{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,27]],"date-time":"2026-06-27T05:22:29Z","timestamp":1782537749342,"version":"3.54.5"},"reference-count":85,"publisher":"Springer Science and Business Media LLC","issue":"6962","license":[{"start":{"date-parts":[[2003,11,1]],"date-time":"2003-11-01T00:00:00Z","timestamp":1067644800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2003,11]]},"DOI":"10.1038\/nature02021","type":"journal-article","created":{"date-parts":[[2003,11,5]],"date-time":"2003-11-05T22:25:29Z","timestamp":1068071129000},"page":"33-38","source":"Crossref","is-referenced-by-count":1250,"title":["The immune response of Drosophila"],"prefix":"10.1038","volume":"426","author":[{"given":"Jules A.","family":"Hoffmann","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","reference":[{"key":"BFnature02021_CR1","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1056\/NEJM200008033430506","volume":"343","author":"R Medzhitov","year":"2000","unstructured":"Medzhitov, R. & Janeway, C. Jr Innate immunity. N. Engl. J. Med. 343, 338\u2013344 (2000)","journal-title":"N. Engl. J. Med."},{"key":"BFnature02021_CR2","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1146\/annurev.immunol.20.083001.084359","volume":"20","author":"CA Janeway Jr","year":"2002","unstructured":"Janeway, C. A. Jr & Medzhitov, R. Innate immune recognition. Annu. Rev. Immunol. 20, 197\u2013216 (2002)","journal-title":"Annu. Rev. Immunol."},{"key":"BFnature02021_CR3","doi-asserted-by":"publisher","first-page":"6154","DOI":"10.1073\/pnas.81.19.6154","volume":"81","author":"RM Rizki","year":"1984","unstructured":"Rizki, R. M. & Rizki, T. M. Selective destruction of a host blood cell type by a parasitoid wasp. Proc. Natl Acad. Sci. USA 81, 6154\u20136158 (1984)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR4","doi-asserted-by":"publisher","first-page":"14337","DOI":"10.1073\/pnas.95.24.14337","volume":"95","author":"A Braun","year":"1998","unstructured":"Braun, A., Hoffmann, J. A. & Meister, M. Analysis of the Drosophila host defense in domino mutant larvae, which are devoid of hemocytes. Proc. Natl Acad. Sci. USA 95, 14337\u201314342 (1998)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR5","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1038\/ni0202-121","volume":"3","author":"JA Hoffmann","year":"2002","unstructured":"Hoffmann, J. A. & Reichhart, J. M. Drosophila innate immunity: an evolutionary perspective. Nature Immunol. 3, 121\u2013126 (2002)","journal-title":"Nature Immunol."},{"key":"BFnature02021_CR6","doi-asserted-by":"publisher","first-page":"1217","DOI":"10.1093\/emboj\/17.5.1217","volume":"17","author":"D Ferrandon","year":"1998","unstructured":"Ferrandon, D. et al. A drosomycin\u2013GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway. EMBO J. 17, 1217\u20131227 (1998)","journal-title":"EMBO J."},{"key":"BFnature02021_CR7","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1016\/S1074-7613(00)00072-8","volume":"13","author":"P Tzou","year":"2000","unstructured":"Tzou, P. et al. Tissue-specific inducible expression of antimicrobial peptide genes in Drosophila surface epithelia. Immunity 13, 737\u2013748 (2000)","journal-title":"Immunity"},{"key":"BFnature02021_CR8","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1016\/S0145-305X(99)00015-4","volume":"23","author":"P Bulet","year":"1999","unstructured":"Bulet, P., Hetru, C., Dimarcq, J. L. & Hoffmann, D. Antimicrobial peptides in insects; structure and function. Dev. Comp. Immunol. 23, 329\u2013344 (1999)","journal-title":"Dev. Comp. Immunol."},{"key":"BFnature02021_CR9","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1006\/jmbi.1993.1392","volume":"232","author":"Y Engstrom","year":"1993","unstructured":"Engstrom, Y. et al. \u03baB-like motifs regulate the induction of immune genes in Drosophila. J. Mol. Biol. 232, 327\u2013333 (1993)","journal-title":"J. Mol. Biol."