morin inhibits sortase A and subsequent biofilm formation in Streptococcus mutans
    • Huang, P.; Hu, P.; Zhou, S. Y.; Li, Q.; Chen, W. M. Morin inhibits sortase A and subsequent biofilm formation in Streptococcus mutans Curr. Microbiol. 2014, 68 (1) 47-52 10.1007/s00284-013-0439-x
    • (2014) Curr. Microbiol. , vol.68 , Issue.1 , pp. 47-52
    • Huang, P.1    Hu, P.2    Zhou, S.Y.3    Li, Q.4    Chen, W.M.5
  • 183
    • 84869496689 scopus 로고    scopus 로고
    • Computational discovery of putative quorum sensing inhibitors against LasR and RhlR receptor proteins of Pseudomonas aeruginosa
    • Annapoorani, A.; Umamageswaran, V.; Parameswari, R.; Pandian, S. K.; Ravi, A. V. Computational discovery of putative quorum sensing inhibitors against LasR and RhlR receptor proteins of Pseudomonas aeruginosa J. Comput.-Aided Mol. Des. 2012, 26 (9) 1067-1077 10.1007/s10822-012-9599-1
    • (2012) J. Comput.-Aided Mol. Des. , vol.26 , Issue.9 , pp. 1067-1077
    • Annapoorani, A.1    Umamageswaran, V.2    Parameswari, R.3    Pandian, S.K.4    Ravi, A.V.5
  • 184
    • 40849142210 scopus 로고    scopus 로고
    • In vitro anti-biofilm activity of macelignan isolated from Myristica fragrans Houtt. Against oral primary colonizer bacteria
    • Yanti; Rukayadi, Y.; Kim, K. H.; Hwang, J. K. In vitro anti-biofilm activity of macelignan isolated from Myristica fragrans Houtt. against oral primary colonizer bacteria Phytother. Res. 2008, 22 (3) 308-312 10.1002/ptr.2312
    • (2008) Phytother. Res. , vol.22 , Issue.3 , pp. 308-312
    • Yanti1    Rukayadi, Y.2    Kim, K.H.3    Hwang, J.K.4
  • 185
    • 80055061451 scopus 로고    scopus 로고
    • Transcriptional and functional analysis of the effects of magnolol: Inhibition of autolysis and biofilms in Staphylococcus aureus
    • Wang, D.; Jin, Q.; Xiang, H.; Wang, W.; Guo, N.; Zhang, K.; Tang, X.; Meng, R.; Feng, H.; Liu, L. et al. Transcriptional and functional analysis of the effects of magnolol: inhibition of autolysis and biofilms in Staphylococcus aureus PLoS One 2011, 6 (10) e26833 10.1371/journal.pone.0026833
    • (2011) PLoS One , vol.6 , Issue.10 , pp. e26833
    • Wang, D.1    Jin, Q.2    Xiang, H.3    Wang, W.4    Guo, N.5    Zhang, K.6    Tang, X.7    Meng, R.8    Feng, H.9    Liu, L.10
  • 186
    • 84881279581 scopus 로고    scopus 로고
    • Synergistic antibacterial and antibiofilm effect between (+)-medioresinol and antibiotics in vitro
    • Hwang, J. H.; Choi, H.; Hwang, I. S.; Kim, A. R.; Woo, E. R.; Lee, D. G. Synergistic antibacterial and antibiofilm effect between (+)-medioresinol and antibiotics in vitro Appl. Biochem. Biotechnol. 2013, 170 (8) 1934-1941 10.1007/s12010-013-0351-7
    • (2013) Appl. Biochem. Biotechnol. , vol.170 , Issue.8 , pp. 1934-1941
    • Hwang, J.H.1    Choi, H.2    Hwang, I.S.3    Kim, A.R.4    Woo, E.R.5    Lee, D.G.6
  • 187
    • 84891740358 scopus 로고    scopus 로고
    • Antistaphylococcal and biofilm inhibitory activities of gallic, caffeic, and chlorogenic acids
    • Luis, A.; Silva, F.; Sousa, S.; Duarte, A. P.; Domingues, F. Antistaphylococcal and biofilm inhibitory activities of gallic, caffeic, and chlorogenic acids Biofouling 2014, 30 (1) 69-79 10.1080/08927014.2013.845878
    • (2014) Biofouling , vol.30 , Issue.1 , pp. 69-79
    • Luis, A.1    Silva, F.2    Sousa, S.3    Duarte, A.P.4    Domingues, F.5
  • 188
    • 84864539034 scopus 로고    scopus 로고
    • The activity of ferulic and gallic acids in biofilm prevention and control of pathogenic bacteria
    • Borges, A.; Saavedra, M. J.; Simoes, M. The activity of ferulic and gallic acids in biofilm prevention and control of pathogenic bacteria Biofouling 2012, 28 (7) 755-767 10.1080/08927014.2012.706751
    • (2012) Biofouling , vol.28 , Issue.7 , pp. 755-767
    • Borges, A.1    Saavedra, M.J.2    Simoes, M.3
  • 189
    • 84930930607 scopus 로고    scopus 로고
    • Inhibition of gallic acid on the growth and biofilm formation of Escherichia coli and Streptococcus mutans
    • Shao, D.; Li, J.; Li, J.; Tang, R.; Liu, L.; Shi, J.; Huang, Q.; Yang, H. Inhibition of gallic acid on the growth and biofilm formation of Escherichia coli and Streptococcus mutans J. Food Sci. 2015, 80 (6) M1299-M1305 10.1111/1750-3841.12902
    • (2015) J. Food Sci. , vol.80 , Issue.6 , pp. M1299-M1305
    • Shao, D.1    Li, J.2    Li, J.3    Tang, R.4    Liu, L.5    Shi, J.6    Huang, Q.7    Yang, H.8
  • 190
    • 84934765639 scopus 로고    scopus 로고
    • Effect of tannic and gallic acids alone or in combination with carbenicillin or tetracycline on Chromobacterium violaceum CV026 growth, motility, and biofilm formation
    • Dusane, D. H.; O'May, C.; Tufenkji, N. Effect of tannic and gallic acids alone or in combination with carbenicillin or tetracycline on Chromobacterium violaceum CV026 growth, motility, and biofilm formation Can. J. Microbiol. 2015, 61 (7) 487-494 10.1139/cjm-2015-0101
    • (2015) Can. J. Microbiol. , vol.61 , Issue.7 , pp. 487-494
    • Dusane, D.H.1    O'May, C.2    Tufenkji, N.3
  • 191
    • 58149133904 scopus 로고    scopus 로고
    • Inhibitory effect of methyl gallate and gallic acid on oral bacteria
    • Kang, M. S.; Oh, J. S.; Kang, I. C.; Hong, S. J.; Choi, C. H. Inhibitory effect of methyl gallate and gallic acid on oral bacteria J. Microbiol. 2008, 46 (6) 744-750 10.1007/s12275-008-0235-7
    • (2008) J. Microbiol. , vol.46 , Issue.6 , pp. 744-750
    • Kang, M.S.1    Oh, J.S.2    Kang, I.C.3    Hong, S.J.4    Choi, C.H.5
  • 192
    • 23944488885 scopus 로고    scopus 로고
    • Down regulation of virulence factors of Pseudomonas aeruginosa by salicylic acid attenuates its virulence on Arabidopsis thaliana and Caenorhabditis elegans
    • Prithiviraj, B.; Bais, H. P.; Weir, T.; Suresh, B.; Najarro, E. H.; Dayakar, B. V.; Schweizer, H. P.; Vivanco, J. M. Down regulation of virulence factors of Pseudomonas aeruginosa by salicylic acid attenuates its virulence on Arabidopsis thaliana and Caenorhabditis elegans Infect. Immun. 2005, 73 (9) 5319-5328 10.1128/IAI.73.9.5319-5328.2005
    • (2005) Infect. Immun. , vol.73 , Issue.9 , pp. 5319-5328
    • Prithiviraj, B.1    Bais, H.P.2    Weir, T.3    Suresh, B.4    Najarro, E.H.5    Dayakar, B.V.6    Schweizer, H.P.7    Vivanco, J.M.8
  • 193
    • 84892844819 scopus 로고    scopus 로고
    • Ginkgolic acids and Ginkgo biloba extract inhibit Escherichia coli O157:H7 and Staphylococcus aureus biofilm formation
    • Lee, J.-H.; Kim, Y.-G.; Ryu, S. Y.; Cho, M. H.; Lee, J. Ginkgolic acids and Ginkgo biloba extract inhibit Escherichia coli O157:H7 and Staphylococcus aureus biofilm formation Int. J. Food Microbiol. 2014, 174 (0) 47-55 10.1016/j.ijfoodmicro.2013.12.030
    • (2014) Int. J. Food Microbiol. , vol.174 , pp. 47-55
    • Lee, J.-H.1    Kim, Y.-G.2    Ryu, S.Y.3    Cho, M.H.4    Lee, J.5
  • 195
    • 84874644637 scopus 로고    scopus 로고
    • In vitro antibacterial and antibiofilm activities of chlorogenic acid against clinical isolates of Stenotrophomonas maltophilia including the trimethoprim/sulfamethoxazole resistant strain
    • Karunanidhi, A.; Thomas, R.; van Belkum, A.; Neela, V. In vitro antibacterial and antibiofilm activities of chlorogenic acid against clinical isolates of Stenotrophomonas maltophilia including the trimethoprim/sulfamethoxazole resistant strain BioMed Res. Int. 2013, 2013, 1-7 10.1155/2013/392058
    • (2013) BioMed Res. Int. , vol.2013 , pp. 1-7
    • Karunanidhi, A.1    Thomas, R.2    Van Belkum, A.3    Neela, V.4
  • 196
    • 84922453919 scopus 로고    scopus 로고
    • Redox-active compounds with a history of human use: Antistaphylococcal action and potential for repurposing as topical antibiofilm agents
    • Ooi, N.; Eady, E. A.; Cove, J. H.; O'Neill, A. J. Redox-active compounds with a history of human use: antistaphylococcal action and potential for repurposing as topical antibiofilm agents J. Antimicrob. Chemother. 2015, 70 (2) 479-488 10.1093/jac/dku409
    • (2015) J. Antimicrob. Chemother. , vol.70 , Issue.2 , pp. 479-488
    • Ooi, N.1    Eady, E.A.2    Cove, J.H.3    O'Neill, A.J.4
  • 197
    • 84892588680 scopus 로고    scopus 로고
    • In silico and in vitro studies of cinnamaldehyde and their derivatives against LuxS in Streptococcus pyogenes: Effects on biofilm and virulence genes
    • Beema Shafreen, R. M.; Selvaraj, C.; Singh, S. K.; Karutha Pandian, S. In silico and in vitro studies of cinnamaldehyde and their derivatives against LuxS in Streptococcus pyogenes: effects on biofilm and virulence genes J. Mol. Recognit. 2014, 27 (2) 106-116 10.1002/jmr.2339
    • (2014) J. Mol. Recognit. , vol.27 , Issue.2 , pp. 106-116
    • Beema Shafreen, R.M.1    Selvaraj, C.2    Singh, S.K.3    Karutha Pandian, S.4
  • 198
    • 80052640506 scopus 로고    scopus 로고
    • Effect of cinnamaldehyde on biofilm formation and sarA expression by methicillin-resistant Staphylococcus aureus
    • Jia, P.; Xue, Y. J.; Duan, X. J.; Shao, S. H. Effect of cinnamaldehyde on biofilm formation and sarA expression by methicillin-resistant Staphylococcus aureus Lett. Appl. Microbiol. 2011, 53 (4) 409-416 10.1111/j.1472-765X.2011.03122.x
    • (2011) Lett. Appl. Microbiol. , vol.53 , Issue.4 , pp. 409-416
    • Jia, P.1    Xue, Y.J.2    Duan, X.J.3    Shao, S.H.4
  • 199
    • 84878897392 scopus 로고    scopus 로고
    • Antibiofilm effect of plant derived antimicrobials on Listeria monocytogenes
    • Upadhyay, A.; Upadhyaya, I.; Kollanoor-Johny, A.; Venkitanarayanan, K. Antibiofilm effect of plant derived antimicrobials on Listeria monocytogenes Food Microbiol. 2013, 36 (1) 79-89 10.1016/j.fm.2013.04.010
    • (2013) Food Microbiol. , vol.36 , Issue.1 , pp. 79-89
    • Upadhyay, A.1    Upadhyaya, I.2    Kollanoor-Johny, A.3    Venkitanarayanan, K.4
  • 200
    • 77953123901 scopus 로고    scopus 로고
    • Antibiofilm effect of trans-cinnamaldehyde on uropathogenic Escherichia coli
    • Amalaradjou, M. A. R.; Narayanan, A.; Baskaran, S. A.; Venkitanarayanan, K. Antibiofilm effect of trans-cinnamaldehyde on uropathogenic Escherichia coli J. Urol. 2010, 184 (1) 358-363 10.1016/j.juro.2010.03.006
    • (2010) J. Urol. , vol.184 , Issue.1 , pp. 358-363
    • Amalaradjou, M.A.R.1    Narayanan, A.2    Baskaran, S.A.3    Venkitanarayanan, K.4
  • 201
    • 84924940363 scopus 로고    scopus 로고
    • Eugenol: A phyto-compound effective against methicillin-resistant and methicillin-sensitive Staphylococcus aureus clinical strain biofilms
    • Yadav, M. K.; Chae, S.-W.; Im, G. J.; Chung, J.-W.; Song, J.-J. Eugenol: a phyto-compound effective against methicillin-resistant and methicillin-sensitive Staphylococcus aureus clinical strain biofilms PLoS One 2015, 10 (3) e0119564 10.1371/journal.pone.0119564
    • (2015) PLoS One , vol.10 , Issue.3 , pp. e0119564
    • Yadav, M.K.1    Chae, S.-W.2    Im, G.J.3    Chung, J.-W.4    Song, J.-J.5
  • 202
    • 84884481451 scopus 로고    scopus 로고
    • Zingerone inhibit biofilm formation and improve antibiofilm efficacy of ciprofloxacin against Pseudomonas aeruginosa PAO1
    • Kumar, L.; Chhibber, S.; Harjai, K. Zingerone inhibit biofilm formation and improve antibiofilm efficacy of ciprofloxacin against Pseudomonas aeruginosa PAO1 Fitoterapia 2013, 90 (0) 73-78 10.1016/j.fitote.2013.06.017
    • (2013) Fitoterapia , vol.90 , pp. 73-78
