메뉴 건너뛰기




Volumn 4, Issue 2012, 2012, Pages

The Drosophila melanogaster host model

Author keywords

Drosophila melanogaster; Pathogen host interactions; Periodontitis; Porphyromonas gingivalis

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PATTERN RECOGNITION RECEPTOR; PEPTIDOGLYCAN RECOGNITION PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; STAT PROTEIN; TETRACYCLINE DERIVATIVE; TOLL LIKE RECEPTOR; TUMOR NECROSIS FACTOR; UPSTREAM STIMULATORY FACTOR;

EID: 84864815485     PISSN: None     EISSN: 20002297     Source Type: Journal    
DOI: 10.3402/jom.v4i0.10368     Document Type: Article
Times cited : (20)

References (314)
  • 1
    • 14044261186 scopus 로고    scopus 로고
    • Secreted bacterial effectors and host-produced eiger/TNF drive death in a Salmonella-infected fruit fly
    • Brandt SM, Dionne MS, Khush RS, Pham LN, Vigdal TJ, Schneider DS. Secreted bacterial effectors and host-produced eiger/TNF drive death in a Salmonella-infected fruit fly. PLoS Biol 2004; 2: e418.
    • (2004) PLoS Biol , vol.2
    • Brandt, S.M.1    Dionne, M.S.2    Khush, R.S.3    Pham, L.N.4    Vigdal, T.J.5    Schneider, D.S.6
  • 2
    • 0345170718 scopus 로고    scopus 로고
    • Drosophila S2 cells: an alternative infection model for Listeria monocytogenes
    • Cheng LW, Portnoy DA. Drosophila S2 cells: an alternative infection model for Listeria monocytogenes. Cell Microbiol 2003; 5: 875-85.
    • (2003) Cell Microbiol , vol.5 , pp. 875-885
    • Cheng, L.W.1    Portnoy, D.A.2
  • 3
    • 0242654003 scopus 로고    scopus 로고
    • In vitro identification of two adherence factors required for in vivo virulence of Pseudomonas fluorescens
    • de Lima Pimenta A, Di Martino P, Le Bouder E, Hulen C, Blight MA. In vitro identification of two adherence factors required for in vivo virulence of Pseudomonas fluorescens. Microbes Infect 2003; 5: 1177-87.
    • (2003) Microbes Infect , vol.5 , pp. 1177-1187
    • de Lima Pimenta, A.1    Di Martino, P.2    Le Bouder, E.3    Hulen, C.4    Blight, M.A.5
  • 4
    • 0345170715 scopus 로고    scopus 로고
    • Exploration of host-pathogen interactions using Listeria monocytogenes and Drosophila melanogaster
    • Mansfield BE, Dionne MS, Schneider DS, Freitag NE. Exploration of host-pathogen interactions using Listeria monocytogenes and Drosophila melanogaster. Cell Microbiol 2003; 5: 901-11.
    • (2003) Cell Microbiol , vol.5 , pp. 901-911
    • Mansfield, B.E.1    Dionne, M.S.2    Schneider, D.S.3    Freitag, N.E.4
  • 6
    • 0038443820 scopus 로고    scopus 로고
    • Drosophila melanogaster is a genetically tractable model host for Mycobacterium marinum
    • Dionne MS, Ghori N, Schneider DS. Drosophila melanogaster is a genetically tractable model host for Mycobacterium marinum. Infect Immun 2003; 71: 3540-50.
    • (2003) Infect Immun , vol.71 , pp. 3540-3550
    • Dionne, M.S.1    Ghori, N.2    Schneider, D.S.3
  • 7
    • 17844409356 scopus 로고    scopus 로고
    • Drosophila melanogaster S2 cells: a model system to study Chlamydia interaction with host cells
    • Elwell C, Engel JN. Drosophila melanogaster S2 cells: a model system to study Chlamydia interaction with host cells. Cell Microbiol 2005; 7: 725-39.
    • (2005) Cell Microbiol , vol.7 , pp. 725-739
    • Elwell, C.1    Engel, J.N.2
  • 8
    • 0036025005 scopus 로고    scopus 로고
    • Role and activation of type III secretion system genes in Pseudomonas aeruginosa-induced Drosophila killing
    • Fauvarque MO, Bergeret E, Chabert J, Dacheux D, Satre M, Attree I. Role and activation of type III secretion system genes in Pseudomonas aeruginosa-induced Drosophila killing. Microb Pathog 2002; 32: 287-95.
    • (2002) Microb Pathog , vol.32 , pp. 287-295
    • Fauvarque, M.O.1    Bergeret, E.2    Chabert, J.3    Dacheux, D.4    Satre, M.5    Attree, I.6
  • 10
    • 2142820096 scopus 로고    scopus 로고
    • Immune-deficient Drosophila melanogaster: a model for the innate immune response to human fungal pathogens
    • Alarco AM, Marcil A, Chen J, Suter B, Thomas D, Whiteway M. Immune-deficient Drosophila melanogaster: a model for the innate immune response to human fungal pathogens. J Immunol 2004; 172: 5622-8.
    • (2004) J Immunol , vol.172 , pp. 5622-5628
    • Alarco, A.M.1    Marcil, A.2    Chen, J.3    Suter, B.4    Thomas, D.5    Whiteway, M.6
  • 12
    • 3343006985 scopus 로고    scopus 로고
    • Disruption of the Aspergillus fumigatus gene encoding nucleolar protein CgrA impairs thermotolerant growth and reduces virulence
    • Bhabhra R, Miley MD, Mylonakis E, Boettner D, Fortwendel J, Panepinto JC, et al. Disruption of the Aspergillus fumigatus gene encoding nucleolar protein CgrA impairs thermotolerant growth and reduces virulence. Infect Immun 2004; 72: 4731-40.
    • (2004) Infect Immun , vol.72 , pp. 4731-4740
    • Bhabhra, R.1    Miley, M.D.2    Mylonakis, E.3    Boettner, D.4    Fortwendel, J.5    Panepinto, J.C.6
  • 13
    • 77950552896 scopus 로고    scopus 로고
    • Exploring the concordance of Aspergillus fumigatus pathogenicity in mice and Toll-deficient flies
    • Chamilos G, Bignell EM, Schrettl M, Lewis RE, Leventakos K, May GS, et al. Exploring the concordance of Aspergillus fumigatus pathogenicity in mice and Toll-deficient flies. Med Mycol 2010; 48: 506-10.
    • (2010) Med Mycol , vol.48 , pp. 506-510
    • Chamilos, G.1    Bignell, E.M.2    Schrettl, M.3    Lewis, R.E.4    Leventakos, K.5    May, G.S.6
  • 14
    • 33645360264 scopus 로고    scopus 로고
    • Drosophila melanogaster as a facile model for large-scale studies of virulence mechanisms and antifungal drug efficacy in Candida species
    • Chamilos G, Lionakis MS, Lewis RE, Lopez-Ribot JL, Saville SP, Albert ND, et al. Drosophila melanogaster as a facile model for large-scale studies of virulence mechanisms and antifungal drug efficacy in Candida species. J Infect Dis 2006; 193: 1014-22.
    • (2006) J Infect Dis , vol.193 , pp. 1014-1022
    • Chamilos, G.1    Lionakis, M.S.2    Lewis, R.E.3    Lopez-Ribot, J.L.4    Saville, S.P.5    Albert, N.D.6
  • 15
    • 79959628056 scopus 로고    scopus 로고
    • Wild-type Drosophila melanogaster as an alternative model system for investigating the pathogenicity of Candida albicans
    • Jul
    • Glittenberg MT, Silas S, Maccallum DM, Gow NA, Ligoxygakis P. Wild-type Drosophila melanogaster as an alternative model system for investigating the pathogenicity of Candida albicans. Dis Model Mech. 2011 Jul; 4(4): 504-14.
    • (2011) Dis Model Mech , vol.4 , Issue.4 , pp. 504-514
    • Glittenberg, M.T.1    Silas, S.2    Maccallum, D.M.3    Gow, N.A.4    Ligoxygakis, P.5
  • 16
    • 39149088004 scopus 로고    scopus 로고
    • Virulence studies of Scedosporium and Fusarium species in Drosophila melanogaster
    • Lamaris GA, Chamilos G, Lewis RE, Kontoyiannis DP. Virulence studies of Scedosporium and Fusarium species in Drosophila melanogaster. J Infect Dis 2007; 196: 1860-4.
    • (2007) J Infect Dis , vol.196 , pp. 1860-1864
    • Lamaris, G.A.1    Chamilos, G.2    Lewis, R.E.3    Kontoyiannis, D.P.4
  • 17
    • 79251477529 scopus 로고    scopus 로고
    • The growing promise of Toll-deficient Drosophila melanogaster as a model for studying Aspergillus pathogenesis and treatment
    • Lionakis MS, Kontoyiannis DP. The growing promise of Toll-deficient Drosophila melanogaster as a model for studying Aspergillus pathogenesis and treatment. Virulence 2010; 1: 488-99.
    • (2010) Virulence , vol.1 , pp. 488-499
    • Lionakis, M.S.1    Kontoyiannis, D.P.2
  • 18
  • 19
    • 44949256129 scopus 로고    scopus 로고
    • West Nile virus infection of Drosophila melanogaster induces a protective RNAi response
    • Chotkowski HL, Ciota AT, Jia Y, Puig-Basagoiti F, Kramer LD, Shi PY, et al. West Nile virus infection of Drosophila melanogaster induces a protective RNAi response. Virology 2008; 377: 197-206.
    • (2008) Virology , vol.377 , pp. 197-206
    • Chotkowski, H.L.1    Ciota, A.T.2    Jia, Y.3    Puig-Basagoiti, F.4    Kramer, L.D.5    Shi, P.Y.6
  • 20
    • 49649127852 scopus 로고    scopus 로고
    • Drosophila RNAi screen identifies host genes important for influenza virus replication
    • Hao L, Sakurai A, Watanabe T, Sorensen E, Nidom CA, Newton MA, et al. Drosophila RNAi screen identifies host genes important for influenza virus replication. Nature 2008; 454: 890-3.
    • (2008) Nature , vol.454 , pp. 890-893
    • Hao, L.1    Sakurai, A.2    Watanabe, T.3    Sorensen, E.4    Nidom, C.A.5    Newton, M.A.6
  • 21
    • 0242439335 scopus 로고    scopus 로고
    • Directed expression of the HIV-1 accessory protein Vpu in Drosophila fat-body cells inhibits Toll-dependent immune responses
    • Leulier F, Marchal C, Miletich I, Limbourg-Bouchon B, Benarous R, Lemaitre B. Directed expression of the HIV-1 accessory protein Vpu in Drosophila fat-body cells inhibits Toll-dependent immune responses. EMBO Rep 2003; 4: 976-81.
    • (2003) EMBO Rep , vol.4 , pp. 976-981
    • Leulier, F.1    Marchal, C.2    Miletich, I.3    Limbourg-Bouchon, B.4    Benarous, R.5    Lemaitre, B.6
  • 22
    • 77951227183 scopus 로고    scopus 로고
    • RNA interference modulates replication of dengue virus in Drosophila melanogaster cells
    • Mukherjee S, Hanley KA. RNA interference modulates replication of dengue virus in Drosophila melanogaster cells. BMC Microbiol 2010; 10: 127.
    • (2010) BMC Microbiol , vol.10 , pp. 127
    • Mukherjee, S.1    Hanley, K.A.2
  • 23
    • 0034733577 scopus 로고    scopus 로고
    • Malaria parasite development in a Drosophila model
    • Schneider D, Shahabuddin M. Malaria parasite development in a Drosophila model. Science 2000; 288: 2376-9.
    • (2000) Science , vol.288 , pp. 2376-2379
    • Schneider, D.1    Shahabuddin, M.2
  • 26
    • 67049167752 scopus 로고    scopus 로고
    • Malaria sporozoite antigen-directed genome-wide response in transgenic Drosophila
    • Yan J, Yang X, Mortin MA. Shahabuddin M. Malaria sporozoite antigen-directed genome-wide response in transgenic Drosophila. Genesis 2009; 47: 196-203.
    • (2009) Genesis , vol.47 , pp. 196-203
    • Yan, J.1    Yang, X.2    Mortin, M.A.3    Shahabuddin, M.4
  • 28
    • 0012340085 scopus 로고    scopus 로고
    • Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence
    • RESEARCH0079
    • Celniker SE, Wheeler DA, Kronmiller B, Carlson JW, Halpern A, Patel S, et al. Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence. Genome Biol 2002; 3: RESEARCH0079.
    • (2002) Genome Biol , vol.3
    • Celniker, S.E.1    Wheeler, D.A.2    Kronmiller, B.3    Carlson, J.W.4    Halpern, A.5    Patel, S.6
  • 30
    • 0036250571 scopus 로고    scopus 로고
    • From sequence to phenotype: reverse genetics in Drosophila melanogaster
    • Adams MD, Sekelsky JJ. From sequence to phenotype: reverse genetics in Drosophila melanogaster. Nat Rev Genet 2002; 3: 189-98.
    • (2002) Nat Rev Genet , vol.3 , pp. 189-198
    • Adams, M.D.1    Sekelsky, J.J.2
  • 31
    • 14344263852 scopus 로고    scopus 로고
    • Emerging technologies for gene manipulation in Drosophila melanogaster
    • Venken KJ, Bellen HJ. Emerging technologies for gene manipulation in Drosophila melanogaster. Nat Rev Genet 2005; 6: 167-78.
    • (2005) Nat Rev Genet , vol.6 , pp. 167-178
    • Venken, K.J.1    Bellen, H.J.2
  • 32
    • 3142686745 scopus 로고    scopus 로고
    • The BDGP gene disruption project: single transposon insertions associated with 40% of Drosophila genes
    • Bellen HJ, Levis RW, Liao G, He Y, Carlson JW, Tsang G, et al. The BDGP gene disruption project: single transposon insertions associated with 40% of Drosophila genes. Genetics 2004; 167: 761-81.
    • (2004) Genetics , vol.167 , pp. 761-781
    • Bellen, H.J.1    Levis, R.W.2    Liao, G.3    He, Y.4    Carlson, J.W.5    Tsang, G.6
  • 34
    • 0021111260 scopus 로고
    • Vectors for P element-mediated gene transfer in Drosophila
    • Rubin GM, Spradling AC. Vectors for P element-mediated gene transfer in Drosophila. Nucleic Acids Res 1983; 11: 6341-51.
    • (1983) Nucleic Acids Res , vol.11 , pp. 6341-6351
    • Rubin, G.M.1    Spradling, A.C.2
  • 36
    • 2442458847 scopus 로고    scopus 로고
    • Construction of transgenic Drosophila by using the site-specific integrase from phage phiC31
    • Groth AC, Fish M, Nusse R, Calos MP. Construction of transgenic Drosophila by using the site-specific integrase from phage phiC31. Genetics 2004; 166: 1775-82.
    • (2004) Genetics , vol.166 , pp. 1775-1782
    • Groth, A.C.1    Fish, M.2    Nusse, R.3    Calos, M.P.4
  • 37
    • 33845698104 scopus 로고    scopus 로고
    • P[acman]: a BAC transgenic platform for targeted insertion of large DNA fragments in D. melanogaster
    • Venken KJ, He Y, Hoskins RA, Bellen HJ. P[acman]: a BAC transgenic platform for targeted insertion of large DNA fragments in D. melanogaster. Science 2006; 314: 1747-51.
    • (2006) Science , vol.314 , pp. 1747-1751
    • Venken, K.J.1    He, Y.2    Hoskins, R.A.3    Bellen, H.J.4
  • 39
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 1993; 118: 401-15.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 40
    • 78650541344 scopus 로고    scopus 로고
    • Participation of the p38 pathway in Drosophila host defense against pathogenic bacteria and fungi
    • Chen J, Xie C, Tian L, Hong L, Wu X, Han J. Participation of the p38 pathway in Drosophila host defense against pathogenic bacteria and fungi. Proc Natl Acad Sci U S A 2010; 107: 20774-9.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20774-20779
    • Chen, J.1    Xie, C.2    Tian, L.3    Hong, L.4    Wu, X.5    Han, J.6
  • 41
    • 48249108357 scopus 로고    scopus 로고
    • Drosophila melanogaster as a model host to dissect the immunopathogenesis of zygomycosis
    • Chamilos G, Lewis RE, Hu J, Xiao L, Zal T, Gilliet M, et al. Drosophila melanogaster as a model host to dissect the immunopathogenesis of zygomycosis. Proc Natl Acad Sci U S A 2008; 105: 9367-72.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9367-9372
    • Chamilos, G.1    Lewis, R.E.2    Hu, J.3    Xiao, L.4    Zal, T.5    Gilliet, M.6
  • 43
    • 78650587738 scopus 로고    scopus 로고
    • RNAi-mediated immunity provides strong protection against the negative-strand RNA vesicular stomatitis virus in Drosophila
    • Mueller S, Gausson V, Vodovar N, Deddouche S, Troxler L, Perot J, et al. RNAi-mediated immunity provides strong protection against the negative-strand RNA vesicular stomatitis virus in Drosophila. Proc Natl Acad Sci U S A 2010; 107: 19390-5.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19390-19395
    • Mueller, S.1    Gausson, V.2    Vodovar, N.3    Deddouche, S.4    Troxler, L.5    Perot, J.6
  • 44
    • 0032473360 scopus 로고    scopus 로고
    • A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway
    • Ferrandon D, Jung AC, Criqui M, Lemaitre B, Uttenweiler-Joseph S, Michaut L, et al. A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway. EMBO J 1998; 17: 1217-27.