},{"key":"BFnature02021_CR10","doi-asserted-by":"publisher","first-page":"1561","DOI":"10.1002\/j.1460-2075.1993.tb05800.x","volume":"12","author":"C Kappler","year":"1993","unstructured":"Kappler, C. et al. Insect immunity. Two 17\u2009bp repeats nesting a \u03baB-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila. EMBO J. 12, 1561\u20131568 (1993)","journal-title":"EMBO J."},{"key":"BFnature02021_CR11","doi-asserted-by":"publisher","first-page":"474","DOI":"10.1038\/283474a0","volume":"283","author":"C Nusslein-Volhard","year":"1980","unstructured":"Nusslein-Volhard, C., Lohs-Schardin, M., Sander, K. & Cremer, C. A dorso-ventral shift of embryonic primordia in a new maternal-effect mutant of Drosophila. Nature 283, 474\u2013476 (1980)","journal-title":"Nature"},{"key":"BFnature02021_CR12","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/0092-8674(92)90466-P","volume":"68","author":"D St Johnston","year":"1992","unstructured":"St Johnston, D. & N\u00fcsslein-Volhard, C. The origin of pattern and polarity in the Drosophila embryo. Cell 68, 201\u2013219 (1992)","journal-title":"Cell"},{"key":"BFnature02021_CR13","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1146\/annurev.ge.29.120195.002103","volume":"29","author":"D Morisato","year":"1995","unstructured":"Morisato, D. & Anderson, K. V. Signaling pathways that establish the dorsal\u2013ventral pattern of the Drosophila embryo. Annu. Rev. Genet. 29, 371\u2013399 (1995)","journal-title":"Annu. Rev. Genet."},{"key":"BFnature02021_CR14","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1146\/annurev.cellbio.12.1.393","volume":"12","author":"MP Belvin","year":"1996","unstructured":"Belvin, M. P. & Anderson, K. V. A conserved signaling pathway: the Drosophila Toll\u2013Dorsal pathway. Annu. Rev. Cell Dev. Biol. 12, 393\u2013416 (1996)","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"BFnature02021_CR15","doi-asserted-by":"publisher","first-page":"973","DOI":"10.1016\/S0092-8674(00)80172-5","volume":"86","author":"B Lemaitre","year":"1996","unstructured":"Lemaitre, B., Nicolas, E., Michaut, L., Reichhart, J. M. & Hoffmann, J. A. The dorsoventral regulatory gene cassette spatzle\/Toll\/cactus controls the potent antifungal response in Drosophila adults. Cell 86, 973\u2013983 (1996)","journal-title":"Cell"},{"key":"BFnature02021_CR16","doi-asserted-by":"crossref","first-page":"10867","DOI":"10.1016\/S0021-9258(18)81700-8","volume":"264","author":"PS Tobias","year":"1989","unstructured":"Tobias, P. S., Soldau, K. & Ulevitch, R. J. Identification of a lipid A binding site in the acute phase reactant lipopolysaccharide binding protein. J. Biol. Chem. 264, 10867\u201310871 (1989)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR17","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1038\/41131","volume":"388","author":"R Medzhitov","year":"1997","unstructured":"Medzhitov, R., Preston-Hurlburt, P. & Janeway, C. A. Jr A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388, 394\u2013397 (1997)","journal-title":"Nature"},{"key":"BFnature02021_CR18","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1126\/science.282.5396.2085","volume":"282","author":"A Poltorak","year":"1998","unstructured":"Poltorak, A. et al. Defective LPS signaling in C3H\/HeJ and C57BL\/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085\u20132088 (1998)","journal-title":"Science"},{"key":"BFnature02021_CR19","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1084\/jem.189.4.615","volume":"189","author":"ST Qureshi","year":"1999","unstructured":"Qureshi, S. T. et al. Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J. Exp. Med. 189, 615\u2013625 (1999)","journal-title":"J. Exp. Med."