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Volumn 8, Issue 1, 2015, Pages 123-150

Antimicrobial peptides in 2014

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DEFENSIN; AMPICILLIN; BACERIDIN; BACTERIOCIN; BETA DEFENSIN; BOVICIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; COPSIN; CROTALICIDIN; DERMCIDIN; DOUBLE STRANDED RNA; EOTAXIN; EOTAXIN 2; EOTAXIN 3; GAGEOTETRIN A; HEAT SHOCK PROTEIN; HISPIDALIN; LACTICIN; LANCOVUTIDE; LANTHIOPEPTIN; LANTIBIOTIC; LUCIFENSIN; MERSACIDIN; NISIN A; PLECTASIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE RICH PROTEIN; RIBONUCLEASE VI; SONORENSIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84930209721     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph8010123     Document Type: Review
Times cited : (169)

References (189)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellullar organisms
    • Zasloff, M. Antimicrobial peptides of multicellullar organisms. Nature 2002, 415, 359-365.
    • (2002) Nature , vol.415 , pp. 359-365
    • Zasloff, M.1
  • 2
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y.; Gallo, R.L. AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009, 30, 131-141.
    • (2009) Trends Immunol , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 3
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R.E.; Lehrer, R. Cationic peptides: A new source of antibiotics. Trends Biotechnol. 1998, 16, 82-88.
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 4
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of Antimicrobial Peptide Action and Resistance. Pharmacol
    • Yeaman, M.R.; Yount, N.Y. Mechanisms of Antimicrobial Peptide Action and Resistance. Pharmacol. Rev. 2003, 55, 27-55.
    • (2003) Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 5
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Natl
    • Brogden, K.A. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Natl. Rev. Microbiol. 2005, 3, 238-250.
    • (2005) Rev. Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 6
    • 84946027595 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology Information
    • NCBI Resource Coordinators
    • NCBI Resource Coordinators. Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 2015, 43, D6-D17.
    • (2015) Nucleic Acids Res , vol.43
  • 7
    • 0347755460 scopus 로고    scopus 로고
    • The antimicrobial peptide database
    • Wang, Z.; Wang, G. APD: The antimicrobial peptide database. Nucleic Acids Res. 2004, 32, D590-D592.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.2
  • 8
    • 58149187882 scopus 로고    scopus 로고
    • The updated antimicrobial peptide database and its application in peptide design
    • Wang, G.; Li, X.; Wang, Z. The updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009, 37, D933-D937.
    • (2009) Nucleic Acids Res , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 9
    • 84921764633 scopus 로고    scopus 로고
    • Improved methods for classification, prediction, and design of antimicrobial peptides
    • Wang, G. Improved methods for classification, prediction, and design of antimicrobial peptides. Methods Mol. Biol. 2015, 1268, 43-66.
    • (2015) Methods Mol. Biol , vol.1268 , pp. 43-66
    • Wang, G.1
  • 11
    • 84896092578 scopus 로고    scopus 로고
    • An antilisterial bacteriocin BacFL31 produced by Enterococcus faecium FL31 with a novel structure containing hydroxyproline residues
    • Chakchouk-Mtibaa, A.; Elleuch, L.; Smaoui, S.; Najah, S.; Sellem, I.; Abdelkafi, S.; Mellouli, L. An antilisterial bacteriocin BacFL31 produced by Enterococcus faecium FL31 with a novel structure containing hydroxyproline residues. Anaerobe 2014, 27C, 1-6.
    • (2014) Anaerobe , vol.27C , pp. 1-6
    • Chakchouk-Mtibaa, A.1    Elleuch, L.2    Smaoui, S.3    Najah, S.4    Sellem, I.5    Abdelkafi, S.6    Mellouli, L.7
  • 13
    • 84899576523 scopus 로고    scopus 로고
    • Bissell, A.; et al. Lassomycin, a ribosomally synthesized cyclic peptide, kills mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2
    • Gavrish, E.; Sit, C.S.; Cao, S.; Kandror, O.; Spoering, A.; Peoples, A.; Ling, L.; Fetterman, A.; Hughes, D.; Bissell, A.; et al. Lassomycin, a ribosomally synthesized cyclic peptide, kills mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2. Chem. Biol. 2014, 21, 509-518.
    • (2014) Chem. Biol , vol.21 , pp. 509-518
    • Gavrish, E.1    Sit, C.S.2    Cao, S.3    Kandror, O.4    Spoering, A.5    Peoples, A.6    Ling, L.7    Fetterman, A.8    Hughes, D.9
  • 16
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang, Y.Q.; Yuan, J.; Osapay, G.; Osapay, K.; Tran, D.; Miller, C.J.; Ouellette, A.J.; Selsted, M.E. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 1999, 286, 498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 17
    • 84933527587 scopus 로고    scopus 로고
    • Vipericidins: A novel family of cathelicidin-related peptides from the venom gland of South American pit vipers
    • Falcao, C.B.; de La Torre, B.G.; Pérez-Peinado, C.; Barron, A.E.; Andreu, D.; Rádis-Baptista, G. Vipericidins: a novel family of cathelicidin-related peptides from the venom gland of South American pit vipers. Amino Acids 2014, 46, 2561-2571.
    • (2014) Amino Acids , vol.46 , pp. 2561-2571
    • Falcao, C.B.1    De La Torre, B.G.2    Pérez-Peinado, C.3    Barron, A.E.4    Andreu, D.5    Rádis-Baptista, G.6
  • 18
    • 84892604414 scopus 로고    scopus 로고
    • Host-defense peptides with therapeutic potential from skin secretions of frogs from the family pipidae
    • Conlon, J.M.; Mechkarska, M. Host-defense peptides with therapeutic potential from skin secretions of frogs from the family pipidae. Pharmaceuticals 2014, 7, 58-77.
    • (2014) Pharmaceuticals , vol.7 , pp. 58-77
    • Conlon, J.M.1    Mechkarska, M.2
  • 19
    • 84907854569 scopus 로고    scopus 로고
    • Identification of multiple peptides with antioxidant and antimicrobial activities from skin and its secretions of Hylarana taipehensis, Amolops lifanensis, and Amolops granulosus
    • Guo, C.; Hu, Y.; Li, J.; Liu, Y.; Li, S.; Yan, K.; Wang, X.; Liu, J.; Wang, H. Identification of multiple peptides with antioxidant and antimicrobial activities from skin and its secretions of Hylarana taipehensis, Amolops lifanensis, and Amolops granulosus. Biochimie. 2014, 105, 192-201.
    • (2014) Biochimie , vol.105 , pp. 192-201
    • Guo, C.1    Hu, Y.2    Li, J.3    Liu, Y.4    Li, S.5    Yan, K.6    Wang, X.7    Liu, J.8    Wang, H.9
  • 20
    • 84894104230 scopus 로고    scopus 로고
    • Novel hairpin-like antimicrobial peptide from barnyard grass (Echinochloa crusgalli L.) seeds: Structure-functional and molecular-genetics characterization
    • Ryazantsev, D.Y.; Rogozhin, E.A.; Dimitrieva, T.V.; Drobyazina, P.E.; Khadeeva, N.V.; Egorov, T.A.; Grishin, E.V.; Zavriev, S.K. A novel hairpin-like antimicrobial peptide from barnyard grass (Echinochloa crusgalli L.) seeds: Structure-functional and molecular-genetics characterization. Biochimie 2014, 99, 63-70.
    • (2014) Biochimie , vol.99 , pp. 63-70
    • Ryazantsev, D.Y.1    Rogozhin, E.A.2    Dimitrieva, T.V.3    Drobyazina, P.E.4    Khadeeva, N.V.5    Egorov, T.A.6    Grishin, E.V.7    Zavriev, S.8
  • 21
    • 84899766972 scopus 로고    scopus 로고
    • Sil: A Streptococcus iniae bacteriocin with dual role as an antimicrobial and an immunomodulator that inhibits innate immune response and promotes S iniae infection
    • Li, M.F.; Zhang, B.C.; Li, J.; Sun, L. Sil: A Streptococcus iniae bacteriocin with dual role as an antimicrobial and an immunomodulator that inhibits innate immune response and promotes S. iniae infection. PLoS One. 2014, 9, e96222.