    • Kumar, L.1    Chhibber, S.2    Harjai, K.3
  • 203
    • 84888042114 scopus 로고    scopus 로고
    • Curcumin reduces Streptococcus mutans biofilm formation by inhibiting sortase A activity
    • Hu, P.; Huang, P.; Chen, M. W. Curcumin reduces Streptococcus mutans biofilm formation by inhibiting sortase A activity Arch. Oral Biol. 2013, 58 (10) 1343-1348 10.1016/j.archoralbio.2013.05.004
    • (2013) Arch. Oral Biol. , vol.58 , Issue.10 , pp. 1343-1348
    • Hu, P.1    Huang, P.2    Chen, M.W.3
  • 204
    • 34247117942 scopus 로고    scopus 로고
    • In vitro inhibition of Streptococcus mutans biofilm formation on hydroxyapatite by subinhibitory concentrations of anthraquinones
    • Coenye, T.; Honraet, K.; Rigole, P.; Jimenez, P. N.; Nelis, H. J. In vitro inhibition of Streptococcus mutans biofilm formation on hydroxyapatite by subinhibitory concentrations of anthraquinones Antimicrob. Agents Chemother. 2007, 51 (4) 1541-1544 10.1128/AAC.00999-06
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.4 , pp. 1541-1544
    • Coenye, T.1    Honraet, K.2    Rigole, P.3    Jimenez, P.N.4    Nelis, H.J.5
  • 205
    • 84920815507 scopus 로고    scopus 로고
    • In-vitro antimicrobial, antibiofilm, cytotoxic, antifeedant and larvicidal properties of novel quinone isolated from Aegle marmelos (Linn.) Correa
    • Rejiniemon, T.; Arasu, M.; Duraipandiyan, V.; Ponmurugan, K.; Al-Dhabi, N.; Arokiyaraj, S.; Agastian, P.; Choi, K. In-vitro antimicrobial, antibiofilm, cytotoxic, antifeedant and larvicidal properties of novel quinone isolated from Aegle marmelos (Linn.) Correa Ann. Clin. Microbiol. Antimicrob. 2014, 13 (1) 48 10.1186/s12941-014-0048-y
    • (2014) Ann. Clin. Microbiol. Antimicrob. , vol.13 , Issue.1 , pp. 48
    • Rejiniemon, T.1    Arasu, M.2    Duraipandiyan, V.3    Ponmurugan, K.4    Al-Dhabi, N.5    Arokiyaraj, S.6    Agastian, P.7    Choi, K.8
  • 206
    • 79953842455 scopus 로고    scopus 로고
    • Antibacterial activity of Thymoquinone, an active principle of Nigella sativa and its potency to prevent bacterial biofilm formation
    • Chaieb, K.; Kouidhi, B.; Jrah, H.; Mahdouani, K.; Bakhrouf, A. Antibacterial activity of Thymoquinone, an active principle of Nigella sativa and its potency to prevent bacterial biofilm formation BMC Complementary Altern. Med. 2011, 11 (1) 29 10.1186/1472-6882-11-29
    • (2011) BMC Complementary Altern. Med. , vol.11 , Issue.1 , pp. 29
    • Chaieb, K.1    Kouidhi, B.2    Jrah, H.3    Mahdouani, K.4    Bakhrouf, A.5
  • 207
    • 84906983077 scopus 로고    scopus 로고
    • Stilbenes reduce Staphylococcus aureus hemolysis, biofilm formation, and virulence
    • Lee, K.; Lee, J.-H.; Ryu, S. Y.; Cho, M. H.; Lee, J. Stilbenes reduce Staphylococcus aureus hemolysis, biofilm formation, and virulence Foodborne Pathog. Dis. 2014, 11 (9) 710-717 10.1089/fpd.2014.1758
    • (2014) Foodborne Pathog. Dis. , vol.11 , Issue.9 , pp. 710-717
    • Lee, K.1    Lee, J.-H.2    Ryu, S.Y.3    Cho, M.H.4    Lee, J.5
  • 208
    • 84863721141 scopus 로고    scopus 로고
    • Inhibition of bacterial growth and biofilm production by constituents from Hypericum spp
    • Sarkisian, S. A.; Janssen, M. J.; Matta, H.; Henry, G. E.; LaPlante, K. L.; Rowley, D. C. Inhibition of bacterial growth and biofilm production by constituents from Hypericum spp Phytother. Res. 2012, 26 (7) 1012-1016 10.1002/ptr.3675
    • (2012) Phytother. Res. , vol.26 , Issue.7 , pp. 1012-1016
    • Sarkisian, S.A.1    Janssen, M.J.2    Matta, H.3    Henry, G.E.4    LaPlante, K.L.5    Rowley, D.C.6
  • 209
    • 68949083468 scopus 로고    scopus 로고
    • Activity of panduratin A isolated from Kaempferia pandurata Roxb. Against multi-species oral biofilms in vitro
    • Yanti; Rukayadi, Y.; Lee, K.-H.; Hwang, J.-K. Activity of panduratin A isolated from Kaempferia pandurata Roxb. against multi-species oral biofilms in vitro J. Oral Sci. 2009, 51 (1) 87-95 10.2334/josnusd.51.87
    • (2009) J. Oral Sci. , vol.51 , Issue.1 , pp. 87-95
    • Yanti1    Rukayadi, Y.2    Lee, K.-H.3    Hwang, J.-K.4
  • 211
    • 79952201070 scopus 로고    scopus 로고
    • Inhibition of Streptococcus mutans biofilm accumulation and development of dental caries in vivo by 7-epiclusianone and fluoride
    • Murata, R. M.; Branco-de-Almeida, L. S.; Franco, E. M.; Yatsuda, R.; dos Santos, M. H.; de Alencar, S. M.; Koo, H.; Rosalen, P. L. Inhibition of Streptococcus mutans biofilm accumulation and development of dental caries in vivo by 7-epiclusianone and fluoride Biofouling 2010, 26 (7) 865-872 10.1080/08927014.2010.527435
    • (2010) Biofouling , vol.26 , Issue.7 , pp. 865-872
    • Murata, R.M.1    Branco-De-Almeida, L.S.2    Franco, E.M.3    Yatsuda, R.4    Dos Santos, M.H.5    De Alencar, S.M.6    Koo, H.7    Rosalen, P.L.8
  • 212
    • 42449117065 scopus 로고    scopus 로고
    • Inhibitory effects of 7-epiclusianone on glucan synthesis, acidogenicity and biofilm formation by Streptococcus mutans
    • Murata, R. M.; Branco de Almeida, L. S. B.; Yatsuda, R.; dos Santos, M. H.; Nagem, T. J.; Rosalen, P. L.; Koo, H. Inhibitory effects of 7-epiclusianone on glucan synthesis, acidogenicity and biofilm formation by Streptococcus mutans FEMS Microbiol. Lett. 2008, 282 (2) 174-181 10.1111/j.1574-6968.2008.01117.x
    • (2008) FEMS Microbiol. Lett. , vol.282 , Issue.2 , pp. 174-181
    • Murata, R.M.1    Branco De Almeida, L.S.B.2    Yatsuda, R.3    Dos Santos, M.H.4    Nagem, T.J.5    Rosalen, P.L.6    Koo, H.7
  • 213
    • 84885056682 scopus 로고    scopus 로고
    • Biological evaluation of hyperforin and its hydrogenated analogue on bacterial growth and biofilm production
    • Schiavone, B. I. P.; Rosato, A.; Marilena, M.; Gibbons, S.; Bombardelli, E.; Verotta, L.; Franchini, C.; Corbo, F. Biological evaluation of hyperforin and its hydrogenated analogue on bacterial growth and biofilm production J. Nat. Prod. 2013, 76 (9) 1819-1823 10.1021/np400394c
    • (2013) J. Nat. Prod. , vol.76 , Issue.9 , pp. 1819-1823
    • Schiavone, B.I.P.1    Rosato, A.2    Marilena, M.3    Gibbons, S.4    Bombardelli, E.5    Verotta, L.6    Franchini, C.7    Corbo, F.8
  • 214
    • 84880791598 scopus 로고    scopus 로고
    • Inhibition of Pseudomonas aeruginosa and Escherichia coli O157:H7 biofilm formation by plant metabolite epsilon-viniferin
    • Cho, H. S.; Lee, J. H.; Ryu, S. Y.; Joo, S. W.; Cho, M. H.; Lee, J. Inhibition of Pseudomonas aeruginosa and Escherichia coli O157:H7 biofilm formation by plant metabolite epsilon-viniferin J. Agric. Food Chem. 2013, 61 (29) 7120-7126 10.1021/jf4009313
    • (2013) J. Agric. Food Chem. , vol.61 , Issue.29 , pp. 7120-7126
    • Cho, H.S.1    Lee, J.H.2    Ryu, S.Y.3    Joo, S.W.4    Cho, M.H.5    Lee, J.6
  • 215
    • 84896494009 scopus 로고    scopus 로고
    • Resveratrol - A potential inhibitor of biofilm formation in Vibrio cholerae
    • Augustine, N.; Goel, A. K.; Sivakumar, K. C.; Kumar, R. A.; Thomas, S. Resveratrol-a potential inhibitor of biofilm formation in Vibrio cholerae Phytomedicine 2014, 21 (3) 286-289 10.1016/j.phymed.2013.09.010
    • (2014) Phytomedicine , vol.21 , Issue.3 , pp. 286-289
    • Augustine, N.1    Goel, A.K.2    Sivakumar, K.C.3    Kumar, R.A.4    Thomas, S.5
  • 216
    • 84885916457 scopus 로고    scopus 로고
    • Diverse plant extracts and trans-resveratrol inhibit biofilm formation and swarming of Escherichia coli O157:H7
    • Lee, J.-H.; Cho, H. S.; Joo, S. W.; Chandra Regmi, S.; Kim, J.-A.; Ryu, C.-M.; Ryu, S. Y.; Cho, M. H.; Lee, J. Diverse plant extracts and trans-resveratrol inhibit biofilm formation and swarming of Escherichia coli O157:H7 Biofouling 2013, 29 (10) 1189-1203 10.1080/08927014.2013.832223
    • (2013) Biofouling , vol.29 , Issue.10 , pp. 1189-1203
    • Lee, J.-H.1    Cho, H.S.2    Joo, S.W.3    Chandra Regmi, S.4    Kim, J.-A.5    Ryu, C.-M.6    Ryu, S.Y.7    Cho, M.H.8    Lee, J.9
  • 217
    • 84893076865 scopus 로고    scopus 로고
    • Resveratrol oligomers inhibit biofilm formation of Escherichia coli O157:H7 and Pseudomonas aeruginosa
    • Lee, J. H.; Kim, Y. G.; Ryu, S. Y.; Cho, M. H.; Lee, J. Resveratrol oligomers inhibit biofilm formation of Escherichia coli O157:H7 and Pseudomonas aeruginosa J. Nat. Prod. 2014, 77 (1) 168-172 10.1021/np400756g
    • (2014) J. Nat. Prod. , vol.77 , Issue.1 , pp. 168-172
    • Lee, J.H.1    Kim, Y.G.2    Ryu, S.Y.3    Cho, M.H.4    Lee, J.5
  • 218
    • 77950506373 scopus 로고    scopus 로고
    • Dietary plant components ellagic acid and tannic acid inhibit Escherichia coli biofilm formation
    • Hancock, V.; Dahl, M.; Vejborg, R. M.; Klemm, P. Dietary plant components ellagic acid and tannic acid inhibit Escherichia coli biofilm formation J. Med. Microbiol. 2010, 59 (4) 496-498 10.1099/jmm.0.013680-0
    • (2010) J. Med. Microbiol. , vol.59 , Issue.4 , pp. 496-498
    • Hancock, V.1    Dahl, M.2    Vejborg, R.M.3    Klemm, P.4
  • 219
    • 84883657057 scopus 로고    scopus 로고
    • The anti-biofilm potential of pomegranate (Punica granatum L.) extract against human bacterial and fungal pathogens
    • Bakkiyaraj, D.; Nandhini, J. R.; Malathy, B.; Pandian, S. K. The anti-biofilm potential of pomegranate (Punica granatum L.) extract against human bacterial and fungal pathogens Biofouling 2013, 29 (8) 929-937 10.1080/08927014.2013.820825
    • (2013) Biofouling , vol.29 , Issue.8 , pp. 929-937
    • Bakkiyaraj, D.1    Nandhini, J.R.2    Malathy, B.3    Pandian, S.K.4
  • 220
    • 79952356812 scopus 로고    scopus 로고
    • Inhibitory effects of 1,2,3,4,6-penta-O-galloyl-β-d-glucopyranose on biofilm formation by Staphylococcus aureus
    • Lin, M.-H.; Chang, F.-R.; Hua, M.-Y.; Wu, Y.-C.; Liu, S.-T. Inhibitory effects of 1,2,3,4,6-penta-O-galloyl-β-d-glucopyranose on biofilm formation by Staphylococcus aureus Antimicrob. Agents Chemother. 2011, 55 (3) 1021-1027 10.1128/AAC.00843-10
    • (2011) Antimicrob. Agents Chemother. , vol.55 , Issue.3 , pp. 1021-1027
    • Lin, M.-H.1    Chang, F.-R.2    Hua, M.-Y.3    Wu, Y.-C.4    Liu, S.-T.5
  • 221
    • 84873034894 scopus 로고    scopus 로고
    • Tannic acid inhibits Staphylococcus aureus surface colonization in an IsaA-dependent manner
    • Payne, D. E.; Martin, N. R.; Parzych, K. R.; Rickard, A. H.; Underwood, A.; Boles, B. R. Tannic acid inhibits Staphylococcus aureus surface colonization in an IsaA-dependent manner Infect. Immun. 2013, 81 (2) 496-504 10.1128/IAI.00877-12
    • (2013) Infect. Immun. , vol.81 , Issue.2 , pp. 496-504
    • Payne, D.E.1    Martin, N.R.2    Parzych, K.R.3    Rickard, A.H.4    Underwood, A.5    Boles, B.R.6
  • 223
    • 84878846663 scopus 로고    scopus 로고
    • Tannins possessing bacteriostatic effect impair Pseudomonas aeruginosa adhesion and biofilm formation
    • Trentin, D. S.; Silva, D. B.; Amaral, M. W.; Zimmer, K. R.; Silva, M. V.; Lopes, N. P.; Giordani, R. B.; Macedo, A. J. Tannins possessing bacteriostatic effect impair Pseudomonas aeruginosa adhesion and biofilm formation PLoS One 2013, 8 (6) e66257 10.1371/journal.pone.0066257
    • (2013) PLoS One , vol.8 , Issue.6 , pp. e66257
    • Trentin, D.S.1    Silva, D.B.2    Amaral, M.W.3    Zimmer, K.R.4    Silva, M.V.5    Lopes, N.P.6    Giordani, R.B.7    Macedo, A.J.8
  • 224
    • 33645006653 scopus 로고    scopus 로고