    • (1998) EMBO J , vol.17 , pp. 1217-1227
    • Ferrandon, D.1    Jung, A.C.2    Criqui, M.3    Lemaitre, B.4    Uttenweiler-Joseph, S.5    Michaut, L.6
  • 45
    • 70350437304 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis infections in Drosophila melanogaster
    • Luce-Fedrow A, Von Ohlen T, Chapes SK. Ehrlichia chaffeensis infections in Drosophila melanogaster. Infect Immun 2009; 77: 4815-26.
    • (2009) Infect Immun , vol.77 , pp. 4815-4826
    • Luce-Fedrow, A.1    Von Ohlen, T.2    Chapes, S.K.3
  • 46
    • 19644366731 scopus 로고    scopus 로고
    • Suppression of Drosophila cellular immunity by directed expression of the ExoS toxin GAP domain of Pseudomonas aeruginosa
    • Avet-Rochex A, Bergeret E, Attree I, Meister M, Fauvarque MO. Suppression of Drosophila cellular immunity by directed expression of the ExoS toxin GAP domain of Pseudomonas aeruginosa. Cell Microbiol 2005; 7: 799-810.
    • (2005) Cell Microbiol , vol.7 , pp. 799-810
    • Avet-Rochex, A.1    Bergeret, E.2    Attree, I.3    Meister, M.4    Fauvarque, M.O.5
  • 47
    • 34447530305 scopus 로고    scopus 로고
    • A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila
    • Dietzl G, Chen D, Schnorrer F, Su KC, Barinova Y, Fellner M, et al. A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila. Nature 2007; 448: 151-6.
    • (2007) Nature , vol.448 , pp. 151-156
    • Dietzl, G.1    Chen, D.2    Schnorrer, F.3    Su, K.C.4    Barinova, Y.5    Fellner, M.6
  • 51
    • 67650831470 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies genes involved in intestinal pathogenic bacterial infection
    • Cronin SJ, Nehme NT, Limmer S, Liegeois S, Pospisilik JA, Schramek D, et al. Genome-wide RNAi screen identifies genes involved in intestinal pathogenic bacterial infection. Science 2009; 325: 340-3.
    • (2009) Science , vol.325 , pp. 340-343
    • Cronin, S.J.1    Nehme, N.T.2    Limmer, S.3    Liegeois, S.4    Pospisilik, J.A.5    Schramek, D.6
  • 52
    • 0035940514 scopus 로고    scopus 로고
    • Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays
    • De Gregorio E, Spellman PT, Rubin GM, Lemaitre B. Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. Proc Natl Acad Sci U S A 2001; 98: 12590-5.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12590-12595
    • De Gregorio, E.1    Spellman, P.T.2    Rubin, G.M.3    Lemaitre, B.4
  • 53
    • 0037013856 scopus 로고    scopus 로고
    • The Toll and Imd pathways are the major regulators of the immune response in Drosophila
    • De Gregorio E, Spellman PT, Tzou P, Rubin GM, Lemaitre B. The Toll and Imd pathways are the major regulators of the immune response in Drosophila. EMBO J 2002; 21: 2568-79.
    • (2002) EMBO J , vol.21 , pp. 2568-2579
    • De Gregorio, E.1    Spellman, P.T.2    Tzou, P.3    Rubin, G.M.4    Lemaitre, B.5
  • 55
    • 14044272776 scopus 로고    scopus 로고
    • New insights into Drosophila larval haemocyte functions through genome-wide analysis
    • Irving P, Ubeda JM, Doucet D, Troxler L, Lagueux M, Zachary D, et al. New insights into Drosophila larval haemocyte functions through genome-wide analysis. Cell Microbiol 2005; 7: 335-50.
    • (2005) Cell Microbiol , vol.7 , pp. 335-350
    • Irving, P.1    Ubeda, J.M.2    Doucet, D.3    Troxler, L.4    Lagueux, M.5    Zachary, D.6
  • 56
    • 0036848010 scopus 로고    scopus 로고
    • Sequential activation of signaling pathways during innate immune responses in Drosophila
    • Boutros M, Agaisse H, Perrimon N. Sequential activation of signaling pathways during innate immune responses in Drosophila. Dev Cell 2002; 3: 711-22.
    • (2002) Dev Cell , vol.3 , pp. 711-722
    • Boutros, M.1    Agaisse, H.2    Perrimon, N.3
  • 58
    • 77955256991 scopus 로고    scopus 로고
    • Molecular bases of proliferation of Francisella tularensis in arthropod vectors
    • Asare R, Akimana C, Jones S, Abu Kwaik Y. Molecular bases of proliferation of Francisella tularensis in arthropod vectors. Environ Microbiol 2010; 12: 2587-612.
    • (2010) Environ Microbiol , vol.12 , pp. 2587-2612
    • Asare, R.1    Akimana, C.2    Jones, S.3    Abu Kwaik, Y.4
  • 60
    • 0035370781 scopus 로고    scopus 로고
    • Of flies and men*studying human disease in Drosophila
    • Bernards A, Hariharan IK. Of flies and men*studying human disease in Drosophila. Curr Opin Genet Dev 2001; 11: 274-8.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 274-278
    • Bernards, A.1    Hariharan, I.K.2
  • 62
    • 0032212173 scopus 로고    scopus 로고
    • Hsp70 and larval thermotolerance in Drosophila melanogaster: how much is enough and when is more too much?
    • Krebs RA, Feder ME. Hsp70 and larval thermotolerance in Drosophila melanogaster: how much is enough and when is more too much? J Insect Physiol 1998; 44: 1091-101.
    • (1998) J Insect Physiol , vol.44 , pp. 1091-1101
    • Krebs, R.A.1    Feder, M.E.2
  • 63
    • 78650859583 scopus 로고    scopus 로고
    • Porphyromonas gingivalis virulence in a Drosophila melanogaster model
    • Igboin CO, Moeschberger ML, Griffen AL, Leys EJ. Porphyromonas gingivalis virulence in a Drosophila melanogaster model. Infect Immun 2011; 79: 439-48.
    • (2011) Infect Immun , vol.79 , pp. 439-448
    • Igboin, C.O.1    Moeschberger, M.L.2    Griffen, A.L.3    Leys, E.J.4
  • 64
    • 79958203035 scopus 로고    scopus 로고
    • Virulence on the fly: Drosophila melanogaster as a model genetic organism to decipher host-pathogen interactions
    • Limmer S, Quintin J, Hetru C, Ferrandon D. Virulence on the fly: Drosophila melanogaster as a model genetic organism to decipher host-pathogen interactions. Curr Drug Targets 2011; 12: 978-99.
    • (2011) Curr Drug Targets , vol.12 , pp. 978-999
    • Limmer, S.1    Quintin, J.2    Hetru, C.3    Ferrandon, D.4
  • 65
    • 79952757149 scopus 로고    scopus 로고
    • NFkappaB/Rel proteins and the humoral immune responses of Drosophila melanogaster
    • Ganesan S, Aggarwal K, Paquette N, Silverman N. NFkappaB/Rel proteins and the humoral immune responses of Drosophila melanogaster. Curr Top Microbiol Immunol 2011; 349: 25-60.
    • (2011) Curr Top Microbiol Immunol , vol.349 , pp. 25-60
    • Ganesan, S.1    Aggarwal, K.2    Paquette, N.3    Silverman, N.4
  • 66
    • 0034305744 scopus 로고    scopus 로고
    • The Drosophila caspase Dredd is required to resist gramnegative bacterial infection
    • Leulier F, Rodriguez A, Khush RS, Abrams JM, Lemaitre B. The Drosophila caspase Dredd is required to resist gramnegative bacterial infection. EMBO Rep 2000; 1: 353-8.
    • (2000) EMBO Rep , vol.1 , pp. 353-358
    • Leulier, F.1    Rodriguez, A.2    Khush, R.S.3    Abrams, J.M.4    Lemaitre, B.5
  • 68
    • 0035423794 scopus 로고    scopus 로고
    • Mutations in the Drosophila dTAK1 gene reveal a conserved function for MAPKKKs in the control of rel/NF-kappaBdependent innate immune responses
    • Vidal S, Khush RS, Leulier F, Tzou P, Nakamura M, Lemaitre B. Mutations in the Drosophila dTAK1 gene reveal a conserved function for MAPKKKs in the control of rel/NF-kappaBdependent innate immune responses. Genes Dev 2001; 15: 1900-12.
    • (2001) Genes Dev , vol.15 , pp. 1900-1912
    • Vidal, S.1    Khush, R.S.2    Leulier, F.3    Tzou, P.4    Nakamura, M.5    Lemaitre, B.6
  • 69
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gramnegative bacteria is mediated by a peptidoglycan recognition protein
    • Gottar M, Gobert V, Michel T, Belvin M, Duyk G, Hoffmann JA, et al. The Drosophila immune response against Gramnegative bacteria is mediated by a peptidoglycan recognition protein. Nature 2002; 416: 640-4.
    • (2002) Nature , vol.416 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3    Belvin, M.4    Duyk, G.5    Hoffmann, J.A.6
  • 70
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet M, Manfruelli P, Pearson A, Mathey-Prevot B, Ezekowitz RA. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 2002; 416: 644-8.
    • (2002) Nature , vol.416 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 71
    • 12844279852 scopus 로고    scopus 로고
    • Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor
    • Choe KM, Lee H, Anderson KV. Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor. Proc Natl Acad Sci U S A 2005; 102: 1122-6.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1122-1126
    • Choe, K.M.1    Lee, H.2    Anderson, K.V.3
  • 72
    • 0028865526 scopus 로고
    • A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense
    • Lemaitre B, Kromer-Metzger E, Michaut L, Nicolas E, Meister M, Georgel P, et al. A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense. Proc Natl Acad Sci U S A 1995; 92: 9465-9.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9465-9469
    • Lemaitre, B.1    Kromer-Metzger, E.2    Michaut, L.3    Nicolas, E.4    Meister, M.5    Georgel, P.6
  • 73
    • 18044400563 scopus 로고    scopus 로고
    • Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis
    • Georgel P, Naitza S, Kappler C, Ferrandon D, Zachary D, Swimmer C, et al. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis. Dev Cell 2001; 1: 503-14.
    • (2001) Dev Cell , vol.1 , pp. 503-514
    • Georgel, P.1    Naitza, S.2    Kappler, C.3    Ferrandon, D.4    Zachary, D.5    Swimmer, C.6
  • 74
    • 0034613376 scopus 로고    scopus 로고
    • dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD
    • Hu S, Yang X. dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD. J Biol Chem 2000; 275: 30761-4.
    • (2000) J Biol Chem , vol.275 , pp. 30761-30764
    • Hu, S.1    Yang, X.2
  • 75
    • 33750330952 scopus 로고    scopus 로고
    • The Drosophila inhibitor of apoptosis protein DIAP2 functions in innate immunity and is essential to resist gram-negative bacterial infection
    • Leulier F, Lhocine N, Lemaitre B, Meier P. The Drosophila inhibitor of apoptosis protein DIAP2 functions in innate immunity and is essential to resist gram-negative bacterial infection. Mol Cell Biol 2006; 26: 7821-31.
    • (2006) Mol Cell Biol , vol.26 , pp. 7821-7831
    • Leulier, F.1    Lhocine, N.2    Lemaitre, B.3    Meier, P.4
  • 77
    • 0033231556 scopus 로고    scopus 로고
    • Relish, a central factor in the control of humoral but not cellular immunity in Drosophila
    • Hedengren M, Asling B, Dushay MS, Ando I, Ekengren S, Wihlborg M, et al. Relish, a central factor in the control of humoral but not cellular immunity in Drosophila. Mol Cell 1999; 4: 827-37.
    • (1999) Mol Cell , vol.4 , pp. 827-837
    • Hedengren, M.1    Asling, B.2    Dushay, M.S.3    Ando, I.4    Ekengren, S.5    Wihlborg, M.6
  • 78
    • 0034287444 scopus 로고    scopus 로고
    • A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity
    • Silverman N, Zhou R, Stoven S, Pandey N, Hultmark D, Maniatis T. A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity. Genes Dev 2000; 14: 2461-71.
    • (2000) Genes Dev , vol.14 , pp. 2461-2471
    • Silverman, N.1    Zhou, R.2    Stoven, S.3    Pandey, N.4    Hultmark, D.5    Maniatis, T.6
  • 79
    • 0035187882 scopus 로고    scopus 로고
    • The antibacterial arm of the Drosophila innate immune response requires an IkappaB kinase
    • Lu Y, Wu LP, Anderson KV. The antibacterial arm of the Drosophila innate immune response requires an IkappaB kinase. Genes Dev 2001; 15: 104-10.
    • (2001) Genes Dev , vol.15 , pp. 104-110
    • Lu, Y.1    Wu, L.P.2    Anderson, K.V.3
  • 81
    • 67649858793 scopus 로고    scopus 로고
    • Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes
    • Erturk-Hasdemir D, Broemer M, Leulier F, Lane WS, Paquette N, Hwang D, et al. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Proc Natl Acad Sci U S A 2009; 106: 9779-84.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9779-9784
    • Erturk-Hasdemir, D.1    Broemer, M.2    Leulier, F.3    Lane, W.S.4    Paquette, N.5    Hwang, D.6
  • 82
    • 33645770760 scopus 로고    scopus 로고
    • Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2
    • Bischoff V, Vignal C, Duvic B, Boneca IG, Hoffmann JA, Royet J. Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2. PLoS Pathog 2006; 2: e14.
    • (2006) PLoS Pathog , vol.2
    • Bischoff, V.1    Vignal, C.2    Duvic, B.3    Boneca, I.G.4    Hoffmann, J.A.5    Royet, J.6
  • 83
    • 0037470091 scopus 로고    scopus 로고
    • A scavenger function for a Drosophila peptidoglycan recognition protein
    • Mellroth P, Karlsson J, Steiner H. A scavenger function for a Drosophila peptidoglycan recognition protein. J Biol Chem 2003; 278: 7059-64.
    • (2003) J Biol Chem , vol.278 , pp. 7059-7064
    • Mellroth, P.1    Karlsson, J.2    Steiner, H.3
  • 84
    • 33645994799 scopus 로고    scopus 로고
    • The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection
    • Zaidman-Remy A, Herve M, Poidevin M, Pili-Floury S, Kim MS, Blanot D, et al. The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection. Immunity 2006; 24: 463-73.
    • (2006) Immunity , vol.24 , pp. 463-473
    • Zaidman-Remy, A.1    Herve, M.2    Poidevin, M.3    Pili-Floury, S.4    Kim, M.S.5    Blanot, D.6
  • 85
    • 43049157518 scopus 로고    scopus 로고
    • The Drosophila peptidoglycan recognition protein PGRP-LF blocks PGRP-LC and IMD/JNK pathway activation
    • Maillet F, Bischoff V, Vignal C, Hoffmann J, Royet J. The Drosophila peptidoglycan recognition protein PGRP-LF blocks PGRP-LC and IMD/JNK pathway activation. Cell Host Microbe 2008; 3: 293-303.
    • (2008) Cell Host Microbe , vol.3 , pp. 293-303
    • Maillet, F.1    Bischoff, V.2    Vignal, C.3    Hoffmann, J.4    Royet, J.5
  • 86
    • 53849093383 scopus 로고    scopus 로고
    • Dnr1-dependent regulation of the Drosophila immune deficiency signaling pathway
    • Guntermann S, Primrose DA, Foley E. Dnr1-dependent regulation of the Drosophila immune deficiency signaling pathway. Dev Comp Immunol 2009; 33: 127-34.
    • (2009) Dev Comp Immunol , vol.33 , pp. 127-134
    • Guntermann, S.1    Primrose, D.A.2    Foley, E.3
  • 87
  • 90
    • 48649085941 scopus 로고    scopus 로고
    • PIMS modulates immune tolerance by negatively regulating Drosophila innate immune signaling
    • Lhocine N, Ribeiro PS, Buchon N, Wepf A, Wilson R, Tenev T, et al. PIMS modulates immune tolerance by negatively regulating Drosophila innate immune signaling. Cell Host Microbe 2008; 4: 147-58.
    • (2008) Cell Host Microbe , vol.4 , pp. 147-158
    • Lhocine, N.1    Ribeiro, P.S.2    Buchon, N.3    Wepf, A.4    Wilson, R.5    Tenev, T.6
  • 91
    • 79952761364 scopus 로고    scopus 로고
    • Drosophila Ras/MAPK signalling regulates innate immune responses in immune and intestinal stem cells
    • Ragab A, Buechling T, Gesellchen V, Spirohn K, Boettcher AL, Boutros M. Drosophila Ras/MAPK signalling regulates innate immune responses in immune and intestinal stem cells. EMBO J 2011; 30: 1123-36.
    • (2011) EMBO J , vol.30 , pp. 1123-1136
    • Ragab, A.1    Buechling, T.2    Gesellchen, V.3    Spirohn, K.4    Boettcher, A.L.5    Boutros, M.6
  • 92
    • 0037108474 scopus 로고    scopus 로고
    • A ubiquitinproteasome pathway represses the Drosophila immune deficiency signaling cascade
    • Khush RS, Cornwell WD, Uram JN, Lemaitre B. A ubiquitinproteasome pathway represses the Drosophila immune deficiency signaling cascade. Curr Biol 2002; 12: 1728-37.