    • (2014) Plos One , vol.9
    • Li, M.F.1    Zhang, B.C.2    Li, J.3    Sun, L.4
  • 22
    • 84905112114 scopus 로고    scopus 로고
    • PPZPMs—A novel group of cyclic lipodepsipeptides produced by the Phytophthora alni associated strain Pseudomonas sp. JX090307—The missing link between the viscosin and amphisin group
    • Weisshoff, H.; Hentschel, S.; Zaspel, I.; Jarling, R.; Krause, E.; Pham, T.L. PPZPMs—A novel group of cyclic lipodepsipeptides produced by the Phytophthora alni associated strain Pseudomonas sp. JX090307—The missing link between the viscosin and amphisin group. Nat. Prod. Commun. 2014, 9, 989-996.
    • (2014) Nat. Prod. Commun , vol.9 , pp. 989-996
    • Weisshoff, H.1    Hentschel, S.2    Zaspel, I.3    Jarling, R.4    Krause, E.5    Pham, T.L.6
  • 24
    • 84924289802 scopus 로고    scopus 로고
    • De novo sequencing and transcriptome analysis for tetramorium bicarinatum: A comprehensive venom gland transcriptome analysis from an ant species
    • Bouzid, W.; Verdenaud, M.; Klopp, C.; Ducancel, F.; Noirot, C.; Vetillard, A. de novo sequencing and transcriptome analysis for tetramorium bicarinatum: A comprehensive venom gland transcriptome analysis from an ant species. BMC Genomics 2014, 15, 987.
    • (2014) BMC Genomics , vol.15 , pp. 987
    • Bouzid, W.1    Verdenaud, M.2    Klopp, C.3    Ducancel, F.4    Noirot, C.5    Vetillard, A.6
  • 25
    • 84942303243 scopus 로고    scopus 로고
    • Development of an analytical strategy for the identification of potential bioactive peptides generated by in vitro tryptic digestion of fish muscle proteins
    • Capriotti, A.L.; Cavaliere, C.; Foglia, P.; Piovesana, S.; Samperi, R.; Zenezini Chiozzi, R.; Lagana, A. Development of an analytical strategy for the identification of potential bioactive peptides generated by in vitro tryptic digestion of fish muscle proteins. Anal. Bioanal. Chem. 2015, 407, 845-854.
    • (2015) Anal. Bioanal. Chem , vol.407 , pp. 845-854
    • Capriotti, A.L.1    Cavaliere, C.2    Foglia, P.3    Piovesana, S.4    Samperi, R.5    Zenezini Chiozzi, R.6    Lagana, A.7
  • 26
    • 84878419915 scopus 로고    scopus 로고
    • Database-guided discovery of potent peptides to combat HIV-1 or superbugs
    • Wang, G. Database-guided discovery of potent peptides to combat HIV-1 or superbugs. Pharmaceuticals 2013, 6, 728-758.
    • (2013) Pharmaceuticals , vol.6 , pp. 728-758
    • Wang, G.1
  • 27
    • 84893834862 scopus 로고    scopus 로고
    • Gageotetrins A-C, Noncytotoxic antimicrobial linear lipopeptides from a marine bacterium Bacillus subtilis
    • Tareq, F.S.; Lee, M.A.; Lee, H.S.; Lee, Y.J.; Lee, J.S.; Hasan, C.M.; Islam, M.T.; Shin, H.J. Gageotetrins A-C, Noncytotoxic antimicrobial linear lipopeptides from a marine bacterium Bacillus subtilis. Org. Lett. 2014, 16, 928-931.
    • (2014) Org. Lett , vol.16 , pp. 928-931
    • Tareq, F.S.1    Lee, M.A.2    Lee, H.S.3    Lee, Y.J.4    Lee, J.S.5    Hasan, C.M.6    Islam, M.T.7    Shin, H.J.8
  • 28
  • 29
    • 1542753502 scopus 로고    scopus 로고
    • First in a New Class of Antibiotics
    • First in a New Class of Antibiotics. FDA Consum. 2003, 37, 4.
    • (2003) FDA Consum , vol.37 , pp. 4
  • 30
    • 84899122716 scopus 로고    scopus 로고
    • Sonorensin: An antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93
    • Chopra, L.; Singh, G.; Choudhary, V.; Sahoo, D.K. Sonorensin: an antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93. Appl. Environ. Microbiol. 2014, 80, 2981-2990.
    • (2014) Appl. Environ. Microbiol , vol.80 , pp. 2981-2990
    • Chopra, L.1    Singh, G.2    Choudhary, V.3    Sahoo, D.K.4
  • 34
    • 84899996364 scopus 로고    scopus 로고
    • Cationic bioactive peptide from the seeds of Benincasa hispida
    • Sharma, S.; Verma, H.N.; Sharma, N.K. Cationic bioactive peptide from the seeds of Benincasa hispida. Int. J. Pept. 2014, 2014, 156060.
    • (2014) Int. J. Pept , vol.2014
    • Sharma, S.1    Verma, H.N.2    Sharma, N.K.3
  • 38
    • 75149184631 scopus 로고    scopus 로고
    • AntiBP2: Improved version of antibacterial peptide prediction
    • Lata, S.; Mishra, N.K.; Raghava, G.P. AntiBP2: Improved version of antibacterial peptide prediction. BMC Bioinformatics 2010, 11, S19.
    • (2010) BMC Bioinformatics , vol.11
    • Lata, S.1    Mishra, N.K.2    Raghava, G.P.3
  • 39
    • 84875074764 scopus 로고    scopus 로고
    • IAMP-2L: A two-level multi-label classifier for identifying antimicrobial peptides and their functional types. Anal
    • Xiao, X.; Wang, P.; Lin, W.Z.; Jia, J.H.; Chou, K.C. iAMP-2L: A two-level multi-label classifier for identifying antimicrobial peptides and their functional types. Anal. Biochem. 2013, 436, 168-177.
    • (2013) Biochem , vol.436 , pp. 168-177
    • Xiao, X.1    Wang, P.2    Lin, W.Z.3    Jia, J.H.4    Chou, K.C.5
  • 40
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti, M. the role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 2005, 7, 179-196.
    • (2005) Curr. Issues Mol. Biol , vol.7 , pp. 179-196
    • Zanetti, M.1
  • 41
    • 84864773148 scopus 로고    scopus 로고
    • Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate
    • Hao, X.; Yang, H.; Wei, L.; Yang, S.; Zhu, W.; Ma, D.; Yu, H.; Lai, R. Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate. Amino acids 2012, 43, 677-685.
    • (2012) Amino Acids , vol.43 , pp. 677-685
    • Hao, X.1    Yang, H.2    Wei, L.3    Yang, S.4    Zhu, W.5    Ma, D.6    Yu, H.7    Lai, R.8
  • 42
    • 84899877398 scopus 로고    scopus 로고
    • Cathelicidins from the bullfrog Rana catesbeiana provides novel template for peptide antibiotic design
    • Ling, G.; Gao, J.; Zhang, S.; Xie, Z.; Wei, L.; Yu, H.; Wang, Y. Cathelicidins from the bullfrog Rana catesbeiana provides novel template for peptide antibiotic design. PLoS One 2014, 9, e93216.
    • (2014) Plos One , vol.9
    • Ling, G.1    Gao, J.2    Zhang, S.3    Xie, Z.4    Wei, L.5    Yu, H.6    Wang, Y.7
  • 44
    • 84896128940 scopus 로고    scopus 로고
    • Production and characterization of recombinant human beta-defensin DEFB120
    • Liu, H.; Yu, H.; Xin, A.; Shi, H.; Gu, Y.; Zhang, Y.; Diao, H.; Lin, D. Production and characterization of recombinant human beta-defensin DEFB120. J. Pept. Sci. 2014, 20, 251-257.
    • (2014) J. Pept. Sci , vol.20 , pp. 251-257
    • Liu, H.1    Yu, H.2    Xin, A.3    Shi, H.4    Gu, Y.5    Zhang, Y.6    Diao, H.7    Lin, D.8
  • 47
    • 84900399090 scopus 로고    scopus 로고
    • Human antimicrobial peptides and proteins
    • Wang, G. Human antimicrobial peptides and proteins. Pharmaceuticals 2014, 7, 545-594.
    • (2014) Pharmaceuticals , vol.7 , pp. 545-594
    • Wang, G.1
  • 48
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman, H.G. Antibacterial peptides: Basic facts and emerging concepts. J. Inter. Med. 2003, 254, 197-215.
    • (2003) J. Inter. Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 49
    • 84904471630 scopus 로고    scopus 로고
    • Fetal human keratinocytes produce large amounts of antimicrobial peptides: Involvement of histone-methylation processes
    • Gschwandtner, M.; Zhong, S.; Tschachler, A.; Mlitz, V.; Karner, S.; Elbe-Bürger, A.; Mildner, M. Fetal human keratinocytes produce large amounts of antimicrobial peptides: Involvement of histone-methylation processes. J. Invest Dermatol. 2014, 134, 2192-2201.