    • Inhibitory effects of cranberry polyphenols on formation and acidogenicity of Streptococcus mutans biofilms
    • Duarte, S.; Gregoire, S.; Singh, A. P.; Vorsa, N.; Schaich, K.; Bowen, W. H.; Koo, H. Inhibitory effects of cranberry polyphenols on formation and acidogenicity of Streptococcus mutans biofilms FEMS Microbiol. Lett. 2006, 257 (1) 50-56 10.1111/j.1574-6968.2006.00147.x
    • (2006) FEMS Microbiol. Lett. , vol.257 , Issue.1 , pp. 50-56
    • Duarte, S.1    Gregoire, S.2    Singh, A.P.3    Vorsa, N.4    Schaich, K.5    Bowen, W.H.6    Koo, H.7
  • 225
    • 77949440100 scopus 로고    scopus 로고
    • Influence of cranberry proanthocyanidins on formation of biofilms by Streptococcus mutans on saliva-coated apatitic surface and on dental caries development in vivo
    • Koo, H.; Duarte, S.; Murata, R. M.; Scott-Anne, K.; Gregoire, S.; Watson, G. E.; Singh, A. P.; Vorsa, N. Influence of cranberry proanthocyanidins on formation of biofilms by Streptococcus mutans on saliva-coated apatitic surface and on dental caries development in vivo Caries Res. 2010, 44 (2) 116-126 10.1159/000296306
    • (2010) Caries Res. , vol.44 , Issue.2 , pp. 116-126
    • Koo, H.1    Duarte, S.2    Murata, R.M.3    Scott-Anne, K.4    Gregoire, S.5    Watson, G.E.6    Singh, A.P.7    Vorsa, N.8
  • 226
    • 84880045543 scopus 로고    scopus 로고
    • The specific degree-of-polymerization of A-type proanthocyanidin oligomers impacts Streptococcus mutans glucan-mediated adhesion and transcriptome responses within biofilms
    • Feng, G.; Klein, M. I.; Gregoire, S.; Singh, A. P.; Vorsa, N.; Koo, H. The specific degree-of-polymerization of A-type proanthocyanidin oligomers impacts Streptococcus mutans glucan-mediated adhesion and transcriptome responses within biofilms Biofouling 2013, 29 (6) 629-640 10.1080/08927014.2013.794456
    • (2013) Biofouling , vol.29 , Issue.6 , pp. 629-640
    • Feng, G.1    Klein, M.I.2    Gregoire, S.3    Singh, A.P.4    Vorsa, N.5    Koo, H.6
  • 227
    • 84924333674 scopus 로고    scopus 로고
    • Cranberry proanthocyanidins have anti-biofilm properties against Pseudomonas aeruginosa
    • Ulrey, R.; Barksdale, S.; Zhou, W.; van Hoek, M. Cranberry proanthocyanidins have anti-biofilm properties against Pseudomonas aeruginosa BMC Complementary Altern. Med. 2014, 14 (1) 499-12 10.1186/1472-6882-14-499
    • (2014) BMC Complementary Altern. Med. , vol.14 , Issue.1 , pp. 499-512
    • Ulrey, R.1    Barksdale, S.2    Zhou, W.3    Van Hoek, M.4
  • 228
    • 84908568733 scopus 로고    scopus 로고
    • α-Mangostin disrupts the development of Streptococcocus mutans biofilms and facilitates its mechanical removal
    • Nguyen, P. T. M.; Falsetta, M. L.; Hwang, G.; Gonzalez-Begne, M.; Koo, H. α-Mangostin disrupts the development of Streptococcocus mutans biofilms and facilitates its mechanical removal PLoS One 2014, 9 (10) e111312 10.1371/journal.pone.0111312
    • (2014) PLoS One , vol.9 , Issue.10 , pp. e111312
    • Nguyen, P.T.M.1    Falsetta, M.L.2    Hwang, G.3    Gonzalez-Begne, M.4    Koo, H.5
  • 230
    • 84930871165 scopus 로고    scopus 로고
    • Chemical composition and anti-biofilm activity of Thymus sipyleus BOISS. Subsp. Sipyleus BOISS. Var. Davisianus RONNIGER essential oil
    • Ceylan, O.; Ugur, A. Chemical composition and anti-biofilm activity of Thymus sipyleus BOISS. subsp. sipyleus BOISS. var. davisianus RONNIGER essential oil Arch. Pharmacal Res. 2015, 38 (6) 957-965 10.1007/s12272-014-0516-0
    • (2015) Arch. Pharmacal Res. , vol.38 , Issue.6 , pp. 957-965
    • Ceylan, O.1    Ugur, A.2
  • 231
    • 84952009504 scopus 로고    scopus 로고
    • Carvacrol and thymol components inhibiting Pseudomonas aeruginosa adherence and biofilm formation
    • Soumya, E. a.; Saad, I. k.; Hassan, L.; Ghizlane, Z.; Hind, M.; Adnane, R. Carvacrol and thymol components inhibiting Pseudomonas aeruginosa adherence and biofilm formation Afr. J. Microbiol. Res. 2011, 5 (20) 3229-3232 10.5897/AJMR11.275
    • (2011) Afr. J. Microbiol. Res. , vol.5 , Issue.20 , pp. 3229-3232
    • Soumya, E.A.1    Saad, I.K.2    Hassan, L.3    Ghizlane, Z.4    Hind, M.5    Adnane, R.6
  • 232
    • 84920554798 scopus 로고    scopus 로고
    • In vitro anti-quorum sensing activity of phytol
    • Pejin, B.; Ciric, A.; Glamoclija, J.; Nikolic, M.; Sokovic, M. In vitro anti-quorum sensing activity of phytol Nat. Prod. Res. 2015, 29 (4) 374-377 10.1080/14786419.2014.945088
    • (2015) Nat. Prod. Res. , vol.29 , Issue.4 , pp. 374-377
    • Pejin, B.1    Ciric, A.2    Glamoclija, J.3    Nikolic, M.4    Sokovic, M.5
  • 233
    • 84885849180 scopus 로고    scopus 로고
    • (+)-Dehydroabietic Acid, an abietane-type diterpene, inhibits Staphylococcus aureus biofilms in vitro
    • Fallarero, A.; Skogman, M.; Kujala, J.; Rajaratnam, M.; Moreira, V.; Yli-Kauhaluoma, J.; Vuorela, P. (+)-Dehydroabietic Acid, an abietane-type diterpene, inhibits Staphylococcus aureus biofilms in vitro Int. J. Mol. Sci. 2013, 14 (6) 12054-12072 10.3390/ijms140612054
    • (2013) Int. J. Mol. Sci. , vol.14 , Issue.6 , pp. 12054-12072
    • Fallarero, A.1    Skogman, M.2    Kujala, J.3    Rajaratnam, M.4    Moreira, V.5    Yli-Kauhaluoma, J.6    Vuorela, P.7
  • 235
    • 33750087577 scopus 로고    scopus 로고
    • Effect of coating the wells of a polystyrene microtiter plate with xanthorrhizol on the biofilm formation of Streptococcus mutans
    • Rukayadi, Y.; Hwang, J. K. Effect of coating the wells of a polystyrene microtiter plate with xanthorrhizol on the biofilm formation of Streptococcus mutans J. Basic Microbiol. 2006, 46 (5) 410-415 10.1002/jobm.200510088
    • (2006) J. Basic Microbiol. , vol.46 , Issue.5 , pp. 410-415
    • Rukayadi, Y.1    Hwang, J.K.2
  • 236
    • 84860356681 scopus 로고    scopus 로고
    • Ent-trachyloban-19-oic acid isolated from Iostephane heterophylla as a promising antibacterial agent against Streptococcus mutans biofilms
    • Hernández, D. M.; Díaz-Ruiz, G.; Rivero-Cruz, B. E.; Bye, R. A.; Aguilar, M. I.; Rivero-Cruz, J. F. Ent-trachyloban-19-oic acid isolated from Iostephane heterophylla as a promising antibacterial agent against Streptococcus mutans biofilms Fitoterapia 2012, 83 (3) 527-531 10.1016/j.fitote.2011.12.022
    • (2012) Fitoterapia , vol.83 , Issue.3 , pp. 527-531
    • Hernández, D.M.1    Díaz-Ruiz, G.2    Rivero-Cruz, B.E.3    Bye, R.A.4    Aguilar, M.I.5    Rivero-Cruz, J.F.6
  • 238
    • 79955440851 scopus 로고    scopus 로고
    • Bioactive sesqui- and diterpenoids from the Argentine liverwort Porella chilensis
    • Gilabert, M.; Ramos, A. N.; Schiavone, M. M.; Arena, M. E.; Bardon, A. Bioactive sesqui- and diterpenoids from the Argentine liverwort Porella chilensis J. Nat. Prod. 2011, 74 (4) 574-579 10.1021/np100472d
    • (2011) J. Nat. Prod. , vol.74 , Issue.4 , pp. 574-579
    • Gilabert, M.1    Ramos, A.N.2    Schiavone, M.M.3    Arena, M.E.4    Bardon, A.5
  • 239
    • 33645786322 scopus 로고    scopus 로고
    • Effect of farnesol on Staphylococcus aureus biofilm formation and antimicrobial susceptibility
    • Jabra-Rizk, M. A.; Meiller, T. F.; James, C. E.; Shirtliff, M. E. Effect of farnesol on Staphylococcus aureus biofilm formation and antimicrobial susceptibility Antimicrob. Agents Chemother. 2006, 50 (4) 1463-1469 10.1128/AAC.50.4.1463-1469.2006
    • (2006) Antimicrob. Agents Chemother. , vol.50 , Issue.4 , pp. 1463-1469
    • Jabra-Rizk, M.A.1    Meiller, T.F.2    James, C.E.3    Shirtliff, M.E.4
  • 240
    • 79955719927 scopus 로고    scopus 로고
    • Influences of trans-trans farnesol, a membrane-targeting sesquiterpenoid, on Streptococcus mutans physiology and survival within mixed-species oral biofilms
    • Jeon, J.-G.; Pandit, S.; Xiao, J.; Gregoire, S.; Falsetta, M. L.; Klein, M. I.; Koo, H. Influences of trans-trans farnesol, a membrane-targeting sesquiterpenoid, on Streptococcus mutans physiology and survival within mixed-species oral biofilms Int. J. Oral Sci. 2011, 3 (2) 98-106 10.4248/IJOS11038
    • (2011) Int. J. Oral Sci. , vol.3 , Issue.2 , pp. 98-106
    • Jeon, J.-G.1    Pandit, S.2    Xiao, J.3    Gregoire, S.4    Falsetta, M.L.5    Klein, M.I.6    Koo, H.7
  • 241
    • 84920255203 scopus 로고    scopus 로고
    • Anti-biofilm, anti-hemolysis, and anti-virulence activities of black pepper, cananga, myrrh oils, and nerolidol against Staphylococcus aureus
    • Lee, K.; Lee, J. H.; Kim, S. I.; Cho, M. H.; Lee, J. Anti-biofilm, anti-hemolysis, and anti-virulence activities of black pepper, cananga, myrrh oils, and nerolidol against Staphylococcus aureus Appl. Microbiol. Biotechnol. 2014, 98 (22) 9447-9457 10.1007/s00253-014-5903-4
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , Issue.22 , pp. 9447-9457
    • Lee, K.1    Lee, J.H.2    Kim, S.I.3    Cho, M.H.4    Lee, J.5
  • 242
    • 84916882386 scopus 로고    scopus 로고
    • Sesqui- and triterpenoids from the liverwort Lepidozia chordulifera inhibitors of bacterial biofilm and elastase activity of human pathogenic bacteria
    • Gilabert, M.; Marcinkevicius, K.; Andujar, S.; Schiavone, M.; Arena, M. E.; Bardón, A. Sesqui- and triterpenoids from the liverwort Lepidozia chordulifera inhibitors of bacterial biofilm and elastase activity of human pathogenic bacteria Phytomedicine 2015, 22 (1) 77-85 10.1016/j.phymed.2014.10.006
    • (2015) Phytomedicine , vol.22 , Issue.1 , pp. 77-85
    • Gilabert, M.1    Marcinkevicius, K.2    Andujar, S.3    Schiavone, M.4    Arena, M.E.5    Bardón, A.6
  • 243
    • 33846081978 scopus 로고    scopus 로고
    • Effects of plant lactones on the production of biofilm of Pseudomonas aeruginosa
    • Cartagena, E.; Colom, O. A.; Neske, A.; Valdez, J. C.; Bardon, A. Effects of plant lactones on the production of biofilm of Pseudomonas aeruginosa Chem. Pharm. Bull. 2007, 55 (1) 22-25 10.1248/cpb.55.22
    • (2007) Chem. Pharm. Bull. , vol.55 , Issue.1 , pp. 22-25
    • Cartagena, E.1    Colom, O.A.2    Neske, A.3    Valdez, J.C.4    Bardon, A.5
  • 244
    • 84868705441 scopus 로고    scopus 로고
    • Isolimonic acid interferes with Escherichia coli O157:H7 biofilm and TTSS in QseBC and QseA dependent fashion
    • Vikram, A.; Jesudhasan, P. R.; Pillai, S. D.; Patil, B. S. Isolimonic acid interferes with Escherichia coli O157:H7 biofilm and TTSS in QseBC and QseA dependent fashion BMC Microbiol. 2012, 12, 261-261 10.1186/1471-2180-12-261
    • (2012) BMC Microbiol. , vol.12 , pp. 261
    • Vikram, A.1    Jesudhasan, P.R.2    Pillai, S.D.3    Patil, B.S.4
  • 245
    • 77953119596 scopus 로고    scopus 로고
    • Grapefruit bioactive limonoids modulate E. Coli O157:H7 TTSS and biofilm
    • Vikram, A.; Jesudhasan, P. R.; Jayaprakasha, G. K.; Pillai, B. S.; Patil, B. S. Grapefruit bioactive limonoids modulate E. coli O157:H7 TTSS and biofilm Int. J. Food Microbiol. 2010, 140 (2-3) 109-116 10.1016/j.ijfoodmicro.2010.04.012
    • (2010) Int. J. Food Microbiol. , vol.140 , Issue.2-3 , pp. 109-116
    • Vikram, A.1    Jesudhasan, P.R.2    Jayaprakasha, G.K.3    Pillai, B.S.4    Patil, B.S.5
  • 249
    • 22144434455 scopus 로고    scopus 로고
    • Differential gene expression for investigation of Escherichia coli biofilm inhibition by plant extract Ursolic Acid
