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Volumn 2, Issue 3, 2011, Pages 125-141

Cleavage of PGRP-LC receptor in the Drosophila IMD pathway in response to live bacterial infection in S2 cells

Author keywords

Drosophila innate immune activation; Elastase; Immune deficiency (IMD) signaling pathway; Matrix metalloproteinase; pgrp lc; Signal transduction

Indexed keywords

ELASTASE; GELATINASE A; PEPTIDOGLYCAN RECOGNITION PROTEIN; TOLL LIKE RECEPTOR;

EID: 84930474287     PISSN: 19382030     EISSN: 19382049     Source Type: Journal    
DOI: 10.4161/self.17882     Document Type: Article
Times cited : (12)

References (100)
  • 1
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • PMID:17201680
    • Lemaitre B, Hoffmann J. The host defense of Drosophila melanogaster. Annu Rev Immunol 2007; 25:697-743; PMID:17201680; http://dx.doi.org/10.1146/annurev.immunol.25.022106.141615.
    • (2007) Annu Rev Immunol , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 2
    • 2442715852 scopus 로고    scopus 로고
    • Drosophila: The genetics of innate immune recognition and response
    • PMID:15032585
    • Brennan CA, Anderson KV. Drosophila: the genetics of innate immune recognition and response. Annu Rev Immunol 2004; 22:457-83; PMID:15032585; http://dx.doi.org/10.1146/annurev.immunol.22.012703.104626.
    • (2004) Annu Rev Immunol , vol.22 , pp. 457-483
    • Brennan, C.A.1    Anderson, K.V.2
  • 3
    • 11844263877 scopus 로고    scopus 로고
    • Sensing and signaling during infection in Drosophila
    • PMID:15653304
    • Royet J, Reichhart JM, Hoffmann JA. Sensing and signaling during infection in Drosophila. Curr Opin Immunol 2005; 17:11-7; PMID:15653304; http://dx.doi.org/10.1016/j.coi.2004.12.002.
    • (2005) Curr Opin Immunol , vol.17 , pp. 11-17
    • Royet, J.1    Reichhart, J.M.2    Hoffmann, J.A.3
  • 4
    • 0033578917 scopus 로고    scopus 로고
    • Constitutive activation of toll-mediated antifungal defense in serpin- deficient Drosophila
    • PMID:10489372
    • Levashina EA, Langley E, Green C, Gubb D, Ashburner M, Hoffmann JA, et al. Constitutive activation of toll-mediated antifungal defense in serpin- deficient Drosophila. Science 1999; 285:1917-9; PMID:10489372; http://dx.doi.org/10.1126/science.285.5435.1917.
    • (1999) Science , vol.285 , pp. 1917-1919
    • Levashina, E.A.1    Langley, E.2    Green, C.3    Gubb, D.4    Ashburner, M.5    Hoffmann, J.A.6
  • 5
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • ID:11742401
    • 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; PMID:11742401; http://dx.doi.org/10.1038/414756a.
    • (2001) Nature , vol.414 , pp. 756-759
    • Michel, T.1    Reichhart, J.M.2    Hoffmann, J.A.3    Royet, J.4
  • 6
    • 0037025213 scopus 로고    scopus 로고
    • Activation of Drosophila Toll during fungal infectionby a blood serine protease
    • PMID:12098703
    • Ligoxygakis P, Pelte N, Hoffmann JA, Reichhart JM. Activation of Drosophila Toll during fungal infectionby a blood serine protease. Science 2002; 297:114-6; PMID:12098703; http://dx.doi.org/10.1126/science.1072391.
    • (2002) Science , vol.297 , pp. 114-116
    • Ligoxygakis, P.1    Pelte, N.2    Hoffmann, J.A.3    Reichhart, J.M.4
  • 7
    • 0345731463 scopus 로고    scopus 로고
    • Dual activation of the Drosophila toll pathway by two pattern recognition receptors
    • PMID:14684822
    • 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; PMID:14684822; http://dx.doi.org/10.1126/science.1085432.
    • (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
  • 8
    • 33750218690 scopus 로고    scopus 로고
    • Sensing of Gram-positive bacteria in Drosophila: GNBP1 is needed to process and present peptidoglycan to PGRP-SA
    • PMID:17024181
    • 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; PMID:17024181; http://dx.doi.org/10.1038/sj.emboj.7601363.