    • (2014) J. Invest Dermatol , vol.134 , pp. 2192-2201
    • Gschwandtner, M.1    Zhong, S.2    Tschachler, A.3    Mlitz, V.4    Karner, S.5    Elbe-Bürger, A.6    Mildner, M.7
  • 50
    • 84923010530 scopus 로고    scopus 로고
    • Innate immunity. Dermal adipocytes protect against invasive Staphylococcus aureus skin infection
    • Zhang, L.J.; Guerrero-Juarez, C.F.; Hata, T.; Bapat, S.P.; Ramos, R.; Plikus, M.V.; Gallo, R.L. Innate immunity. Dermal adipocytes protect against invasive Staphylococcus aureus skin infection. Science 2015, 347, 67-71.
    • (2015) Science , vol.347 , pp. 67-71
    • Zhang, L.J.1    Guerrero-Juarez, C.F.2    Hata, T.3    Bapat, S.P.4    Ramos, R.5    Plikus, M.V.6    Gallo, R.L.7
  • 52
    • 0030569343 scopus 로고    scopus 로고
    • Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells
    • Zhao, C.; Wang, I.; Lehrer, R.I. Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells. FEBS Lett. 1996, 396, 319-322.
    • (1996) FEBS Lett , vol.396 , pp. 319-322
    • Zhao, C.1    Wang, I.2    Lehrer, R.I.3
  • 53
    • 84923039622 scopus 로고    scopus 로고
    • New role for human alpha-defensin 5 in the fight against Clostridium difficile hypervirulent strains. Infect
    • Furci, L.; Baldan, R.; Bianchini, V.; Trovato, A.; Ossi, C.; Cichero, P.; Cirillo, D.M. A new role for human alpha-defensin 5 in the fight against Clostridium difficile hypervirulent strains. Infect. Immun. 2015, 83, 986-995.
    • (2015) Immun , vol.83 , pp. 986-995
    • Furci, L.1    Baldan, R.2    Bianchini, V.3    Trovato, A.4    Ossi, C.5    Cichero, P.6    Cirillo, D.7
  • 54
    • 84910635010 scopus 로고    scopus 로고
    • Altered alpha-defensin 5 expression in cervical squamocolumnar junction: Implication in the formation of a viral/tumour-permissive microenvironment
    • Hubert, P.; Herman, L.; Roncarati, P.; Maillard, C.; Renoux, V.; Demoulin, S.; Erpicum, C.; Foidart, J.M.; Boniver, J.; Noel, A. et al. Altered alpha-defensin 5 expression in cervical squamocolumnar junction: implication in the formation of a viral/tumour-permissive microenvironment. J. Pathol. 2014, 234, 464-477.
    • (2014) J. Pathol , vol.234 , pp. 464-477
    • Hubert, P.1    Herman, L.2    Roncarati, P.3    Maillard, C.4    Renoux, V.5    Demoulin, S.6    Erpicum, C.7    Foidart, J.M.8    Boniver, J.9    Noel, A.10
  • 55
    • 84922970369 scopus 로고    scopus 로고
    • Alpha-Defensin HD5 Inhibits Furin Cleavage of HPV16 L2 to Block Infection
    • Wiens, M.E.; Smith, J.G. Alpha-Defensin HD5 Inhibits Furin Cleavage of HPV16 L2 to Block Infection. J. Virol. 2014, 89, 2866-2874.
    • (2014) J. Virol , vol.89 , pp. 2866-2874
    • Wiens, M.E.1    Smith, J.G.2
  • 58
    • 0032436008 scopus 로고    scopus 로고
    • Isolation of human intestinal defensins from ileal neobladder urine
    • Porter, E.M.; Poles, M.A.; Lee, J.S.; Naitoh, J; Bevins, C.L.; Ganz, T. Isolation of human intestinal defensins from ileal neobladder urine. FEBS Lett. 1998, 434, 272-276.
    • (1998) FEBS Lett , vol.434 , pp. 272-276
    • Porter, E.M.1    Poles, M.A.2    Lee, J.S.3    Naitoh, J.4    Bevins, C.L.5    Ganz, T.6
  • 61
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson, J.; Gudmundsson, G.H.; Rottenberg, M.E.; Berndt, K.D.; Agerberth, B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 1998, 273, 3718-3724.
    • (1998) J. Biol. Chem , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 62
    • 84890942880 scopus 로고    scopus 로고
    • Native oligomerization determines the mode of action and biological activities of human cathelicidin LL-37
    • Xhindoli, D.; Pacor, S.; Guida, F.; Antcheva, N.; Tossi, A. Native oligomerization determines the mode of action and biological activities of human cathelicidin LL-37. Biochem. J. 2014, 457, 263-275.
    • (2014) Biochem. J , vol.457 , pp. 263-275
    • Xhindoli, D.1    Pacor, S.2    Guida, F.3    Antcheva, N.4    Tossi, A.5
  • 64
    • 84907484277 scopus 로고    scopus 로고
    • LL-37 peptide enhancement of signal transduction by toll-like receptor 3 is regulated by pH: Identification of a peptide antagonist of LL-37
    • Singh, D.; Vaughan, R.; Kao, C.C. LL-37 peptide enhancement of signal transduction by toll-like receptor 3 is regulated by pH: identification of a peptide antagonist of LL-37. J. Biol. Chem. 2014, 289, 27614-27624.
    • (2014) J. Biol. Chem , vol.289 , pp. 27614-27624
    • Singh, D.1    Vaughan, R.2    Kao, C.C.3
  • 66
    • 84903701599 scopus 로고    scopus 로고
    • High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments
    • Wang, G.; Mishra, B.; Epand, R.F.; Epand, R.M. High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments. Biochim. Biophys. Acta 2014, 1838, 2160-2172.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2160-2172
    • Wang, G.1    Mishra, B.2    Epand, R.F.3    Epand, R.M.4
  • 68
    • 84924815162 scopus 로고    scopus 로고
    • NAD-Dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1
    • Picchianti, M.; Russo, C.; Castagnini, M.; Biagini, M.; Soldaini, E.; Balducci, E. NAD-Dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1. Innate Immun. 2015, 21, 314-321.
    • (2015) Innate Immun , vol.21 , pp. 314-321
    • Picchianti, M.1    Russo, C.2    Castagnini, M.3    Biagini, M.4    Soldaini, E.5    Balducci, E.6
  • 70
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen, L.T.; Haney, E.F.; Vogel, H.J. The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 2011, 29, 464-472.
    • (2011) Trends Biotechnol , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 71
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin p1 within phospholipid membranes
    • Gazit, E.; Miller, I.R.; Biggin, P.C.; Sansom, M.S.; Shai, Y. Structure and orientation of the mammalian antibacterial peptide cecropin p1 within phospholipid membranes. J. Mol. Biol. 1996, 258, 860-870.
    • (1996) J. Mol. Biol , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.4    Shai, Y.5
  • 72
    • 84897694506 scopus 로고    scopus 로고
    • High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion
    • Perrin, B.S., Jr; Tian, Y.; Fu, R.; Grant, C.V.; Chekmenev, E.Y.; Wieczorek, W.E.; Dao, A.E.; Hayden, R.M.; Burzynski, C.M.; Venable, R.M.; et al. High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion. J. Am. Chem. Soc. 2014, 136, 3491-3504.
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 3491-3504
    • Perrin, B.S.1    Tian, Y.2    Fu, R.3    Grant, C.V.4    Chekmenev, E.Y.5    Wieczorek, W.E.6    Dao, A.E.7    Hayden, R.M.8    Burzynski, C.M.9    Venable, R.M.10
  • 73
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Â resolution
    • Fox, R.O., Jr.; Richards, F.M. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Â resolution. Nature 1982, 300, 325-330.
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox, R.O.1    Richards, F.M.2
  • 74
    • 0033529260 scopus 로고    scopus 로고
    • Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR
    • Kovacs, F.; Quine, J.; Cross, T.A. Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 7910-7915.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 7910-7915
    • Kovacs, F.1    Quine, J.2    Cross, T.A.3
  • 75
  • 78
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman, K.A.; Lee, D.K.; Ramamoorthy, A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 2003, 42, 6545-6558.
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 79
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z.; Lerman, J.C.; Gudmundsson, G.H.; Agerberth, B.; Shai, Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 1999, 341(Pt 3), 501-513.