    • Ren, D.; Zuo, R.; González Barrios, A. F.; Bedzyk, L. A.; Eldridge, G. R.; Pasmore, M. E.; Wood, T. K. Differential gene expression for investigation of Escherichia coli biofilm inhibition by plant extract Ursolic Acid Appl. Environ. Microbiol. 2005, 71 (7) 4022-4034 10.1128/AEM.71.7.4022-4034.2005
    • (2005) Appl. Environ. Microbiol. , vol.71 , Issue.7 , pp. 4022-4034
    • Ren, D.1    Zuo, R.2    González Barrios, A.F.3    Bedzyk, L.A.4    Eldridge, G.R.5    Pasmore, M.E.6    Wood, T.K.7
  • 250
    • 84901340705 scopus 로고    scopus 로고
    • The role of the bacterial flagellum in adhesion and virulence
    • Haiko, J.; Westerlund-Wikström, B. The role of the bacterial flagellum in adhesion and virulence Biology 2013, 2 (4) 1242-1267 10.3390/biology2041242
    • (2013) Biology , vol.2 , Issue.4 , pp. 1242-1267
    • Haiko, J.1    Westerlund-Wikström, B.2
  • 251
    • 0242609023 scopus 로고    scopus 로고
    • Bacterial motility on a surface: Many ways to a common goal
    • Harshey, R. M. Bacterial motility on a surface: many ways to a common goal Annu. Rev. Microbiol. 2003, 57, 249-273 10.1146/annurev.micro.57.030502.091014
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 249-273
    • Harshey, R.M.1
  • 252
    • 77955652704 scopus 로고    scopus 로고
    • A field guide to bacterial swarming motility
    • Kearns, D. B. A field guide to bacterial swarming motility Nat. Rev. Microbiol. 2010, 8 (9) 634-644 10.1038/nrmicro2405
    • (2010) Nat. Rev. Microbiol. , vol.8 , Issue.9 , pp. 634-644
    • Kearns, D.B.1
  • 253
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick, J. S. Type IV pili and twitching motility Annu. Rev. Microbiol. 2002, 56, 289-314 10.1146/annurev.micro.56.012302.160938
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 254
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel, M. E.; Klena, J. D.; Rivera-Amill, V.; Monteville, M. R.; Biswas, D.; Raphael, B.; Mickelson, J. Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus J. Bacteriol. 2004, 186 (11) 3296-3303 10.1128/JB.186.11.3296-3303.2004
    • (2004) J. Bacteriol. , vol.186 , Issue.11 , pp. 3296-3303
    • Konkel, M.E.1    Klena, J.D.2    Rivera-Amill, V.3    Monteville, M.R.4    Biswas, D.5    Raphael, B.6    Mickelson, J.7
  • 256
    • 84911963600 scopus 로고    scopus 로고
    • The complex interplay among bacterial motility and virulence factors in different Escherichia coli infections
    • Kao, C. Y.; Lin, W. H.; Tseng, C. C.; Wu, A. B.; Wang, M. C.; Wu, J. J. The complex interplay among bacterial motility and virulence factors in different Escherichia coli infections Eur. J. Clin. Microbiol. Infect. Dis. 2014, 33 (12) 2157-2162 10.1007/s10096-014-2171-2
    • (2014) Eur. J. Clin. Microbiol. Infect. Dis. , vol.33 , Issue.12 , pp. 2157-2162
    • Kao, C.Y.1    Lin, W.H.2    Tseng, C.C.3    Wu, A.B.4    Wang, M.C.5    Wu, J.J.6
  • 257
    • 0038013943 scopus 로고    scopus 로고
    • From motility to virulence: Sensing and responding to environmental signals in Vibrio cholerae
    • Krukonis, E. S.; DiRita, V. J. From motility to virulence: sensing and responding to environmental signals in Vibrio cholerae Curr. Opin. Microbiol. 2003, 6 (2) 186-190 10.1016/S1369-5274(03)00032-8
    • (2003) Curr. Opin. Microbiol. , vol.6 , Issue.2 , pp. 186-190
    • Krukonis, E.S.1    DiRita, V.J.2
  • 258
    • 0036128606 scopus 로고    scopus 로고
    • Helicobacter pylori uses motility for initial colonization and to attain robust infection
    • Ottemann, K. M.; Lowenthal, A. C. Helicobacter pylori uses motility for initial colonization and to attain robust infection Infect. Immun. 2002, 70 (4) 1984-1990 10.1128/IAI.70.4.1984-1990.2002
    • (2002) Infect. Immun. , vol.70 , Issue.4 , pp. 1984-1990
    • Ottemann, K.M.1    Lowenthal, A.C.2
  • 259
    • 84911448684 scopus 로고    scopus 로고
    • Alkaloids modulate motility, biofilm formation and antibiotic susceptibility of uropathogenic Escherichia coli
    • Dusane, D. H.; Hosseinidoust, Z.; Asadishad, B.; Tufenkji, N. Alkaloids modulate motility, biofilm formation and antibiotic susceptibility of uropathogenic Escherichia coli PLoS One 2014, 9 (11) e112093 10.1371/journal.pone.0112093
    • (2014) PLoS One , vol.9 , Issue.11 , pp. e112093
    • Dusane, D.H.1    Hosseinidoust, Z.2    Asadishad, B.3    Tufenkji, N.4
  • 260
    • 84946576631 scopus 로고    scopus 로고
    • Inhibitory effect of piperine on Helicobacter pylori growth and adhesion to gastric adenocarcinoma cells
    • Tharmalingam, N.; Kim, S.-H.; Park, M.; Woo, H.; Kim, H.; Yang, J.; Rhee, K.-J.; Kim, J. Inhibitory effect of piperine on Helicobacter pylori growth and adhesion to gastric adenocarcinoma cells Infect. Agents Cancer 2014, 9 (1) 43 10.1186/1750-9378-9-43
    • (2014) Infect. Agents Cancer , vol.9 , Issue.1 , pp. 43
    • Tharmalingam, N.1    Kim, S.-H.2    Park, M.3    Woo, H.4    Kim, H.5    Yang, J.6    Rhee, K.-J.7    Kim, J.8
  • 261
    • 40349100697 scopus 로고    scopus 로고
    • Inhibition of swarming motility of Pseudomonas aeruginosa by branched-chain fatty acids
    • Inoue, T.; Shingaki, R.; Fukui, K. Inhibition of swarming motility of Pseudomonas aeruginosa by branched-chain fatty acids FEMS Microbiol. Lett. 2008, 281 (1) 81-86 10.1111/j.1574-6968.2008.01089.x
    • (2008) FEMS Microbiol. Lett. , vol.281 , Issue.1 , pp. 81-86
    • Inoue, T.1    Shingaki, R.2    Fukui, K.3
  • 262
    • 9244261620 scopus 로고    scopus 로고
    • Modulation of swarming and virulence by fatty acids through the RsbA protein in Proteus mirabilis
    • Liaw, S.-J.; Lai, H.-C.; Wang, W.-B. Modulation of swarming and virulence by fatty acids through the RsbA protein in Proteus mirabilis Infect. Immun. 2004, 72 (12) 6836-6845 10.1128/IAI.72.12.6836-6845.2004
    • (2004) Infect. Immun. , vol.72 , Issue.12 , pp. 6836-6845
    • Liaw, S.-J.1    Lai, H.-C.2    Wang, W.-B.3
  • 263
    • 84868552670 scopus 로고    scopus 로고
    • Tannin derived materials can block swarming motility and enhance biofilm formation in Pseudomonas aeruginosa
    • O'May, C.; Ciobanu, A.; Lam, H.; Tufenkji, N. Tannin derived materials can block swarming motility and enhance biofilm formation in Pseudomonas aeruginosa Biofouling 2012, 28 (10) 1063-1076 10.1080/08927014.2012.725130
    • (2012) Biofouling , vol.28 , Issue.10 , pp. 1063-1076
    • O'May, C.1    Ciobanu, A.2    Lam, H.3    Tufenkji, N.4
  • 264
    • 79951557425 scopus 로고    scopus 로고
    • Citrus flavonoid represses salmonella pathogenicity island 1 and motility in S. Typhimurium LT2
    • Vikram, A.; Jesudhasan, P. R.; Jayaprakasha, G. K.; Pillai, S. D.; Jayaraman, A.; Patil, B. S. Citrus flavonoid represses salmonella pathogenicity island 1 and motility in S. typhimurium LT2 Int. J. Food Microbiol. 2011, 145 (1) 28-36 10.1016/j.ijfoodmicro.2010.11.013
    • (2011) Int. J. Food Microbiol. , vol.145 , Issue.1 , pp. 28-36
    • Vikram, A.1    Jesudhasan, P.R.2    Jayaprakasha, G.K.3    Pillai, S.D.4    Jayaraman, A.5    Patil, B.S.6
  • 265
    • 79955637388 scopus 로고    scopus 로고
    • The swarming motility of Pseudomonas aeruginosa is blocked by cranberry proanthocyanidins and other tannin-containing materials
    • O'May, C.; Tufenkji, N. The swarming motility of Pseudomonas aeruginosa is blocked by cranberry proanthocyanidins and other tannin-containing materials Appl. Environ. Microbiol. 2011, 77 (9) 3061-3067 10.1128/AEM.02677-10
    • (2011) Appl. Environ. Microbiol. , vol.77 , Issue.9 , pp. 3061-3067
    • O'May, C.1    Tufenkji, N.2
  • 266
    • 84861760525 scopus 로고    scopus 로고
    • Plant-derived antimicrobials reduce Listeria monocytogenes virulence factors in vitro, and down-regulate expression of virulence genes
    • Upadhyay, A.; Johny, A. K.; Amalaradjou, M. A. R.; Ananda Baskaran, S.; Kim, K. S.; Venkitanarayanan, K. Plant-derived antimicrobials reduce Listeria monocytogenes virulence factors in vitro, and down-regulate expression of virulence genes Int. J. Food Microbiol. 2012, 157 (1) 88-94 10.1016/j.ijfoodmicro.2012.04.018
    • (2012) Int. J. Food Microbiol. , vol.157 , Issue.1 , pp. 88-94
    • Upadhyay, A.1    Johny, A.K.2    Amalaradjou, M.A.R.3    Ananda Baskaran, S.4    Kim, K.S.5    Venkitanarayanan, K.6
  • 268
    • 84866726938 scopus 로고    scopus 로고
    • The natural antimicrobial carvacrol inhibits Campylobacter jejuni motility and infection of epithelial cells
    • van Alphen, L. B.; Burt, S. A.; Veenendaal, A. K. J.; Bleumink-Pluym, N. M. C.; van Putten, J. P. M. The natural antimicrobial carvacrol inhibits Campylobacter jejuni motility and infection of epithelial cells PLoS One 2012, 7 (9) e45343 10.1371/journal.pone.0045343
    • (2012) PLoS One , vol.7 , Issue.9 , pp. e45343
    • Van Alphen, L.B.1    Burt, S.A.2    Veenendaal, A.K.J.3    Bleumink-Pluym, N.M.C.4    Van Putten, J.P.M.5
  • 269
    • 58149267863 scopus 로고    scopus 로고
    • The effect of monoterpenes on swarming differentiation and haemolysin activity in Proteus mirabilis
    • Echeverrigaray, S.; Michelim, L.; Longaray Delamare, A.; Andrade, C.; Pinto da Costa, S.; Zacaria, J. The effect of monoterpenes on swarming differentiation and haemolysin activity in Proteus mirabilis Molecules 2008, 13 (12) 3107-3116 10.3390/molecules13123107
    • (2008) Molecules , vol.13 , Issue.12 , pp. 3107-3116
    • Echeverrigaray, S.1    Michelim, L.2    Longaray Delamare, A.3    Andrade, C.4    Pinto Da Costa, S.5    Zacaria, J.6
  • 270
    • 84891372554 scopus 로고    scopus 로고
    • Cell targeting by the Staphylococcus aureus pore-forming toxins: It's not just about lipids
    • DuMont, A. L.; Torres, V. J. Cell targeting by the Staphylococcus aureus pore-forming toxins: it's not just about lipids Trends Microbiol. 2014, 22 (1) 21-27 10.1016/j.tim.2013.10.004
    • (2014) Trends Microbiol. , vol.22 , Issue.1 , pp. 21-27
    • DuMont, A.L.1    Torres, V.J.2
  • 271
    • 84890105937 scopus 로고    scopus 로고
    • Staphylococcus aureus toxins
    • Otto, M. Staphylococcus aureus toxins Curr. Opin. Microbiol. 2014, 17, 32-37 10.1016/j.mib.2013.11.004
    • (2014) Curr. Opin. Microbiol. , vol.17 , pp. 32-37
    • Otto, M.1
  • 272
    • 84879131303 scopus 로고    scopus 로고
    • Staphylococcus aureus α-toxin: Nearly a century of intrigue
    • Berube, B.; Wardenburg, J. Staphylococcus aureus α-toxin: nearly a century of intrigue Toxins 2013, 5 (6) 1140-1166 10.3390/toxins5061140
    • (2013) Toxins , vol.5 , Issue.6 , pp. 1140-1166
    • Berube, B.1    Wardenburg, J.2
  • 273
    • 84893728733 scopus 로고    scopus 로고
    • Staphylococcus aureus toxins - Their functions and genetics
    • Grumann, D.; Nubel, U.; Broker, B. M. Staphylococcus aureus toxins-their functions and genetics Infect., Genet. Evol. 2014, 21, 583-592 10.1016/j.meegid.2013.03.013
    • (2014) Infect., Genet. Evol. , vol.21 , pp. 583-592
    • Grumann, D.1    Nubel, U.2    Broker, B.M.3
  • 274
    • 84877757139 scopus 로고    scopus 로고
    • Staphylococcus aureus hemolysins, bi-component leukocidins, and cytolytic peptides: A redundant arsenal of membrane-damaging virulence factors?
    • Vandenesch, F.; Lina, G.; Henry, T. Staphylococcus aureus hemolysins, bi-component leukocidins, and cytolytic peptides: a redundant arsenal of membrane-damaging virulence factors? Front. Cell. Infect. Microbiol. 2012, 10.3389/fcimb.2012.00012
    • (2012) Front. Cell. Infect. Microbiol.