    • (2002) Curr Biol , vol.12 , pp. 1728-1737
    • Khush, R.S.1    Cornwell, W.D.2    Uram, J.N.3    Lemaitre, B.4
  • 93
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette Spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette Spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996; 86: 973-83.
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 94
    • 0033711445 scopus 로고    scopus 로고
    • The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila
    • Rutschmann S, Jung AC, Hetru C, Reichhart JM, Hoffmann JA, Ferrandon D. The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila. Immunity 2000; 12: 569-80.
    • (2000) Immunity , vol.12 , pp. 569-580
    • Rutschmann, S.1    Jung, A.C.2    Hetru, C.3    Reichhart, J.M.4    Hoffmann, J.A.5    Ferrandon, D.6
  • 95
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • Michel T, Reichhart JM, Hoffmann JA, Royet J. Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature 2001; 414: 756-9.
    • (2001) Nature , vol.414 , pp. 756-759
    • Michel, T.1    Reichhart, J.M.2    Hoffmann, J.A.3    Royet, J.4
  • 96
    • 0036141954 scopus 로고    scopus 로고
    • Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections
    • Tauszig-Delamasure S, Bilak H, Capovilla M, Hoffmann JA, Imler JL. Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections. Nat Immunol 2002; 3: 91-7.
    • (2002) Nat Immunol , vol.3 , pp. 91-97
    • Tauszig-Delamasure, S.1    Bilak, H.2    Capovilla, M.3    Hoffmann, J.A.4    Imler, J.L.5
  • 97
    • 0037083557 scopus 로고    scopus 로고
    • Cutting edge: the toll pathway is required for resistance to gram-positive bacterial infections in Drosophila
    • Rutschmann S, Kilinc A, Ferrandon D. Cutting edge: the toll pathway is required for resistance to gram-positive bacterial infections in Drosophila. J Immunol 2002; 168: 1542-6.
    • (2002) J Immunol , vol.168 , pp. 1542-1546
    • Rutschmann, S.1    Kilinc, A.2    Ferrandon, D.3
  • 98
    • 0345731463 scopus 로고    scopus 로고
    • Dual activation of the Drosophila toll pathway by two pattern recognition receptors
    • Gobert V, Gottar M, Matskevich AA, Rutschmann S, Royet J, Belvin M, et al. Dual activation of the Drosophila toll pathway by two pattern recognition receptors. Science 2003; 302: 2126-30.
    • (2003) Science , vol.302 , pp. 2126-2130
    • Gobert, V.1    Gottar, M.2    Matskevich, A.A.3    Rutschmann, S.4    Royet, J.5    Belvin, M.6
  • 99
    • 33750218690 scopus 로고    scopus 로고
    • Sensing of Gram-positive bacteria in Drosophila: GNBP1 is needed to process and present peptidoglycan to PGRP-SA
    • Wang L, Weber AN, Atilano ML, Filipe SR, Gay NJ, Ligoxygakis P. Sensing of Gram-positive bacteria in Drosophila: GNBP1 is needed to process and present peptidoglycan to PGRP-SA. EMBO J 2006; 25: 5005-14.
    • (2006) EMBO J , vol.25 , pp. 5005-5014
    • Wang, L.1    Weber, A.N.2    Atilano, M.L.3    Filipe, S.R.4    Gay, N.J.5    Ligoxygakis, P.6
  • 100
    • 9244251126 scopus 로고    scopus 로고
    • Function of the Drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria
    • Bischoff V, Vignal C, Boneca IG, Michel T, Hoffmann JA, Royet J. Function of the Drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria. Nat Immunol 2004; 5: 1175-80.
    • (2004) Nat Immunol , vol.5 , pp. 1175-1180
    • Bischoff, V.1    Vignal, C.2    Boneca, I.G.3    Michel, T.4    Hoffmann, J.A.5    Royet, J.6
  • 101
    • 0037025213 scopus 로고    scopus 로고
    • Activation of Drosophila Toll during fungal infection by a blood serine protease
    • Ligoxygakis P, Pelte N, Hoffmann JA, Reichhart JM. Activation of Drosophila Toll during fungal infection by a blood serine protease. Science 2002; 297: 114-6.
    • (2002) Science , vol.297 , pp. 114-116
    • Ligoxygakis, P.1    Pelte, N.2    Hoffmann, J.A.3    Reichhart, J.M.4
  • 102
    • 0034693324 scopus 로고    scopus 로고
    • Gram-negative bacteria-binding protein, a pattern recognition receptor for lipopolysaccharide and beta-1 3-glucan that mediates the signaling for the induction of innate immune genes in Drosophila melanogaster cells
    • Kim YS, Ryu JH, Han SJ, Choi KH, Nam KB, Jang IH, et al. Gram-negative bacteria-binding protein, a pattern recognition receptor for lipopolysaccharide and beta-1,3-glucan that mediates the signaling for the induction of innate immune genes in Drosophila melanogaster cells. J Biol Chem 2000; 275: 32721-7.
    • (2000) J Biol Chem , vol.275 , pp. 32721-32727
    • Kim, Y.S.1    Ryu, J.H.2    Han, S.J.3    Choi, K.H.4    Nam, K.B.5    Jang, I.H.6
  • 103
    • 33845666959 scopus 로고    scopus 로고
    • Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors
    • Gottar M, Gobert V, Matskevich AA, Reichhart JM, Wang C, Butt TM, et al. Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors. Cell 2006; 127: 1425-37.
    • (2006) Cell , vol.127 , pp. 1425-1437
    • Gottar, M.1    Gobert, V.2    Matskevich, A.A.3    Reichhart, J.M.4    Wang, C.5    Butt, T.M.6
  • 104
    • 52549093726 scopus 로고    scopus 로고
    • Sensing of danger signals and pathogen-associated molecular patterns defines binary signaling pathways upstream of Toll
    • El Chamy L, Leclerc V, Caldelari I, Reichhart JM. Sensing of danger signals and pathogen-associated molecular patterns defines binary signaling pathways upstream of Toll. Nat Immunol 2008; 9: 1165-70.
    • (2008) Nat Immunol , vol.9 , pp. 1165-1170
    • El Chamy, L.1    Leclerc, V.2    Caldelari, I.3    Reichhart, J.M.4
  • 105
    • 33646037067 scopus 로고    scopus 로고
    • Drosophila immunity: a large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation
    • Kambris Z, Brun S, Jang IH, Nam HJ, Romeo Y, Takahashi K, et al. Drosophila immunity: a large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation. Curr Biol 2006; 16: 808-13.
    • (2006) Curr Biol , vol.16 , pp. 808-813
    • Kambris, Z.1    Brun, S.2    Jang, I.H.3    Nam, H.J.4    Romeo, Y.5    Takahashi, K.6
  • 106
    • 29744438644 scopus 로고    scopus 로고
    • A Spatzle-processing enzyme required for toll signaling activation in Drosophila innate immunity
    • Jang IH, Chosa N, Kim SH, Nam HJ, Lemaitre B, Ochiai M, et al. A Spatzle-processing enzyme required for toll signaling activation in Drosophila innate immunity. Dev Cell 2006; 10: 45-55.
    • (2006) Dev Cell , vol.10 , pp. 45-55
    • Jang, I.H.1    Chosa, N.2    Kim, S.H.3    Nam, H.J.4    Lemaitre, B.5    Ochiai, M.6
  • 108
    • 0027368433 scopus 로고
    • Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila
    • Reichhart JM, Georgel P, Meister M, Lemaitre B, Kappler C, Hoffmann JA. Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila. C R Acad Sci III 1993; 316: 1218-24.
    • (1993) C R Acad Sci III , vol.316 , pp. 1218-1224
    • Reichhart, J.M.1    Georgel, P.2    Meister, M.3    Lemaitre, B.4    Kappler, C.5    Hoffmann, J.A.6
  • 109
    • 0027443688 scopus 로고
    • Dif, a dorsal-related gene that mediates an immune response in Drosophila
    • Ip YT, Reach M, Engstrom Y, Kadalayil L, Cai H, Gonzalez-Crespo S, et al. Dif, a dorsal-related gene that mediates an immune response in Drosophila. Cell 1993; 75: 753-63.
    • (1993) Cell , vol.75 , pp. 753-763
    • Ip, Y.T.1    Reach, M.2    Engstrom, Y.3    Kadalayil, L.4    Cai, H.5    Gonzalez-Crespo, S.6
  • 110
    • 0028877993 scopus 로고
    • Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila
    • Lemaitre B, Meister M, Govind S, Georgel P, Steward R, Reichhart JM, et al. Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila. EMBO J 1995; 14: 536-45.
    • (1995) EMBO J , vol.14 , pp. 536-545
    • Lemaitre, B.1    Meister, M.2    Govind, S.3    Georgel, P.4    Steward, R.5    Reichhart, J.M.6
  • 111
    • 0032485392 scopus 로고    scopus 로고
    • Regulated nuclear import of Rel proteins in the Drosophila immune response
    • Wu LP, Anderson KV. Regulated nuclear import of Rel proteins in the Drosophila immune response. Nature 1998; 392: 93-7.
    • (1998) Nature , vol.392 , pp. 93-97
    • Wu, L.P.1    Anderson, K.V.2
  • 112
    • 0033564614 scopus 로고    scopus 로고
    • A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF
    • Manfruelli P, Reichhart JM, Steward R, Hoffmann JA, Lemaitre B. A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF. EMBO J 1999; 18: 3380-91.
    • (1999) EMBO J , vol.18 , pp. 3380-3391
    • Manfruelli, P.1    Reichhart, J.M.2    Steward, R.3    Hoffmann, J.A.4    Lemaitre, B.5
  • 113
    • 0033118490 scopus 로고    scopus 로고
    • Toll receptor-mediated Drosophila immune response requires Dif, an NF-kappaB factor
    • Meng X, Khanuja BS, Ip YT. Toll receptor-mediated Drosophila immune response requires Dif, an NF-kappaB factor. Genes Dev 1999; 13: 792-7.
    • (1999) Genes Dev , vol.13 , pp. 792-797
    • Meng, X.1    Khanuja, B.S.2    Ip, Y.T.3
  • 114
    • 77953449985 scopus 로고    scopus 로고
    • A large-scale RNAi screen identifies Deaf1 as a regulator of innate immune responses in Drosophila
    • Kuttenkeuler D, Pelte N, Ragab A, Gesellchen V, Schneider L, Blass C, et al. A large-scale RNAi screen identifies Deaf1 as a regulator of innate immune responses in Drosophila. J Innate Immun 2010; 2: 181-94.
    • (2010) J Innate Immun , vol.2 , pp. 181-194
    • Kuttenkeuler, D.1    Pelte, N.2    Ragab, A.3    Gesellchen, V.4    Schneider, L.5    Blass, C.6
  • 115
    • 0032562285 scopus 로고    scopus 로고
    • In vivo regulation of the IkappaB homologue cactus during the immune response of Drosophila
    • Nicolas E, Reichhart JM, Hoffmann JA, Lemaitre B. In vivo regulation of the IkappaB homologue cactus during the immune response of Drosophila. J Biol Chem 1998; 273: 10463-9.
    • (1998) J Biol Chem , vol.273 , pp. 10463-10469
    • Nicolas, E.1    Reichhart, J.M.2    Hoffmann, J.A.3    Lemaitre, B.4
  • 116
    • 26944485185 scopus 로고    scopus 로고
    • WntD is a feedback inhibitor of Dorsal/NF-kappaB in Drosophila development and immunity
    • Gordon MD, Dionne MS, Schneider DS, Nusse R. WntD is a feedback inhibitor of Dorsal/NF-kappaB in Drosophila development and immunity. Nature 2005; 437: 746-9.
    • (2005) Nature , vol.437 , pp. 746-749
    • Gordon, M.D.1    Dionne, M.S.2    Schneider, D.S.3    Nusse, R.4
  • 117
    • 28244454824 scopus 로고    scopus 로고
    • Govind S. dUbc9 negatively regulates the Toll-NF-kappa B pathways in larval hematopoiesis and drosomycin activation in Drosophila
    • Chiu H, Ring BC, Sorrentino RP, Kalamarz M, Garza D, Govind S. dUbc9 negatively regulates the Toll-NF-kappa B pathways in larval hematopoiesis and drosomycin activation in Drosophila. Dev Biol 2005; 288: 60-72.
    • (2005) Dev Biol , vol.288 , pp. 60-72
    • Chiu, H.1    Ring, B.C.2    Sorrentino, R.P.3    Kalamarz, M.4    Garza, D.5
  • 119
    • 34250221179 scopus 로고    scopus 로고
    • Toll and IMD pathways synergistically activate an innate immune response in Drosophila melanogaster
    • Tanji T, Hu X, Weber AN, Ip YT. Toll and IMD pathways synergistically activate an innate immune response in Drosophila melanogaster. Mol Cell Biol 2007; 27: 4578-88.
    • (2007) Mol Cell Biol , vol.27 , pp. 4578-4588
    • Tanji, T.1    Hu, X.2    Weber, A.N.3    Ip, Y.T.4
  • 120
    • 77957078396 scopus 로고    scopus 로고
    • Heterodimers of NF-kappaB transcription factors DIF and Relish regulate antimicrobial peptide genes in Drosophila
    • Tanji T, Yun EY, Ip YT. Heterodimers of NF-kappaB transcription factors DIF and Relish regulate antimicrobial peptide genes in Drosophila. Proc Natl Acad Sci U S A 2010; 107: 14715-20.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14715-14720
    • Tanji, T.1    Yun, E.Y.2    Ip, Y.T.3
  • 121
    • 73349134037 scopus 로고    scopus 로고
    • Identification of lipoteichoic acid as a ligand for draper in the phagocytosis of Staphylococcus aureus by Drosophila hemocytes
    • Hashimoto Y, Tabuchi Y, Sakurai K, Kutsuna M, Kurokawa K, Awasaki T, et al. Identification of lipoteichoic acid as a ligand for draper in the phagocytosis of Staphylococcus aureus by Drosophila hemocytes. J Immunol 2009; 183: 7451-60.
    • (2009) J Immunol , vol.183 , pp. 7451-7460
    • Hashimoto, Y.1    Tabuchi, Y.2    Sakurai, K.3    Kutsuna, M.4    Kurokawa, K.5    Awasaki, T.6
  • 122
    • 0037972466 scopus 로고    scopus 로고
    • The Drosophila melanogaster toll pathway participates in resistance to infection by the gramnegative human pathogen Pseudomonas aeruginosa
    • Lau GW, Goumnerov BC, Walendziewicz CL, Hewitson J, XiaoW, Mahajan-Miklos S, et al. The Drosophila melanogaster toll pathway participates in resistance to infection by the gramnegative human pathogen Pseudomonas aeruginosa. Infect Immun 2003; 71: 4059-66.
    • (2003) Infect Immun , vol.71 , pp. 4059-4066
    • Lau, G.W.1    Goumnerov, B.C.2    Walendziewicz, C.L.3    Hewitson, J.4    Xiao, W.5    Mahajan-Miklos, S.6
  • 124
    • 0025190557 scopus 로고
    • The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection
    • Kylsten P, Samakovlis C, Hultmark D. The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection. EMBO J 1990; 9: 217-24.
    • (1990) EMBO J , vol.9 , pp. 217-224
    • Kylsten, P.1    Samakovlis, C.2    Hultmark, D.3
  • 125
    • 0028208333 scopus 로고
    • Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin A study in insect immunity
    • Dimarcq JL, Hoffmann D, Meister M, Bulet P, Lanot R, Reichhart JM, et al. Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity. Eur J Biochem 1994; 221: 201-9.
    • (1994) Eur J Biochem , vol.221 , pp. 201-209
    • Dimarcq, J.L.1    Hoffmann, D.2    Meister, M.3    Bulet, P.4    Lanot, R.5    Reichhart, J.M.6
  • 126
    • 0018820115 scopus 로고
    • Insect immunity Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark D, Steiner H, Rasmuson T, Boman HG. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur J Biochem 1980; 106: 7-16.
    • (1980) Eur J Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 127
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus
    • Cociancich S, Ghazi A, Hetru C, Hoffmann JA, Letellier L. Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J Biol Chem 1993; 268: 19239-45.
    • (1993) J Biol Chem , vol.268 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 128
    • 0025642716 scopus 로고
    • Insect immunity Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides
    • Wicker C, Reichhart JM, Hoffmann D, Hultmark D, Samakovlis C, Hoffmann JA. Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides. J Biol Chem 1990; 265: 22493-8.
    • (1990) J Biol Chem , vol.265 , pp. 22493-22498
    • Wicker, C.1    Reichhart, J.M.2    Hoffmann, D.3    Hultmark, D.4    Samakovlis, C.5    Hoffmann, J.A.6
  • 129
    • 0028587829 scopus 로고
    • Insect immunity Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides
    • Fehlbaum P, Bulet P, Michaut L, Lagueux M, Broekaert WF, Hetru C, et al. Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. J Biol Chem 1994; 269: 33159-63.