    • (1999) Biochem. J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 80
    • 84901992689 scopus 로고    scopus 로고
    • Sensitivity to the two-peptide bacteriocin lactococcin G is dependent on UppP, an enzyme involved in cell-wall synthesis
    • Kjos, M.; Oppegard, C.; Diep, D.B.; Nes, I.F.; Veening, J.W.; Nissen-Meyer, J.; Kristensen, T. Sensitivity to the two-peptide bacteriocin lactococcin G is dependent on UppP, an enzyme involved in cell-wall synthesis. Mol. Microbiol. 2014, 92, 1177-1187.
    • (2014) Mol. Microbiol , vol.92 , pp. 1177-1187
    • Kjos, M.1    Oppegard, C.2    Diep, D.B.3    Nes, I.F.4    Veening, J.W.5    Nissen-Meyer, J.6    Kristensen, T.7
  • 81
    • 84902081895 scopus 로고    scopus 로고
    • An "Upp"-turn in bacteriocin receptor identification
    • Cotter, P.D. An 'Upp'-turn in bacteriocin receptor identification. Mol. Microbiol. 2014, 92, 1159-1163.
    • (2014) Mol Microbiol , vol.92 , pp. 1159-1163
    • Cotter, P.D.1
  • 83
    • 2942696237 scopus 로고    scopus 로고
    • Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel
    • Mukhopadhyay, J.; Sineva, E.; Knight, J.; Levy, R.M.; Ebright, R.H. Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel. Mol. Cell 2004, 14, 739-751.
    • (2004) Mol. Cell , vol.14 , pp. 739-751
  • 84
    • 84911468505 scopus 로고    scopus 로고
    • Insect-derived proline-rich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70S ribosome
    • Krizsan, A.; Volke, D.; Weinert, S.; Strater, N.; Knappe, D.; Hoffmann, R. Insect-derived proline-rich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70S ribosome. Angew. Chem. Int. Ed. Engl. 2014, 53, 12236-12239.
    • (2014) Angew. Chem. Int. Ed. Engl , vol.53 , pp. 12236-12239
    • Krizsan, A.1    Volke, D.2    Weinert, S.3    Strater, N.4    Knappe, D.5    Hoffmann, R.6
  • 85
    • 84919917867 scopus 로고    scopus 로고
    • The Host antimicrobial peptide Bac7(1-35) binds to bacterial ribosomal proteins and inhibits protein synthesis
    • Mardirossian, M.; Grzela, R.; Giglione, C.; Meinnel, T.; Gennaro, R.; Mergaert, P.; Scocchi, M. The Host antimicrobial peptide Bac7(1-35) binds to bacterial ribosomal proteins and inhibits protein synthesis. Chem. Biol. 2014, 21, 1639-1647.
    • (2014) Chem. Biol , vol.21 , pp. 1639-1647
    • Mardirossian, M.1    Grzela, R.2    Giglione, C.3    Meinnel, T.4    Gennaro, R.5    Mergaert, P.6    Scocchi, M.7
  • 86
    • 77951271759 scopus 로고    scopus 로고
    • Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II
    • De Leeuw, E.; Li, C.; Zeng, P.; Li, C.; Diepeveen-de Buin, M.; Lu, W.Y.; Breukink, E.; Lu, W. Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II. FEBSLett. 2010, 584, 1543-1548.
    • (2010) Febslett , vol.584 , pp. 1543-1548
    • De Leeuw, E.1    Li, C.2    Zeng, P.3    Li, C.4    Diepeveen-De Buin, M.5    Lu, W.Y.6    Breukink, E.7    Lu, W.8
  • 88
    • 65949089371 scopus 로고    scopus 로고
    • Lantibiotics: Mode of action, biosynthesis and bioengineering
    • Bierbaum, G.; Sahl, H.G. Lantibiotics: Mode of action, biosynthesis and bioengineering. Curr. Pharm. Biotechnol. 2009, 10, 2-18.
    • (2009) Curr. Pharm. Biotechnol , vol.10 , pp. 2-18
    • Bierbaum, G.1    Sahl, H.G.2
  • 89
    • 34548637974 scopus 로고    scopus 로고
    • Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin
    • Iwamoto, K.; Hayakawa, T.; Murate, M.; Makino, A.; Ito, K.; Fujisawa, T.; Kobayashi, T. Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin. Biophys. J. 2007, 93, 1608-1619.
    • (2007) Biophys. J , vol.93 , pp. 1608-1619
    • Iwamoto, K.1    Hayakawa, T.2    Murate, M.3    Makino, A.4    Ito, K.5    Fujisawa, T.6    Kobayashi, T.7
  • 91
    • 85027946602 scopus 로고    scopus 로고
    • Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting
    • Troeira Henriques, S.; Huang, Y.H.; Chaousis, S.; Wang, C.K.; Craik, D.J. anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting. Chembiochem 2014, 15, 1956-1965.
    • (2014) Chembiochem , vol.15 , pp. 1956-1965
    • Troeira Henriques, S.1    Huang, Y.H.2    Chaousis, S.3    Wang, C.K.4    Craik, D.J.5
  • 95
    • 0034704122 scopus 로고    scopus 로고
    • Novel membrane anchor function for the N-terminal amphipathic sequence of the signal-transducing protein IIAglucose of the Escherichia coli phosphotransferase system
    • Wang, G.; Peterkofsky, A.; Clore, G.M. A novel membrane anchor function for the N-terminal amphipathic sequence of the signal-transducing protein IIAglucose of the Escherichia coli phosphotransferase system. J. Biol. Chem. 2000, 275, 39811-39814.
    • (2000) J. Biol. Chem , vol.275 , pp. 39811-39814
    • Wang, G.1    Peterkofsky, A.2    Clore, G.3
  • 96
    • 14044268292 scopus 로고    scopus 로고
    • Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor
    • Wang, G.; Li, Y.; Li, X. Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor. J. Biol. Chem. 2005, 280, 5803-5811.
    • (2005) J. Biol. Chem , vol.280 , pp. 5803-5811
    • Wang, G.1    Li, Y.2    Li, X.3
  • 97
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • Wang, G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J. Biol. Chem. 2008, 283, 32637-32643.
    • (2008) J. Biol. Chem , vol.283 , pp. 32637-32643
    • Wang, G.1
  • 98
    • 70349119495 scopus 로고    scopus 로고
    • Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37. Antimicrob
    • Epand, RF; Wang, G.; Berno, B.; Epand, R.M. Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37. Antimicrob. Agents Chemother. 2009, 53, 3705-3714.
    • (2009) Agents Chemother , vol.53 , pp. 3705-3714
    • Epand, R.F.1    Wang, G.2    Berno, B.3    Epand, R.M.4
  • 99
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins—A family of multifunctional antimicrobial peptides
    • Bals, R.; Wilson, J.M. Cathelicidins—A family of multifunctional antimicrobial peptides. Cell. Mol. Life Sci. 2003, 60, 711-720.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 100
    • 84862968750 scopus 로고    scopus 로고
    • Decoding the functional roles of cationic side chains of the major antimicrobial region of human cathelicidin LL-37. Antimicrob
    • Wang, G.; Epand, R.F.; Mishra, B.; Lushnikova, T.; Thomas, V.C.; Bayles, K.W.; Epand, R.M. Decoding the functional roles of cationic side chains of the major antimicrobial region of human cathelicidin LL-37. Antimicrob. Agents Chemother. 2012, 56, 845-856.
    • (2012) Agents Chemother , vol.56 , pp. 845-856
    • Wang, G.1    Epand, R.F.2    Mishra, B.3    Lushnikova, T.4    Thomas, V.C.5    Bayles, K.W.6    Epand, R.M.7
  • 101
    • 84921492987 scopus 로고    scopus 로고
    • Endogenous intracellular cathelicidin enhances TLR9 activation in dendritic cells and macrophages
    • Nakagawa, Y.; Gallo, R.L. Endogenous intracellular cathelicidin enhances TLR9 activation in dendritic cells and macrophages. J. Immunol. 2015, 194, 1274-1284.
    • (2015) J. Immunol , vol.194 , pp. 1274-1284
    • Nakagawa, Y.1    Gallo, R.L.2
  • 103
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang, D.; Chen, Q.; Schmidt, A.P.; Anderson, G.M.; Wang, J.M.; Wooters, J.; Oppenheim, J.J.; Chertov, O. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 2000, 192, 1069-1074.
    • (2000) J. Exp. Med , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 104
    • 1842581655 scopus 로고    scopus 로고
    • A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release
    • Elssner, A.; Duncan, M.; Gavrilin, M.; Wewers, M.D. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J. Immunol. 2004, 172, 4987-4994.