    • Vandenesch, F.1    Lina, G.2    Henry, T.3
  • 276
    • 84906313204 scopus 로고    scopus 로고
    • The biology of pneumolysin
    • Mitchell, T. J.; Dalziel, C. E. The biology of pneumolysin Subcell. Biochem. 2014, 80, 145-160 10.1007/978-94-017-8881-6-8
    • (2014) Subcell. Biochem. , vol.80 , pp. 145-160
    • Mitchell, T.J.1    Dalziel, C.E.2
  • 277
    • 0033763785 scopus 로고    scopus 로고
    • Pathogenesis of Proteus mirabilis urinary tract infection
    • Coker, C.; Poore, C. A.; Li, X.; Mobley, H. L. Pathogenesis of Proteus mirabilis urinary tract infection Microbes Infect. 2000, 2 (12) 1497-1505 10.1016/S1286-4579(00)01304-6
    • (2000) Microbes Infect. , vol.2 , Issue.12 , pp. 1497-1505
    • Coker, C.1    Poore, C.A.2    Li, X.3    Mobley, H.L.4
  • 279
    • 84884279163 scopus 로고    scopus 로고
    • Phenol-soluble modulins and staphylococcal infection
    • Peschel, A.; Otto, M. Phenol-soluble modulins and staphylococcal infection Nat. Rev. Microbiol. 2013, 11 (10) 667-673 10.1038/nrmicro3110
    • (2013) Nat. Rev. Microbiol. , vol.11 , Issue.10 , pp. 667-673
    • Peschel, A.1    Otto, M.2
  • 280
    • 0342751302 scopus 로고    scopus 로고
    • Superantigens - Powerful modifiers of the immune system
    • Fraser, J.; Arcus, V.; Kong, P.; Baker, E.; Proft, T. Superantigens-powerful modifiers of the immune system Mol. Med. Today 2000, 6 (3) 125-132 10.1016/S1357-4310(99)01657-3
    • (2000) Mol. Med. Today , vol.6 , Issue.3 , pp. 125-132
    • Fraser, J.1    Arcus, V.2    Kong, P.3    Baker, E.4    Proft, T.5
  • 281
    • 0035290122 scopus 로고    scopus 로고
    • Toxic shock syndrome: Broadening the differential diagnosis
    • Herzer, C. M. Toxic shock syndrome: Broadening the differential diagnosis J. Am. Board Fam. Pract. 2001, 14 (2) 131-136
    • (2001) J. Am. Board Fam. Pract. , vol.14 , Issue.2 , pp. 131-136
    • Herzer, C.M.1
  • 282
    • 84888344291 scopus 로고    scopus 로고
    • The staphylococcal enterotoxin (SE) family: SEB and siblings
    • Krakauer, T.; Stiles, B. G. The staphylococcal enterotoxin (SE) family: SEB and siblings Virulence 2013, 4 (8) 759-773 10.4161/viru.23905
    • (2013) Virulence , vol.4 , Issue.8 , pp. 759-773
    • Krakauer, T.1    Stiles, B.G.2
  • 283
    • 84877802168 scopus 로고    scopus 로고
    • Bacterial toxin inhibitors based on multivalent scaffolds
    • Branson, T. R.; Turnbull, W. B. Bacterial toxin inhibitors based on multivalent scaffolds Chem. Soc. Rev. 2013, 42 (11) 4613-4622 10.1039/C2CS35430F
    • (2013) Chem. Soc. Rev. , vol.42 , Issue.11 , pp. 4613-4622
    • Branson, T.R.1    Turnbull, W.B.2
  • 284
    • 84877583385 scopus 로고    scopus 로고
    • A biomimetic nanosponge that absorbs pore-forming toxins
    • Hu, C.-M. J.; Fang, R. H.; Copp, J.; Luk, B. T.; Zhang, L. A biomimetic nanosponge that absorbs pore-forming toxins Nat. Nanotechnol. 2013, 8 (5) 336-340 10.1038/nnano.2013.54
    • (2013) Nat. Nanotechnol. , vol.8 , Issue.5 , pp. 336-340
    • Hu, C.-M.J.1    Fang, R.H.2    Copp, J.3    Luk, B.T.4    Zhang, L.5
  • 285
    • 84870946824 scopus 로고    scopus 로고
    • Obstructing toxin pathways by targeted pore blockage
    • Nestorovich, E. M.; Bezrukov, S. M. Obstructing toxin pathways by targeted pore blockage Chem. Rev. 2012, 112 (12) 6388-6430 10.1021/cr300141q
    • (2012) Chem. Rev. , vol.112 , Issue.12 , pp. 6388-6430
    • Nestorovich, E.M.1    Bezrukov, S.M.2
  • 288
    • 84878457598 scopus 로고    scopus 로고
    • Programmed cell death in bacteria and implications for antibiotic therapy
    • Tanouchi, Y.; Lee, A. J.; Meredith, H.; You, L. Programmed cell death in bacteria and implications for antibiotic therapy Trends Microbiol. 2013, 21 (6) 265-270 10.1016/j.tim.2013.04.001
    • (2013) Trends Microbiol. , vol.21 , Issue.6 , pp. 265-270
    • Tanouchi, Y.1    Lee, A.J.2    Meredith, H.3    You, L.4
  • 289
    • 84876393994 scopus 로고    scopus 로고
    • Disease-enhancing antibodies improve the efficacy of bacterial toxin-neutralizing antibodies
    • Chow, S. K.; Smith, C.; MacCarthy, T.; Pohl, M. A.; Bergman, A.; Casadevall, A. Disease-enhancing antibodies improve the efficacy of bacterial toxin-neutralizing antibodies Cell Host Microbe 2013, 13 (4) 417-428 10.1016/j.chom.2013.03.001
    • (2013) Cell Host Microbe , vol.13 , Issue.4 , pp. 417-428
    • Chow, S.K.1    Smith, C.2    MacCarthy, T.3    Pohl, M.A.4    Bergman, A.5    Casadevall, A.6
  • 290
    • 77953633873 scopus 로고    scopus 로고
    • Paradigm shift in discovering next-generation anti-infective agents: Targeting quorum sensing, c-di-GMP signaling and biofilm formation in bacteria with small molecules
    • Sintim, H. O.; Smith, J. A.; Wang, J.; Nakayama, S.; Yan, L. Paradigm shift in discovering next-generation anti-infective agents: targeting quorum sensing, c-di-GMP signaling and biofilm formation in bacteria with small molecules Future Med. Chem. 2010, 2 (6) 1005-1035 10.4155/fmc.10.185
    • (2010) Future Med. Chem. , vol.2 , Issue.6 , pp. 1005-1035
    • Sintim, H.O.1    Smith, J.A.2    Wang, J.3    Nakayama, S.4    Yan, L.5
  • 291
    • 84940007260 scopus 로고    scopus 로고
    • One cannot rule them all: Are bacterial toxins-antitoxins druggable?
    • Chan, W. T.; Balsa, D.; Espinosa, M. One cannot rule them all: Are bacterial toxins-antitoxins druggable? FEMS Microbiol Rev. 2015, 39 (4) 522-540 10.1093/femsre/fuv002
    • (2015) FEMS Microbiol Rev. , vol.39 , Issue.4 , pp. 522-540
    • Chan, W.T.1    Balsa, D.2    Espinosa, M.3
  • 292
    • 84862783125 scopus 로고    scopus 로고
    • Artificial activation of toxin-antitoxin systems as an antibacterial strategy
    • Williams, J. J.; Hergenrother, P. J. Artificial activation of toxin-antitoxin systems as an antibacterial strategy Trends Microbiol. 2012, 20 (6) 291-298 10.1016/j.tim.2012.02.005
    • (2012) Trends Microbiol. , vol.20 , Issue.6 , pp. 291-298
    • Williams, J.J.1    Hergenrother, P.J.2
  • 293
    • 23844527805 scopus 로고    scopus 로고
    • Specific inhibitory action of anisodamine against a staphylococcal superantigenic toxin, toxic shock syndrome toxin 1 (TSST-1), leading to down-regulation of cytokine production and blocking of TSST-1 toxicity in mice
    • Nakagawa, S.; Kushiya, K.; Taneike, I.; Imanishi, K. i.; Uchiyama, T.; Yamamoto, T. Specific inhibitory action of anisodamine against a staphylococcal superantigenic toxin, toxic shock syndrome toxin 1 (TSST-1), leading to down-regulation of cytokine production and blocking of TSST-1 toxicity in mice Clin. Diagn. Lab. Immunol. 2005, 12 (3) 399-408 10.1128/CDLI.12.3.399-408.2005
    • (2005) Clin. Diagn. Lab. Immunol. , vol.12 , Issue.3 , pp. 399-408
    • Nakagawa, S.1    Kushiya, K.2    Taneike, I.3    Imanishi, K.I.4    Uchiyama, T.5    Yamamoto, T.6
  • 294
    • 79952362439 scopus 로고    scopus 로고
    • Allicin from garlic neutralizes the hemolytic activity of intra- and extra-cellular pneumolysin O in vitro
    • Arzanlou, M.; Bohlooli, S.; Jannati, E.; Mirzanejad-Asl, H. Allicin from garlic neutralizes the hemolytic activity of intra- and extra-cellular pneumolysin O in vitro Toxicon 2011, 57 (4) 540-545 10.1016/j.toxicon.2010.12.009
    • (2011) Toxicon , vol.57 , Issue.4 , pp. 540-545
    • Arzanlou, M.1    Bohlooli, S.2    Jannati, E.3    Mirzanejad-Asl, H.4
  • 295
    • 66149140548 scopus 로고    scopus 로고
    • Surfactants, aromatic and isoprenoid compounds, and fatty acid biosynthesis inhibitors suppress Staphylococcus aureus production of toxic shock syndrome toxin 1
    • McNamara, P. J.; Syverson, R. E.; Milligan-Myhre, K.; Frolova, O.; Schroeder, S.; Kidder, J.; Hoang, T.; Proctor, R. A. Surfactants, aromatic and isoprenoid compounds, and fatty acid biosynthesis inhibitors suppress Staphylococcus aureus production of toxic shock syndrome toxin 1 Antimicrob. Agents Chemother. 2009, 53 (5) 1898-1906 10.1128/AAC.01293-08
    • (2009) Antimicrob. Agents Chemother. , vol.53 , Issue.5 , pp. 1898-1906
    • McNamara, P.J.1    Syverson, R.E.2    Milligan-Myhre, K.3    Frolova, O.4    Schroeder, S.5    Kidder, J.6    Hoang, T.7    Proctor, R.A.8
  • 296
    • 77952609952 scopus 로고    scopus 로고
    • Influence of subinhibitory concentrations of licochalcone A on the secretion of enterotoxins A and B by Staphylococcus aureus
    • Qiu, J.; Feng, H.; Xiang, H.; Wang, D.; Xia, L.; Jiang, Y.; Song, K.; Lu, J.; Yu, L.; Deng, X. Influence of subinhibitory concentrations of licochalcone A on the secretion of enterotoxins A and B by Staphylococcus aureus FEMS Microbiol. Lett. 2010, 307 (2) 135-141 10.1111/j.1574-6968.2010.01973.x
    • (2010) FEMS Microbiol. Lett. , vol.307 , Issue.2 , pp. 135-141
    • Qiu, J.1    Feng, H.2    Xiang, H.3    Wang, D.4    Xia, L.5    Jiang, Y.6    Song, K.7    Lu, J.8    Yu, L.9    Deng, X.10
  • 297
    • 38349113481 scopus 로고    scopus 로고
    • The polyphenol (-)-epicatechin gallate disrupts the secretion of virulence-related proteins by Staphylococcus aureus
    • Shah, S.; Stapleton, P. D.; Taylor, P. W. The polyphenol (-)-epicatechin gallate disrupts the secretion of virulence-related proteins by Staphylococcus aureus Lett. Appl. Microbiol. 2008, 46 (2) 181-185 10.1111/j.1472-765X.2007.02296.x
    • (2008) Lett. Appl. Microbiol. , vol.46 , Issue.2 , pp. 181-185
    • Shah, S.1    Stapleton, P.D.2    Taylor, P.W.3
  • 298
    • 84873047989 scopus 로고    scopus 로고
    • Molecular insight into the inhibition mechanism of cyrtominetin to α-hemolysin by molecular dynamics simulation
    • Niu, X.; Qiu, J.; Wang, X.; Gao, X.; Dong, J.; Wang, J.; Li, H.; Zhang, Y.; Dai, X.; Lu, C. et al. Molecular insight into the inhibition mechanism of cyrtominetin to α-hemolysin by molecular dynamics simulation Eur. J. Med. Chem. 2013, 62 (0) 320-328 10.1016/j.ejmech.2013.01.008
    • (2013) Eur. J. Med. Chem. , vol.62 , pp. 320-328
    • Niu, X.1    Qiu, J.2    Wang, X.3    Gao, X.4    Dong, J.5    Wang, J.6    Li, H.7    Zhang, Y.8    Dai, X.9    Lu, C.10
  • 299
    • 84873509636 scopus 로고    scopus 로고
    • Oroxylin A inhibits hemolysis via hindering the self-assembly of alpha-hemolysin heptameric transmembrane pore
    • Dong, J.; Qiu, J.; Zhang, Y.; Lu, C.; Dai, X.; Wang, J.; Li, H.; Wang, X.; Tan, W.; Luo, M. et al. Oroxylin A inhibits hemolysis via hindering the self-assembly of alpha-hemolysin heptameric transmembrane pore PLoS Comput. Biol. 2013, 9 (1) e1002869 10.1371/journal.pcbi.1002869
    • (2013) PLoS Comput. Biol. , vol.9 , Issue.1 , pp. e1002869
    • Dong, J.1    Qiu, J.2    Zhang, Y.3    Lu, C.4    Dai, X.5    Wang, J.6    Li, H.7    Wang, X.8    Tan, W.9    Luo, M.10
  • 300
    • 84862884568 scopus 로고    scopus 로고
    • Baicalin protects mice from Staphylococcus aureus pneumonia via inhibition of the cytolytic activity of alpha-hemolysin
    • Qiu, J.; Niu, X.; Dong, J.; Wang, D.; Wang, J.; Li, H.; Luo, M.; Li, S.; Feng, H.; Deng, X. Baicalin protects mice from Staphylococcus aureus pneumonia via inhibition of the cytolytic activity of alpha-hemolysin J. Infect. Dis. 2012, 206 (2) 292-301 10.1093/infdis/jis336
    • (2012) J. Infect. Dis. , vol.206 , Issue.2 , pp. 292-301
    • Qiu, J.1    Niu, X.2    Dong, J.3    Wang, D.4    Wang, J.5    Li, H.6    Luo, M.7    Li, S.8    Feng, H.9    Deng, X.10
  • 301
    • 84926180820 scopus 로고    scopus 로고