    • (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
  • 9
    • 9244251126 scopus 로고    scopus 로고
    • Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Grampositive bacteria
    • PMID:15448690
    • 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 Grampositive bacteria. Nat Immunol 2004; 5:1175-80; PMID:15448690; http://dx.doi.org/10.1038/ni1123
    • (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
  • 10
    • 39449112512 scopus 로고    scopus 로고
    • Toll-like receptors--taking an evolutionary approach
    • PMID:18227810
    • Leulier F, Lemaitre B. Toll-like receptors--taking an evolutionary approach. Nat Rev Genet 2008; 9:165-78; PMID:18227810; http://dx.doi.org/10.1038/nrg2303
    • (2008) Nat Rev Genet , vol.9 , pp. 165-178
    • Leulier, F.1    Lemaitre, B.2
  • 11
    • 29744438644 scopus 로고    scopus 로고
    • A Spätzle-processing enzyme required for toll signaling activation in Drosophila innate immunity
    • PMID:16399077
    • Jang IH, Chosa N, Kim SH, Nam HJ, Lemaitre B, Ochiai M, et al. A Spätzle-processing enzyme required for toll signaling activation in Drosophila innate immunity. Dev Cell 2006; 10:45-55; PMID:16399077; http://dx.doi.org/10.1016/j.devcel.2005.11.013
    • (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
  • 12
    • 33646037067 scopus 로고    scopus 로고
    • Drosophila immunity: A large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation
    • PMID:16631589
    • 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; PMID:16631589; http://dx.doi.org/10.1016/j.cub.2006.03.020
    • (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
  • 13
    • 33845666959 scopus 로고    scopus 로고
    • Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors
    • PMID:17190605
    • 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; PMID:17190605; http://dx.doi.org/10.1016/j.cell.2006.10.046
    • (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
  • 14
    • 0041989575 scopus 로고    scopus 로고
    • Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling
    • PMID:12872120
    • Weber AN, Tauszig-Delamasure S, Hoffmann JA, Lelièvre E, Gascan H, Ray KP, et al. Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling. Nat Immunol 2003; 4:794-800; PMID:12872120; http://dx.doi.org/10.1038/ni955
    • (2003) Nat Immunol , vol.4 , pp. 794-800
    • Weber, A.N.1    Tauszig-Delamasure, S.2    Hoffmann, J.A.3    Lelièvre, E.4    Gascan, H.5    Ray, K.P.6
  • 15
    • 3042645409 scopus 로고    scopus 로고
    • Multimerization and interaction of Toll and Spätzle in Drosophila
    • PMID:15197269
    • Hu X, Yagi Y, Tanji T, Zhou S, Ip YT. Multimerization and interaction of Toll and Spätzle in Drosophila. Proc Natl Acad Sci U S A 2004; 101:9369-74; PMID:15197269; http://dx.doi.org/10.1073/pnas.0307062101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9369-9374
    • Hu, X.1    Yagi, Y.2    Tanji, T.3    Zhou, S.4    Ip, Y.T.5
  • 16
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein
    • PMID:11912488
    • Gottar M, Gobert V, Michel T, Belvin M, Duyk G, Hoffmann JA, et al. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 2002; 416:640-4; PMID:11912488; http://dx.doi.org/10.1038/nature734
    • (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
  • 17
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for
    • PMID:11912489
    • Rämet 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; PMID:11912489; http://dx.doi.org/10.1038/nature735
    • (2002) E. Coli. Nature , vol.416 , pp. 644-648
    • Rämet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 18
    • 0037066464 scopus 로고    scopus 로고
    • Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila
    • PMID:11872802
    • Choe KM, Werner T, Stöven S, Hultmark D, Anderson KV. Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science 2002; 296:359-62; PMID:11872802; http://dx.doi.org/10.1126/science.1070216
    • (2002) Science , vol.296 , pp. 359-362
    • Choe, K.M.1    Werner, T.2    Stöven, S.3    Hultmark, D.4    Anderson, K.V.5
  • 19
    • 0037108754 scopus 로고    scopus 로고
    • Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein- LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae
    • PMID:12359879
    • Takehana A, Katsuyama T, Yano T, Oshima Y, Takada H, Aigaki T, et al. Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein- LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae. Proc Natl Acad Sci U S A 2002; 99:13705-10; PMID:12359879; http://dx.doi.org/10.1073/pnas.212301199
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13705-13710
    • Takehana, A.1    Katsuyama, T.2    Yano, T.3    Oshima, Y.4    Takada, H.5    Aigaki, T.6
  • 20
    • 0038036294 scopus 로고    scopus 로고
    • Functional diversity of the Drosophila PGRP-LC gene cluster in the response to lipopolysaccharide and peptidoglycan
    • PMID:12777387
    • Werner T, Borge-Renberg K, Mellroth P, Steiner H, Hultmark D. Functional diversity of the Drosophila PGRP-LC gene cluster in the response to lipopolysaccharide and peptidoglycan. J Biol Chem 2003; 278:26319-22; PMID:12777387; http://dx.doi.org/10.1074/jbc.C300184200
    • (2003) J Biol Chem , vol.278 , pp. 26319-26322
    • Werner, T.1    Borge-Renberg, K.2    Mellroth, P.3    Steiner, H.4    Hultmark, D.5
  • 21
    • 0038664357 scopus 로고    scopus 로고
    • The Drosophila immune system detects bacteria through specific peptidoglycan recognition
    • PMID:12692550
    • Leulier F, Parquet C, Pili-Floury S, Ryu JH, Caroff M, Lee WJ, et al. The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nat Immunol 2003; 4:478-84; PMID:12692550; http://dx.doi.org/10.1038/ni922