    • (1994) J Biol Chem , vol.269 , pp. 33159-33163
    • Fehlbaum, P.1    Bulet, P.2    Michaut, L.3    Lagueux, M.4    Broekaert, W.F.5    Hetru, C.6
  • 130
    • 70349206320 scopus 로고    scopus 로고
    • Drosomycin, an essential component of antifungal defence in Drosophila
    • Zhang ZT, Zhu SY. Drosomycin, an essential component of antifungal defence in Drosophila. Insect Mol Biol 2009; 18: 549-56.
    • (2009) Insect Mol Biol , vol.18 , pp. 549-556
    • Zhang, Z.T.1    Zhu, S.Y.2
  • 131
    • 84990406394 scopus 로고
    • Mode of action of diptericin A, a bactericidal peptide induced in the hemolymph of Phormia terranovae larvae
    • Keppi E, Pugsley P, Lambert J, Wicker C, Dimarcq JL, Hoffmann J, et al. Mode of action of diptericin A, a bactericidal peptide induced in the hemolymph of Phormia terranovae larvae. Arch Insect Biochem Physiol 1989; 10: 229-39.
    • (1989) Arch Insect Biochem Physiol , vol.10 , pp. 229-239
    • Keppi, E.1    Pugsley, P.2    Lambert, J.3    Wicker, C.4    Dimarcq, J.L.5    Hoffmann, J.6
  • 132
    • 49449099707 scopus 로고    scopus 로고
    • Gene expression, antiparasitic activity, and functional evolution of the drosomycin family
    • Tian C, Gao B, Rodriguez Mdel C, Lanz-Mendoza H, Ma B, Zhu S. Gene expression, antiparasitic activity, and functional evolution of the drosomycin family. Mol Immunol 2008; 45: 3909-16.
    • (2008) Mol Immunol , vol.45 , pp. 3909-3916
    • Tian, C.1    Gao, B.2    Rodriguez Mdel, C.3    Lanz-Mendoza, H.4    Ma, B.5    Zhu, S.6
  • 133
    • 0029278804 scopus 로고
    • Identification of early genes in the Drosophila immune response by PCR-based differential display: the Attacin A gene and the evolution of attacin-like proteins
    • Asling B, Dushay MS, Hultmark D. Identification of early genes in the Drosophila immune response by PCR-based differential display: the Attacin A gene and the evolution of attacin-like proteins. Insect Biochem Mol Biol 1995; 25: 511-8.
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 511-518
    • Asling, B.1    Dushay, M.S.2    Hultmark, D.3
  • 134
    • 0027201086 scopus 로고
    • A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution
    • Bulet P, Dimarcq JL, Hetru C, Lagueux M, Charlet M, Hegy G, et al. A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J Biol Chem 1993; 268: 14893-7.
    • (1993) J Biol Chem , vol.268 , pp. 14893-14897
    • Bulet, P.1    Dimarcq, J.L.2    Hetru, C.3    Lagueux, M.4    Charlet, M.5    Hegy, G.6
  • 136
    • 0028884812 scopus 로고
    • Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties
    • Levashina EA, Ohresser S, Bulet P, Reichhart JM, Hetru C, Hoffmann JA. Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties. Eur J Biochem 1995; 233: 694-700.
    • (1995) Eur J Biochem , vol.233 , pp. 694-700
    • Levashina, E.A.1    Ohresser, S.2    Bulet, P.3    Reichhart, J.M.4    Hetru, C.5    Hoffmann, J.A.6
  • 137
    • 45549104911 scopus 로고    scopus 로고
    • Drosophila immunity: methods for monitoring the activity of Toll and Imd signaling pathways
    • Romeo Y, Lemaitre B. Drosophila immunity: methods for monitoring the activity of Toll and Imd signaling pathways. Methods Mol Biol 2008; 415: 379-94.
    • (2008) Methods Mol Biol , vol.415 , pp. 379-394
    • Romeo, Y.1    Lemaitre, B.2
  • 138
    • 0032532120 scopus 로고    scopus 로고
    • Drosophila unpaired encodes a secreted protein that activates the JAK signaling pathway
    • Harrison DA, McCoon PE, Binari R, Gilman M, Perrimon N. Drosophila unpaired encodes a secreted protein that activates the JAK signaling pathway. Genes Dev 1998; 12: 3252-63.
    • (1998) Genes Dev , vol.12 , pp. 3252-3263
    • Harrison, D.A.1    McCoon, P.E.2    Binari, R.3    Gilman, M.4    Perrimon, N.5
  • 139
    • 0042697323 scopus 로고    scopus 로고
    • Signaling role of hemocytes in Drosophila JAK/STAT-dependent response to septic injury
    • Agaisse H, Petersen UM, Boutros M, Mathey-Prevot B, Perrimon N. Signaling role of hemocytes in Drosophila JAK/STAT-dependent response to septic injury. Dev Cell 2003; 5: 441-50.
    • (2003) Dev Cell , vol.5 , pp. 441-450
    • Agaisse, H.1    Petersen, U.M.2    Boutros, M.3    Mathey-Prevot, B.4    Perrimon, N.5
  • 140
    • 0035975940 scopus 로고    scopus 로고
    • Identification of the first invertebrate interleukin JAK/STAT receptor, the Drosophila gene domeless
    • Brown S, Hu N, Hombria JC. Identification of the first invertebrate interleukin JAK/STAT receptor, the Drosophila gene domeless. Curr Biol 2001; 11: 1700-5.
    • (2001) Curr Biol , vol.11 , pp. 1700-1705
    • Brown, S.1    Hu, N.2    Hombria, J.C.3
  • 141
    • 0036468052 scopus 로고    scopus 로고
    • mom identifies a receptor for the Drosophila JAK/STAT signal transduction pathway and encodes a protein distantly related to the mammalian cytokine receptor family
    • Chen HW, Chen X, Oh SW, Marinissen MJ, Gutkind JS, Hou SX. mom identifies a receptor for the Drosophila JAK/STAT signal transduction pathway and encodes a protein distantly related to the mammalian cytokine receptor family. Genes Dev 2002; 16: 388-98.
    • (2002) Genes Dev , vol.16 , pp. 388-398
    • Chen, H.W.1    Chen, X.2    Oh, S.W.3    Marinissen, M.J.4    Gutkind, J.S.5    Hou, S.X.6
  • 142
    • 1642463842 scopus 로고    scopus 로고
    • The roles of JAK/STAT signaling in Drosophila immune responses
    • Agaisse H, Perrimon N. The roles of JAK/STAT signaling in Drosophila immune responses. Immunol Rev 2004; 198: 72-82.
    • (2004) Immunol Rev , vol.198 , pp. 72-82
    • Agaisse, H.1    Perrimon, N.2
  • 143
    • 33746826011 scopus 로고    scopus 로고
    • JAK/STAT signalling in Drosophila: insights into conserved regulatory and cellular functions
    • Arbouzova NI, Zeidler MP. JAK/STAT signalling in Drosophila: insights into conserved regulatory and cellular functions. Development 2006; 133: 2605-16.
    • (2006) Development , vol.133 , pp. 2605-2616
    • Arbouzova, N.I.1    Zeidler, M.P.2
  • 144
    • 33645135075 scopus 로고    scopus 로고
    • The MAPKKK Mekk1 regulates the expression of Turandot stress genes in response to septic injury in Drosophila
    • Brun S, Vidal S, Spellman P, Takahashi K, Tricoire H, Lemaitre B. The MAPKKK Mekk1 regulates the expression of Turandot stress genes in response to septic injury in Drosophila. Genes Cells 2006; 11: 397-407.
    • (2006) Genes Cells , vol.11 , pp. 397-407
    • Brun, S.1    Vidal, S.2    Spellman, P.3    Takahashi, K.4    Tricoire, H.5    Lemaitre, B.6
  • 145
    • 0034817068 scopus 로고    scopus 로고
    • A family of Turandot-related genes in the humoral stress response of Drosophila
    • Ekengren S, Hultmark D. A family of Turandot-related genes in the humoral stress response of Drosophila. Biochem Biophys Res Commun 2001; 284: 998-1003.
    • (2001) Biochem Biophys Res Commun , vol.284 , pp. 998-1003
    • Ekengren, S.1    Hultmark, D.2
  • 146
    • 77950455135 scopus 로고    scopus 로고
    • JAK-STAT is restrained by Notch to control cell proliferation of the Drosophila intestinal stem cells
    • Liu W, Singh SR, Hou SX. JAK-STAT is restrained by Notch to control cell proliferation of the Drosophila intestinal stem cells. J Cell Biochem 2010; 109: 992-9.
    • (2010) J Cell Biochem , vol.109 , pp. 992-999
    • Liu, W.1    Singh, S.R.2    Hou, S.X.3
  • 148
    • 0036768114 scopus 로고    scopus 로고
    • Cloning and expression of Drosophila SOCS36E and its potential regulation by the JAK/STAT pathway
    • Karsten P, Hader S, Zeidler MP. Cloning and expression of Drosophila SOCS36E and its potential regulation by the JAK/STAT pathway. Mech Dev 2002; 117: 343-6.
    • (2002) Mech Dev , vol.117 , pp. 343-346
    • Karsten, P.1    Hader, S.2    Zeidler, M.P.3
  • 149
    • 0037130445 scopus 로고    scopus 로고
    • SOCS36E, a novel Drosophila SOCS protein, suppresses JAK/STAT and EGF-R signalling in the imaginal wing disc
    • Callus BA, Mathey-Prevot B. SOCS36E, a novel Drosophila SOCS protein, suppresses JAK/STAT and EGF-R signalling in the imaginal wing disc. Oncogene 2002; 21: 4812-21.
    • (2002) Oncogene , vol.21 , pp. 4812-4821
    • Callus, B.A.1    Mathey-Prevot, B.2
  • 150
    • 0037106184 scopus 로고    scopus 로고
    • Negative regulation of STAT92E by an N-terminally truncated STAT protein derived from an alternative promoter site
    • Henriksen MA, Betz A, Fuccillo MV, Darnell JE Jr. Negative regulation of STAT92E by an N-terminally truncated STAT protein derived from an alternative promoter site. Genes Dev 2002; 16: 2379-89.
    • (2002) Genes Dev , vol.16 , pp. 2379-2389
    • Henriksen, M.A.1    Betz, A.2    Fuccillo, M.V.3    Darnell Jr., J.E.4
  • 152
    • 77954852349 scopus 로고    scopus 로고
    • A short receptor downregulates JAK/STAT signalling to control the Drosophila cellular immune response
    • e1000441
    • Makki R, Meister M, Pennetier D, Ubeda JM, Braun A, Daburon V, et al. A short receptor downregulates JAK/STAT signalling to control the Drosophila cellular immune response. PLoS Biol 2010; 8: e1000441.
    • (2010) PLoS Biol , vol.8
    • Makki, R.1    Meister, M.2    Pennetier, D.3    Ubeda, J.M.4    Braun, A.5    Daburon, V.6
  • 153
    • 23944468103 scopus 로고    scopus 로고
    • Genome-wide RNAi analysis of JAK/STAT signaling components in Drosophila
    • Baeg GH, Zhou R, Perrimon N. Genome-wide RNAi analysis of JAK/STAT signaling components in Drosophila. Genes Dev 2005; 19: 1861-70.
    • (2005) Genes Dev , vol.19 , pp. 1861-1870
    • Baeg, G.H.1    Zhou, R.2    Perrimon, N.3
  • 154
    • 23844483215 scopus 로고    scopus 로고
    • Identification of JAK/STAT signalling components by genome-wide RNA interference
    • Muller P, Kuttenkeuler D, Gesellchen V, Zeidler MP, Boutros M. Identification of JAK/STAT signalling components by genome-wide RNA interference. Nature 2005; 436: 871-5.
    • (2005) Nature , vol.436 , pp. 871-875
    • Muller, P.1    Kuttenkeuler, D.2    Gesellchen, V.3    Zeidler, M.P.4    Boutros, M.5
  • 155
    • 0345730824 scopus 로고    scopus 로고
    • A sensitized genetic screen to identify novel regulators and components of the Drosophila janus kinase/signal transducer and activator of transcription pathway
    • Bach EA, Vincent S, Zeidler MP, Perrimon N. A sensitized genetic screen to identify novel regulators and components of the Drosophila janus kinase/signal transducer and activator of transcription pathway. Genetics 2003; 165: 1149-66.
    • (2003) Genetics , vol.165 , pp. 1149-1166
    • Bach, E.A.1    Vincent, S.2    Zeidler, M.P.3    Perrimon, N.4
  • 156
    • 70349663498 scopus 로고    scopus 로고
    • A novel system for the launch of alphavirus RNA synthesis reveals a role for the Imd pathway in arthropod antiviral response
    • e1000582
    • Avadhanula V, Weasner BP, Hardy GG, Kumar JP, Hardy RW. A novel system for the launch of alphavirus RNA synthesis reveals a role for the Imd pathway in arthropod antiviral response. PLoS Pathog 2009; 5: e1000582.
    • (2009) PLoS Pathog , vol.5
    • Avadhanula, V.1    Weasner, B.P.2    Hardy, G.G.3    Kumar, J.P.4    Hardy, R.W.5
  • 157
    • 70449382807 scopus 로고    scopus 로고
    • The Imd pathway is involved in antiviral immune responses in Drosophila
    • Costa A, Jan E, Sarnow P, Schneider D. The Imd pathway is involved in antiviral immune responses in Drosophila. PLoS One 2009; 4: e7436.
    • (2009) PLoS One , vol.4
    • Costa, A.1    Jan, E.2    Sarnow, P.3    Schneider, D.4
  • 159
    • 24944485547 scopus 로고    scopus 로고
    • The Jak-STAT signaling pathway is required but not sufficient for the antiviral response of Drosophila
    • Dostert C, Jouanguy E, Irving P, Troxler L, Galiana-Arnoux D, Hetru C, et al. The Jak-STAT signaling pathway is required but not sufficient for the antiviral response of Drosophila. Nat Immunol 2005; 6: 946-53.
    • (2005) Nat Immunol , vol.6 , pp. 946-953
    • Dostert, C.1    Jouanguy, E.2    Irving, P.3    Troxler, L.4    Galiana-Arnoux, D.5    Hetru, C.6
  • 160
    • 0035865050 scopus 로고    scopus 로고
    • Postembryonic hematopoiesis in Drosophila
    • Lanot R, Zachary D, Holder F, Meister M. Postembryonic hematopoiesis in Drosophila. Dev Biol 2001; 230: 243-57.
    • (2001) Dev Biol , vol.230 , pp. 243-257
    • Lanot, R.1    Zachary, D.2    Holder, F.3    Meister, M.4
  • 161
    • 26844466658 scopus 로고    scopus 로고
    • Eater, a transmembrane protein mediating phagocytosis of bacterial pathogens in Drosophila
    • Kocks C, Cho JH, Nehme N, Ulvila J, Pearson AM, Meister M, et al. Eater, a transmembrane protein mediating phagocytosis of bacterial pathogens in Drosophila. Cell 2005; 123: 335-46.
    • (2005) Cell , vol.123 , pp. 335-346
    • Kocks, C.1    Cho, J.H.2    Nehme, N.3    Ulvila, J.4    Pearson, A.M.5    Meister, M.6
  • 163
    • 0035690765 scopus 로고    scopus 로고
    • Drosophila scavenger receptor CI is a pattern recognition receptor for bacteria
    • Ramet M, Pearson A, Manfruelli P, Li X, Koziel H, Gobel V, et al. Drosophila scavenger receptor CI is a pattern recognition receptor for bacteria. Immunity 2001; 15: 1027-38.
    • (2001) Immunity , vol.15 , pp. 1027-1038
    • Ramet, M.1    Pearson, A.2    Manfruelli, P.3    Li, X.4    Koziel, H.5    Gobel, V.6
  • 164
  • 165
    • 23844531867 scopus 로고    scopus 로고
    • Drosophila RNAi screen reveals CD36 family member required for mycobacterial infection
    • Philips JA, Rubin EJ, Perrimon N. Drosophila RNAi screen reveals CD36 family member required for mycobacterial infection. Science 2005; 309: 1251-3.
    • (2005) Science , vol.309 , pp. 1251-1253
    • Philips, J.A.1    Rubin, E.J.2    Perrimon, N.3
  • 166
    • 71449095250 scopus 로고    scopus 로고
    • Toll-dependent antimicrobial responses in Drosophila larval fat body require Spatzle secreted by haemocytes
    • Shia AK, Glittenberg M, Thompson G, Weber AN, Reichhart JM, Ligoxygakis P. Toll-dependent antimicrobial responses in Drosophila larval fat body require Spatzle secreted by haemocytes. J Cell Sci 2009; 122: 4505-15.
    • (2009) J Cell Sci , vol.122 , pp. 4505-4515
    • Shia, A.K.1    Glittenberg, M.2    Thompson, G.3    Weber, A.N.4    Reichhart, J.M.5    Ligoxygakis, P.6
  • 167
    • 67649878194 scopus 로고    scopus 로고
    • Elimination of plasmatocytes by targeted apoptosis reveals their role in multiple aspects of the Drosophila immune response
    • Charroux B, Royet J. Elimination of plasmatocytes by targeted apoptosis reveals their role in multiple aspects of the Drosophila immune response. Proc Natl Acad Sci U S A 2009; 106: 9797-802.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9797-9802
    • Charroux, B.1    Royet, J.2
  • 168
    • 79952285913 scopus 로고    scopus 로고
    • Relative roles of the cellular and humoral responses in the Drosophila host defense against three gram-positive bacterial infections
    • Nehme NT, Quintin J, Cho JH, Lee J, Lafarge MC, Kocks C, et al. Relative roles of the cellular and humoral responses in the Drosophila host defense against three gram-positive bacterial infections. PLoS One 2011; 6: e14743.