    • Morin hydrate attenuates Staphylococcus aureus virulence by inhibiting the self-assembly of alpha-hemolysin
    • Wang, J.; Zhou, X.; Liu, S.; Li, G.; Shi, L.; Dong, J.; Li, W.; Deng, X.; Niu, X. Morin hydrate attenuates Staphylococcus aureus virulence by inhibiting the self-assembly of alpha-hemolysin J. Appl. Microbiol. 2015, 118 (3) 753-763 10.1111/jam.12743
    • (2015) J. Appl. Microbiol. , vol.118 , Issue.3 , pp. 753-763
    • Wang, J.1    Zhou, X.2    Liu, S.3    Li, G.4    Shi, L.5    Dong, J.6    Li, W.7    Deng, X.8    Niu, X.9
  • 302
    • 84894232590 scopus 로고    scopus 로고
    • Molecular modeling reveals the novel inhibition mechanism and binding mode of three natural compounds to staphylococcal alpha-hemolysin
    • Qiu, J.; Wang, D.; Zhang, Y.; Dong, J.; Wang, J.; Niu, X. Molecular modeling reveals the novel inhibition mechanism and binding mode of three natural compounds to staphylococcal alpha-hemolysin PLoS One 2013, 8 (11) e80197 10.1371/journal.pone.0080197
    • (2013) PLoS One , vol.8 , Issue.11 , pp. e80197
    • Qiu, J.1    Wang, D.2    Zhang, Y.3    Dong, J.4    Wang, J.5    Niu, X.6
  • 303
    • 84928881614 scopus 로고    scopus 로고
    • Fisetin inhibits Listeria monocytogenes virulence by interfering with the oligomerization of listeriolysin O
    • Wang, J.; Qiu, J.; Tan, W.; Zhang, Y.; Wang, H.; Zhou, X.; Liu, S.; Feng, H.; Li, W.; Niu, X. et al. Fisetin inhibits Listeria monocytogenes virulence by interfering with the oligomerization of listeriolysin O J. Infect. Dis. 2015, 211 (9) 1376-1387 10.1093/infdis/jiu520
    • (2015) J. Infect. Dis. , vol.211 , Issue.9 , pp. 1376-1387
    • Wang, J.1    Qiu, J.2    Tan, W.3    Zhang, Y.4    Wang, H.5    Zhou, X.6    Liu, S.7    Feng, H.8    Li, W.9    Niu, X.10
  • 304
    • 84924371141 scopus 로고    scopus 로고
    • Novel inhibitor discovery and the conformational analysis of inhibitors of listeriolysin O via protein-ligand modeling
    • Wang, J.; Zhou, X.; Liu, S.; Li, G.; Zhang, B.; Deng, X.; Niu, X. Novel inhibitor discovery and the conformational analysis of inhibitors of listeriolysin O via protein-ligand modeling Sci. Rep. 2015, 5, 8864-7 10.1038/srep08864
    • (2015) Sci. Rep. , vol.5 , pp. 8864-8867
    • Wang, J.1    Zhou, X.2    Liu, S.3    Li, G.4    Zhang, B.5    Deng, X.6    Niu, X.7
  • 305
    • 77950366427 scopus 로고    scopus 로고
    • Influence of magnolol on the secretion of alpha-toxin by Staphylococcus aureus
    • Xiang, H.; Qiu, J. Z.; Wang, D. C.; Jiang, Y. S.; Xia, L. J.; Deng, X. M. Influence of magnolol on the secretion of alpha-toxin by Staphylococcus aureus Molecules 2010, 15 (3) 1679-1689 10.3390/molecules15031679
    • (2010) Molecules , vol.15 , Issue.3 , pp. 1679-1689
    • Xiang, H.1    Qiu, J.Z.2    Wang, D.C.3    Jiang, Y.S.4    Xia, L.J.5    Deng, X.M.6
  • 306
    • 80054720873 scopus 로고    scopus 로고
    • The olive compound 4-hydroxytyrosol inactivates Staphylococcus aureus bacteria and staphylococcal enterotoxin A (SEA)
    • Friedman, M.; Rasooly, R.; Do, P. M.; Henika, P. R. The olive compound 4-hydroxytyrosol inactivates Staphylococcus aureus bacteria and staphylococcal enterotoxin A (SEA) J. Food Sci. 2011, 76, M558-M563 10.1111/j.1750-3841.2011.02365.x
    • (2011) J. Food Sci. , vol.76 , pp. M558-M563
    • Friedman, M.1    Rasooly, R.2    Do, P.M.3    Henika, P.R.4
  • 307
    • 84906978886 scopus 로고    scopus 로고
    • Effect of subinhibitory concentrations of chlorogenic acid on reducing the virulence factor production by Staphylococcus aureus
    • Li, G.; Qiao, M.; Guo, Y.; Wang, X.; Xu, Y.; Xia, X. Effect of subinhibitory concentrations of chlorogenic acid on reducing the virulence factor production by Staphylococcus aureus Foodborne Pathog. Dis. 2014, 11 (9) 677-683 10.1089/fpd.2013.1731
    • (2014) Foodborne Pathog. Dis. , vol.11 , Issue.9 , pp. 677-683
    • Li, G.1    Qiao, M.2    Guo, Y.3    Wang, X.4    Xu, Y.5    Xia, X.6
  • 308
    • 84879174099 scopus 로고    scopus 로고
    • Influence of carvacrol and thymol on the physiological attributes, enterotoxin production and surface characteristics of Staphylococcus aureus strains isolated from foods
    • Souza, E. L.; Oliveira, C. E. V.; Stamford, T. L. M.; Conceição, M. L.; Gomes Neto, N. J. Influence of carvacrol and thymol on the physiological attributes, enterotoxin production and surface characteristics of Staphylococcus aureus strains isolated from foods Braz. J. Microbiol. 2013, 44, 29-36 10.1590/S1517-83822013005000001
    • (2013) Braz. J. Microbiol. , vol.44 , pp. 29-36
    • Souza, E.L.1    Oliveira, C.E.V.2    Stamford, T.L.M.3    Conceição, M.L.4    Gomes Neto, N.J.5
  • 309
    • 69749095952 scopus 로고    scopus 로고
    • Color me bad: Microbial pigments as virulence factors
    • Liu, G. Y.; Nizet, V. Color me bad: microbial pigments as virulence factors Trends Microbiol. 2009, 17 (9) 406-413 10.1016/j.tim.2009.06.006
    • (2009) Trends Microbiol. , vol.17 , Issue.9 , pp. 406-413
    • Liu, G.Y.1    Nizet, V.2
  • 310
    • 25444443095 scopus 로고    scopus 로고
    • Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus
    • Pelz, A.; Wieland, K. P.; Putzbach, K.; Hentschel, P.; Albert, K.; Gotz, F. Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus J. Biol. Chem. 2005, 280 (37) 32493-32498 10.1074/jbc.M505070200
    • (2005) J. Biol. Chem. , vol.280 , Issue.37 , pp. 32493-32498
    • Pelz, A.1    Wieland, K.P.2    Putzbach, K.3    Hentschel, P.4    Albert, K.5    Gotz, F.6
  • 311
    • 40449088993 scopus 로고    scopus 로고
    • A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus virulence
    • Liu, C. I.; Liu, G. Y.; Song, Y.; Yin, F.; Hensler, M. E.; Jeng, W. Y.; Nizet, V.; Wang, A. H.; Oldfield, E. A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus virulence Science 2008, 319 (5868) 1391-1394 10.1126/science.1153018
    • (2008) Science , vol.319 , Issue.5868 , pp. 1391-1394
    • Liu, C.I.1    Liu, G.Y.2    Song, Y.3    Yin, F.4    Hensler, M.E.5    Jeng, W.Y.6    Nizet, V.7    Wang, A.H.8    Oldfield, E.9
  • 312
    • 22944462082 scopus 로고    scopus 로고
    • Staphylococcus aureus golden pigment impairs neutrophil killing and promotes virulence through its antioxidant activity
    • Liu, G. Y.; Essex, A.; Buchanan, J. T.; Datta, V.; Hoffman, H. M.; Bastian, J. F.; Fierer, J.; Nizet, V. Staphylococcus aureus golden pigment impairs neutrophil killing and promotes virulence through its antioxidant activity J. Exp. Med. 2005, 202 (2) 209-215 10.1084/jem.20050846
    • (2005) J. Exp. Med. , vol.202 , Issue.2 , pp. 209-215
    • Liu, G.Y.1    Essex, A.2    Buchanan, J.T.3    Datta, V.4    Hoffman, H.M.5    Bastian, J.F.6    Fierer, J.7    Nizet, V.8
  • 313
    • 33746601080 scopus 로고    scopus 로고
    • Staphyloxanthin plays a role in the fitness of Staphylococcus aureus and its ability to cope with oxidative stress
    • Clauditz, A.; Resch, A.; Wieland, K.-P.; Peschel, A.; Götz, F. Staphyloxanthin plays a role in the fitness of Staphylococcus aureus and its ability to cope with oxidative stress Infect. Immun. 2006, 74 (8) 4950-4953 10.1128/IAI.00204-06
    • (2006) Infect. Immun. , vol.74 , Issue.8 , pp. 4950-4953
    • Clauditz, A.1    Resch, A.2    Wieland, K.-P.3    Peschel, A.4    Götz, F.5
  • 314
    • 53549128065 scopus 로고    scopus 로고
    • Sterol Biosynthesis Inhibitors as Staphylococcus aureus Antibiotics: Following a Golden Compass?
    • Walsh, C. T.; Fischbach, M. A. Sterol Biosynthesis Inhibitors as Staphylococcus aureus Antibiotics: Following a Golden Compass? Angew. Chem., Int. Ed. 2008, 47 (31) 5700-5702 10.1002/anie.200801801
    • (2008) Angew. Chem., Int. Ed. , vol.47 , Issue.31 , pp. 5700-5702
    • Walsh, C.T.1    Fischbach, M.A.2
  • 315
    • 84893786916 scopus 로고    scopus 로고
    • Targeting virulence: Can we make evolution-proof drugs?
    • Allen, R. C.; Popat, R.; Diggle, S. P.; Brown, S. P. Targeting virulence: can we make evolution-proof drugs? Nat. Rev. Microbiol. 2014, 12 (4) 300-308 10.1038/nrmicro3232
    • (2014) Nat. Rev. Microbiol. , vol.12 , Issue.4 , pp. 300-308
    • Allen, R.C.1    Popat, R.2    Diggle, S.P.3    Brown, S.P.4
  • 316
    • 84925406070 scopus 로고    scopus 로고
    • Chemistry and biology of pyoverdines, Pseudomonas primary siderophores
    • Cezard, C.; Farvacques, N.; Sonnet, P. Chemistry and biology of pyoverdines, Pseudomonas primary siderophores Curr. Med. Chem. 2014, 22 (2) 165-186 10.2174/0929867321666141011194624
    • (2014) Curr. Med. Chem. , vol.22 , Issue.2 , pp. 165-186
    • Cezard, C.1    Farvacques, N.2    Sonnet, P.3
  • 317
    • 84900631791 scopus 로고    scopus 로고
    • Pyocyanin: Production, applications, challenges and new insights
    • Jayaseelan, S.; Ramaswamy, D.; Dharmaraj, S. Pyocyanin: production, applications, challenges and new insights World J. Microbiol. Biotechnol. 2014, 30 (4) 1159-1168 10.1007/s11274-013-1552-5
    • (2014) World J. Microbiol. Biotechnol. , vol.30 , Issue.4 , pp. 1159-1168
    • Jayaseelan, S.1    Ramaswamy, D.2    Dharmaraj, S.3
  • 318
    • 33747082622 scopus 로고    scopus 로고
    • The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa
    • Dietrich, L. E.; Price-Whelan, A.; Petersen, A.; Whiteley, M.; Newman, D. K. The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa Mol. Microbiol. 2006, 61 (5) 1308-1321 10.1111/j.1365-2958.2006.05306.x
    • (2006) Mol. Microbiol. , vol.61 , Issue.5 , pp. 1308-1321
    • Dietrich, L.E.1    Price-Whelan, A.2    Petersen, A.3    Whiteley, M.4    Newman, D.K.5
  • 319
    • 84859032202 scopus 로고    scopus 로고
    • The regulatory repertoire of Pseudomonas aeruginosa AmpC β-lactamase regulator AmpR includes virulence genes
    • Balasubramanian, D.; Schneper, L.; Merighi, M.; Smith, R.; Narasimhan, G.; Lory, S.; Mathee, K. The regulatory repertoire of Pseudomonas aeruginosa AmpC β-lactamase regulator AmpR includes virulence genes PLoS One 2012, 7 (3) e34067 10.1371/journal.pone.0034067
    • (2012) PLoS One , vol.7 , Issue.3 , pp. e34067
    • Balasubramanian, D.1    Schneper, L.2    Merighi, M.3    Smith, R.4    Narasimhan, G.5    Lory, S.6    Mathee, K.7
  • 320
    • 9644257146 scopus 로고    scopus 로고
    • The role of pyocyanin in Pseudomonas aeruginosa infection
    • Lau, G. W.; Hassett, D. J.; Ran, H.; Kong, F. The role of pyocyanin in Pseudomonas aeruginosa infection Trends Mol. Med. 2004, 10 (12) 599-606 10.1016/j.molmed.2004.10.002
    • (2004) Trends Mol. Med. , vol.10 , Issue.12 , pp. 599-606
    • Lau, G.W.1    Hassett, D.J.2    Ran, H.3    Kong, F.4
  • 322
    • 0036185786 scopus 로고    scopus 로고
    • VanT, a homologue of Vibrio harveyi LuxR, regulates serine, metalloprotease, pigment, and biofilm production in Vibrio anguillarum
    • Croxatto, A.; Chalker, V. J.; Lauritz, J.; Jass, J.; Hardman, A.; Williams, P.; Camara, M.; Milton, D. L. VanT, a homologue of Vibrio harveyi LuxR, regulates serine, metalloprotease, pigment, and biofilm production in Vibrio anguillarum J. Bacteriol. 2002, 184 (6) 1617-1629 10.1128/JB.184.6.1617-1629.2002
    • (2002) J. Bacteriol. , vol.184 , Issue.6 , pp. 1617-1629
    • Croxatto, A.1    Chalker, V.J.2    Lauritz, J.3    Jass, J.4    Hardman, A.5    Williams, P.6    Camara, M.7    Milton, D.L.8
  • 323
    • 0026671830 scopus 로고
    • Induction of melanin biosynthesis in Vibrio cholerae