    • (2003) Nat Immunol , vol.4 , pp. 478-484
    • Leulier, F.1    Parquet, C.2    Pili-Floury, S.3    Ryu, J.H.4    Caroff, M.5    Lee, W.J.6
  • 22
    • 2442456719 scopus 로고    scopus 로고
    • Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway
    • PMID:15142531
    • Kaneko T, Goldman WE, Mellroth P, Steiner H, Fukase K, Kusumoto S, et al. Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity 2004; 20:637-49; PMID:15142531; http://dx.doi.org/10.1016/S1074-7613(04)00104-9
    • (2004) Immunity , vol.20 , pp. 637-649
    • Kaneko, T.1    Goldman, W.E.2    Mellroth, P.3    Steiner, H.4    Fukase, K.5    Kusumoto, S.6
  • 23
    • 33745225236 scopus 로고    scopus 로고
    • PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan
    • PMID:16767093
    • Kaneko T, Yano T, Aggarwal K, Lim JH, Ueda K, Oshima Y, et al. PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan. Nat Immunol 2006; 7:715-23; PMID:16767093; http://dx.doi.org/10.1038/ni1356
    • (2006) Nat Immunol , vol.7 , pp. 715-723
    • Kaneko, T.1    Yano, T.2    Aggarwal, K.3    Lim, J.H.4    Ueda, K.5    Oshima, Y.6
  • 24
    • 12844279852 scopus 로고    scopus 로고
    • Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor
    • PMID:15657141
    • 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; PMID:15657141; http://dx.doi.org/10.1073/pnas.0404952102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1122-1126
    • Choe, K.M.1    Lee, H.2    Anderson, K.V.3
  • 25
    • 18144401356 scopus 로고    scopus 로고
    • Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro
    • PMID:15843462
    • Mellroth P, Karlsson J, Håkansson J, Schultz N, Goldman WE, Steiner H. Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro. Proc Natl Acad Sci U S A 2005; 102:6455-60; PMID:15843462; http://dx.doi.org/10.1073/pnas.0407559102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6455-6460
    • Mellroth, P.1    Karlsson, J.2    Håkansson, J.3    Schultz, N.4    Goldman, W.E.5    Steiner, H.6
  • 26
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • PMID:11687497
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17:463-516; PMID:11687497; http://dx.doi.org/10.1146/annurev.cellbio.17.1.463
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 27
    • 1642279517 scopus 로고    scopus 로고
    • Protease-activated receptors: Contribution to physiology and disease
    • PMID:15044683
    • Ossovskaya VS, Bunnett NW. Protease-activated receptors: contribution to physiology and disease. Physiol Rev 2004; 84:579-621; PMID:15044683; http://dx.doi.org/10.1152/physrev.00028.2003
    • (2004) Physiol Rev , vol.84 , pp. 579-621
    • Ossovskaya, V.S.1    Bunnett, N.W.2
  • 28
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • PMID:11990853
    • Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002; 2:161-74; PMID:11990853; http://dx.doi.org/10.1038/nrc745
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 29
    • 0036470428 scopus 로고    scopus 로고
    • Evolution of enzyme cascades from embryonic development to blood coagulation
    • PMID:11852243
    • Krem MM, Di Cera E. Evolution of enzyme cascades from embryonic development to blood coagulation. Trends Biochem Sci 2002; 27:67-74; PMID:11852243; http://dx.doi.org/10.1016/S0968-0004(01)02007-2
    • (2002) Trends Biochem Sci , vol.27 , pp. 67-74
    • Krem, M.M.1    di Cera, E.2
  • 30
    • 0035883151 scopus 로고    scopus 로고
    • NF-kappaB signaling pathways in mammalian and insect innate immunity
    • PMID:11562344
    • Silverman N, Maniatis T. NF-kappaB signaling pathways in mammalian and insect innate immunity. Genes Dev 2001; 15:2321-42; PMID:11562344; http://dx.doi.org/10.1101/gad.909001
    • (2001) Genes Dev , vol.15 , pp. 2321-2342
    • Silverman, N.1    Maniatis, T.2
  • 31
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • PMID:9585238
    • Belaaouaj A, McCarthy R, Baumann M, Gao Z, Ley TJ, Abraham SN, et al. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat Med 1998; 4:615-8; PMID:9585238; http://dx.doi.org/10.1038/nm0598-615
    • (1998) Nat Med , vol.4 , pp. 615-618
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5    Abraham, S.N.6
  • 32
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • PMID:10426423
    • Kanost MR. Serine proteinase inhibitors in arthropod immunity. Dev Comp Immunol 1999; 23:291-301; PMID:10426423; http://dx.doi.org/10.1016/S0145-305X(99)00012-9
    • (1999) Dev Comp Immunol , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 33
    • 0036183148 scopus 로고    scopus 로고
    • The coagulation of insect hemolymph
    • PMID:11915949
    • Theopold U, Li D, Fabbri M, Scherfer C, Schmidt O. The coagulation of insect hemolymph. Cell Mol Life Sci 2002; 59:363-72; PMID:11915949; http://dx.doi.org/10.1007/s00018-002-8428-4
    • (2002) Cell Mol Life Sci , vol.59 , pp. 363-372
    • Theopold, U.1    Li, D.2    Fabbri, M.3    Scherfer, C.4    Schmidt, O.5
  • 34
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidaseactivating system in invertebrate immunity
    • PMID:9523106
    • Söderhäll K, Cerenius L. Role of the prophenoloxidaseactivating system in invertebrate immunity. Curr Opin Immunol 1998; 10:23-8; PMID:9523106; http://dx.doi.org/10.1016/S0952-7915(98)80026-5
    • (1998) Curr Opin Immunol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 35
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase
    • PMID:10947984