    • (2011) PLoS One , vol.6
    • Nehme, N.T.1    Quintin, J.2    Cho, J.H.3    Lee, J.4    Lafarge, M.C.5    Kocks, C.6
  • 169
  • 170
    • 43449134699 scopus 로고    scopus 로고
    • Drosophila melanogaster as a model for elucidating the pathogenicity of Francisella tularensis
    • Vonkavaara M, Telepnev MV, Ryden P, Sjostedt A, Stoven S. Drosophila melanogaster as a model for elucidating the pathogenicity of Francisella tularensis. Cell Microbiol 2008; 10: 1327-38.
    • (2008) Cell Microbiol , vol.10 , pp. 1327-1338
    • Vonkavaara, M.1    Telepnev, M.V.2    Ryden, P.3    Sjostedt, A.4    Stoven, S.5
  • 171
    • 69949130364 scopus 로고    scopus 로고
    • Genetic ablation of Drosophila phagocytes reveals their contribution to both development and resistance to bacterial infection
    • Defaye A, Evans I, Crozatier M, Wood W, Lemaitre B, Leulier F. Genetic ablation of Drosophila phagocytes reveals their contribution to both development and resistance to bacterial infection. J Innate Immun 2009; 1: 322-34.
    • (2009) J Innate Immun , vol.1 , pp. 322-334
    • Defaye, A.1    Evans, I.2    Crozatier, M.3    Wood, W.4    Lemaitre, B.5    Leulier, F.6
  • 173
    • 69949175169 scopus 로고    scopus 로고
    • p38 MAPK-dependent phagocytic encapsulation confers infection tolerance in Drosophila
    • Shinzawa N, Nelson B, Aonuma H, Okado K, Fukumoto S, Miura M, et al. p38 MAPK-dependent phagocytic encapsulation confers infection tolerance in Drosophila. Cell Host Microbe 2009; 6: 244-52.
    • (2009) Cell Host Microbe , vol.6 , pp. 244-252
    • Shinzawa, N.1    Nelson, B.2    Aonuma, H.3    Okado, K.4    Fukumoto, S.5    Miura, M.6
  • 174
    • 80052823818 scopus 로고    scopus 로고
    • Drosophila phagocytosis*still many unknowns under the surface
    • Ulvila J, Vanha-Aho LM, Ramet M. Drosophila phagocytosis*still many unknowns under the surface. APMIS 2011; 119: 651-62.
    • (2011) APMIS , vol.119 , pp. 651-662
    • Ulvila, J.1    Vanha-Aho, L.M.2    Ramet, M.3
  • 175
    • 0030152160 scopus 로고    scopus 로고
    • Croquemort, a novel Drosophila hemocyte/macrophage receptor that recognizes apoptotic cells
    • Franc NC, Dimarcq JL, Lagueux M, Hoffmann J, Ezekowitz RA. Croquemort, a novel Drosophila hemocyte/macrophage receptor that recognizes apoptotic cells. Immunity 1996; 4: 431-43.
    • (1996) Immunity , vol.4 , pp. 431-443
    • Franc, N.C.1    Dimarcq, J.L.2    Lagueux, M.3    Hoffmann, J.4    Ezekowitz, R.A.5
  • 176
    • 0034633786 scopus 로고    scopus 로고
    • Constitutive expression of a complement-like protein in toll and JAK gain-of-function mutants of Drosophila
    • Lagueux M, Perrodou E, Levashina EA, Capovilla M, Hoffmann JA. Constitutive expression of a complement-like protein in toll and JAK gain-of-function mutants of Drosophila. Proc Natl Acad Sci U S A 2000; 97: 11427-32.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11427-11432
    • Lagueux, M.1    Perrodou, E.2    Levashina, E.A.3    Capovilla, M.4    Hoffmann, J.A.5
  • 177
    • 31144437860 scopus 로고    scopus 로고
    • Identification of Drosophila gene products required for phagocytosis of Candida albicans
    • Stroschein-Stevenson SL, Foley E, O'Farrell PH, Johnson AD. Identification of Drosophila gene products required for phagocytosis of Candida albicans. PLoS Biol 2006; 4: e4.
    • (2006) PLoS Biol , vol.4
    • Stroschein-Stevenson, S.L.1    Foley, E.2    O'Farrell, P.H.3    Johnson, A.D.4
  • 179
    • 78650510069 scopus 로고    scopus 로고
    • Analysis of thioester-containing proteins during the innate immune response of Drosophila melanogaster
    • Bou Aoun R, Hetru C, Troxler L, Doucet D, Ferrandon D, Matt N. Analysis of thioester-containing proteins during the innate immune response of Drosophila melanogaster. J Innate Immun 2011; 3: 52-64.
    • (2011) J Innate Immun , vol.3 , pp. 52-64
    • Bou Aoun, R.1    Hetru, C.2    Troxler, L.3    Doucet, D.4    Ferrandon, D.5    Matt, N.6
  • 180
    • 79959848082 scopus 로고    scopus 로고
    • Functional analysis of host factors that mediate the intracellular lifestyle of Cryptococcus neoformans
    • e1002078
    • Qin QM, Luo J, Lin X, Pei J, Li L, Ficht TA, et al. Functional analysis of host factors that mediate the intracellular lifestyle of Cryptococcus neoformans. PLoS Pathog 2011; 7: e1002078.
    • (2011) PLoS Pathog , vol.7
    • Qin, Q.M.1    Luo, J.2    Lin, X.3    Pei, J.4    Li, L.5    Ficht, T.A.6
  • 181
    • 47849094901 scopus 로고    scopus 로고
    • Autophagic control of listeria through intracellular innate immune recognition in Drosophila
    • Yano T, Mita S, Ohmori H, Oshima Y, Fujimoto Y, Ueda R, et al. Autophagic control of listeria through intracellular innate immune recognition in Drosophila. Nat Immunol 2008; 9: 908-16.
    • (2008) Nat Immunol , vol.9 , pp. 908-916
    • Yano, T.1    Mita, S.2    Ohmori, H.3    Oshima, Y.4    Fujimoto, Y.5    Ueda, R.6
  • 182
    • 64049114864 scopus 로고    scopus 로고
    • Autophagy is an essential component of Drosophila immunity against vesicular stomatitis virus
    • Shelly S, Lukinova N, Bambina S, Berman A, Cherry S. Autophagy is an essential component of Drosophila immunity against vesicular stomatitis virus. Immunity 2009; 30: 588-98.
    • (2009) Immunity , vol.30 , pp. 588-598
    • Shelly, S.1    Lukinova, N.2    Bambina, S.3    Berman, A.4    Cherry, S.5
  • 183
    • 0026734517 scopus 로고
    • Lamellocyte differentiation in Drosophila larvae parasitized by Leptopilina
    • Rizki TM, Rizki RM. Lamellocyte differentiation in Drosophila larvae parasitized by Leptopilina. Dev Comp Immunol 1992; 16: 103-10.
    • (1992) Dev Comp Immunol , vol.16 , pp. 103-110
    • Rizki, T.M.1    Rizki, R.M.2
  • 184
    • 0021208904 scopus 로고
    • Cell surface changes associated with cellular immune reactions in Drosophila
    • Nappi AJ, Silvers M. Cell surface changes associated with cellular immune reactions in Drosophila. Science 1984; 225: 1166-8.
    • (1984) Science , vol.225 , pp. 1166-1168
    • Nappi, A.J.1    Silvers, M.2
  • 185
    • 0032425086 scopus 로고    scopus 로고
    • Hydrogen peroxide production in immunereactive Drosophila melanogaster
    • Nappi AJ, Vass E. Hydrogen peroxide production in immunereactive Drosophila melanogaster. J Parasitol 1998; 84: 1150-7.
    • (1998) J Parasitol , vol.84 , pp. 1150-1157
    • Nappi, A.J.1    Vass, E.2
  • 186
    • 0029582852 scopus 로고
    • Superoxide anion generation in Drosophila during melanotic encapsulation of parasites
    • Nappi AJ, Vass E, Frey F, Carton Y. Superoxide anion generation in Drosophila during melanotic encapsulation of parasites. Eur J Cell Biol 1995; 68: 450-6.
    • (1995) Eur J Cell Biol , vol.68 , pp. 450-456
    • Nappi, A.J.1    Vass, E.2    Frey, F.3    Carton, Y.4
  • 187
    • 0033838191 scopus 로고    scopus 로고
    • Nitric oxide involvement in Drosophila immunity
    • Nappi AJ, Vass E, Frey F, Carton Y. Nitric oxide involvement in Drosophila immunity. Nitric Oxide 2000; 4: 423-30.
    • (2000) Nitric Oxide , vol.4 , pp. 423-430
    • Nappi, A.J.1    Vass, E.2    Frey, F.3    Carton, Y.4
  • 188
    • 0025652684 scopus 로고
    • The prophenoloxidase cascade in insect immunity
    • Ashida M. The prophenoloxidase cascade in insect immunity. Res Immunol 1990; 141: 908-10.
    • (1990) Res Immunol , vol.141 , pp. 908-910
    • Ashida, M.1
  • 189
    • 0027620526 scopus 로고
    • Melanogenesis and the generation of cytotoxic molecules during insect cellular immune reactions
    • Nappi AJ, Vass E. Melanogenesis and the generation of cytotoxic molecules during insect cellular immune reactions. Pigment Cell Res 1993; 6: 117-26.
    • (1993) Pigment Cell Res , vol.6 , pp. 117-126
    • Nappi, A.J.1    Vass, E.2
  • 190
    • 1842665810 scopus 로고    scopus 로고
    • Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a pullout method
    • Scherfer C, Karlsson C, Loseva O, Bidla G, Goto A, Havemann J, et al. Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a pullout method. Curr Biol 2004; 14: 625-9.
    • (2004) Curr Biol , vol.14 , pp. 625-629
    • Scherfer, C.1    Karlsson, C.2    Loseva, O.3    Bidla, G.4    Goto, A.5    Havemann, J.6
  • 191
    • 18044376633 scopus 로고    scopus 로고
    • Hemolymph coagulation and phenoloxidase in Drosophila larvae
    • Bidla G, Lindgren M, Theopold U, Dushay MS. Hemolymph coagulation and phenoloxidase in Drosophila larvae. Dev Comp Immunol 2005; 29: 669-79.
    • (2005) Dev Comp Immunol , vol.29 , pp. 669-679
    • Bidla, G.1    Lindgren, M.2    Theopold, U.3    Dushay, M.S.4
  • 192
    • 0035477868 scopus 로고    scopus 로고
    • A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor
    • Goto A, Kumagai T, Kumagai C, Hirose J, Narita H, Mori H, et al. A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor. Biochem J 2001; 359: 99-108.
    • (2001) Biochem J , vol.359 , pp. 99-108
    • Goto, A.1    Kumagai, T.2    Kumagai, C.3    Hirose, J.4    Narita, H.5    Mori, H.6
  • 193
    • 33745973003 scopus 로고    scopus 로고
    • The Toll immune-regulated Drosophila protein Fondue is involved in hemolymph clotting and puparium formation
    • Scherfer C, Qazi MR, Takahashi K, Ueda R, Dushay MS, Theopold U, et al. The Toll immune-regulated Drosophila protein Fondue is involved in hemolymph clotting and puparium formation. Dev Biol 2006; 295: 156-63.
    • (2006) Dev Biol , vol.295 , pp. 156-163
    • Scherfer, C.1    Qazi, M.R.2    Takahashi, K.3    Ueda, R.4    Dushay, M.S.5    Theopold, U.6
  • 195
    • 77649265237 scopus 로고    scopus 로고
    • Pathogen entrapment by transglutaminase*a conserved early innate immune mechanism
    • e1000763
    • Wang Z, Wilhelmsson C, Hyrsl P, Loof TG, Dobes P, Klupp M, et al. Pathogen entrapment by transglutaminase*a conserved early innate immune mechanism. PLoS Pathog 2010; 6: e1000763.
    • (2010) PLoS Pathog , vol.6
    • Wang, Z.1    Wilhelmsson, C.2    Hyrsl, P.3    Loof, T.G.4    Dobes, P.5    Klupp, M.6
  • 196
    • 0031962080 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a Drosophila p38 mitogen-activated protein kinase
    • Han SJ, Choi KY, Brey PT, Lee WJ. Molecular cloning and characterization of a Drosophila p38 mitogen-activated protein kinase. J Biol Chem 1998; 273: 369-74.
    • (1998) J Biol Chem , vol.273 , pp. 369-374
    • Han, S.J.1    Choi, K.Y.2    Brey, P.T.3    Lee, W.J.4
  • 197
    • 10044243508 scopus 로고    scopus 로고
    • A Drosophila p38 orthologue is required for environmental stress responses
    • Craig CR, Fink JL, Yagi Y, Ip YT, Cagan RL. A Drosophila p38 orthologue is required for environmental stress responses. EMBO Rep 2004; 5: 1058-63.
    • (2004) EMBO Rep , vol.5 , pp. 1058-1063
    • Craig, C.R.1    Fink, J.L.2    Yagi, Y.3    Ip, Y.T.4    Cagan, R.L.5
  • 199
    • 0031866058 scopus 로고    scopus 로고
    • A conserved p38 mitogen-activated protein kinase pathway regulates Drosophila immunity gene expression
    • Han ZS, Enslen H, Hu X, Meng X, Wu IH, Barrett T, et al. A conserved p38 mitogen-activated protein kinase pathway regulates Drosophila immunity gene expression. Mol Cell Biol 1998; 18: 3527-39.
    • (1998) Mol Cell Biol , vol.18 , pp. 3527-3539
    • Han, Z.S.1    Enslen, H.2    Hu, X.3    Meng, X.4    Wu, I.H.5    Barrett, T.6
  • 200
    • 29144535648 scopus 로고    scopus 로고
    • Regulation of Drosophila p38 activation by specific MAP2 kinase and MAP3 kinase in response to different stimuli
    • Zhuang ZH, Zhou Y, Yu MC, Silverman N, Ge BX. Regulation of Drosophila p38 activation by specific MAP2 kinase and MAP3 kinase in response to different stimuli. Cell Signal 2006; 18: 441-8.
    • (2006) Cell Signal , vol.18 , pp. 441-448
    • Zhuang, Z.H.1    Zhou, Y.2    Yu, M.C.3    Silverman, N.4    Ge, B.X.5
  • 201
    • 19644368665 scopus 로고    scopus 로고
    • Drosophila activating transcription factor-2 is involved in stress response via activation by p38, but not c-Jun NH(2)-terminal kinase
    • Sano Y, Akimaru H, Okamura T, Nagao T, Okada M, Ishii S. Drosophila activating transcription factor-2 is involved in stress response via activation by p38, but not c-Jun NH(2)-terminal kinase. Mol Biol Cell 2005; 16: 2934-46.
    • (2005) Mol Biol Cell , vol.16 , pp. 2934-2946
    • Sano, Y.1    Akimaru, H.2    Okamura, T.3    Nagao, T.4    Okada, M.5    Ishii, S.6
  • 202
    • 62449265216 scopus 로고    scopus 로고
    • The PP2C Alphabet is a negative regulator of stressactivated protein kinase signaling in Drosophila
    • Baril C, Sahmi M, Ashton-Beaucage D, Stronach B, Therrien M. The PP2C Alphabet is a negative regulator of stressactivated protein kinase signaling in Drosophila. Genetics 2009; 181: 567-79.
    • (2009) Genetics , vol.181 , pp. 567-579
    • Baril, C.1    Sahmi, M.2    Ashton-Beaucage, D.3    Stronach, B.4    Therrien, M.5
  • 203
    • 0037124314 scopus 로고    scopus 로고
    • Eiger, a TNF superfamily ligand that triggers the Drosophila JNK pathway
    • Igaki T, Kanda H, Yamamoto-Goto Y, Kanuka H, Kuranaga E, Aigaki T, et al. Eiger, a TNF superfamily ligand that triggers the Drosophila JNK pathway. EMBO J 2002; 21: 3009-18.
    • (2002) EMBO J , vol.21 , pp. 3009-3018
    • Igaki, T.1    Kanda, H.2    Yamamoto-Goto, Y.3    Kanuka, H.4    Kuranaga, E.5    Aigaki, T.6
  • 204
    • 0037047362 scopus 로고    scopus 로고
    • Wengen, a member of the Drosophila tumor necrosis factor receptor superfamily, is required for Eiger signaling
    • Kanda H, Igaki T, Kanuka H, Yagi T, Miura M. Wengen, a member of the Drosophila tumor necrosis factor receptor superfamily, is required for Eiger signaling. J Biol Chem 2002; 277: 28372-5.