    • Coyne, V. E.; al-Harthi, L. Induction of melanin biosynthesis in Vibrio cholerae Appl. Environ. Microbiol. 1992, 58 (9) 2861-2865
    • (1992) Appl. Environ. Microbiol. , vol.58 , Issue.9 , pp. 2861-2865
    • Coyne, V.E.1    Al-Harthi, L.2
  • 324
    • 84874209409 scopus 로고    scopus 로고
    • Inhibition of staphyloxanthin biosynthesis in Staphylococcus aureus by rhodomyrtone, a novel antibiotic candidate
    • Leejae, S.; Hasap, L.; Voravuthikunchai, S. P. Inhibition of staphyloxanthin biosynthesis in Staphylococcus aureus by rhodomyrtone, a novel antibiotic candidate J. Med. Microbiol. 2013, 62 (3) 421-428 10.1099/jmm.0.047316-0
    • (2013) J. Med. Microbiol. , vol.62 , Issue.3 , pp. 421-428
    • Leejae, S.1    Hasap, L.2    Voravuthikunchai, S.P.3
  • 325
    • 84910680420 scopus 로고    scopus 로고
    • An ideal target for anti-virulence drug development
    • Cascioferro, S.; Totsika, M.; Schillaci, D. An ideal target for anti-virulence drug development Microb. Pathog. 2014, 77, 105-112 10.1016/j.micpath.2014.10.007
    • (2014) Microb. Pathog. , vol.77 , pp. 105-112
    • Cascioferro, S.1    Totsika, M.2    Schillaci, D.3
  • 326
    • 41149117526 scopus 로고    scopus 로고
    • Sortase as a target of anti-infective therapy
    • Maresso, A. W.; Schneewind, O. Sortase as a target of anti-infective therapy Pharmacol Rev. 2008, 60 (1) 128-141 10.1124/pr.107.07110
    • (2008) Pharmacol Rev. , vol.60 , Issue.1 , pp. 128-141
    • Maresso, A.W.1    Schneewind, O.2
  • 328
    • 4644255644 scopus 로고    scopus 로고
    • Staphylococci in colonization and disease: Prospective targets for drugs and vaccines
    • Gotz, F. Staphylococci in colonization and disease: prospective targets for drugs and vaccines Curr. Opin. Microbiol. 2004, 7 (5) 477-487 10.1016/j.mib.2004.08.014
    • (2004) Curr. Opin. Microbiol. , vol.7 , Issue.5 , pp. 477-487
    • Gotz, F.1
  • 329
    • 80055076614 scopus 로고    scopus 로고
    • Preventing Staphylococcus aureus sepsis through the inhibition of Its agglutination in blood
    • McAdow, M.; Kim, H. K.; DeDent, A. C.; Hendrickx, A. P. A.; Schneewind, O.; Missiakas, D. M. Preventing Staphylococcus aureus sepsis through the inhibition of Its agglutination in blood PLoS Pathog. 2011, 7 (10) e1002307 10.1371/journal.ppat.1002307
    • (2011) PLoS Pathog. , vol.7 , Issue.10 , pp. e1002307
    • McAdow, M.1    Kim, H.K.2    DeDent, A.C.3    Hendrickx, A.P.A.4    Schneewind, O.5    Missiakas, D.M.6
  • 330
    • 77958121661 scopus 로고    scopus 로고
    • Contribution of coagulases towards Staphylococcus aureus disease and protective immunity
    • Cheng, A. G.; McAdow, M.; Kim, H. K.; Bae, T.; Missiakas, D. M.; Schneewind, O. Contribution of coagulases towards Staphylococcus aureus disease and protective immunity PLoS Pathog. 2010, 6 (8) e1001036 10.1371/journal.ppat.1001036
    • (2010) PLoS Pathog. , vol.6 , Issue.8 , pp. e1001036
    • Cheng, A.G.1    McAdow, M.2    Kim, H.K.3    Bae, T.4    Missiakas, D.M.5    Schneewind, O.6
  • 331
    • 0028834487 scopus 로고
    • Role of Staphylococcus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis
    • Moreillon, P.; Entenza, J. M.; Francioli, P.; McDevitt, D.; Foster, T. J.; Francois, P.; Vaudaux, P. Role of Staphylococcus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis Infect. Immun. 1995, 63 (12) 4738-4743
    • (1995) Infect. Immun. , vol.63 , Issue.12 , pp. 4738-4743
    • Moreillon, P.1    Entenza, J.M.2    Francioli, P.3    McDevitt, D.4    Foster, T.J.5    Francois, P.6    Vaudaux, P.7
  • 333
    • 84866952450 scopus 로고    scopus 로고
    • Bacterial proteolytic complexes as therapeutic targets
    • Raju, R. M.; Goldberg, A. L.; Rubin, E. J. Bacterial proteolytic complexes as therapeutic targets Nat. Rev. Drug Discovery 2012, 11 (10) 777-789 10.1038/nrd3846
    • (2012) Nat. Rev. Drug Discovery , vol.11 , Issue.10 , pp. 777-789
    • Raju, R.M.1    Goldberg, A.L.2    Rubin, E.J.3
  • 334
    • 0020857013 scopus 로고
    • Pseudomonas aeruginosa elastase and its role in pseudomonas infections
    • Wretlind, B.; Pavlovskis, O. R. Pseudomonas aeruginosa elastase and its role in pseudomonas infections Clin. Infect. Dis. 1983, 5, S998-S1004 10.1093/clinids/5.Supplement-5.S998
    • (1983) Clin. Infect. Dis. , vol.5 , pp. S998-S1004
    • Wretlind, B.1    Pavlovskis, O.R.2
  • 335
    • 0001663398 scopus 로고
    • Production of elastase and proteinase by Pseudomonas aeruginosa
    • Morihara, K. Production of elastase and proteinase by Pseudomonas aeruginosa J. Bacteriol. 1964, 88, 745-757
    • (1964) J. Bacteriol. , vol.88 , pp. 745-757
    • Morihara, K.1
  • 336
    • 0030188736 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa and epithelial permeability: Role of virulence factors elastase and exotoxin A
    • Azghani, A. O. Pseudomonas aeruginosa and epithelial permeability: role of virulence factors elastase and exotoxin A Am. J. Respir. Cell Mol. Biol. 1996, 15 (1) 132-140 10.1165/ajrcmb.15.1.8679217
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , Issue.1 , pp. 132-140
    • Azghani, A.O.1
  • 337
    • 0026009410 scopus 로고
    • Pseudomonas aeruginosa alkaline protease: Evidence for secretion genes and study of secretion mechanism
    • Guzzo, J.; Pages, J. M.; Duong, F.; Lazdunski, A.; Murgier, M. Pseudomonas aeruginosa alkaline protease: evidence for secretion genes and study of secretion mechanism J. Bacteriol. 1991, 173 (17) 5290-5297
    • (1991) J. Bacteriol. , vol.173 , Issue.17 , pp. 5290-5297
    • Guzzo, J.1    Pages, J.M.2    Duong, F.3    Lazdunski, A.4    Murgier, M.5
  • 338
    • 77951659581 scopus 로고    scopus 로고
    • Ureases as a target for the treatment of gastric and urinary infections
    • Follmer, C. Ureases as a target for the treatment of gastric and urinary infections J. Clin. Pathol. 2010, 63 (5) 424-430 10.1136/jcp.2009.072595
    • (2010) J. Clin. Pathol. , vol.63 , Issue.5 , pp. 424-430
    • Follmer, C.1
  • 339
    • 84901658815 scopus 로고    scopus 로고
    • The emerging role of urease as a general microbial virulence factor
    • Rutherford, J. C. The emerging role of urease as a general microbial virulence factor PLoS Pathog. 2014, 10 (5) e1004062 10.1371/journal.ppat.1004062
    • (2014) PLoS Pathog. , vol.10 , Issue.5 , pp. e1004062
    • Rutherford, J.C.1
  • 340
    • 84920091151 scopus 로고    scopus 로고
    • An overview on the potential of natural products as ureases inhibitors: A review
    • Modolo, L. V.; de Souza, A. X.; Horta, L. P.; Araujo, D. P.; de Fátima, Â. An overview on the potential of natural products as ureases inhibitors: a review IJAR 2015, 6 (1) 35-44 10.1016/j.jare.2014.09.001
    • (2015) IJAR , vol.6 , Issue.1 , pp. 35-44
    • Modolo, L.V.1    De Souza, A.X.2    Horta, L.P.3    Araujo, D.P.4    De Fátima, Â.5
  • 342
    • 69049109896 scopus 로고    scopus 로고
    • The NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation
    • Parker, D.; Soong, G.; Planet, P.; Brower, J.; Ratner, A. J.; Prince, A. The NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation Infect. Immun. 2009, 77 (9) 3722-3730 10.1128/IAI.00228-09
    • (2009) Infect. Immun. , vol.77 , Issue.9 , pp. 3722-3730
    • Parker, D.1    Soong, G.2    Planet, P.3    Brower, J.4    Ratner, A.J.5    Prince, A.6
  • 343
    • 84863564702 scopus 로고    scopus 로고
    • Pneumococcal neuraminidase A: An essential upper airway colonization factor for Streptococcus pneumoniae
    • Brittan, J. L.; Buckeridge, T. J.; Finn, A.; Kadioglu, A.; Jenkinson, H. F. Pneumococcal neuraminidase A: an essential upper airway colonization factor for Streptococcus pneumoniae Mol. Oral Microbiol. 2012, 27 (4) 270-283 10.1111/j.2041-1014.2012.00658.x
    • (2012) Mol. Oral Microbiol. , vol.27 , Issue.4 , pp. 270-283
    • Brittan, J.L.1    Buckeridge, T.J.2    Finn, A.3    Kadioglu, A.4    Jenkinson, H.F.5
  • 344
    • 0026619682 scopus 로고
    • Bacterial sialidases - Roles in pathogenicity and nutrition
    • Corfield, T. Bacterial sialidases-roles in pathogenicity and nutrition Glycobiology 1992, 2 (6) 509-521 10.1093/glycob/2.6.509
    • (1992) Glycobiology , vol.2 , Issue.6 , pp. 509-521
    • Corfield, T.1
  • 345
    • 84863951031 scopus 로고    scopus 로고
    • Synthesis of selective inhibitors against V. Cholerae sialidase and human cytosolic sialidase NEU2
    • Khedri, Z.; Li, Y.; Cao, H.; Qu, J.; Yu, H.; Muthana, M. M.; Chen, X. Synthesis of selective inhibitors against V. cholerae sialidase and human cytosolic sialidase NEU2 Org. Biomol. Chem. 2012, 10 (30) 6112-6120 10.1039/c2ob25335f
    • (2012) Org. Biomol. Chem. , vol.10 , Issue.30 , pp. 6112-6120
    • Khedri, Z.1    Li, Y.2    Cao, H.3    Qu, J.4    Yu, H.5    Muthana, M.M.6    Chen, X.7
  • 346
    • 77950832743 scopus 로고    scopus 로고
    • Advances in the structure-based design of the influenza A neuraminidase inhibitors
    • Mitrasinovic, P. M. Advances in the structure-based design of the influenza A neuraminidase inhibitors Curr. Drug Targets 2010, 11 (3) 315-326 10.2174/138945010790711932
    • (2010) Curr. Drug Targets , vol.11 , Issue.3 , pp. 315-326
    • Mitrasinovic, P.M.1
  • 347
    • 36749056771 scopus 로고    scopus 로고
    • The war against influenza: Discovery and development of sialidase inhibitors
    • von Itzstein, M. The war against influenza: discovery and development of sialidase inhibitors Nat. Rev. Drug Discovery 2007, 6 (12) 967-974 10.1038/nrd2400
    • (2007) Nat. Rev. Drug Discovery , vol.6 , Issue.12 , pp. 967-974
    • Von Itzstein, M.1
  • 348
    • 2942555515 scopus 로고    scopus 로고
    • Inhibition of the bacterial surface protein anchoring transpeptidase sortase by isoquinoline alkaloids
    • Kim, S. H.; Shin, D. S.; Oh, M. N.; Chung, S. C.; Lee, J. S.; Oh, K. B. Inhibition of the bacterial surface protein anchoring transpeptidase sortase by isoquinoline alkaloids Biosci., Biotechnol., Biochem. 2004, 68 (2) 421-424 10.1271/bbb.68.421
    • (2004) Biosci., Biotechnol., Biochem. , vol.68 , Issue.2 , pp. 421-424
    • Kim, S.H.1    Shin, D.S.2    Oh, M.N.3    Chung, S.C.4    Lee, J.S.5    Oh, K.B.6
  • 349
    • 38549146906 scopus 로고    scopus 로고
    • In vitro anti-Helicobacter pylori activity of diallyl sulphides and protocatechuic acid
    • Liu, W. H.; Hsu, C. C.; Yin, M. C. In vitro anti-Helicobacter pylori activity of diallyl sulphides and protocatechuic acid Phytother. Res. 2008, 22 (1) 53-57 10.1002/ptr.2259
    • (2008) Phytother. Res. , vol.22 , Issue.1 , pp. 53-57
    • Liu, W.H.1    Hsu, C.C.2    Yin, M.C.3
  • 350
    • 79953307290 scopus 로고    scopus 로고
    • In vitro sortase A inhibitory and antimicrobial activity of flavonoids isolated from the roots of Sophora flavescens
    • Oh, I.; Yang, W. Y.; Chung, S. C.; Kim, T. Y.; Oh, K. B.; Shin, J. In vitro sortase A inhibitory and antimicrobial activity of flavonoids isolated from the roots of Sophora flavescens Arch. Pharmacal Res. 2011, 34 (2) 217-222 10.1007/s12272-011-0206-0
    • (2011) Arch. Pharmacal Res. , vol.34 , Issue.2 , pp. 217-222
    • Oh, I.1    Yang, W.Y.2    Chung, S.C.3    Kim, T.Y.4    Oh, K.B.5    Shin, J.6
  • 351
    • 33746731113 scopus 로고    scopus 로고
    • Flavonols inhibit sortases and sortase-mediated Staphylococcus aureus clumping to fibrinogen