    • Belaaouaj A, Kim KS, Shapiro SD. Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science 2000; 289:1185-8; PMID:10947984; http://dx.doi.org/10.1126/science.289.5482.1185
    • (2000) Science , vol.289 , pp. 1185-1188
    • Belaaouaj, A.1    Kim, K.S.2    Shapiro, S.D.3
  • 36
    • 0001878583 scopus 로고    scopus 로고
    • Overview of the complement system
    • Volanakis JE, Frank MM, eds, New York: Marcel Dekker, Inc
    • Volanakis JE. Overview of the complement system. In: Volanakis JE, Frank MM, eds. The Human Complement System in Health and Disease. New York: Marcel Dekker, Inc., 1998:9-32
    • (1998) The Human Complement System In Health and Disease , pp. 9-32
    • Volanakis, J.E.1
  • 37
    • 0034144636 scopus 로고    scopus 로고
    • Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G
    • PMID:10714686
    • Tkalcevic J, Novelli M, Phylactides M, Iredale JP, Segal AW, Roes J. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity 2000; 12:201-10; PMID:10714686; http://dx.doi.org/10.1016/S1074-7613(00)80173-9
    • (2000) Immunity , vol.12 , pp. 201-210
    • Tkalcevic, J.1    Novelli, M.2    Phylactides, M.3    Iredale, J.P.4    Segal, A.W.5    Roes, J.6
  • 38
    • 0035423403 scopus 로고    scopus 로고
    • Essential role of neutrophils in the initiation and progression of a murine model of rheumatoid arthritis
    • PMID:11466382
    • Wipke BT, Allen PM. Essential role of neutrophils in the initiation and progression of a murine model of rheumatoid arthritis. J Immunol 2001; 167:1601-8; PMID:11466382
    • (2001) J Immunol , vol.167 , pp. 1601-1608
    • Wipke, B.T.1    Allen, P.M.2
  • 39
    • 0037074016 scopus 로고    scopus 로고
    • Conversion of proepithelin to epithelins: Roles of SLPI and elastase in host defense and wound repair
    • PMID:12526812
    • Zhu J, Nathan C, Jin W, Sim D, Ashcroft GS, Wahl SM, et al. Conversion of proepithelin to epithelins: roles of SLPI and elastase in host defense and wound repair. Cell 2002; 111:867-78; PMID:12526812; http://dx.doi.org/10.1016/S0092-8674(02)01141-8
    • (2002) Cell , vol.111 , pp. 867-878
    • Zhu, J.1    Nathan, C.2    Jin, W.3    Sim, D.4    Ashcroft, G.S.5    Wahl, S.M.6
  • 40
    • 14844292593 scopus 로고    scopus 로고
    • Blood coagulation and its regulation by anticoagulant pathways: Genetic pathogenesis of bleeding and thrombotic diseases
    • PMID:15715678
    • Dahlbäck B. Blood coagulation and its regulation by anticoagulant pathways: genetic pathogenesis of bleeding and thrombotic diseases. J Intern Med 2005; 257:209-23; PMID:15715678; http://dx.doi.org/10.1111/j.1365-2796.2004.01444.x
    • (2005) J Intern Med , vol.257 , pp. 209-223
    • Dahlbäck, B.1
  • 41
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: A renewed sense of self
    • PMID:11951032
    • Matzinger P. The danger model: a renewed sense of self. Science 2002; 296:301-5; PMID:11951032; http://dx.doi.org/10.1126/science.1071059
    • (2002) Science , vol.296 , pp. 301-305
    • Matzinger, P.1
  • 42
    • 18144379144 scopus 로고    scopus 로고
    • Conditional signaling by Toll-like receptor 4
    • PMID:15738005
    • Brunn GJ, Bungum MK, Johnson GB, Platt JL. Conditional signaling by Toll-like receptor 4. FASEB J 2005; 19:872-4; PMID:15738005
    • (2005) FASEB J , vol.19 , pp. 872-874
    • Brunn, G.J.1    Bungum, M.K.2    Johnson, G.B.3    Platt, J.L.4
  • 43
    • 40449089747 scopus 로고    scopus 로고
    • Infection-induced proteolysis of PGRP-LC controls the IMD activation and melanization cascades in Drosophila
    • PMID:18308747
    • Schmidt RL, Trejo TR, Plummer TB, Platt JL, Tang AH. Infection-induced proteolysis of PGRP-LC controls the IMD activation and melanization cascades in Drosophila. FASEB J 2008; 22:918-29; PMID:18308747; http://dx.doi.org/10.1096/fj.06-7907com
    • (2008) FASEB J , vol.22 , pp. 918-929
    • Schmidt, R.L.1    Trejo, T.R.2    Plummer, T.B.3    Platt, J.L.4    Tang, A.H.5
  • 44
    • 18044400563 scopus 로고    scopus 로고
    • Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis
    • PMID:11703941
    • 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; PMID:11703941; http://dx.doi.org/10.1016/S1534-5807(01)00059-4
    • (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
  • 45
    • 0036141954 scopus 로고    scopus 로고
    • Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections
    • PMID:11743586
    • 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; PMID:11743586; http://dx.doi.org/10.1038/ni747
    • (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
  • 46
    • 0037279629 scopus 로고    scopus 로고
    • Analysis of Ras-induced overproliferation in Drosophila hemocytes
    • PMID:12586708
    • Asha H, Nagy I, Kovacs G, Stetson D, Ando I, Dearolf CR. Analysis of Ras-induced overproliferation in Drosophila hemocytes. Genetics 2003; 163:203-15; PMID:12586708
    • (2003) Genetics , vol.163 , pp. 203-215
    • Asha, H.1    Nagy, I.2    Kovacs, G.3    Stetson, D.4    Ando, I.5    Dearolf, C.R.6
  • 47
    • 0029054158 scopus 로고
    • Pentobarbital-induced changes in Drosophila glutathione S-transferase D21 mRNA stability
    • PMID:7775439
    • Tang AH, Tu C-PD. Pentobarbital-induced changes in Drosophila glutathione S-transferase D21 mRNA stability. J Biol Chem 1995; 270:13819-25; PMID:7775439; http://dx.doi.org/10.1074/jbc.270.23.13819
    • (1995) J Biol Chem , vol.270 , pp. 13819-13825
    • Tang, A.H.1    Tu, C.-P.D.2
  • 48
    • 0028112999 scopus 로고
    • Biochemical characterization of Drosophila dlutathione S-transferase D1 and D21
    • PMID:7961718