    • (2004) J. Immunol , vol.172 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 108
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel, A. How do bacteria resist human antimicrobial peptides? Trends Microbiol. 2002, 10, 179-186.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 110
    • 79960409025 scopus 로고    scopus 로고
    • Coevolution of ABC transporters and two-component regulatory systems as resistance modules against antimicrobial peptides in Firmicutes Bacteria
    • Dintner, S.; Staron, A.; Berchtold, E.; Petri, T.; Mascher, T.; Gebhard, S. Coevolution of ABC transporters and two-component regulatory systems as resistance modules against antimicrobial peptides in Firmicutes Bacteria. J. Bacteriol. 2011, 193, 3851-3862.
    • (2011) J. Bacteriol , vol.193 , pp. 3851-3862
    • Dintner, S.1    Staron, A.2    Berchtold, E.3    Petri, T.4    Mascher, T.5    Gebhard, S.6
  • 111
    • 84856069886 scopus 로고    scopus 로고
    • GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus
    • Falord, M.; Karimova, G.; Hiron, A.; Msadek, T. GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 2012, 56, 1047-1058.
    • (2012) Antimicrob. Agents Chemother , vol.56 , pp. 1047-1058
    • Falord, M.1    Karimova, G.2    Hiron, A.3    Msadek, T.4
  • 112
    • 28444471602 scopus 로고    scopus 로고
    • DltABCD-and mprF-mediated cell envelope modifications of Staphylococcus aureus confer resistance to platelet microbicidal proteins and contribute to virulence in a rabbit endocarditis model
    • Weidenmaier, C.; Peschel, A.; Kempf, V.A.; Lucindo, N.; Yeaman, M.R.; Bayer, A.S. DltABCD-and mprF-mediated cell envelope modifications of Staphylococcus aureus confer resistance to platelet microbicidal proteins and contribute to virulence in a rabbit endocarditis model. Infect. Immun. 2005, 73, 8033-8038.
    • (2005) Infect. Immun , vol.73 , pp. 8033-8038
    • Weidenmaier, C.1    Peschel, A.2    Kempf, V.A.3    Lucindo, N.4    Yeaman, M.R.5    Bayer, A.S.6
  • 113
    • 36148999436 scopus 로고    scopus 로고
    • The antimicrobial peptide-sensing system aps of Staphylococcus aureus
    • Li, M; Cha, D.J.; Lai, Y.; Villaruz, A.E.; Sturdevant, D.E.; Otto, M. The antimicrobial peptide-sensing system aps of Staphylococcus aureus. Mol. Microbiol. 2007, 66, 1136-1147.
    • (2007) Mol. Microbiol , vol.66 , pp. 1136-1147
    • Li, M.1    Cha, D.J.2    Lai, Y.3    Villaruz, A.E.4    Sturdevant, D.E.5    Otto, M.6
  • 114
    • 84863230616 scopus 로고    scopus 로고
    • The Staphylococcus aureus two-component regulatory system, GraRS, senses and confers resistance to selected cationic antimicrobial peptides. Infect
    • Yang, S.-J.; Bayer, A.S.; Mishra, N.N.; Meehl, M.; Ledala, N.; Yeaman, M.R.; Xiong, Y.Q.; Cheung, A.L. The Staphylococcus aureus two-component regulatory system, GraRS, senses and confers resistance to selected cationic antimicrobial peptides. Infect. Immun. 2012, 80, 74-81.
    • (2012) Immun , vol.80 , pp. 74-81
    • Yang, S.-J.1    Bayer, A.S.2    Mishra, N.N.3    Meehl, M.4    Ledala, N.5    Yeaman, M.R.6    Xiong, Y.Q.7    Cheung, A.L.8
  • 115
    • 84911421857 scopus 로고    scopus 로고
    • Site-specific mutation of the sensor kinase GraS in Staphylococcus aureus alters the adaptive response to distinct cationic antimicrobial peptides
    • Cheung, A.L.; Bayer, A.S.; Yeaman, M.R.; Xiong, Y.Q.; Waring, A.J.; Memmi, G.; Donegan, N.; Chaili, S.; Yang, S.J. Site-specific mutation of the sensor kinase GraS in Staphylococcus aureus alters the adaptive response to distinct cationic antimicrobial peptides. Infect. Immun. 2014, 82, 5336-5345.
    • (2014) Infect. Immun , vol.82 , pp. 5336-5345
    • Cheung, A.L.1    Bayer, A.S.2    Yeaman, M.R.3    Xiong, Y.Q.4    Waring, A.J.5    Memmi, G.6    Donegan, N.7    Chaili, S.8    Yang, S.J.9
  • 116
    • 84919784538 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 binds directly to CsrS, a sensor histidine kinase of group A Streptococcus, to activate expression of virulence factors
    • Velarde, J.J.; Ashbaugh, M.; Wessels, M.R. The human antimicrobial peptide LL-37 binds directly to CsrS, a sensor histidine kinase of group A Streptococcus, to activate expression of virulence factors. J. Biol. Chem. 2014, 289, 36315-36324.
    • (2014) J. Biol. Chem , vol.289 , pp. 36315-36324
    • Velarde, J.J.1    Ashbaugh, M.2    Wessels, M.R.3
  • 117
    • 84884513953 scopus 로고    scopus 로고
    • The biology of the PmrA/PmrB two-component system: The major regulator of lipopolysaccharide modifications
    • Chen, H.D.; Groisman, E.A. The biology of the PmrA/PmrB two-component system: The major regulator of lipopolysaccharide modifications. Annu. Rev. Microbiol. 2013, 67, 83-112.
    • (2013) Annu. Rev. Microbiol , vol.67 , pp. 83-112
    • Chen, H.D.1    Groisman, E.A.2
  • 118
    • 84908137882 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance of Vibrio cholerae results from an lps modification pathway related to nonribosomal peptide synthetases
    • Henderson, J.C.; Fage, C.D.; Cannon, J.R.; Brodbelt, J.S.; Keatinge-Clay, A.T.; Trent, M.S. Antimicrobial peptide resistance of Vibrio cholerae results from an lps modification pathway related to nonribosomal peptide synthetases. ACS Chem. Biol. 2014, 9, 2382-2392.
    • (2014) ACS Chem. Biol , vol.9 , pp. 2382-2392
    • Henderson, J.C.1    Fage, C.D.2    Cannon, J.R.3    Brodbelt, J.S.4    Keatinge-Clay, A.T.5    Trent, M.S.6
  • 120
    • 84867625400 scopus 로고    scopus 로고
    • Lipooligosaccharide structure is an important determinant in the resistance of Neisseria gonorrhoeae to antimicrobial agents of innate host defense
    • Balthazar, J.T.; Gusa, A.; Martin, L.E.; Choudhury, B.; Carlson, R.; Shafer, W.M. Lipooligosaccharide structure is an important determinant in the resistance of Neisseria gonorrhoeae to antimicrobial agents of innate host defense. Front. Microbiol. 2011, 2, 30.
    • (2011) Front. Microbiol , vol.2 , pp. 30
    • Balthazar, J.T.1    Gusa, A.2    Martin, L.E.3    Choudhury, B.4    Carlson, R.5    Shafer, W.M.6
  • 121
    • 84929517735 scopus 로고    scopus 로고
    • The lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils
    • Handing, J.W.; Criss, A.K. The lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils. Cell. Microbiol. 2014, doi: 10.1111/cmi.12411.
    • (2014) Cell. Microbiol
    • Handing, J.W.1    Criss, A.K.2
  • 123
    • 84900448784 scopus 로고    scopus 로고
    • Phosphoethanolamine decoration of Neisseria gonorrhoeae lipid a plays a dual immunostimulatory and protective role during experimental genital tract infection
    • Packiam, M.; Yedery, R.D.; Begum, A.A.; Carlson, R.W.; Ganguly, J.; Sempowski, G.D.; Ventevogel, M.S.; Shafer, W.M.; Jerse, A.E. Phosphoethanolamine decoration of Neisseria gonorrhoeae lipid a plays a dual immunostimulatory and protective role during experimental genital tract infection. Infect. Immun. 2014, 82, 2170-2179.