    • (2002) J Biol Chem , vol.277 , pp. 28372-28375
    • Kanda, H.1    Igaki, T.2    Kanuka, H.3    Yagi, T.4    Miura, M.5
  • 205
    • 0042066408 scopus 로고    scopus 로고
    • Eiger and its receptor, Wengen, comprise a TNF-like system in Drosophila
    • Kauppila S, Maaty WS, Chen P, Tomar RS, Eby MT, Chapo J, et al. Eiger and its receptor, Wengen, comprise a TNF-like system in Drosophila. Oncogene 2003; 22: 4860-7.
    • (2003) Oncogene , vol.22 , pp. 4860-4867
    • Kauppila, S.1    Maaty, W.S.2    Chen, P.3    Tomar, R.S.4    Eby, M.T.5    Chapo, J.6
  • 206
    • 0037162294 scopus 로고    scopus 로고
    • Evolution of TNF signaling mechanisms: JNK-dependent apoptosis triggered by Eiger, the Drosophila homolog of the TNF superfamily
    • Moreno E, Yan M, Basler K. Evolution of TNF signaling mechanisms: JNK-dependent apoptosis triggered by Eiger, the Drosophila homolog of the TNF superfamily. Curr Biol 2002; 12: 1263-8.
    • (2002) Curr Biol , vol.12 , pp. 1263-1268
    • Moreno, E.1    Yan, M.2    Basler, K.3
  • 207
    • 0029824847 scopus 로고    scopus 로고
    • A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila
    • Sluss HK, Han Z, Barrett T, Goberdhan DC, Wilson C, Davis RJ, et al. A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila. Genes Dev 1996; 10: 2745-58.
    • (1996) Genes Dev , vol.10 , pp. 2745-2758
    • Sluss, H.K.1    Han, Z.2    Barrett, T.3    Goberdhan, D.C.4    Wilson, C.5    Davis, R.J.6
  • 208
    • 34248216101 scopus 로고    scopus 로고
    • Crystal cell rupture after injury in Drosophila requires the JNK pathway, small GTPases and the TNF homolog Eiger
    • Bidla G, Dushay MS, Theopold U. Crystal cell rupture after injury in Drosophila requires the JNK pathway, small GTPases and the TNF homolog Eiger. J Cell Sci 2007; 120: 1209-15.
    • (2007) J Cell Sci , vol.120 , pp. 1209-1215
    • Bidla, G.1    Dushay, M.S.2    Theopold, U.3
  • 209
    • 0346890213 scopus 로고    scopus 로고
    • Stimulus-specific requirements for MAP3 kinases in activating the JNK pathway
    • Chen W, White MA, Cobb MH. Stimulus-specific requirements for MAP3 kinases in activating the JNK pathway. J Biol Chem 2002; 277: 49105-10.
    • (2002) J Biol Chem , vol.277 , pp. 49105-49110
    • Chen, W.1    White, M.A.2    Cobb, M.H.3
  • 210
    • 33646244962 scopus 로고    scopus 로고
    • Alphabet, a Ser/Thr phosphatase of the protein phosphatase 2C family, negatively regulates RAS/MAPK signaling in Drosophila
    • Baril C, Therrien M. Alphabet, a Ser/Thr phosphatase of the protein phosphatase 2C family, negatively regulates RAS/MAPK signaling in Drosophila. Dev Biol 2006; 294: 232-45.
    • (2006) Dev Biol , vol.294 , pp. 232-245
    • Baril, C.1    Therrien, M.2
  • 211
    • 0035971422 scopus 로고    scopus 로고
    • Drosophila AP-1: lessons from an invertebrate
    • Kockel L, Homsy JG, Bohmann D. Drosophila AP-1: lessons from an invertebrate. Oncogene 2001; 20: 2347-64.
    • (2001) Oncogene , vol.20 , pp. 2347-2364
    • Kockel, L.1    Homsy, J.G.2    Bohmann, D.3
  • 212
    • 33746319307 scopus 로고    scopus 로고
    • Cooperative control of Drosophila immune responses by the JNK and NF-kappaB signaling pathways
    • Delaney JR, Stoven S, Uvell H, Anderson KV, Engstrom Y, Mlodzik M. Cooperative control of Drosophila immune responses by the JNK and NF-kappaB signaling pathways. EMBO J 2006; 25: 3068-77.
    • (2006) EMBO J , vol.25 , pp. 3068-3077
    • Delaney, J.R.1    Stoven, S.2    Uvell, H.3    Anderson, K.V.4    Engstrom, Y.5    Mlodzik, M.6
  • 213
    • 20444506693 scopus 로고    scopus 로고
    • Functional analysis of immune response genes in Drosophila identifies JNK pathway as a regulator of antimicrobial peptide gene expression in S2 cells
    • Kallio J, Leinonen A, Ulvila J, Valanne S, Ezekowitz RA, Ramet M. Functional analysis of immune response genes in Drosophila identifies JNK pathway as a regulator of antimicrobial peptide gene expression in S2 cells. Microbes Infect 2005; 7: 811-9.
    • (2005) Microbes Infect , vol.7 , pp. 811-819
    • Kallio, J.1    Leinonen, A.2    Ulvila, J.3    Valanne, S.4    Ezekowitz, R.A.5    Ramet, M.6
  • 215
    • 70449597294 scopus 로고    scopus 로고
    • A non-redundant role for Drosophila Mkk4 and hemipterous/Mkk7 in TAK1-mediated activation of JNK
    • Geuking P, Narasimamurthy R, Lemaitre B, Basler K, Leulier F. A non-redundant role for Drosophila Mkk4 and hemipterous/Mkk7 in TAK1-mediated activation of JNK. PLoS One 2009; 4: e7709.
    • (2009) PLoS One , vol.4
    • Geuking, P.1    Narasimamurthy, R.2    Lemaitre, B.3    Basler, K.4    Leulier, F.5
  • 216
    • 73549097550 scopus 로고    scopus 로고
    • A quantitative RNAi screen for JNK modifiers identifies Pvr as a novel regulator of Drosophila immune signaling
    • e1000655
    • Bond D, Foley E. A quantitative RNAi screen for JNK modifiers identifies Pvr as a novel regulator of Drosophila immune signaling. PLoS Pathog 2009; 5: e1000655.
    • (2009) PLoS Pathog , vol.5
    • Bond, D.1    Foley, E.2
  • 217
  • 218
    • 0032519787 scopus 로고    scopus 로고
    • puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila
    • Martin-Blanco E, Gampel A, Ring J, Virdee K, Kirov N, Tolkovsky AM, et al. puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila. Genes Dev 1998; 12: 557-70.
    • (1998) Genes Dev , vol.12 , pp. 557-570
    • Martin-Blanco, E.1    Gampel, A.2    Ring, J.3    Virdee, K.4    Kirov, N.5    Tolkovsky, A.M.6
  • 219
    • 12144288602 scopus 로고    scopus 로고
    • Targeting of TAK1 by the NF-kappa B protein Relish regulates the JNK-mediated immune response in Drosophila
    • Park JM, Brady H, Ruocco MG, Sun H, Williams D, Lee SJ, et al. Targeting of TAK1 by the NF-kappa B protein Relish regulates the JNK-mediated immune response in Drosophila. Genes Dev 2004; 18: 584-94.
    • (2004) Genes Dev , vol.18 , pp. 584-594
    • Park, J.M.1    Brady, H.2    Ruocco, M.G.3    Sun, H.4    Williams, D.5    Lee, S.J.6
  • 220
    • 33847020707 scopus 로고    scopus 로고
    • Alternative measures of response to Pseudomonas aeruginosa infection in Drosophila melanogaster
    • Corby-Harris V, Habel KE, Ali FG, Promislow DE. Alternative measures of response to Pseudomonas aeruginosa infection in Drosophila melanogaster. J Evol Biol 2007; 20: 526-33.
    • (2007) J Evol Biol , vol.20 , pp. 526-533
    • Corby-Harris, V.1    Habel, K.E.2    Ali, F.G.3    Promislow, D.E.4
  • 221
    • 33750023633 scopus 로고    scopus 로고
    • Akt and FOXO dysregulation contribute to infection-induced wasting in Drosophila
    • Dionne MS, Pham LN, Shirasu-Hiza M, Schneider DS. Akt and FOXO dysregulation contribute to infection-induced wasting in Drosophila. Curr Biol 2006; 16: 1977-85.
    • (2006) Curr Biol , vol.16 , pp. 1977-1985
    • Dionne, M.S.1    Pham, L.N.2    Shirasu-Hiza, M.3    Schneider, D.S.4
  • 222
    • 77950612276 scopus 로고    scopus 로고
    • A signaling protease required for melanization in Drosophila affects resistance and tolerance of infections
    • Ayres JS, Schneider DS. A signaling protease required for melanization in Drosophila affects resistance and tolerance of infections. PLoS Biol 2008; 6: 2764-73.
    • (2008) PLoS Biol , vol.6 , pp. 2764-2773
    • Ayres, J.S.1    Schneider, D.S.2
  • 223
    • 1542357677 scopus 로고    scopus 로고
    • Fluorescence-activated cell sorting (FACS) of Drosophila hemocytes reveals important functional similarities to mammalian leukocytes
    • Tirouvanziam R, Davidson CJ, Lipsick JS, Herzenberg LA. Fluorescence-activated cell sorting (FACS) of Drosophila hemocytes reveals important functional similarities to mammalian leukocytes. Proc Natl Acad Sci U S A 2004; 101: 2912-7.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2912-2917
    • Tirouvanziam, R.1    Davidson, C.J.2    Lipsick, J.S.3    Herzenberg, L.A.4
  • 224
    • 27644498442 scopus 로고    scopus 로고
    • A direct role for dual oxidase in Drosophila gut immunity
    • Ha EM, Oh CT, Bae YS, Lee WJ. A direct role for dual oxidase in Drosophila gut immunity. Science 2005; 310: 847-50.
    • (2005) Science , vol.310 , pp. 847-850
    • Ha, E.M.1    Oh, C.T.2    Bae, Y.S.3    Lee, W.J.4
  • 225
    • 0037227097 scopus 로고    scopus 로고
    • Nitric oxide contributes to induction of innate immune responses to gram-negative bacteria in Drosophila
    • Foley E, O'Farrell PH. Nitric oxide contributes to induction of innate immune responses to gram-negative bacteria in Drosophila. Genes Dev 2003; 17: 115-25.
    • (2003) Genes Dev , vol.17 , pp. 115-125
    • Foley, E.1    O'Farrell, P.H.2
  • 226
    • 11244343895 scopus 로고    scopus 로고
    • An antioxidant system required for host protection against gut infection in Drosophila
    • Ha EM, Oh CT, Ryu JH, Bae YS, Kang SW, Jang IH, et al. An antioxidant system required for host protection against gut infection in Drosophila. Dev Cell 2005; 8: 125-32.
    • (2005) Dev Cell , vol.8 , pp. 125-132
    • Ha, E.M.1    Oh, C.T.2    Ryu, J.H.3    Bae, Y.S.4    Kang, S.W.5    Jang, I.H.6
  • 227
    • 0033106306 scopus 로고    scopus 로고
    • Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection
    • Yoshiga T, Georgieva T, Dunkov BC, Harizanova N, Ralchev K, Law JH. Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection. Eur J Biochem 1999; 260: 414-20.
    • (1999) Eur J Biochem , vol.260 , pp. 414-420
    • Yoshiga, T.1    Georgieva, T.2    Dunkov, B.C.3    Harizanova, N.4    Ralchev, K.5    Law, J.H.6
  • 228
    • 0036489168 scopus 로고    scopus 로고
    • Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal and tissue specific expression of both subunit types
    • Georgieva T, Dunkov BC, Dimov S, Ralchev K, Law JH. Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal and tissue specific expression of both subunit types. Insect Biochem Mol Biol 2002; 32: 295-302.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 295-302
    • Georgieva, T.1    Dunkov, B.C.2    Dimov, S.3    Ralchev, K.4    Law, J.H.5
  • 229
    • 0347635519 scopus 로고    scopus 로고
    • A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph
    • Vierstraete E, Verleyen P, Baggerman G, D'Hertog W, Van den Bergh G, Arckens L, et al. A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph. Proc Natl Acad Sci U S A 2004; 101: 470-5.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 470-475
    • Vierstraete, E.1    Verleyen, P.2    Baggerman, G.3    D'Hertog, W.4    Van den Bergh, G.5    Arckens, L.6
  • 230
    • 33751120715 scopus 로고    scopus 로고
    • The RNA silencing endonuclease Argonaute 2 mediates specific antiviral immunity in Drosophila melanogaster
    • van Rij RP, Saleh MC, Berry B, Foo C, Houk A, Antoniewski C, et al. The RNA silencing endonuclease Argonaute 2 mediates specific antiviral immunity in Drosophila melanogaster. Genes Dev 2006; 20: 2985-95.
    • (2006) Genes Dev , vol.20 , pp. 2985-2995
    • van Rij, R.P.1    Saleh, M.C.2    Berry, B.3    Foo, C.4    Houk, A.5    Antoniewski, C.6
  • 231
    • 33645979325 scopus 로고    scopus 로고
    • RNA interference directs innate immunity against viruses in adult Drosophila
    • Wang XH, Aliyari R, Li WX, Li HW, Kim K, Carthew R, et al. RNA interference directs innate immunity against viruses in adult Drosophila. Science 2006; 312: 452-4.
    • (2006) Science , vol.312 , pp. 452-454
    • Wang, X.H.1    Aliyari, R.2    Li, W.X.3    Li, H.W.4    Kim, K.5    Carthew, R.6
  • 232
    • 0037123630 scopus 로고    scopus 로고
    • Induction and suppression of RNA silencing by an animal virus
    • Li H, Li WX, Ding SW. Induction and suppression of RNA silencing by an animal virus. Science 2002; 296: 1319-21.
    • (2002) Science , vol.296 , pp. 1319-1321
    • Li, H.1    Li, W.X.2    Ding, S.W.3
  • 233
    • 33744494279 scopus 로고    scopus 로고
    • Essential function in vivo for Dicer-2 in host defense against RNA viruses in Drosophila
    • Galiana-Arnoux D, Dostert C, Schneemann A, Hoffmann JA, Imler JL. Essential function in vivo for Dicer-2 in host defense against RNA viruses in Drosophila. Nat Immunol 2006; 7: 590-7.
    • (2006) Nat Immunol , vol.7 , pp. 590-597
    • Galiana-Arnoux, D.1    Dostert, C.2    Schneemann, A.3    Hoffmann, J.A.4    Imler, J.L.5
  • 234
    • 33645537549 scopus 로고    scopus 로고
    • RNAi is an antiviral immune response against a dsRNA virus in Drosophila melanogaster
    • Zambon RA, Vakharia VN, Wu LP. RNAi is an antiviral immune response against a dsRNA virus in Drosophila melanogaster. Cell Microbiol 2006; 8: 880-9.
    • (2006) Cell Microbiol , vol.8 , pp. 880-889
    • Zambon, R.A.1    Vakharia, V.N.2    Wu, L.P.3
  • 236
    • 33744910636 scopus 로고    scopus 로고
    • Double-stranded RNA is internalized by scavenger receptor-mediated endocytosis in Drosophila S2 cells
    • Ulvila J, Parikka M, Kleino A, Sormunen R, Ezekowitz RA, Kocks C, et al. Double-stranded RNA is internalized by scavenger receptor-mediated endocytosis in Drosophila S2 cells. J Biol Chem 2006; 281: 14370-5.
    • (2006) J Biol Chem , vol.281 , pp. 14370-14375
    • Ulvila, J.1    Parikka, M.2    Kleino, A.3    Sormunen, R.4    Ezekowitz, R.A.5    Kocks, C.6
  • 237
    • 62649144073 scopus 로고    scopus 로고
    • Antiviral immunity in Drosophila requires systemic RNA interference spread
    • Saleh MC, Tassetto M, van Rij RP, Goic B, Gausson V, Berry B, et al. Antiviral immunity in Drosophila requires systemic RNA interference spread. Nature 2009; 458: 346-50.
    • (2009) Nature , vol.458 , pp. 346-350
    • Saleh, M.C.1    Tassetto, M.2    van Rij, R.P.3    Goic, B.4    Gausson, V.5    Berry, B.6
  • 239
    • 77958554947 scopus 로고    scopus 로고
    • Lethality and developmental delay in Drosophila melanogaster larvae after ingestion of selected Pseudomonas fluorescens strains
    • e12504
    • Olcott MH, Henkels MD, Rosen KL, Walker FL, Sneh B, Loper JE, et al. Lethality and developmental delay in Drosophila melanogaster larvae after ingestion of selected Pseudomonas fluorescens strains. PLoS One 2010; 5: e12504.
    • (2010) PLoS One , vol.5
    • Olcott, M.H.1    Henkels, M.D.2    Rosen, K.L.3    Walker, F.L.4    Sneh, B.5    Loper, J.E.6
  • 240
    • 51949106514 scopus 로고    scopus 로고
    • Drosophila melanogasterbased screening for multihost virulence factors of Pseudomonas aeruginosa PA14 and identification of a virulence-attenuating factor
    • Kim SH, Park SY, Heo YJ, Cho YH. Drosophila melanogasterbased screening for multihost virulence factors of Pseudomonas aeruginosa PA14 and identification of a virulence-attenuating factor, HudA. Infect Immun 2008; 76: 4152-62.