    • Tang AH, Tu C-PD. Biochemical characterization of Drosophila dlutathione S-transferase D1 and D21. J Biol Chem 1994; 269:27876-84; PMID:7961718
    • (1994) J Biol Chem , vol.269 , pp. 27876-27884
    • Tang, A.H.1    Tu, C.-P.D.2
  • 49
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • PMID:10612281
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999; 20:3551-67; PMID:10612281; http://dx.doi.org/10.1002/(SICI)1522-2683(19991201)20:183551::AIDELPS35513.0.CO;2-2
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 50
    • 0037472685 scopus 로고    scopus 로고
    • Serine proteases and their homologs in the Drosophila melanogaster genome: An initial analysis of sequence conservation and phylogenetic relationships
    • PMID:12568721
    • Ross J, Jiang H, Kanost MR, Wang Y. Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene 2003; 304:117-31; PMID:12568721; http://dx.doi.org/10.1016/S0378-1119(02)01187-3
    • (2003) Gene , vol.304 , pp. 117-131
    • Ross, J.1    Jiang, H.2    Kanost, M.R.3    Wang, Y.4
  • 51
    • 0037013856 scopus 로고    scopus 로고
    • The Toll and Imd pathways are the major regulators of the immune response in Drosophila
    • PMID:12032070
    • 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; PMID:12032070; http://dx.doi.org/10.1093/emboj/21.11.2568
    • (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
  • 52
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • PMID:14603309
    • Hoffmann JA. The immune response of Drosophila. Nature 2003; 426:33-8; PMID:14603309; http://dx.doi.org/10.1038/nature02021
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffmann, J.A.1
  • 53
    • 0037094084 scopus 로고    scopus 로고
    • Receptormediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4
    • PMID:11994480
    • Johnson GB, Brunn GJ, Kodaira Y, Platt JL. Receptormediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4. J Immunol 2002; 168:5233-9; PMID:11994480
    • (2002) J Immunol , vol.168 , pp. 5233-5239
    • Johnson, G.B.1    Brunn, G.J.2    Kodaira, Y.3    Platt, J.L.4
  • 54
    • 0032851160 scopus 로고    scopus 로고
    • Functions of cell surface heparan sulfate proteoglycans
    • PMID:10872465
    • Bernfield M, Götte M, Park PW, Reizes O, Fitzgerald ML, Lincecum J, et al. Functions of cell surface heparan sulfate proteoglycans. Annu Rev Biochem 1999; 68:729-77; PMID:10872465; http://dx.doi.org/10.1146/annurev.biochem.68.1.729
    • (1999) Annu Rev Biochem , vol.68 , pp. 729-777
    • Bernfield, M.1    Götte, M.2    Park, P.W.3    Reizes, O.4    Fitzgerald, M.L.5    Lincecum, J.6
  • 55
    • 0034643323 scopus 로고    scopus 로고
    • Specificities of heparan sulphate proteoglycans in developmental processes
    • PMID:10783877
    • Perrimon N, Bernfield M. Specificities of heparan sulphate proteoglycans in developmental processes. Nature 2000; 404:725-8; PMID:10783877; http://dx.doi.org/10.1038/35008000
    • (2000) Nature , vol.404 , pp. 725-728
    • Perrimon, N.1    Bernfield, M.2
  • 56
    • 0034707667 scopus 로고    scopus 로고
    • The elusive functions of proteoglycans: In vivo veritas
    • PMID:10648554
    • Lander AD, Selleck SB. The elusive functions of proteoglycans: in vivo veritas. J Cell Biol 2000; 148:227-32; PMID:10648554; http://dx.doi.org/10.1083/jcb.148.2.227
    • (2000) J Cell Biol , vol.148 , pp. 227-232
    • Lander, A.D.1    Selleck, S.B.2
  • 57
    • 0025911987 scopus 로고
    • Regulation of murine splenocyte responses by heparan sulfate
    • PMID:1830063
    • Wrenshall LE, Cerra FB, Carlson A, Bach FH, Platt JL. Regulation of murine splenocyte responses by heparan sulfate. J Immunol 1991; 147:455-9; PMID:1830063
    • (1991) J Immunol , vol.147 , pp. 455-459
    • Wrenshall, L.E.1    Cerra, F.B.2    Carlson, A.3    Bach, F.H.4    Platt, J.L.5
  • 58
    • 0029764505 scopus 로고    scopus 로고
    • Shedding of heparan sulfate proteoglycan by stimulated endothelial cells: Evidence for proteolysis of cell-surface molecules
    • PMID:8816917
    • Ihrcke NS, Platt JL. Shedding of heparan sulfate proteoglycan by stimulated endothelial cells: evidence for proteolysis of cell-surface molecules. J Cell Physiol 1996; 168:625-37; PMID:8816917;http://dx.doi.org/10.1002/(SICI)1097-4652(199609)168:3625::AID-JCP153.0.CO;2-Y
    • (1996) J Cell Physiol , vol.168 , pp. 625-637
    • Ihrcke, N.S.1    Platt, J.L.2
  • 59
    • 0348048803 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins (PGRPs)
    • PMID:14698226
    • Dziarski R. Peptidoglycan recognition proteins (PGRPs). Mol Immunol 2004; 40:877-86; PMID:14698226; http://dx.doi.org/10.1016/j.molimm.2003.10.011
    • (2004) Mol Immunol , vol.40 , pp. 877-886
    • Dziarski, R.1
  • 60
    • 34247134954 scopus 로고    scopus 로고
    • Peptidoglycan detection by mammals and flies
    • PMID:17383922
    • Chaput C, Boneca IG. Peptidoglycan detection by mammals and flies. Microbes Infect 2007; 9:637-47; PMID:17383922; http://dx.doi.org/10.1016/j.micinf.2007.01.022
    • (2007) Microbes Infect , vol.9 , pp. 637-647
    • Chaput, C.1    Boneca, I.G.2
  • 61
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • PMID:15286728
    • Parks WC, Wilson CL, López-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 2004; 4:617-29; PMID:15286728; http://dx.doi.org/10.1038/nri1418
    • (2004) Nat Rev Immunol , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    López-Boado, Y.S.3
  • 62
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • PMID:17318226
    • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 2007; 8:221-33; PMID:17318226; http://dx.doi.org/10.1038/nrm2125