    • (2014) Infect. Immun , vol.82 , pp. 2170-2179
    • Packiam, M.1    Yedery, R.D.2    Begum, A.A.3    Carlson, R.W.4    Ganguly, J.5    Sempowski, G.D.6    Ventevogel, M.S.7    Shafer, W.M.8    Jerse, A.E.9
  • 126
    • 84943662452 scopus 로고    scopus 로고
    • Typhimurium strategies to resist killing by cationic antimicrobial peptides
    • Matamouros, S.; Miller, S.I. S. Typhimurium strategies to resist killing by cationic antimicrobial peptides. Biochim. Biophys. Acta 2015, doi: 10.1016/j.bbamem.2015.01.013.
    • (2015) Biochim. Biophys. Acta
    • Matamouros, S.1    Miller, S.2
  • 127
    • 84894104284 scopus 로고    scopus 로고
    • Salmonellae PhoPQ regulation of the outer membrane to resist innate immunity
    • Dalebroux, Z.D.; Miller, S.I. Salmonellae PhoPQ regulation of the outer membrane to resist innate immunity. Curr Opin Microbiol. 2014, 17, 106-113.
    • (2014) Curr Opin Microbiol , vol.17 , pp. 106-113
    • Dalebroux, Z.D.1    Miller, S.I.2
  • 129
    • 84912095002 scopus 로고    scopus 로고
    • Kielian, T. Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds
    • Wang, G.; Hanke, M.L.; Mishra, B.; Lushnikova, T.; Heim, C.E.; Chittezham Thomas, V.; Bayles, K.W.; Kielian, T. Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds. ACS Chem. Biol. 2014, 9, 1997-2002.
    • (2014) ACS Chem. Biol , vol.9 , pp. 1997-2002
    • Wang, G.1    Hanke, M.L.2    Mishra, B.3    Lushnikova, T.4    Heim, C.E.5    Chittezham Thomas, V.6    Bayles, K.W.7
  • 130
    • 33646597266 scopus 로고    scopus 로고
    • Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region
    • Li, X.; Li, Y.; Han, H.; Miller, D.W.; Wang, G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J. Am. Chem. Soc. 2006, 128, 5776-5785.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 5776-5785
    • Li, X.1    Li, Y.2    Han, H.3    Miller, D.W.4    Wang, G.5
  • 131
    • 84926186335 scopus 로고    scopus 로고
    • IBD: Cathelicidin can reverse intestinal fibrosis in models of colitis
    • Leake, I. IBD: cathelicidin can reverse intestinal fibrosis in models of colitis. Nat. Rev. Gastroenterol. Hepatol. 2015, 12, 3.
    • (2015) Nat. Rev. Gastroenterol. Hepatol , vol.12 , pp. 3
    • Leake, I.1
  • 133
    • 84920392961 scopus 로고    scopus 로고
    • Therapeutic potential of adenovirus-mediated delivery of beta-defensin 2 for experimental otitis media
    • Woo, J.I.; Kil, S.H.; Brough, D.E.; Lee, Y.J.; Lim, D.J.; Moon, S.K. Therapeutic potential of adenovirus-mediated delivery of beta-defensin 2 for experimental otitis media. Innate Immun. 2015, 21, 215-224.
    • (2015) Innate Immun , vol.21 , pp. 215-224
    • Woo, J.I.1    Kil, S.H.2    Brough, D.E.3    Lee, Y.J.4    Lim, D.J.5    Moon, S.K.6
  • 137
    • 84900408056 scopus 로고    scopus 로고
    • Green tea consumption after intense taekwondo training enhances salivary defense factors and antibacterial capacity
    • Lin, S.P.; Li, C.Y.; Suzuki, K.; Chang, C.K.; Chou, K.M.; Fang, S.H. Green tea consumption after intense taekwondo training enhances salivary defense factors and antibacterial capacity. PLoS One 2014, 9, e87580.
    • (2014) Plos One , vol.9
    • Lin, S.P.1    Li, C.Y.2    Suzuki, K.3    Chang, C.K.4    Chou, K.M.5    Fang, S.H.6
  • 138
    • 84871019068 scopus 로고    scopus 로고
    • Design of a novel cyclotide-based CXCR4 antagonist with anti-human immunodeficiency virus (HIV)-1 activity
    • Aboye, T.L.; Ha, H.; Majumder, S.; Christ, F.; Debyser, Z.; Shekhtman, A.; Neamati, N.; Camarero, J.A. Design of a novel cyclotide-based CXCR4 antagonist with anti-human immunodeficiency virus (HIV)-1 activity. J. Med. Chem. 2012, 55, 10729-10734.
    • (2012) J. Med. Chem , vol.55 , pp. 10729-10734
    • Aboye, T.L.1    Ha, H.2    Majumder, S.3    Christ, F.4    Debyser, Z.5    Shekhtman, A.6    Neamati, N.7    Camarero, J.A.8
  • 139
    • 58149089532 scopus 로고    scopus 로고
    • Engineering stabilized vascular endothelial growth factor-a antagonists: Synthesis, structural characterization, and bioactivity of grafted analogues of cyclotides
    • Gunasekera, S.; Foley, F.M.; Clark, R.J.; Sando, L.; Fabri, L.J.; Craik, D.J.; Daly, N.L. Engineering stabilized vascular endothelial growth factor-a antagonists: synthesis, structural characterization, and bioactivity of grafted analogues of cyclotides. J. Med. Chem. 2008, 51, 7697-7704.
    • (2008) J. Med. Chem , vol.51 , pp. 7697-7704
    • Gunasekera, S.1    Foley, F.M.2    Clark, R.J.3    Sando, L.4    Fabri, L.J.5    Craik, D.J.6    Daly, N.L.7
  • 142
    • 33749128301 scopus 로고    scopus 로고
    • Chemical synthesis and biosynthesis of the cyclotide family of circular proteins
    • Gunasekera, S.; Daly, N.L.; Anderson, M.A.; Craik, D.J. Chemical synthesis and biosynthesis of the cyclotide family of circular proteins. IUBMB Life 2006, 58, 515-524.
    • (2006) IUBMB Life , vol.58 , pp. 515-524
    • Gunasekera, S.1    Daly, N.L.2    Anderson, M.A.3    Craik, D.J.4
  • 144
    • 84910617831 scopus 로고    scopus 로고
    • Backbone cyclization of a recombinant cystine-knot peptide by engineered sortase A
    • Stanger, K.; Maurer, T.; Kaluarachchi, H.; Coons, M.; Franke, Y.; Hannoush, R.N. backbone cyclization of a recombinant cystine-knot peptide by engineered sortase A. FEBS Lett. 2014, 588, 4487-4496.
    • (2014) FEBS Lett , vol.588 , pp. 4487-4496
    • Stanger, K.1    Maurer, T.2    Kaluarachchi, H.3    Coons, M.4    Franke, Y.5    Hannoush, R.N.6
  • 145
    • 84922735649 scopus 로고    scopus 로고
    • Development of a catheter functionalized by a polydopamine peptide coating with antimicrobial and antibiofilm properties
    • Lim, K.; Chua, R.R.; Ho, B.; Tambyah, P.A.; Hadinoto, K.; Leong, S.S. Development of a catheter functionalized by a polydopamine peptide coating with antimicrobial and antibiofilm properties. ActaBiomater. 2014, 15, 127-138.
    • (2014) Actabiomater , vol.15 , pp. 127-138
    • Lim, K.1    Chua, R.R.2    Ho, B.3    Tambyah, P.A.4    Hadinoto, K.5    Leong, S.S.6
  • 148
    • 84901687471 scopus 로고    scopus 로고
    • Molecular structures of C- and N-terminus cysteine modified cecropin P1 chemically immobilized onto maleimide-terminated self-assembled monolayers investigated by molecular dynamics simulation
    • Wang, Z.; Han, X.; He, N.; Chen, Z.; Brooks, C.L, 3rd. Molecular structures of C- and N-terminus cysteine modified cecropin P1 chemically immobilized onto maleimide-terminated self-assembled monolayers investigated by molecular dynamics simulation. J. Phys. Chem. B 2014, 118, 5670-5680.
    • (2014) J. Phys. Chem. B , vol.118 , pp. 5670-5680
    • Wang, Z.1    Han, X.2    He, N.3    Chen, Z.4    Brooks, C.L.5
  • 149
    • 84894751392 scopus 로고    scopus 로고
    • Site specific immobilization of a potent antimicrobial peptide onto silicone catheters: Evaluation against urinary tract infection pathogens
    • Mishra, B.; Basu, A.; Chua, R.R.Y.; Saravanan, R.; Tambyah, P.P.; Ho, B.; Chang, M.W.; Leong, S.S.J. Site specific immobilization of a potent antimicrobial peptide onto silicone catheters: evaluation against urinary tract infection pathogens. J. Mater. Chem. B, 2014, 2, 1706-1716.