},{"key":"BFnature02021_CR20","doi-asserted-by":"publisher","first-page":"588","DOI":"10.1073\/pnas.95.2.588","volume":"95","author":"FL Rock","year":"1998","unstructured":"Rock, F. L., Hardiman, G., Timans, J. C., Kastelein, R. A. & Bazan, J. F. A family of human receptors structurally related to Drosophila Toll. Proc. Natl Acad. Sci. USA 95, 588\u2013593 (1998)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR21","doi-asserted-by":"publisher","first-page":"1542","DOI":"10.4049\/jimmunol.168.4.1542","volume":"168","author":"S Rutschmann","year":"2002","unstructured":"Rutschmann, S., Kilinc, A. & Ferrandon, D. Cutting edge: the Toll pathway is required for resistance to Gram-positive bacterial infections in Drosophila. J. Immunol. 168, 1542\u20131546 (2002)","journal-title":"J. Immunol."},{"key":"BFnature02021_CR22","doi-asserted-by":"publisher","first-page":"9465","DOI":"10.1073\/pnas.92.21.9465","volume":"92","author":"B Lemaitre","year":"1995","unstructured":"Lemaitre, B. et al. A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense. Proc. Natl Acad. Sci. USA 92, 9465\u20139469 (1995)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR23","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/S0968-0004(98)01216-X","volume":"23","author":"K Mizuguchi","year":"1998","unstructured":"Mizuguchi, K., Parker, J. S., Blundell, T. L. & Gay, N. J. Getting knotted: a model for the structure and activation of Spatzle. Trends Biochem. Sci. 23, 239\u2013242 (1998)","journal-title":"Trends Biochem. Sci."},{"key":"BFnature02021_CR24","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/S0925-4773(98)00024-0","volume":"72","author":"Y DeLotto","year":"1998","unstructured":"DeLotto, Y. & DeLotto, R. Proteolytic processing of the Drosophila Spatzle protein by easter generates a dimeric NGF-like molecule with ventralising activity. Mech. Dev. 72, 141\u2013148 (1998)","journal-title":"Mech. Dev."},{"key":"BFnature02021_CR25","doi-asserted-by":"publisher","first-page":"794","DOI":"10.1038\/ni955","volume":"8","author":"ANR Weber","year":"2003","unstructured":"Weber, A. N. R. et al. Binding of the Drosophila cytokine Spaetzle to Toll is direct and establishes signaling. Nature Immunol. 8, 794\u2013800 (2003)","journal-title":"Nature Immunol."},{"key":"BFnature02021_CR26","doi-asserted-by":"publisher","first-page":"12654","DOI":"10.1073\/pnas.231471798","volume":"98","author":"T Horng","year":"2001","unstructured":"Horng, T. & Medzhitov, R. Drosophila MyD88 is an adapter in the Toll signaling pathway. Proc. Natl Acad. Sci. USA 98, 12654\u201312658 (2001)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR27","doi-asserted-by":"publisher","first-page":"12871","DOI":"10.1073\/pnas.202396399","volume":"99","author":"H Sun","year":"2002","unstructured":"Sun, H., Bristow, B. N., Qu, G. & Wasserman, S. A. A heterotrimeric death domain complex in Toll signaling. Proc. Natl Acad. Sci. USA 99, 12871\u201312876 (2002)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR28","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1038\/ni747","volume":"3","author":"S Tauszig-Delamasure","year":"2002","unstructured":"Tauszig-Delamasure, S., Bilak, H., Capovilla, M., Hoffmann, J. A. & Imler, J. L. Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections. Nature Immunol. 3, 91\u201397 (2002)","journal-title":"Nature Immunol."},{"key":"BFnature02021_CR29","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1016\/S0925-4773(02)00410-0","volume":"120","author":"I Charatsi","year":"2003","unstructured":"Charatsi, I., Luschnig, S., Bartoszewski, S., Nusslein-Volhard, C. & Moussian, B. Krapfen\/dMyd88 is required for the establishment of dorsoventral pattern in the Drosophila embryo. Mech. Dev. 120, 219\u2013226 (2003)","journal-title":"Mech. Dev."