    • Kang, S. S.; Kim, J.-G.; Lee, T.-H.; Oh, K.-B. Flavonols inhibit sortases and sortase-mediated Staphylococcus aureus clumping to fibrinogen Biol. Pharm. Bull. 2006, 29 (8) 1751-1755 10.1248/bpb.29.1751
    • (2006) Biol. Pharm. Bull. , vol.29 , Issue.8 , pp. 1751-1755
    • Kang, S.S.1    Kim, J.-G.2    Lee, T.-H.3    Oh, K.-B.4
  • 352
    • 84928781782 scopus 로고    scopus 로고
    • Quercitrin, an inhibitor of sortase A, interferes with the adhesion of Staphylococcal aureus
    • Liu, B.; Chen, F.; Bi, C.; Wang, L.; Zhong, X.; Cai, H.; Deng, X.; Niu, X.; Wang, D. Quercitrin, an inhibitor of sortase A, interferes with the adhesion of Staphylococcal aureus Molecules 2015, 20 (4) 6533-6543 10.3390/molecules20046533
    • (2015) Molecules , vol.20 , Issue.4 , pp. 6533-6543
    • Liu, B.1    Chen, F.2    Bi, C.3    Wang, L.4    Zhong, X.5    Cai, H.6    Deng, X.7    Niu, X.8    Wang, D.9
  • 353
    • 84925061503 scopus 로고    scopus 로고
    • Streptococcus mutans sortase A inhibitory metabolites from the flowers of Sophora japonica
    • Yang, W.-Y.; Won, T. H.; Ahn, C.-H.; Lee, S.-H.; Yang, H.-C.; Shin, J.; Oh, K.-B. Streptococcus mutans sortase A inhibitory metabolites from the flowers of Sophora japonica Bioorg. Med. Chem. Lett. 2015, 25 (7) 1394-1397 10.1016/j.bmcl.2015.02.051
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , Issue.7 , pp. 1394-1397
    • Yang, W.-Y.1    Won, T.H.2    Ahn, C.-H.3    Lee, S.-H.4    Yang, H.-C.5    Shin, J.6    Oh, K.-B.7
  • 354
    • 84885184449 scopus 로고    scopus 로고
    • Bacterial neuraminidase inhibitory effects of prenylated isoflavones from roots of Flemingia philippinensis
    • Wang, Y.; Curtis-Long, M. J.; Yuk, H. J.; Kim, D. W.; Tan, X. F.; Park, K. H. Bacterial neuraminidase inhibitory effects of prenylated isoflavones from roots of Flemingia philippinensis Bioorg. Med. Chem. 2013, 21 (21) 6398-6404 10.1016/j.bmc.2013.08.049
    • (2013) Bioorg. Med. Chem. , vol.21 , Issue.21 , pp. 6398-6404
    • Wang, Y.1    Curtis-Long, M.J.2    Yuk, H.J.3    Kim, D.W.4    Tan, X.F.5    Park, K.H.6
  • 356
    • 80052920361 scopus 로고    scopus 로고
    • Potent inhibition of bacterial neuraminidase activity by pterocarpans isolated from the roots of Lespedeza bicolor
    • Woo, H. S.; Kim, D. W.; Curtis-Long, M. J.; Lee, B. W.; Lee, J. H.; Kim, J. Y.; Kang, J. E.; Park, K. H. Potent inhibition of bacterial neuraminidase activity by pterocarpans isolated from the roots of Lespedeza bicolor Bioorg. Med. Chem. Lett. 2011, 21 (20) 6100-6103 10.1016/j.bmcl.2011.08.046
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.20 , pp. 6100-6103
    • Woo, H.S.1    Kim, D.W.2    Curtis-Long, M.J.3    Lee, B.W.4    Lee, J.H.5    Kim, J.Y.6    Kang, J.E.7    Park, K.H.8
  • 358
    • 84891486379 scopus 로고    scopus 로고
    • Sortase A inhibitory metabolites from the roots of Pulsatilla koreana
    • Lee, S.; Song, I.-H.; Lee, J.-H.; Yang, W.-Y.; Oh, K.-B.; Shin, J. Sortase A inhibitory metabolites from the roots of Pulsatilla koreana Bioorg. Med. Chem. Lett. 2014, 24 (1) 44-48 10.1016/j.bmcl.2013.12.006
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , Issue.1 , pp. 44-48
    • Lee, S.1    Song, I.-H.2    Lee, J.-H.3    Yang, W.-Y.4    Oh, K.-B.5    Shin, J.6
  • 359
    • 84883795659 scopus 로고    scopus 로고
    • Curcumin inhibits the Sortase A activity of the Streptococcus mutans UA159
    • Hu, P.; Huang, P.; Chen, W. M. Curcumin inhibits the Sortase A activity of the Streptococcus mutans UA159 Appl. Biochem. Biotechnol. 2013, 171 (2) 396-402 10.1007/s12010-013-0378-9
    • (2013) Appl. Biochem. Biotechnol. , vol.171 , Issue.2 , pp. 396-402
    • Hu, P.1    Huang, P.2    Chen, W.M.3
  • 360
    • 28444481060 scopus 로고    scopus 로고
    • Curcuma longa L. Constituents inhibit sortase A and Staphylococcus aureus cell adhesion to fibronectin
    • Park, B. S.; Kim, J. G.; Kim, M. R.; Lee, S. E.; Takeoka, G. R.; Oh, K. B.; Kim, J. H. Curcuma longa L. constituents inhibit sortase A and Staphylococcus aureus cell adhesion to fibronectin J. Agric. Food Chem. 2005, 53 (23) 9005-9009 10.1021/jf051765z
    • (2005) J. Agric. Food Chem. , vol.53 , Issue.23 , pp. 9005-9009
    • Park, B.S.1    Kim, J.G.2    Kim, M.R.3    Lee, S.E.4    Takeoka, G.R.5    Oh, K.B.6    Kim, J.H.7
  • 362
    • 84915789454 scopus 로고    scopus 로고
    • Catechin-based procyanidins from Peumus boldus Mol aqueous extract inhibit Helicobacter pylori urease and adherence to adenocarcinoma gastric cells
    • Pastene, E.; Parada, V.; Avello, M.; Ruiz, A.; García, A. Catechin-based procyanidins from Peumus boldus Mol. aqueous extract inhibit Helicobacter pylori urease and adherence to adenocarcinoma gastric cells Phytother. Res. 2014, 28 (11) 1637-1645 10.1002/ptr.5176
    • (2014) Phytother. Res. , vol.28 , Issue.11 , pp. 1637-1645
    • Pastene, E.1    Parada, V.2    Avello, M.3    Ruiz, A.4    García, A.5
  • 363
    • 2942622529 scopus 로고    scopus 로고
    • Inhibition of sortase, a bacterial surface protein anchoring transpeptidase, by β-sitosterol-3-O-glucopyranoside from Fritillaria verticillata
    • Kim, S.-H.; Shin, D.-S.; Oh, M.-N.; Chung, S.-C.; Lee, J.-S.; Chang, I.-M.; Oh, K.-B. Inhibition of sortase, a bacterial surface protein anchoring transpeptidase, by β-sitosterol-3-O-glucopyranoside from Fritillaria verticillata Biosci., Biotechnol., Biochem. 2003, 67 (11) 2477-2479 10.1271/bbb.67.2477
    • (2003) Biosci., Biotechnol., Biochem. , vol.67 , Issue.11 , pp. 2477-2479
    • Kim, S.-H.1    Shin, D.-S.2    Oh, M.-N.3    Chung, S.-C.4    Lee, J.-S.5    Chang, I.-M.6    Oh, K.-B.7
  • 364
    • 84921021894 scopus 로고    scopus 로고
    • Selective antibacterial activity of patchouli alcohol against Helicobacter pylori based on inhibition of urease
    • Yu, X. D.; Xie, J. H.; Wang, Y. H.; Li, Y. C.; Mo, Z. Z.; Zheng, Y. F.; Su, J. Y.; Liang, Y. E.; Liang, J. Z.; Su, Z. R. et al. Selective antibacterial activity of patchouli alcohol against Helicobacter pylori based on inhibition of urease Phytother. Res. 2015, 29 (1) 67-72 10.1002/ptr.5227
    • (2015) Phytother. Res. , vol.29 , Issue.1 , pp. 67-72
    • Yu, X.D.1    Xie, J.H.2    Wang, Y.H.3    Li, Y.C.4    Mo, Z.Z.5    Zheng, Y.F.6    Su, J.Y.7    Liang, Y.E.8    Liang, J.Z.9    Su, Z.R.10
  • 365
    • 77952891391 scopus 로고    scopus 로고
    • Rhamnolipids: Diversity of structures, microbial origins and roles
    • Abdel-Mawgoud, A. M.; Lépine, F.; Déziel, E. Rhamnolipids: diversity of structures, microbial origins and roles Appl. Microbiol. Biotechnol. 2010, 86 (5) 1323-1336 10.1007/s00253-010-2498-2
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , Issue.5 , pp. 1323-1336
    • Abdel-Mawgoud, A.M.1    Lépine, F.2    Déziel, E.3
  • 366
    • 33646908499 scopus 로고    scopus 로고
    • Rhamnolipids are virulence factors that promote early infiltration of primary human airway epithelia by Pseudomonas aeruginosa
    • Zulianello, L.; Canard, C.; Kohler, T.; Caille, D.; Lacroix, J. S.; Meda, P. Rhamnolipids are virulence factors that promote early infiltration of primary human airway epithelia by Pseudomonas aeruginosa Infect. Immun. 2006, 74 (6) 3134-3147 10.1128/IAI.01772-05
    • (2006) Infect. Immun. , vol.74 , Issue.6 , pp. 3134-3147
    • Zulianello, L.1    Canard, C.2    Kohler, T.3    Caille, D.4    Lacroix, J.S.5    Meda, P.6
  • 367
    • 84891060015 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa biofilms: Mechanisms of immune evasion
    • Alhede, M.; Bjarnsholt, T.; Givskov, M.; Alhede, M. Pseudomonas aeruginosa biofilms: mechanisms of immune evasion Adv. Appl. Microbiol. 2014, 86, 1-40 10.1016/B978-0-12-800262-9.00001-9
    • (2014) Adv. Appl. Microbiol. , vol.86 , pp. 1-40
    • Alhede, M.1    Bjarnsholt, T.2    Givskov, M.3    Alhede, M.4
  • 368
    • 84905988067 scopus 로고    scopus 로고
    • A new assay for rhamnolipid detection-important virulence factors of Pseudomonas aeruginosa
    • Laabei, M.; Jamieson, W. D.; Lewis, S. E.; Diggle, S. P.; Jenkins, A. T. A new assay for rhamnolipid detection-important virulence factors of Pseudomonas aeruginosa Appl. Microbiol. Biotechnol. 2014, 98 (16) 7199-7209 10.1007/s00253-014-5904-3
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , Issue.16 , pp. 7199-7209
    • Laabei, M.1    Jamieson, W.D.2    Lewis, S.E.3    Diggle, S.P.4    Jenkins, A.T.5
  • 369
    • 79955473657 scopus 로고    scopus 로고
    • Gene regulation of rhamnolipid production in Pseudomonas aeruginosa - A review
    • Reis, R. S.; Pereira, A. G.; Neves, B. C.; Freire, D. M. G. Gene regulation of rhamnolipid production in Pseudomonas aeruginosa-A review Bioresour. Technol. 2011, 102 (11) 6377-6384 10.1016/j.biortech.2011.03.074
    • (2011) Bioresour. Technol. , vol.102 , Issue.11 , pp. 6377-6384
    • Reis, R.S.1    Pereira, A.G.2    Neves, B.C.3    Freire, D.M.G.4
  • 370
    • 0030930248 scopus 로고    scopus 로고
    • Roles of Pseudomonas aeruginosa las and rhl quorum-sensing systems in control of elastase and rhamnolipid biosynthesis genes
    • Pearson, J. P.; Pesci, E. C.; Iglewski, B. H. Roles of Pseudomonas aeruginosa las and rhl quorum-sensing systems in control of elastase and rhamnolipid biosynthesis genes J. Bacteriol. 1997, 179 (18) 5756-5767
    • (1997) J. Bacteriol. , vol.179 , Issue.18 , pp. 5756-5767
    • Pearson, J.P.1    Pesci, E.C.2    Iglewski, B.H.3
  • 371
    • 84897475718 scopus 로고    scopus 로고
    • Elastase LasB of Pseudomonas aeruginosa promotes biofilm formation partly through rhamnolipid-mediated regulation
    • Yu, H.; He, X.; Xie, W.; Xiong, J.; Sheng, H.; Guo, S.; Huang, C.; Zhang, D.; Zhang, K. Elastase LasB of Pseudomonas aeruginosa promotes biofilm formation partly through rhamnolipid-mediated regulation Can. J. Microbiol. 2014, 60 (4) 227-235 10.1139/cjm-2013-0667
    • (2014) Can. J. Microbiol. , vol.60 , Issue.4 , pp. 227-235
    • Yu, H.1    He, X.2    Xie, W.3    Xiong, J.4    Sheng, H.5    Guo, S.6    Huang, C.7    Zhang, D.8    Zhang, K.9
  • 372
    • 79958751007 scopus 로고    scopus 로고
    • Flavanones and rotenoids from the roots of Amorpha fruticosa L that inhibit bacterial neuraminidase
    • Kim, Y. S.; Ryu, Y. B.; Curtis-Long, M. J.; Yuk, H. J.; Cho, J. K.; Kim, J. Y.; Kim, K. D.; Lee, W. S.; Park, K. H. Flavanones and rotenoids from the roots of Amorpha fruticosa L. that inhibit bacterial neuraminidase Food Chem. Toxicol. 2011, 49 (8) 1849-1856 10.1016/j.fct.2011.04.038
    • (2011) Food Chem. Toxicol. , vol.49 , Issue.8 , pp. 1849-1856
    • Kim, Y.S.1    Ryu, Y.B.2    Curtis-Long, M.J.3    Yuk, H.J.4    Cho, J.K.5    Kim, J.Y.6    Kim, K.D.7    Lee, W.S.8    Park, K.H.9
  • 373
    • 79959690712 scopus 로고    scopus 로고
    • Recent advances in understanding the antibacterial properties of flavonoids
    • Cushnie, T. P.; Lamb, A. J. Recent advances in understanding the antibacterial properties of flavonoids Int. J. Antimicrob. Agents 2011, 38 (2) 99-107 10.1016/j.ijantimicag.2011.02.014
    • (2011) Int. J. Antimicrob. Agents , vol.38 , Issue.2 , pp. 99-107
    • Cushnie, T.P.1    Lamb, A.J.2
  • 374
    • 84859161959 scopus 로고    scopus 로고
    • Polyphenols as antimicrobial agents
    • Daglia, M. Polyphenols as antimicrobial agents Curr. Opin. Biotechnol. 2012, 23 (2) 174-181 10.1016/j.copbio.2011.08.007
    • (2012) Curr. Opin. Biotechnol. , vol.23 , Issue.2 , pp. 174-181
    • Daglia, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.