    • (2014) J. Mater. Chem. B , vol.2 , pp. 1706-1716
    • Mishra, B.1    Basu, A.2    Chua, R.3    Saravanan, R.4    Tambyah, P.P.5    Ho, B.6    Chang, M.W.7    Leong, S.8
  • 151
    • 84899866692 scopus 로고    scopus 로고
    • Biocompatibility of antimicrobial melimine lenses: Rabbit and human studies
    • Dutta, D.; Ozkan, J.; Willcox, M.D. Biocompatibility of antimicrobial melimine lenses: Rabbit and human studies. Optom. Vis. Sci. 2014, 91, 570-581.
    • (2014) Optom. Vis. Sci , vol.91 , pp. 570-581
    • Dutta, D.1    Ozkan, J.2    Willcox, M.D.3
  • 152
    • 84906096027 scopus 로고    scopus 로고
    • Effectiveness of antimicrobial peptide immobilization for preventing perioperative cornea implant-associated bacterial infection. Antimicrob
    • Tan, X.W.; Goh, T.W.; Saraswathi, P.; Nyein, C.L.; Setiawan, M.; Riau, A.; Lakshminarayanan, R.; Liu, S.; Tan, D.; Beuerman, R.W.; et al. Effectiveness of antimicrobial peptide immobilization for preventing perioperative cornea implant-associated bacterial infection. Antimicrob. Agents Chemother. 2014, 58, 5229-5238.
    • (2014) Agents Chemother , vol.58 , pp. 5229-5238
    • Tan, X.W.1    Goh, T.W.2    Saraswathi, P.3    Nyein, C.L.4    Setiawan, M.5    Riau, A.6    Lakshminarayanan, R.7    Liu, S.8    Tan, D.9    Beuerman, R.W.10
  • 153
    • 84895074906 scopus 로고    scopus 로고
    • Chitosan nanoparticles for dermaseptin peptide delivery toward tumor cells in vitro
    • Medeiros, K.A.; Joanitti, G.A.; Silva, L.P. Chitosan nanoparticles for dermaseptin peptide delivery toward tumor cells in vitro. Anticancer Drugs 2014, 25, 323-331.
    • (2014) Anticancer Drugs , vol.25 , pp. 323-331
    • Medeiros, K.A.1    Joanitti, G.A.2    Silva, L.P.3
  • 154
    • 84891814166 scopus 로고    scopus 로고
    • Gao, X.; et al. Co-administration of dual-targeting nanoparticles with penetration enhancement peptide for antiglioblastoma therapy
    • Miao, D.; Jiang, M.; Liu, Z.; Gu, G.; Hu, Q.; Kang, T.; Song, Q.; Yao, L.; Li, W.; Gao, X.; et al. Co-administration of dual-targeting nanoparticles with penetration enhancement peptide for antiglioblastoma therapy. Mol. Pharm. 2014, 11, 90-101.
    • (2014) Mol. Pharm , vol.11 , pp. 90-101
    • Miao, D.1    Jiang, M.2    Liu, Z.3    Gu, G.4    Hu, Q.5    Kang, T.6    Song, Q.7    Yao, L.8    Li, W.9
  • 155
    • 84914129162 scopus 로고
    • Novel endosomolytic peptides for enhancing gene delivery in nanoparticles. Biochim. Biophys
    • Ahmad, A.; Ranjan, S.; Zhang, W.; Zou, J.; Pyykko, I.; Kinnunen, P.K. Novel endosomolytic peptides for enhancing gene delivery in nanoparticles. Biochim. Biophys. Acta 2015, 1848, 544-553.
    • (1848) Acta , vol.2015 , pp. 544-553
    • Ahmad, A.1    Ranjan, S.2    Zhang, W.3    Zou, J.4    Pyykko, I.5    Kinnunen, P.K.6
  • 156
    • 84898471250 scopus 로고    scopus 로고
    • Silicon microfluidic flow focusing devices for the production of size-controlled PLGA based drug loaded microparticles
    • Keohane, K.; Brennan, D.; Galvin, P.; Griffin, B.T. Silicon microfluidic flow focusing devices for the production of size-controlled PLGA based drug loaded microparticles. Int. J. Pharm. 2014, 467, 60-69.
    • (2014) Int. J. Pharm , vol.467 , pp. 60-69
    • Keohane, K.1    Brennan, D.2    Galvin, P.3    Griffin, B.T.4
  • 158
    • 84907556309 scopus 로고    scopus 로고
    • Ultrashort cationic naphthalene-derived self-assembled peptides as antimicrobial nanomaterials
    • Laverty, G.; McCloskey, A.P.; Gilmore, B.F.; Jones, D.S.; Zhou, J; Xu, B. Ultrashort cationic naphthalene-derived self-assembled peptides as antimicrobial nanomaterials. Biomacromolecules 2014, 15, 3429-3439.
    • (2014) Biomacromolecules , vol.15 , pp. 3429-3439
    • Laverty, G.1    McCloskey, A.P.2    Gilmore, B.F.3    Jones, D.S.4    Zhou, J.5    Xu, B.6
  • 159
    • 84891776568 scopus 로고    scopus 로고
    • Rapid, electrical impedance detection of bacterial pathogens using immobilized antimicrobial peptides
    • Lillehoj, P.B.; Kaplan, C.W.; He, J.; Shi, W.; Ho, C.M. Rapid, electrical impedance detection of bacterial pathogens using immobilized antimicrobial peptides. J. Lab. Autom. 2014, 19, 42-49.
    • (2014) J. Lab. Autom , vol.19 , pp. 42-49
    • Lillehoj, P.B.1    Kaplan, C.W.2    He, J.3    Shi, W.4    Ho, C.M.5
  • 160
    • 84893580828 scopus 로고    scopus 로고
    • Impedimetric detection of pathogenic gram-positive bacteria using an antimicrobial peptide from class IIa bacteriocins
    • Etayash, H.; Jiang, K.; Thundat, T.; Kaur, K. impedimetric detection of pathogenic gram-positive bacteria using an antimicrobial peptide from class IIa bacteriocins. Anal. Chem. 2014, 86, 1693-1700.
    • (2014) Anal. Chem , vol.86 , pp. 1693-1700
    • Etayash, H.1    Jiang, K.2    Thundat, T.3    Kaur, K.4
  • 161
    • 84921723580 scopus 로고    scopus 로고
    • Design and evaluation of peptide nucleic acid probes for specific identification of Candida albicans
    • Kim, H.J.; Brehm-Stecher, B.F. Design and evaluation of peptide nucleic acid probes for specific identification of Candida albicans. J. Clin. Microbiol. 2015, 53, 511-521.
    • (2015) J. Clin. Microbiol , vol.53 , pp. 511-521
    • Kim, H.J.1    Brehm-Stecher, B.F.2
  • 162
    • 84920851400 scopus 로고    scopus 로고
    • Decade-long use of the antimicrobial peptide combination tyrothricin does not pose a major risk of acquired resistance with gram-positive bacteria and Candida spp
    • Strauss-Grabo, M.; Atiyem S.; Le, T.; Kretschmar, M. Decade-long use of the antimicrobial peptide combination tyrothricin does not pose a major risk of acquired resistance with gram-positive bacteria and Candida spp. Pharmazie 2014, 69, 838-841.
    • (2014) Pharmazie , vol.69 , pp. 838-841
    • Strauss-Grabo, M.1    Atiyem, S.2    Le, T.3    Kretschmar, M.4
  • 166
    • 84905983880 scopus 로고    scopus 로고
    • Unique properties of human P-defensin 6 (HBD6) and glycosaminoglycan complex: Sandwich-like dimerization and competition with the chemokine receptor 2 (CCR2) binding site
    • De Paula, V.S.; Pomin, V.H.; Valente, A.P. Unique properties of human P-defensin 6 (hBD6) and glycosaminoglycan complex: sandwich-like dimerization and competition with the chemokine receptor 2 (CCR2) binding site. J. Biol. Chem. 2014, 289, 22969-22979.
    • (2014) J. Biol. Chem , vol.289 , pp. 22969-22979
    • De Paula, V.S.1    Pomin, V.H.2    Valente, A.P.3
  • 167
    • 84893519181 scopus 로고    scopus 로고
    • Potential of host defense peptide prodrugs as neutrophil elastase-dependent anti-infective agents for cystic fibrosis. Antimicrob
    • Forde, E.; Humphreys, H.; Greene, C.M.; Fitzgerald-Hughes, D.; Devocelle, M. Potential of host defense peptide prodrugs as neutrophil elastase-dependent anti-infective agents for cystic fibrosis. Antimicrob. Agents Chemother. 2014, 58, 978-985.