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 63
    • 0037239819 scopus 로고    scopus 로고
    • Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development
    • PMID:12530966
    • Page-McCaw A, Serano J, Santé JM, Rubin GM. Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development. Dev Cell 2003; 4:95-106; PMID:12530966; http://dx.doi.org/10.1016/S1534-5807(02)00400-8
    • (2003) Dev Cell , vol.4 , pp. 95-106
    • Page-McCaw, A.1    Serano, J.2    Santé, J.M.3    Rubin, G.M.4
  • 64
    • 0037189532 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane- bound matrix metalloproteinase with tissuespecific expression
    • PMID:11967260
    • Llano E, Adam G, Pendás AM, Quesada V, Sánchez LM, Santamariá I, et al. Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane- bound matrix metalloproteinase with tissuespecific expression. J Biol Chem 2002; 277:23321-9; PMID:11967260; http://dx.doi.org/10.1074/jbc.M200121200
    • (2002) J Biol Chem , vol.277 , pp. 23321-23329
    • Llano, E.1    Adam, G.2    Pendás, A.M.3    Quesada, V.4    Sánchez, L.M.5    Santamariá, I.6
  • 65
    • 0000926038 scopus 로고    scopus 로고
    • Recent advances in research on the insect prophenoloxidase cascade
    • In: Brey PT, Hultmark D, eds., London: Chapman and Hall
    • Ashida M, Brey PT. Recent advances in research on the insect prophenoloxidase cascade. In: Brey PT, Hultmark D, eds. Molecular Mechanisms of Immune Response in Insects. London: Chapman and Hall, 1998:135-72
    • (1998) Molecular Mechanisms of Immune Response In Insects , pp. 135-172
    • Ashida, M.1    Brey, P.T.2
  • 66
    • 18644376155 scopus 로고    scopus 로고
    • An immune-responsive Serpin regulates the melanization cascade in Drosophila
    • PMID:12408809
    • De Gregorio E, Han SJ, Lee WJ, Baek MJ, Osaki T, Kawabata S, et al. An immune-responsive Serpin regulates the melanization cascade in Drosophila. Dev Cell 2002; 3:581-92; PMID:12408809; http://dx.doi.org/10.1016/S1534-5807(02)00267-8
    • (2002) Dev Cell , vol.3 , pp. 581-592
    • de Gregorio, E.1    Han, S.J.2    Lee, W.J.3    Baek, M.J.4    Osaki, T.5    Kawabata, S.6
  • 67
    • 0026488402 scopus 로고
    • A surface protease and the invasive character of plague
    • PMID:1439793
    • Sodeinde OA, Subrahmanyam YV, Stark K, Quan T, Bao Y, Goguen JD. A surface protease and the invasive character of plague. Science 1992; 258:1004-7; PMID:1439793; http://dx.doi.org/10.1126/science.1439793
    • (1992) Science , vol.258 , pp. 1004-1007
    • Sodeinde, O.A.1    Subrahmanyam, Y.V.2    Stark, K.3    Quan, T.4    Bao, Y.5    Goguen, J.D.6
  • 68
    • 0026939349 scopus 로고
    • Prevalence of ompT among Escherichia coli isolates of human origin
    • MID:1427004
    • Lundrigan MD, Webb RM. Prevalence of ompT among Escherichia coli isolates of human origin. FEMS Microbiol Lett 1992; 76:51-6; PMID:1427004; http://dx.doi.org/10.1111/j.1574-6968.1992.tb05438.x
    • (1992) FEMS Microbiol Lett , vol.76 , pp. 51-56
    • Lundrigan, M.D.1    Webb, R.M.2
  • 69
    • 0031831037 scopus 로고    scopus 로고
    • Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli
    • PMID:9683502
    • Stumpe S, Schmid R, Stephens DL, Georgiou G, Bakker EP. Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. J Bacteriol 1998; 180:4002-6; PMID:9683502
    • (1998) J Bacteriol , vol.180 , pp. 4002-4006
    • Stumpe, S.1    Schmid, R.2    Stephens, D.L.3    Georgiou, G.4    Bakker, E.P.5
  • 70
    • 0033919460 scopus 로고    scopus 로고
    • A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to α-helical antimicrobial peptides
    • PMID:10869088
    • Guina T, Yi EC, Wang H, Hackett M, Miller SI. A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to α-helical antimicrobial peptides. J Bacteriol 2000; 182:4077-86; PMID:10869088; http://dx.doi.org/10.1128/JB.182.14.4077-4086.2000
    • (2000) J Bacteriol , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 71
    • 0036796983 scopus 로고    scopus 로고
    • Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B
    • PMID:12356789
    • Ulvatne H, Haukland HH, Samuelsen O, Krämer M, Vorland LH. Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B. J Antimicrob Chemother 2002; 50:461-7; PMID:12356789; http://dx.doi.org/10.1093/jac/dkf156
    • (2002) J Antimicrob Chemother , vol.50 , pp. 461-467
    • Ulvatne, H.1    Haukland, H.H.2    Samuelsen, O.3    Krämer, M.4    Vorland, L.H.5
  • 72
    • 0036227315 scopus 로고    scopus 로고
    • Lipopolysaccharide regions involved in the activation of Escherichia coli outer membrane protease OmpT
    • PMID:11895445
    • Kramer RA, Brandenburg K, Vandeputte-Rutten L, Werkhoven M, Gros P, Dekker N, et al. Lipopolysaccharide regions involved in the activation of Escherichia coli outer membrane protease OmpT. Eur J Biochem 2002; 269:1746-52; PMID:11895445; http://dx.doi.org/10.1046/j.1432-1327.2002.02820.x
    • (2002) Eur J Biochem , vol.269 , pp. 1746-1752
    • Kramer, R.A.1    Brandenburg, K.2    Vandeputte-Rutten, L.3    Werkhoven, M.4    Gros, P.5    Dekker, N.6
  • 73
    • 4344603667 scopus 로고    scopus 로고
    • Substrate specificity of the Escherichia coli outer membrane protease OmpT
    • PMID:15317797
    • McCarter JD, Stephens D, Shoemaker K, Rosenberg S, Kirsch JF, Georgiou G. Substrate specificity of the Escherichia coli outer membrane protease OmpT. J Bacteriol 2004; 186:5919-25; PMID:15317797; http://dx.doi.org/10.1128/JB.186.17.5919-5925.2004
    • (2004) J Bacteriol , vol.186 , pp. 5919-5925