},{"key":"BFnature02021_CR30","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1016\/S1097-2765(03)00053-4","volume":"11","author":"S Janssens","year":"2003","unstructured":"Janssens, S. & Beyaert, R. Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members. Mol. Cell 11, 293\u2013302 (2003)","journal-title":"Mol. Cell"},{"key":"BFnature02021_CR31","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1016\/0092-8674(93)90495-C","volume":"75","author":"YT Ip","year":"1993","unstructured":"Ip, Y. T. et al. Dif, a dorsal-related gene that mediates an immune response in Drosophila. Cell 75, 753\u2013763 (1993)","journal-title":"Cell"},{"key":"BFnature02021_CR32","doi-asserted-by":"publisher","first-page":"792","DOI":"10.1101\/gad.13.7.792","volume":"13","author":"X Meng","year":"1999","unstructured":"Meng, X., Khanuja, B. S. & Ip, Y. T. Toll receptor-mediated Drosophila immune response requires Dif, an NF-\u03baB factor. Genes Dev. 13, 792\u2013797 (1999)","journal-title":"Genes Dev."},{"key":"BFnature02021_CR33","doi-asserted-by":"publisher","first-page":"3380","DOI":"10.1093\/emboj\/18.12.3380","volume":"18","author":"P Manfruelli","year":"1999","unstructured":"Manfruelli, P., Reichhart, J. M., Steward, R., Hoffmann, J. A. & 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. 18, 3380\u20133391 (1999)","journal-title":"EMBO J."},{"key":"BFnature02021_CR34","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/S1074-7613(00)80208-3","volume":"12","author":"S Rutschmann","year":"2000","unstructured":"Rutschmann, S. et al. The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila. Immunity 12, 569\u2013580 (2000)","journal-title":"Immunity"},{"key":"BFnature02021_CR35","doi-asserted-by":"publisher","first-page":"10463","DOI":"10.1074\/jbc.273.17.10463","volume":"273","author":"E Nicolas","year":"1998","unstructured":"Nicolas, E., Reichhart, J. M., Hoffmann, J. A. & Lemaitre, B. In vivo regulation of the I\u03baB homologue cactus during the immune response of Drosophila. J. Biol. Chem. 273, 10463\u201310469 (1998)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR36","doi-asserted-by":"crossref","first-page":"2963","DOI":"10.1242\/dev.128.15.2963","volume":"128","author":"NQ Fernandez","year":"2001","unstructured":"Fernandez, N. Q., Grosshans, J., Goltz, J. S. & Stein, D. Separable and redundant regulatory determinants in Cactus mediate its dorsal group dependent degradation. Development 128, 2963\u20132974 (2001)","journal-title":"Development"},{"key":"BFnature02021_CR37","doi-asserted-by":"publisher","first-page":"556","DOI":"10.1101\/gad.13.5.556","volume":"13","author":"EA Drier","year":"1999","unstructured":"Drier, E. A., Huang, L. H. & Steward, R. Nuclear import of the Drosophila Rel protein Dorsal is regulated by phosphorylation. Genes Dev. 13, 556\u2013568 (1999)","journal-title":"Genes Dev."},{"key":"BFnature02021_CR38","doi-asserted-by":"publisher","first-page":"8787","DOI":"10.1128\/MCB.22.24.8787-8795.2002","volume":"22","author":"A Avila","year":"2002","unstructured":"Avila, A., Silverman, N., Diaz-Meco, M. T. & Moscat, J. The Drosophila atypical protein kinase C\u2013ref(2)p complex constitutes a conserved module for signaling in the toll pathway. Mol. Cell. Biol. 22, 8787\u20138795 (2002)","journal-title":"Mol. Cell. Biol."},{"key":"BFnature02021_CR39","doi-asserted-by":"publisher","first-page":"12590","DOI":"10.1073\/pnas.221458698","volume":"98","author":"E De Gregorio","year":"2001","unstructured":"De Gregorio, E., Spellman, P. T., Rubin, G. M. & Lemaitre, B. Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. Proc. Natl Acad. Sci. USA 98, 12590\u201312595 (2001)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR40","doi-asserted-by":"publisher","first-page":"15119","DOI":"10.1073\/pnas.261573998","volume":"98","author":"P Irving","year":"2001","unstructured":"Irving, P. et al. A genome-wide analysis of immune responses in Drosophila. Proc. Natl Acad. Sci. USA 98, 15119\u201315124 (2001)","journal-title":"Natl Acad. Sci. USA"},{"key":"BFnature02021_CR41","doi-asserted-by":"publisher","first-page":"10520","DOI":"10.1073\/pnas.180130797","volume":"97","author":"S Tauszig","year":"2000","unstructured":"Tauszig, S., Jouanguy, E., Hoffmann, J. A. & Imler, J. L. Toll-related receptors and the control of antimicrobial peptide expression in Drosophila. Proc. Natl Acad. Sci. USA 97, 10520\u201310525 (2000)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR42","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/S1567-133X(02)00020-0","volume":"2","author":"Z Kambris","year":"2002","unstructured":"Kambris, Z., Hoffmann, J. A., Imler, J. L. & Capovilla, M. Tissue and stage-specific expression of the Tolls in Drosophila embryos. Gene Expr. Patterns 2, 311\u2013317 (2002)","journal-title":"Gene Expr. Patterns"},{"key":"BFnature02021_CR43","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1002\/prot.1125","volume":"45","author":"JS Parker","year":"2001","unstructured":"Parker, J. S., Mizuguchi, K. & Gay, N. J. A family of proteins related to Spatzle, the toll receptor ligand, are encoded in the Drosophila genome. Proteins 45, 71\u201380 (2001)","journal-title":"Proteins"},{"key":"BFnature02021_CR44","doi-asserted-by":"publisher","first-page":"4299","DOI":"10.1002\/j.1460-2075.1990.tb07878.x","volume":"9","author":"FJ Keith","year":"1990","unstructured":"Keith, F. J. & Gay, N. J. The Drosophila membrane receptor Toll can function to promote cellular adhesion. EMBO J. 9, 4299\u20134306 (1990)","journal-title":"EMBO J."},{"key":"BFnature02021_CR45","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1016\/S1534-5807(01)00059-4","volume":"1","author":"P Georgel","year":"2001","unstructured":"Georgel, P. et al. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis. Dev. Cell 1, 503\u2013514 (2001)","journal-title":"Dev. Cell"},{"key":"BFnature02021_CR46","doi-asserted-by":"publisher","first-page":"10343","DOI":"10.1073\/pnas.93.19.10343","volume":"93","author":"MS Dushay","year":"1996","unstructured":"Dushay, M. S., Asling, B. & Hultmark, D. Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila. Proc. Natl Acad. Sci. USA 93, 10343\u201310347 (1996)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR47","doi-asserted-by":"publisher","first-page":"827","DOI":"10.1016\/S1097-2765(00)80392-5","volume":"4","author":"M Hedengren","year":"1999","unstructured":"Hedengren, M. et al. Relish, a central factor in the control of humoral but not cellular immunity in Drosophila. Mol. Cell 4, 827\u2013837 (1999)","journal-title":"Mol. Cell"},{"key":"BFnature02021_CR48","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1093\/embo-reports\/kvd072","volume":"1","author":"S Stoven","year":"2000","unstructured":"Stoven, S., Ando, I., Kadalayil, L., Engstrom, Y. & Hultmark, D. Activation of the Drosophila NF-\u03baB factor Relish by rapid endoproteolytic cleavage. EMBO Rep. 1, 347\u2013352 (2000)","journal-title":"EMBO Rep."},{"key":"BFnature02021_CR49","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1016\/S1074-7613(02)00454-5","volume":"17","author":"S Naitza","year":"2002","unstructured":"Naitza, S. et al. The Drosophila immune defense against Gram-negative infection requires the death protein dFADD. Immunity 17, 575\u2013581 (2002)","journal-title":"Immunity"},{"key":"BFnature02021_CR50","doi-asserted-by":"publisher","first-page":"996","DOI":"10.1016\/S0960-9822(02)00873-4","volume":"12","author":"F Leulier","year":"2002","unstructured":"Leulier, F., Vidal, S., Saigo, K., Ueda, R. & Lemaitre, B. Inducible expression of double-stranded RNA reveals a role for dFADD in the regulation of the antibacterial response in Drosophila adults. Curr. Biol. 12, 996\u20131000 (2002)","journal-title":"Curr. Biol."