    • (2014) Agents Chemother , vol.58 , pp. 978-985
    • Forde, E.1    Humphreys, H.2    Greene, C.M.3    Fitzgerald-Hughes, D.4    Devocelle, M.5
  • 168
    • 84921691389 scopus 로고    scopus 로고
    • Pro-moieties of antimicrobial peptide prodrugs
    • Forde, E.; Devocelle, M. Pro-moieties of antimicrobial peptide prodrugs. Molecules 2015, 20, 1210-1227.
    • (2015) Molecules , vol.20 , pp. 1210-1227
    • Forde, E.1    Devocelle, M.2
  • 171
    • 84921263550 scopus 로고    scopus 로고
    • Interaction of the core fragments of the LL-37 host defense peptide with actin
    • Sol, A.; Wang, G.; Blotnick, E.; Golla, R.; Bachrach, G. Interaction of the core fragments of the LL-37 host defense peptide with actin. RSC Adv. 2015, 5, 9361-9367.
    • (2015) RSC Adv , vol.5 , pp. 9361-9367
    • Sol, A.1    Wang, G.2    Blotnick, E.3    Golla, R.4    Bachrach, G.5
  • 175
    • 84907875522 scopus 로고    scopus 로고
    • Exploring the potential of magnetic antimicrobial agents for water disinfection
    • Pina, A.S.; Batalha, I.L.; Fernandes, C.S.; Aoki, M.A.; Roque, A.C. Exploring the potential of magnetic antimicrobial agents for water disinfection. Water Res. 2014, 66, 160-168.
    • (2014) Water Res , vol.66 , pp. 160-168
    • Pina, A.S.1    Batalha, I.L.2    Fernandes, C.S.3    Aoki, M.A.4    Roque, A.C.5
  • 178
    • 84906858151 scopus 로고    scopus 로고
    • Bovicin HC5 and nisin reduce Staphylococcus aureus adhesion to polystyrene and change the hydrophobicity profile and gibbs free energy of adhesion
    • Pimentel-Filho Nde, J.; Martins, M.C.; Nogueira, G.B.; Mantovani, H.C.; Vanetti, M.C. Bovicin HC5 and nisin reduce Staphylococcus aureus adhesion to polystyrene and change the hydrophobicity profile and gibbs free energy of adhesion. Int. J. Food Microbiol. 2014, 190, 1-8.
    • (2014) Int. J. Food Microbiol , vol.190 , pp. 1-8
    • Pimentel-Filho Nde, J.1    Martins, M.C.2    Nogueira, G.B.3    Mantovani, H.C.4    Vanetti, M.C.5
  • 179
    • 84915790922 scopus 로고    scopus 로고
    • Inhibitory effects of nisin-coated multi-walled carbon nanotube sheet on biofilm formation from Bacillus anthracis spores
    • Dong, X.; McCoy, E.; Zhang, M.; Yang, L. Inhibitory effects of nisin-coated multi-walled carbon nanotube sheet on biofilm formation from Bacillus anthracis spores. J. Environ. Sci. (China) 2014, 26, 2526-2534.
    • (2014) J. Environ. Sci. (China) , vol.26 , pp. 2526-2534
    • Dong, X.1    McCoy, E.2    Zhang, M.3    Yang, L.4
  • 180
    • 84902467078 scopus 로고    scopus 로고
    • Nisin/p-Lactam adjunct therapy against Salmonella enterica serovar Typhimurium: A mechanistic approach
    • Singh, A.P.; Preet, S.; Rishi, P. Nisin/p-Lactam adjunct therapy against Salmonella enterica serovar Typhimurium: a mechanistic approach. J. Antimicrob. Chemother. 2014, 69, 1877-1887.
    • (2014) J. Antimicrob. Chemother , vol.69 , pp. 1877-1887
    • Singh, A.P.1    Preet, S.2    Rishi, P.3
  • 181
    • 84907993181 scopus 로고    scopus 로고
    • Inhibition and destruction of Pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides
    • Dosler, S.; Karaaslan, E. Inhibition and destruction of Pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides. Peptides 2014, 62, 32-37.
    • (2014) Peptides , vol.62 , pp. 32-37
    • Dosler, S.1    Karaaslan, E.2
  • 182
    • 84908637012 scopus 로고    scopus 로고
    • Effective control of Salmonella infections by employing combinations of recombinant antimicrobial human P-defensins hBD-1 and hBD-2
    • Maiti, S.; Patro, S.; Purohit, S.; Jain, S.; Senapati, S.; Dey, N. Effective control of Salmonella infections by employing combinations of recombinant antimicrobial human P-defensins hBD-1 and hBD-2. Antimicrob Agents Chemother. 2014, 58, 6896-6903.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 6896-6903
    • Maiti, S.1    Patro, S.2    Purohit, S.3    Jain, S.4    Senapati, S.5    Dey, N.6
  • 183
    • 34547646366 scopus 로고    scopus 로고
    • Synergistic activity of dispersin B and cefamandole nafate in inhibition of staphylococcal biofilm growth on polyurethanes
    • Donelli, G.; Francolini, I.; Romoli, D.; Guaglianone, E.; Piozzi, A.; Ragunath, C.; Kaplan, J.B. Synergistic activity of dispersin B and cefamandole nafate in inhibition of staphylococcal biofilm growth on polyurethanes. Antimicrob Agents Chemother. 2007, 51, 2733-2740.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2733-2740
    • Donelli, G.1    Francolini, I.2    Romoli, D.3    Guaglianone, E.4    Piozzi, A.5    Ragunath, C.6    Kaplan, J.B.7
  • 184
    • 84903318216 scopus 로고    scopus 로고
    • An in vitro study on the effect of free amino acids alone or in combination with nisin on biofilms as well as on planktonic bacteria of Streptococcus mutans
    • Tong, Z.; Zhang, L.; Ling, J.; Jian, Y.; Huang, L.; Deng, D. An in vitro study on the effect of free amino acids alone or in combination with nisin on biofilms as well as on planktonic bacteria of Streptococcus mutans. PLoS One 2014, 9, e99513.
    • (2014) Plos One , vol.9
    • Tong, Z.1    Zhang, L.2    Ling, J.3    Jian, Y.4    Huang, L.5    Deng, D.6
  • 187
    • 84898742185 scopus 로고    scopus 로고
    • Mevalonolactone: An inhibitor of Staphylococcus epidermidis adherence and biofilm formation. Med
    • Scopel, M.; Abraham, W.R.; Antunes, A.L.; Henriques, A.T.; Macedo, A.J. Mevalonolactone: an inhibitor of Staphylococcus epidermidis adherence and biofilm formation. Med. Chem. 2014, 10, 246-251.
    • (2014) Chem , vol.10 , pp. 246-251
    • Scopel, M.1    Abraham, W.R.2    Antunes, A.L.3    Henriques, A.T.4    Macedo, A.J.5
  • 188
    • 84893924801 scopus 로고    scopus 로고
    • Type 2 quorum sensing monitoring, inhibition and biofilm formation in marine microrganisms
    • Liaqat, I.; Bachmann, R.T.; Edyvean, R.G. Type 2 quorum sensing monitoring, inhibition and biofilm formation in marine microrganisms. Curr. Microbiol. 2014, 68, 342-351.
    • (2014) Curr. Microbiol , vol.68 , pp. 342-351
    • Liaqat, I.1    Bachmann, R.T.2    Edyvean, R.G.3
  • 189
    • 84893770389 scopus 로고    scopus 로고
    • Y-Alkylidene-y-lactones and isobutylpyrrol-2(5H)-ones analogues to rubrolides as inhibitors of biofilm formation by gram-positive and gram-negative bacteria
    • Pereira, U.A.; Barbosa, L.C.; Maltha, C.R.; Demuner, A.J.; Masood, M.A.; Pimenta, A.L. y-Alkylidene-y-lactones and isobutylpyrrol-2(5H)-ones analogues to rubrolides as inhibitors of biofilm formation by gram-positive and gram-negative bacteria. Bioorg. Med. Chem. Lett. 2014, 24, 1052-1056.
    • (2014) Bioorg. Med. Chem. Lett , vol.24 , pp. 1052-1056
    • Pereira, U.A.1    Barbosa, L.C.2    Maltha, C.R.3    Demuner, A.J.4    Masood, M.A.5    Pimenta, A.L.6


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