    • McCarter, J.D.1    Stephens, D.2    Shoemaker, K.3    Rosenberg, S.4    Kirsch, J.F.5    Georgiou, G.6
  • 74
    • 0024965999 scopus 로고
    • The role of easter, an apparent serine protease, in organizing the dorsal-ventral pattern of the Drosophila embryo
    • PMID:2492450
    • Chasan R, Anderson KV. The role of easter, an apparent serine protease, in organizing the dorsal-ventral pattern of the Drosophila embryo. Cell 1989; 56:391-400; PMID:2492450; http://dx.doi.org/10.1016/0092-8674(89)90242-0
    • (1989) Cell , vol.56 , pp. 391-400
    • Chasan, R.1    Anderson, K.V.2
  • 75
    • 21044432369 scopus 로고    scopus 로고
    • MMP-1 activation by serine proteases and MMP-10 induces human capillary tubular network collapse and regression in 3D collagen matrices
    • PMID:15870107
    • Saunders WB, Bayless KJ, Davis GE. MMP-1 activation by serine proteases and MMP-10 induces human capillary tubular network collapse and regression in 3D collagen matrices. J Cell Sci 2005; 118:2325-40; PMID:15870107; http://dx.doi.org/10.1242/jcs.02360
    • (2005) J Cell Sci , vol.118 , pp. 2325-2340
    • Saunders, W.B.1    Bayless, K.J.2    Davis, G.E.3
  • 76
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • PMID:11951031
    • Medzhitov R, Janeway CA Jr. Decoding the patterns of self and nonself by the innate immune system. Science 2002; 296:298-300; PMID:11951031; http://dx.doi.org/10.1126/science.1068883
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 77
    • 0036212849 scopus 로고    scopus 로고
    • Innate immune recognition
    • PMID:11861602
    • Janeway CA Jr., Medzhitov R. Innate immune recognition. Annu Rev Immunol 2002; 20:197-216; PMID:11861602; http://dx.doi.org/10.1146/annurev.immunol.20.083001.084359
    • (2002) Annu Rev Immunol , vol.20 , pp. 197-216
    • Janeway Jr., C.A.1    Medzhitov, R.2
  • 78
    • 0037317763 scopus 로고    scopus 로고
    • Innate immune sensing and its roots: The story of endotoxin
    • PMID:12563300
    • Beutler B, Rietschel ET. Innate immune sensing and its roots: the story of endotoxin. Nat Rev Immunol 2003; 3:169-76; PMID:12563300; http://dx.doi.org/10.1038/nri1004
    • (2003) Nat Rev Immunol , vol.3 , pp. 169-176
    • Beutler, B.1    Rietschel, E.T.2
  • 79
    • 5444262511 scopus 로고    scopus 로고
    • Toll-like receptor control of the adaptive immune responses
    • PMID:15454922
    • Iwasaki A, Medzhitov R. Toll-like receptor control of the adaptive immune responses. Nat Immunol 2004; 5:987-95; PMID:15454922; http://dx.doi.org/10.1038/ni1112
    • (2004) Nat Immunol , vol.5 , pp. 987-995
    • Iwasaki, A.1    Medzhitov, R.2
  • 80
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • PMID:16497588
    • Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell 2006; 124:783-801; PMID:16497588; http://dx.doi.org/10.1016/j.cell.2006.02.015
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 81
    • 33750326113 scopus 로고    scopus 로고
    • The love-hate relationship between bacterial polysaccharides and the host immune system
    • PMID:17024229
    • Mazmanian SK, Kasper DL. The love-hate relationship between bacterial polysaccharides and the host immune system. Nat Rev Immunol 2006; 6:849-58; PMID:17024229; http://dx.doi.org/10.1038/nri1956
    • (2006) Nat Rev Immunol , vol.6 , pp. 849-858
    • Mazmanian, S.K.1    Kasper, D.L.2
  • 82
    • 38949153861 scopus 로고    scopus 로고
    • Innate immune homeostasis by the homeobox gene caudal and commensal-gut mutualism in Drosophila
    • PMID:18218863
    • Ryu JH, Kim SH, Lee HY, Bai JY, Nam YD, Bae JW, etal. Innate immune homeostasis by the homeobox gene caudal and commensal-gut mutualism in Drosophila. Science 2008; 319:777-82; PMID:18218863; http://dx.doi.org/10.1126/science.1149357
    • (2008) Science , vol.319 , pp. 777-782
    • Ryu, J.H.1    Kim, S.H.2    Lee, H.Y.3    Bai, J.Y.4    Nam, Y.D.5    Bae, J.W.6
  • 83
    • 38949186536 scopus 로고    scopus 로고
    • Immunology. The right resident bugs
    • PMID:18218861
    • Silverman N, Paquette N. Immunology. The right resident bugs. Science 2008; 319:734-5; PMID:18218861; http://dx.doi.org/10.1126/science.1154209
    • (2008) Science , vol.319 , pp. 734-735
    • Silverman, N.1    Paquette, N.2
  • 84
    • 40149095898 scopus 로고    scopus 로고
    • Bugs inside Bugs: What the fruit fly can teach us about immune and microbial balance in the gut
    • PMID:18329607
    • Muyskens JB, Guillemin K. Bugs inside Bugs: what the fruit fly can teach us about immune and microbial balance in the gut. Cell Host Microbe 2008; 3:117-8; PMID:18329607; http://dx.doi.org/10.1016/j.chom.2008.02.011
    • (2008) Cell Host Microbe , vol.3 , pp. 117-118
    • Muyskens, J.B.1    Guillemin, K.2
  • 85
    • 10244226689 scopus 로고    scopus 로고
    • War and peace at mucosal surfaces
    • PMID:15573130
    • Sansonetti PJ. War and peace at mucosal surfaces. Nat Rev Immunol 2004; 4:953-64; PMID:15573130; http://dx.doi.org/10.1038/nri1499
    • (2004) Nat Rev Immunol , vol.4 , pp. 953-964
    • Sansonetti, P.J.1
  • 86
    • 15544369658 scopus 로고    scopus 로고
    • Host-bacterial mutualism in the human intestine
    • PMID:15790844
    • Bäckhed F, Ley RE, Sonnenburg JL, Peterson DA, Gordon JI. Host-bacterial mutualism in the human intestine. Science 2005; 307:1915-20; PMID:15790844; http://dx.doi.org/10.1126/science.1104816
    • (2005) Science , vol.307 , pp. 1915-1920
    • Bäckhed, F.1    Ley, R.E.2    Sonnenburg, J.L.3    Peterson, D.A.4    Gordon, J.I.5
  • 87
    • 33846319348 scopus 로고    scopus 로고
    • The innate signaling of dangers and the dangers of innate signaling