    • (2008) HudA. Infect Immun , vol.76 , pp. 4152-4162
    • Kim, S.H.1    Park, S.Y.2    Heo, Y.J.3    Cho, Y.H.4
  • 242
    • 59849086113 scopus 로고    scopus 로고
    • Genetic analysis of Drosophila melanogaster susceptibility to intestinal Vibrio cholerae infection
    • Berkey CD, Blow N, Watnick PI. Genetic analysis of Drosophila melanogaster susceptibility to intestinal Vibrio cholerae infection. Cell Microbiol 2009; 11: 461-74.
    • (2009) Cell Microbiol , vol.11 , pp. 461-474
    • Berkey, C.D.1    Blow, N.2    Watnick, P.I.3
  • 243
    • 33644850810 scopus 로고    scopus 로고
    • Drosophila melanogaster is susceptible to Vibrio cholerae infection
    • Park SY, Heo YJ, Kim KS, Cho YH. Drosophila melanogaster is susceptible to Vibrio cholerae infection. Mol Cells 2005; 20: 409-15.
    • (2005) Mol Cells , vol.20 , pp. 409-415
    • Park, S.Y.1    Heo, Y.J.2    Kim, K.S.3    Cho, Y.H.4
  • 244
    • 55449099633 scopus 로고    scopus 로고
    • Identification and functional analysis of antifungal immune response genes in Drosophila
    • e1000168
    • Jin LH, Shim J, Yoon JS, Kim B, Kim J, Kim-Ha J, et al. Identification and functional analysis of antifungal immune response genes in Drosophila. PLoS Pathog 2008; 4: e1000168.
    • (2008) PLoS Pathog , vol.4
    • Jin, L.H.1    Shim, J.2    Yoon, J.S.3    Kim, B.4    Kim, J.5    Kim-Ha, J.6
  • 245
    • 77956909955 scopus 로고    scopus 로고
    • Inhibitory role for D-alanylation of wall teichoic acid in activation of insect Toll pathway by peptidoglycan of Staphylococcus aureus
    • Tabuchi Y, Shiratsuchi A, Kurokawa K, Gong JH, Sekimizu K, Lee BL, et al. Inhibitory role for D-alanylation of wall teichoic acid in activation of insect Toll pathway by peptidoglycan of Staphylococcus aureus. J Immunol 2010; 185: 2424-31.
    • (2010) J Immunol , vol.185 , pp. 2424-2431
    • Tabuchi, Y.1    Shiratsuchi, A.2    Kurokawa, K.3    Gong, J.H.4    Sekimizu, K.5    Lee, B.L.6
  • 247
    • 60549098793 scopus 로고    scopus 로고
    • Host glycosaminoglycan confers susceptibility to bacterial infection in Drosophila melanogaster
    • Baron MJ, Wong SL, Nybakken K, Carey VJ, Madoff LC. Host glycosaminoglycan confers susceptibility to bacterial infection in Drosophila melanogaster. Infect Immun 2009; 77: 860-6.
    • (2009) Infect Immun , vol.77 , pp. 860-866
    • Baron, M.J.1    Wong, S.L.2    Nybakken, K.3    Carey, V.J.4    Madoff, L.C.5
  • 248
    • 29944441034 scopus 로고    scopus 로고
    • Lovastatin has significant activity against zygomycetes and interacts synergistically with voriconazole
    • Chamilos G, Lewis RE, Kontoyiannis DP. Lovastatin has significant activity against zygomycetes and interacts synergistically with voriconazole. Antimicrob Agents Chemother 2006; 50: 96-103.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 96-103
    • Chamilos, G.1    Lewis, R.E.2    Kontoyiannis, D.P.3
  • 249
    • 65649120359 scopus 로고    scopus 로고
    • Increased virulence of Zygomycetes organisms following exposure to voriconazole: a study involving fly and murine models of zygomycosis
    • Lamaris GA, Ben-Ami R, Lewis RE, Chamilos G, Samonis G, Kontoyiannis DP. Increased virulence of Zygomycetes organisms following exposure to voriconazole: a study involving fly and murine models of zygomycosis. J Infect Dis 2009; 199: 1399-406.
    • (2009) J Infect Dis , vol.199 , pp. 1399-1406
    • Lamaris, G.A.1    Ben-Ami, R.2    Lewis, R.E.3    Chamilos, G.4    Samonis, G.5    Kontoyiannis, D.P.6
  • 250
    • 49649120958 scopus 로고    scopus 로고
    • Does pre-exposure of Aspergillus fumigatus to voriconazole or posaconazole in vitro affect its virulence and the in vivo activity of subsequent posaconazole or voriconazole, respectively? A study in a fly model of aspergillosis
    • Lamaris GA, Ben-Ami R, Lewis RE, Kontoyiannis DP. Does pre-exposure of Aspergillus fumigatus to voriconazole or posaconazole in vitro affect its virulence and the in vivo activity of subsequent posaconazole or voriconazole, respectively? A study in a fly model of aspergillosis. J Antimicrob Chemother 2008; 62: 539-42.
    • (2008) J Antimicrob Chemother , vol.62 , pp. 539-542
    • Lamaris, G.A.1    Ben-Ami, R.2    Lewis, R.E.3    Kontoyiannis, D.P.4
  • 251
    • 15544363784 scopus 로고    scopus 로고
    • Toll-deficient Drosophila flies as a fast, highthroughput model for the study of antifungal drug efficacy against invasive aspergillosis and Aspergillus virulence
    • Lionakis MS, Lewis RE, May GS, Wiederhold NP, Albert ND, Halder G, et al. Toll-deficient Drosophila flies as a fast, highthroughput model for the study of antifungal drug efficacy against invasive aspergillosis and Aspergillus virulence. J Infect Dis 2005; 191: 1188-95.
    • (2005) J Infect Dis , vol.191 , pp. 1188-1195
    • Lionakis, M.S.1    Lewis, R.E.2    May, G.S.3    Wiederhold, N.P.4    Albert, N.D.5    Halder, G.6
  • 253
    • 33748668209 scopus 로고    scopus 로고
    • The nitric oxide scavenger cobinamide profoundly improves survival in a Drosophila melanogaster model of bacterial sepsis
    • Broderick KE, Feala J, McCulloch A, Paternostro G, Sharma VS, Pilz RB, et al. The nitric oxide scavenger cobinamide profoundly improves survival in a Drosophila melanogaster model of bacterial sepsis. FASEB J 2006; 20: 1865-73.
    • (2006) FASEB J , vol.20 , pp. 1865-1873
    • Broderick, K.E.1    Feala, J.2    McCulloch, A.3    Paternostro, G.4    Sharma, V.S.5    Pilz, R.B.6
  • 254
    • 4344634458 scopus 로고    scopus 로고
    • Drosophila melanogaster as a model host for Staphylococcus aureus infection
    • Needham AJ, Kibart M, Crossley H, Ingham PW, Foster SJ. Drosophila melanogaster as a model host for Staphylococcus aureus infection. Microbiology 2004; 150: 2347-55.
    • (2004) Microbiology , vol.150 , pp. 2347-2355
    • Needham, A.J.1    Kibart, M.2    Crossley, H.3    Ingham, P.W.4    Foster, S.J.5
  • 255
    • 79953219953 scopus 로고    scopus 로고
    • Paraoxonase 1, quorum sensing, and P. aeruginosa infection: a novel model
    • Estin ML, Stoltz DA, Zabner J. Paraoxonase 1, quorum sensing, and P. aeruginosa infection: a novel model. Adv Exp Med Biol 2010; 660: 183-93.
    • (2010) Adv Exp Med Biol , vol.660 , pp. 183-193
    • Estin, M.L.1    Stoltz, D.A.2    Zabner, J.3
  • 256
    • 67049086922 scopus 로고    scopus 로고
    • Antibacterial efficacy of phages against Pseudomonas aeruginosa infections in mice and Drosophila melanogaster
    • Heo YJ, Lee YR, Jung HH, Lee J, Ko G, Cho YH. Antibacterial efficacy of phages against Pseudomonas aeruginosa infections in mice and Drosophila melanogaster. Antimicrob Agents Chemother 2009; 53: 2469-74.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 2469-2474
    • Heo, Y.J.1    Lee, Y.R.2    Jung, H.H.3    Lee, J.4    Ko, G.5    Cho, Y.H.6
  • 257
    • 48249117081 scopus 로고    scopus 로고
    • Circulating blood cells function as a surveillance system for damaged tissue in Drosophila larvae
    • Babcock DT, Brock AR, Fish GS, Wang Y, Perrin L, Krasnow MA, et al. Circulating blood cells function as a surveillance system for damaged tissue in Drosophila larvae. Proc Natl Acad Sci U S A 2008; 105: 10017-22.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10017-10022
    • Babcock, D.T.1    Brock, A.R.2    Fish, G.S.3    Wang, Y.4    Perrin, L.5    Krasnow, M.A.6
  • 258
    • 77955284566 scopus 로고    scopus 로고
    • Defining a core set of actin cytoskeletal proteins critical for actin-based motility of Rickettsia
    • Serio AW, Jeng RL, Haglund CM, Reed SC, Welch MD. Defining a core set of actin cytoskeletal proteins critical for actin-based motility of Rickettsia. Cell Host Microbe 2010; 7: 388-98.
    • (2010) Cell Host Microbe , vol.7 , pp. 388-398
    • Serio, A.W.1    Jeng, R.L.2    Haglund, C.M.3    Reed, S.C.4    Welch, M.D.5
  • 259
    • 45549093024 scopus 로고    scopus 로고
    • Investigating the involvement of host factors involved in intracellular pathogen infection by RNAi in Drosophila cells
    • Agaisse H. Investigating the involvement of host factors involved in intracellular pathogen infection by RNAi in Drosophila cells. Methods Mol Biol 2008; 415: 395-402.
    • (2008) Methods Mol Biol , vol.415 , pp. 395-402
    • Agaisse, H.1
  • 260
    • 77956196659 scopus 로고    scopus 로고
    • Host factors required for modulation of phagosome biogenesis and proliferation of Francisella tularensis within the cytosol
    • Akimana C, Al-Khodor S, Abu Kwaik Y. Host factors required for modulation of phagosome biogenesis and proliferation of Francisella tularensis within the cytosol. PLoS One 2010; 5: e11025.
    • (2010) PLoS One , vol.5
    • Akimana, C.1    Al-Khodor, S.2    Abu Kwaik, Y.3
  • 261
    • 23844442475 scopus 로고    scopus 로고
    • Genome-wide RNAi screen for host factors required for intracellular bacterial infection
    • Agaisse H, Burrack LS, Philips JA, Rubin EJ, Perrimon N, Higgins DE. Genome-wide RNAi screen for host factors required for intracellular bacterial infection. Science 2005; 309: 1248-51.
    • (2005) Science , vol.309 , pp. 1248-1251
    • Agaisse, H.1    Burrack, L.S.2    Philips, J.A.3    Rubin, E.J.4    Perrimon, N.5    Higgins, D.E.6
  • 264
    • 32544452682 scopus 로고    scopus 로고
    • Modeling early Epstein-Barr virus infection in Drosophila melanogaster: the BZLF1 protein
    • Adamson AL, Wright N, LaJeunesse DR. Modeling early Epstein-Barr virus infection in Drosophila melanogaster: the BZLF1 protein. Genetics 2005; 171: 1125-35.
    • (2005) Genetics , vol.171 , pp. 1125-1135
    • Adamson, A.L.1    Wright, N.2    LaJeunesse, D.R.3
  • 266
    • 0027419167 scopus 로고
    • Pertussis toxin expression in Drosophila alters the visual response and blocks eating behaviour
    • Fitch CL, de Sousa SM, O'Day PM, Neubert TA, Plantilla CM, Spencer M, et al. Pertussis toxin expression in Drosophila alters the visual response and blocks eating behaviour. Cell Signal 1993; 5: 187-207.
    • (1993) Cell Signal , vol.5 , pp. 187-207
    • Fitch, C.L.1    de Sousa, S.M.2    O'Day, P.M.3    Neubert, T.A.4    Plantilla, C.M.5    Spencer, M.6
  • 267
    • 77955409156 scopus 로고    scopus 로고
    • Drosophila melanogaster as a model host for the Burkholderia cepacia complex
    • Castonguay-Vanier J, Vial L, Tremblay J, Deziel E. Drosophila melanogaster as a model host for the Burkholderia cepacia complex. PLoS One 2010; 5: e11467.
    • (2010) PLoS One , vol.5
    • Castonguay-Vanier, J.1    Vial, L.2    Tremblay, J.3    Deziel, E.4
  • 268
    • 77958148847 scopus 로고    scopus 로고
    • Reciprocal analysis of Francisella novicida infections of a Drosophila melanogaster model reveal host-pathogen conflicts mediated by reactive oxygen and imd-regulated innate immune response
    • e1001065
    • Moule MG, Monack DM, Schneider DS. Reciprocal analysis of Francisella novicida infections of a Drosophila melanogaster model reveal host-pathogen conflicts mediated by reactive oxygen and imd-regulated innate immune response. PLoS Pathog 2010; 6: e1001065.
    • (2010) PLoS Pathog , vol.6
    • Moule, M.G.1    Monack, D.M.2    Schneider, D.S.3
  • 270
    • 1642447175 scopus 로고    scopus 로고
    • MglA regulates transcription of virulence factors necessary for Francisella tularensis intraamoebae and intramacrophage survival
    • Lauriano CM, Barker JR, Yoon SS, Nano FE, Arulanandam BP, Hassett DJ, et al. MglA regulates transcription of virulence factors necessary for Francisella tularensis intraamoebae and intramacrophage survival. Proc Natl Acad Sci U S A 2004; 101: 4246-9.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4246-4249
    • Lauriano, C.M.1    Barker, J.R.2    Yoon, S.S.3    Nano, F.E.4    Arulanandam, B.P.5    Hassett, D.J.6
  • 271
    • 77953955392 scopus 로고    scopus 로고
    • Directed screen of Francisella novicida virulence determinants using Drosophila melanogaster
    • Ahlund MK, Ryden P, Sjostedt A, Stoven S. Directed screen of Francisella novicida virulence determinants using Drosophila melanogaster. Infect Immun 2010; 78: 3118-28.
    • (2010) Infect Immun , vol.78 , pp. 3118-3128
    • Ahlund, M.K.1    Ryden, P.2    Sjostedt, A.3    Stoven, S.4
  • 272
    • 77955425900 scopus 로고    scopus 로고
    • Imd pathway is involved in the interaction of Drosophila melanogaster with the entomopathogenic bacteria Xenorhabdus nematophila and Photorhabdus luminescens
    • Aymeric JL, Givaudan A, Duvic B. Imd pathway is involved in the interaction of Drosophila melanogaster with the entomopathogenic bacteria, Xenorhabdus nematophila and Photorhabdus luminescens. Mol Immunol 2010; 47: 2342-8.
    • (2010) Mol Immunol , vol.47 , pp. 2342-2348
    • Aymeric, J.L.1    Givaudan, A.2    Duvic, B.3
  • 273
  • 274
    • 34848926903 scopus 로고    scopus 로고
    • Rac2 is a major actor of Drosophila resistance to Pseudomonas aeruginosa acting in phagocytic cells
    • Avet-Rochex A, Perrin J, Bergeret E, Fauvarque MO. Rac2 is a major actor of Drosophila resistance to Pseudomonas aeruginosa acting in phagocytic cells. Genes Cells 2007; 12: 1193-204.
    • (2007) Genes Cells , vol.12 , pp. 1193-1204
    • Avet-Rochex, A.1    Perrin, J.2    Bergeret, E.3    Fauvarque, M.O.4
  • 275
    • 31444440362 scopus 로고    scopus 로고
    • The peptidoglycan recognition protein PGRP-SC1a is essential for Toll signaling and phagocytosis of Staphylococcus aureus in Drosophila
    • Garver LS, Wu J, Wu LP. The peptidoglycan recognition protein PGRP-SC1a is essential for Toll signaling and phagocytosis of Staphylococcus aureus in Drosophila. Proc Natl Acad Sci U S A 2006; 103: 660-5.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 660-665
    • Garver, L.S.1    Wu, J.2    Wu, L.P.3
  • 276
    • 56349124824 scopus 로고    scopus 로고
    • TM9SF4 is required for Drosophila cellular immunity via cell adhesion and phagocytosis
    • Bergeret E, Perrin J, Williams M, Grunwald D, Engel E, Thevenon D, et al. TM9SF4 is required for Drosophila cellular immunity via cell adhesion and phagocytosis. J Cell Sci 2008; 121: 3325-34.
    • (2008) J Cell Sci , vol.121 , pp. 3325-3334
    • Bergeret, E.1    Perrin, J.2    Williams, M.3    Grunwald, D.4    Engel, E.5    Thevenon, D.6
  • 277
    • 45149096655 scopus 로고    scopus 로고
    • Identification of Drosophila mutants altering defense of and endurance to Listeria monocytogenes infection
    • Ayres JS, Freitag N, Schneider DS. Identification of Drosophila mutants altering defense of and endurance to Listeria monocytogenes infection. Genetics 2008; 178: 1807-15.
    • (2008) Genetics , vol.178 , pp. 1807-1815
    • Ayres, J.S.1    Freitag, N.2    Schneider, D.S.3
  • 278
    • 51349160074 scopus 로고    scopus 로고
    • Drosophila are protected from Pseudomonas aeruginosa lethality by transgenic expression of paraoxonase-1
    • Stoltz DA, Ozer EA, Taft PJ, Barry M, Liu L, Kiss PJ, et al. Drosophila are protected from Pseudomonas aeruginosa lethality by transgenic expression of paraoxonase-1. J Clin Invest 2008; 118: 3123-31.