    • PMID:17110939
    • Sansonetti PJ. The innate signaling of dangers and the dangers of innate signaling. Nat Immunol 2006; 7:1237-42; PMID:17110939; http://dx.doi.org/10.1038/ni1420
    • (2006) Nat Immunol , vol.7 , pp. 1237-1242
    • Sansonetti, P.J.1
  • 88
    • 0036839577 scopus 로고    scopus 로고
    • Endogenous ligands of Toll-like receptors: Implications for regulating inflammatory and immune responses
    • PMID:12401394
    • Beg AA. Endogenous ligands of Toll-like receptors: implications for regulating inflammatory and immune responses. Trends Immunol 2002; 23:509-12; PMID:12401394; http://dx.doi.org/10.1016/S1471-4906(02)02317-7
    • (2002) Trends Immunol , vol.23 , pp. 509-512
    • Beg, A.A.1
  • 89
    • 0037213692 scopus 로고    scopus 로고
    • Evolutionary clues to the functions of the Toll-like family as surveillance receptors
    • PMID:12495720
    • Johnson GB, Brunn GJ, Tang AH, Platt JL. Evolutionary clues to the functions of the Toll-like family as surveillance receptors. Trends Immunol 2003; 24:19-24; PMID:12495720; http://dx.doi.org/10.1016/S1471-4906(02)00014-5
    • (2003) Trends Immunol , vol.24 , pp. 19-24
    • Johnson, G.B.1    Brunn, G.J.2    Tang, A.H.3    Platt, J.L.4
  • 90
    • 34547763337 scopus 로고    scopus 로고
    • Pivotal advance: Endogenous pathway to SIRS, sepsis, and related conditions
    • PMID:17495051
    • Tang AH, Brunn GJ, Cascalho M, Platt JL. Pivotal advance: endogenous pathway to SIRS, sepsis, and related conditions. J Leukoc Biol 2007; 82:282-5; PMID:17495051; http://dx.doi.org/10.1189/jlb.1206752
    • (2007) J Leukoc Biol , vol.82 , pp. 282-285
    • Tang, A.H.1    Brunn, G.J.2    Cascalho, M.3    Platt, J.L.4
  • 91
    • 0026791975 scopus 로고
    • The immune system evolved to discriminate infectious nonself from noninfectious self
    • PMID:1739426
    • Janeway CA Jr. The immune system evolved to discriminate infectious nonself from noninfectious self. Immunol Today 1992; 13:11-6; PMID:1739426; http://dx.doi.org/10.1016/0167-5699(92)90198-G
    • (1992) Immunol Today , vol.13 , pp. 11-16
    • Janeway Jr., C.A.1
  • 92
    • 3142654210 scopus 로고    scopus 로고
    • Inferences, questions and possibilities in Toll-like receptor signalling
    • PMID:15241424
    • Beutler B. Inferences, questions and possibilities in Toll-like receptor signalling. Nature 2004; 430:257-63; PMID:15241424; http://dx.doi.org/10.1038/nature02761
    • (2004) Nature , vol.430 , pp. 257-263
    • Beutler, B.1
  • 93
    • 23944489424 scopus 로고    scopus 로고
    • Deregulated matriptase causes rasindependent multistage carcinogenesis and promotes ras-mediated malignant transformation
    • PMID:16103220
    • List K, Szabo R, Molinolo A, Sriuranpong V, Redeye V, Murdock T, et al. Deregulated matriptase causes rasindependent multistage carcinogenesis and promotes ras-mediated malignant transformation. Genes Dev 2005; 19:1934-50; PMID:16103220; http://dx.doi.org/10.1101/gad.1300705
    • (2005) Genes Dev , vol.19 , pp. 1934-1950
    • List, K.1    Szabo, R.2    Molinolo, A.3    Sriuranpong, V.4    Redeye, V.5    Murdock, T.6
  • 94
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: A double-edged sword
    • PMID:12949498
    • Aggarwal BB. Signalling pathways of the TNF superfamily: a double-edged sword. Nat Rev Immunol 2003; 3:745-56; PMID:12949498; http://dx.doi.org/10.1038/nri1184
    • (2003) Nat Rev Immunol , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 95
    • 0036162436 scopus 로고    scopus 로고
    • The molecular architecture of the TNF superfamily
    • PMID:11796220
    • Bodmer JL, Schneider P, Tschopp J. The molecular architecture of the TNF superfamily. Trends Biochem Sci 2002; 27:19-26; PMID:11796220; http://dx.doi.org/10.1016/S0968-0004(01)01995-8
    • (2002) Trends Biochem Sci , vol.27 , pp. 19-26
    • Bodmer, J.L.1    Schneider, P.2    Tschopp, J.3
  • 96
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease- activated receptors
    • PMID:11001069
    • Coughlin SR. Thrombin signalling and protease- activated receptors. Nature 2000; 407:258-64; PMID:11001069; http://dx.doi.org/10.1038/35025229
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 97
    • 0037253347 scopus 로고    scopus 로고
    • PARticipation in inflammation
    • PMID:12511583
    • Coughlin SR, Camerer E. PARticipation in inflammation. J Clin Invest 2003; 111:25-7; PMID:12511583
    • (2003) J Clin Invest , vol.111 , pp. 25-27
    • Coughlin, S.R.1    Camerer, E.2
  • 98
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • PMID:10221902
    • Artavanis-Tsakonas S, Rand MD, Lake RJ. Notch signaling: cell fate control and signal integration in development. Science 1999; 284:770-6; PMID:10221902; http://dx.doi.org/10.1126/science.284.5415.770
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsakonas, S.1    Rand, M.D.2    Lake, R.J.3
  • 99
    • 33846236394 scopus 로고    scopus 로고
    • The multifaceted role of Notch in cancer
    • PMID:17178457
    • Roy M, Pear WS, Aster JC. The multifaceted role of Notch in cancer. Curr Opin Genet Dev 2007; 17:52-9; PMID:17178457; http://dx.doi.org/10.1016/j.gde.2006.12.001.
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 52-59
    • Roy, M.1    Pear, W.S.2    Aster, J.C.3
  • 100
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • PMID:8808632
    • Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996; 86:973-83; PMID:8808632; http://dx.doi.org/10.1016/S0092-8674(00)80172-5.
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.