    • (2008) J Clin Invest , vol.118 , pp. 3123-3131
    • Stoltz, D.A.1    Ozer, E.A.2    Taft, P.J.3    Barry, M.4    Liu, L.5    Kiss, P.J.6
  • 279
    • 39349099557 scopus 로고    scopus 로고
    • Cyanide produced by human isolates of Pseudomonas aeruginosa contributes to lethality in Drosophila melanogaster
    • Broderick KE, Chan A, Balasubramanian M, Feala J, Reed SL, Panda M, et al. Cyanide produced by human isolates of Pseudomonas aeruginosa contributes to lethality in Drosophila melanogaster. J Infect Dis 2008; 197: 457-64.
    • (2008) J Infect Dis , vol.197 , pp. 457-464
    • Broderick, K.E.1    Chan, A.2    Balasubramanian, M.3    Feala, J.4    Reed, S.L.5    Panda, M.6
  • 280
    • 14044277610 scopus 로고    scopus 로고
    • Profiling early infection responses: Pseudomonas aeruginosa eludes host defenses by suppressing antimicrobial peptide gene expression
    • Apidianakis Y, Mindrinos MN, Xiao W, Lau GW, Baldini RL, Davis RW, et al. Profiling early infection responses: Pseudomonas aeruginosa eludes host defenses by suppressing antimicrobial peptide gene expression. Proc Natl Acad Sci U S A 2005; 102: 2573-8.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2573-2578
    • Apidianakis, Y.1    Mindrinos, M.N.2    Xiao, W.3    Lau, G.W.4    Baldini, R.L.5    Davis, R.W.6
  • 281
    • 48249126253 scopus 로고    scopus 로고
    • Pathogenesis of listeria-infected Drosophila wntD mutants is associated with elevated levels of the novel immunity gene edin
    • e1000111
    • Gordon MD, Ayres JS, Schneider DS, Nusse R. Pathogenesis of listeria-infected Drosophila wntD mutants is associated with elevated levels of the novel immunity gene edin. PLoS Pathog 2008; 4: e1000111.
    • (2008) PLoS Pathog , vol.4
    • Gordon, M.D.1    Ayres, J.S.2    Schneider, D.S.3    Nusse, R.4
  • 282
    • 41949106708 scopus 로고    scopus 로고
    • Involvement of skeletal muscle gene regulatory network in susceptibility to wound infection following trauma
    • Apidianakis Y, Mindrinos MN, Xiao W, Tegos GP, Papisov MI, Hamblin MR, et al. Involvement of skeletal muscle gene regulatory network in susceptibility to wound infection following trauma. PLoS One 2007; 2: e1356.
    • (2007) PLoS One , vol.2
    • Apidianakis, Y.1    Mindrinos, M.N.2    Xiao, W.3    Tegos, G.P.4    Papisov, M.I.5    Hamblin, M.R.6
  • 283
    • 19344370696 scopus 로고    scopus 로고
    • Functional dissection of an innate immune response by a genome-wide RNAi screen
    • Foley E, O'Farrell PH. Functional dissection of an innate immune response by a genome-wide RNAi screen. PLoS Biol 2004; 2: E203.
    • (2004) PLoS Biol , vol.2
    • Foley, E.1    O'Farrell, P.H.2
  • 285
    • 79960065503 scopus 로고    scopus 로고
    • RNAi screening for host factors involved in viral infection using Drosophila cells
    • Cherry S. RNAi screening for host factors involved in viral infection using Drosophila cells. Methods Mol Biol 2011; 721: 375-82.
    • (2011) Methods Mol Biol , vol.721 , pp. 375-382
    • Cherry, S.1
  • 287
    • 26444472477 scopus 로고    scopus 로고
    • Use of RNA interference in Drosophila S2 cells to identify host pathways controlling compartmentalization of an intracellular pathogen
    • Cheng LW, Viala JP, Stuurman N, Wiedemann U, Vale RD, Portnoy DA. Use of RNA interference in Drosophila S2 cells to identify host pathways controlling compartmentalization of an intracellular pathogen. Proc Natl Acad Sci U S A 2005; 102: 13646-51.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13646-13651
    • Cheng, L.W.1    Viala, J.P.2    Stuurman, N.3    Wiedemann, U.4    Vale, R.D.5    Portnoy, D.A.6
  • 288
    • 42949086499 scopus 로고    scopus 로고
    • RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry
    • e1000021
    • Elwell CA, Ceesay A, Kim JH, Kalman D, Engel JN. RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry. PLoS Pathog 2008; 4: e1000021.
    • (2008) PLoS Pathog , vol.4
    • Elwell, C.A.1    Ceesay, A.2    Kim, J.H.3    Kalman, D.4    Engel, J.N.5
  • 289
  • 291
    • 34248635940 scopus 로고    scopus 로고
    • Changes in periodontal health status are associated with bacterial community shifts as assessed by quantitative 16S cloning and sequencing
    • Kumar PS, Leys EJ, Bryk JM, Martinez FJ, Moeschberger ML, Griffen AL. Changes in periodontal health status are associated with bacterial community shifts as assessed by quantitative 16S cloning and sequencing. J Clin Microbiol 2006; 44: 3665-73.
    • (2006) J Clin Microbiol , vol.44 , pp. 3665-3673
    • Kumar, P.S.1    Leys, E.J.2    Bryk, J.M.3    Martinez, F.J.4    Moeschberger, M.L.5    Griffen, A.L.6
  • 292
    • 23744438967 scopus 로고    scopus 로고
    • Identification of candidate periodontal pathogens and beneficial species by quantitative 16S clonal analysis
    • Kumar PS, Griffen AL, Moeschberger ML, Leys EJ. Identification of candidate periodontal pathogens and beneficial species by quantitative 16S clonal analysis. J Clin Microbiol 2005; 43: 3944-55.
    • (2005) J Clin Microbiol , vol.43 , pp. 3944-3955
    • Kumar, P.S.1    Griffen, A.L.2    Moeschberger, M.L.3    Leys, E.J.4
  • 295
  • 296
    • 0027959873 scopus 로고
    • Transposon-induced pigment-deficient mutants of Porphyromonas gingivalis
    • Hoover CI, Yoshimura F. Transposon-induced pigment-deficient mutants of Porphyromonas gingivalis. FEMS Microbiol Lett 1994; 124: 43-8.
    • (1994) FEMS Microbiol Lett , vol.124 , pp. 43-48
    • Hoover, C.I.1    Yoshimura, F.2
  • 297
    • 0033966030 scopus 로고    scopus 로고
    • Identification and cloning of genes from Porphyromonas gingivalis after mutagenesis with a modified Tn4400 transposon from Bacteroides fragilis
    • Chen T, Dong H, Tang YP, Dallas MM, Malamy MH, Duncan MJ. Identification and cloning of genes from Porphyromonas gingivalis after mutagenesis with a modified Tn4400 transposon from Bacteroides fragilis. Infect Immun 2000; 68: 420-3.
    • (2000) Infect Immun , vol.68 , pp. 420-423
    • Chen, T.1    Dong, H.2    Tang, Y.P.3    Dallas, M.M.4    Malamy, M.H.5    Duncan, M.J.6
  • 298
    • 0036232069 scopus 로고    scopus 로고
    • Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains
    • Shoji M, Ratnayake DB, Shi Y, Kadowaki T, Yamamoto K, Yoshimura F, et al. Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains. Microbiology 2002; 148: 1183-91.
    • (2002) Microbiology , vol.148 , pp. 1183-1191
    • Shoji, M.1    Ratnayake, D.B.2    Shi, Y.3    Kadowaki, T.4    Yamamoto, K.5    Yoshimura, F.6
  • 299
    • 65649142573 scopus 로고    scopus 로고
    • Lipopolysaccharide biosynthesis-related genes are required for colony pigmentation of Porphyromonas gingivalis
    • Sato K, Kido N, Murakami Y, Hoover CI, Nakayama K, Yoshimura F. Lipopolysaccharide biosynthesis-related genes are required for colony pigmentation of Porphyromonas gingivalis. Microbiology 2009; 155: 1282-93.
    • (2009) Microbiology , vol.155 , pp. 1282-1293
    • Sato, K.1    Kido, N.2    Murakami, Y.3    Hoover, C.I.4    Nakayama, K.5    Yoshimura, F.6
  • 300
    • 33746615215 scopus 로고    scopus 로고
    • Enhanced biofilm formation and loss of capsule synthesis: deletion of a putative glycosyltransferase in Porphyromonas gingivalis
    • Davey ME, Duncan MJ. Enhanced biofilm formation and loss of capsule synthesis: deletion of a putative glycosyltransferase in Porphyromonas gingivalis. J Bacteriol 2006; 188: 5510-23.
    • (2006) J Bacteriol , vol.188 , pp. 5510-5523
    • Davey, M.E.1    Duncan, M.J.2
  • 301
    • 79959453401 scopus 로고    scopus 로고
    • Shift in ribonucleotide reductase gene expression in Pseudomonas aeruginosa during infection
    • Sjoberg BM, Torrents E. Shift in ribonucleotide reductase gene expression in Pseudomonas aeruginosa during infection. Infect Immun 2011; 79: 2663-9.
    • (2011) Infect Immun , vol.79 , pp. 2663-2669
    • Sjoberg, B.M.1    Torrents, E.2
  • 302
    • 78650835419 scopus 로고    scopus 로고
    • Identification of mutants with altered phenazine production in Pseudomonas aeruginosa
    • Liang H, Duan J, Sibley CD, Surette MG, Duan K. Identification of mutants with altered phenazine production in Pseudomonas aeruginosa. J Med Microbiol 2011; 60: 22-34.
    • (2011) J Med Microbiol , vol.60 , pp. 22-34
    • Liang, H.1    Duan, J.2    Sibley, C.D.3    Surette, M.G.4    Duan, K.5
  • 303
    • 74749093665 scopus 로고    scopus 로고
    • IscR modulates catalase A (KatA) activity, peroxide resistance and full virulence of Pseudomonas aeruginosa PA14
    • Kim SH, Lee BY, Lau GW, Cho YH. IscR modulates catalase A (KatA) activity, peroxide resistance and full virulence of Pseudomonas aeruginosa PA14. J Microbiol Biotechnol 2009; 19: 1520-6.
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 1520-1526
    • Kim, S.H.1    Lee, B.Y.2    Lau, G.W.3    Cho, Y.H.4
  • 304
    • 21544440596 scopus 로고    scopus 로고
    • KatA, the major catalase, is critical for osmoprotection and virulence in Pseudomonas aeruginosa PA14
    • Lee JS, Heo YJ, Lee JK, Cho YH. KatA, the major catalase, is critical for osmoprotection and virulence in Pseudomonas aeruginosa PA14. Infect Immun 2005; 73: 4399-403.
    • (2005) Infect Immun , vol.73 , pp. 4399-4403
    • Lee, J.S.1    Heo, Y.J.2    Lee, J.K.3    Cho, Y.H.4
  • 305
    • 41949131504 scopus 로고    scopus 로고
    • Unusual properties of catalase A (KatA) of Pseudomonas aeruginosa PA14 are associated with its biofilm peroxide resistance
    • Shin DH, Choi YS, Cho YH. Unusual properties of catalase A (KatA) of Pseudomonas aeruginosa PA14 are associated with its biofilm peroxide resistance. J Bacteriol 2008; 190: 2663-70.
    • (2008) J Bacteriol , vol.190 , pp. 2663-2670
    • Shin, D.H.1    Choi, Y.S.2    Cho, Y.H.3
  • 306
    • 16244393355 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa OxyR is required for full virulence in rodent and insect models of infection and for resistance to human neutrophils
    • Lau GW, Britigan BE, Hassett DJ. Pseudomonas aeruginosa OxyR is required for full virulence in rodent and insect models of infection and for resistance to human neutrophils. Infect Immun 2005; 73: 2550-3.
    • (2005) Infect Immun , vol.73 , pp. 2550-2553
    • Lau, G.W.1    Britigan, B.E.2    Hassett, D.J.3
  • 307
    • 4644238893 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa relA contributes to virulence in Drosophila melanogaster
    • Erickson DL, Lines JL, Pesci EC, Venturi V, Storey DG. Pseudomonas aeruginosa relA contributes to virulence in Drosophila melanogaster. Infect Immun 2004; 72: 5638-45.
    • (2004) Infect Immun , vol.72 , pp. 5638-5645
    • Erickson, D.L.1    Lines, J.L.2    Pesci, E.C.3    Venturi, V.4    Storey, D.G.5
  • 308
    • 80855127680 scopus 로고    scopus 로고
    • The stringent response is essential for Pseudomonas aeruginosa virulence in the rat lung agar bead and Drosophila melanogaster feeding models of infection
    • Vogt SL, Green C, Stevens KM, Day B, Erickson DL, Woods DE, et al. The stringent response is essential for Pseudomonas aeruginosa virulence in the rat lung agar bead and Drosophila melanogaster feeding models of infection. Infect Immun 2011; 79: 4094-104.
    • (2011) Infect Immun , vol.79 , pp. 4094-4104
    • Vogt, S.L.1    Green, C.2    Stevens, K.M.3    Day, B.4    Erickson, D.L.5    Woods, D.E.6
  • 309
    • 0035140125 scopus 로고    scopus 로고
    • Drosophila as a model host for Pseudomonas aeruginosa infection
    • D'Argenio DA, Gallagher LA, Berg CA, Manoil C. Drosophila as a model host for Pseudomonas aeruginosa infection. J Bacteriol 2001; 183: 1466-71.
    • (2001) J Bacteriol , vol.183 , pp. 1466-1471
    • D'Argenio, D.A.1    Gallagher, L.A.2    Berg, C.A.3    Manoil, C.4
  • 310
    • 79952204015 scopus 로고    scopus 로고
    • Inactivation of MuxABC-OpmB transporter system in Pseudomonas aeruginosa leads to increased ampicillin and carbenicillin resistance and decreased virulence
    • Yang L, Chen L, Shen L, Surette M, Duan K. Inactivation of MuxABC-OpmB transporter system in Pseudomonas aeruginosa leads to increased ampicillin and carbenicillin resistance and decreased virulence. J Microbiol 2011; 49: 107-14.
    • (2011) J Microbiol , vol.49 , pp. 107-114
    • Yang, L.1    Chen, L.2    Shen, L.3    Surette, M.4    Duan, K.5
  • 311
    • 0348196787 scopus 로고    scopus 로고
    • In vivo functional genomics of Pseudomonas aeruginosa for high-throughput screening of new virulence factors and antibacterial targets
    • Potvin E, Lehoux DE, Kukavica-Ibrulj I, Richard KL, Sanschagrin F, Lau GW, et al. In vivo functional genomics of Pseudomonas aeruginosa for high-throughput screening of new virulence factors and antibacterial targets. Environ Microbiol 2003; 5: 1294-308.
    • (2003) Environ Microbiol , vol.5 , pp. 1294-1308
    • Potvin, E.1    Lehoux, D.E.2    Kukavica-Ibrulj, I.3    Richard, K.L.4    Sanschagrin, F.5    Lau, G.W.6
  • 312
    • 0344091555 scopus 로고    scopus 로고
    • Virulence factors of the human opportunistic pathogen Serratia marcescens identified by in vivo screening
    • Kurz CL, Chauvet S, Andres E, Aurouze M, Vallet I, Michel GP, et al. Virulence factors of the human opportunistic pathogen Serratia marcescens identified by in vivo screening. EMBO J 2003; 22: 1451-60.
    • (2003) EMBO J , vol.22 , pp. 1451-1460
    • Kurz, C.L.1    Chauvet, S.2    Andres, E.3    Aurouze, M.4    Vallet, I.5    Michel, G.P.6
  • 313
    • 1842529395 scopus 로고    scopus 로고
    • In vivo RNA interference analysis reveals an unexpected role for GNBP1 in the defense against Grampositive bacterial infection in Drosophila adults
    • Pili-Floury S, Leulier F, Takahashi K, Saigo K, Samain E, Ueda R, et al. In vivo RNA interference analysis reveals an unexpected role for GNBP1 in the defense against Grampositive bacterial infection in Drosophila adults. J Biol Chem 2004; 279: 12848-53.
    • (2004) J Biol Chem , vol.279 , pp. 12848-12853
    • Pili-Floury, S.1    Leulier, F.2    Takahashi, K.3    Saigo, K.4    Samain, E.5    Ueda, R.6
  • 314
    • 79955817261 scopus 로고    scopus 로고
    • Cofilin regulator 14-3-3{zeta} is an evolutionarily conserved protein required for phagocytosis and microbial resistance
    • Ulvila J, Vanha-Aho LM, Kleino A, Vaha-Makila M, Vuoksio M, Eskelinen S, et al. Cofilin regulator 14-3-3{zeta} is an evolutionarily conserved protein required for phagocytosis and microbial resistance. J Leukoc Biol 2011; 89: 649-59
    • (2011) J Leukoc Biol , vol.89 , pp. 649-659
    • Ulvila, J.1    Vanha-Aho, L.M.2    Kleino, A.3    Vaha-Makila, M.4    Vuoksio, M.5    Eskelinen, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.