},{"key":"BFnature02021_CR51","doi-asserted-by":"publisher","first-page":"1900","DOI":"10.1101\/gad.203301","volume":"15","author":"S Vidal","year":"2001","unstructured":"Vidal, S. et al. Mutations in the Drosophila dTAK1 gene reveal a conserved function for MAPKKKs in the control of rel\/NF-\u03baB-dependent innate immune responses. Genes Dev. 15, 1900\u20131912 (2001)","journal-title":"Genes Dev."},{"key":"BFnature02021_CR52","doi-asserted-by":"publisher","first-page":"342","DOI":"10.1038\/79801","volume":"1","author":"S Rutschmann","year":"2000","unstructured":"Rutschmann, S. et al. Role of Drosophila IKK\u03b3 in a Toll-independent antibacterial immune response. Nature Immunol. 1, 342\u2013347 (2000)","journal-title":"Nature Immunol."},{"key":"BFnature02021_CR53","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1101\/gad.856901","volume":"15","author":"Y Lu","year":"2001","unstructured":"Lu, Y., Wu, L. P. & Anderson, K. V. The antibacterial arm of the Drosophila innate immune response requires an I\u03baB kinase. Genes Dev. 15, 104\u2013110 (2001)","journal-title":"Genes Dev."},{"key":"BFnature02021_CR54","doi-asserted-by":"publisher","first-page":"2461","DOI":"10.1101\/gad.817800","volume":"14","author":"N Silverman","year":"2000","unstructured":"Silverman, N. et al. A Drosophila I\u03baB kinase complex required for Relish cleavage and antibacterial immunity. Genes Dev. 14, 2461\u20132471 (2000)","journal-title":"Genes Dev."},{"key":"BFnature02021_CR55","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1093\/embo-reports\/kvd073","volume":"1","author":"F Leulier","year":"2000","unstructured":"Leulier, F., Rodriguez, A., Khush, R. S., Abrams, J. M. & Lemaitre, B. The Drosophila caspase Dredd is required to resist Gram-negative bacterial infection. EMBO Rep. 1, 353\u2013358 (2000)","journal-title":"EMBO Rep."},{"key":"BFnature02021_CR56","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1016\/S0960-9822(00)00569-8","volume":"10","author":"M Elrod-Erickson","year":"2000","unstructured":"Elrod-Erickson, M., Mishra, S. & Schneider, D. Interactions between the cellular and humoral immune responses in Drosophila. Curr. Biol. 10, 781\u2013784 (2000)","journal-title":"Curr. Biol."},{"key":"BFnature02021_CR57","doi-asserted-by":"publisher","first-page":"30761","DOI":"10.1074\/jbc.C000341200","volume":"275","author":"S Hu","year":"2000","unstructured":"Hu, S. & Yang, X. dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD. J. Biol. Chem. 275, 30761\u201330764 (2000)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR58","doi-asserted-by":"publisher","first-page":"5991","DOI":"10.1073\/pnas.1035902100","volume":"100","author":"S Stoven","year":"2003","unstructured":"Stoven, S. et al. Caspase-mediated processing of the Drosophila NF-\u03baB factor Relish. Proc. Natl Acad. Sci. USA 100, 5991\u20135996 (2003)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR59","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1016\/S1534-5807(02)00325-8","volume":"3","author":"M Boutros","year":"2002","unstructured":"Boutros, M., Agaisse, H. & Perrimon, N. Sequential activation of signaling pathways during innate immune responses in Drosophila. Dev. Cell 3, 711\u2013722 (2002)","journal-title":"Dev. Cell"},{"key":"BFnature02021_CR60","doi-asserted-by":"publisher","first-page":"2568","DOI":"10.1093\/emboj\/21.11.2568","volume":"21","author":"E De Gregorio","year":"2002","unstructured":"De Gregorio, E., Spellman, P. T., Tzou, P., Rubin, G. M. & Lemaitre, B. The Toll and Imd pathways are the major regulators of the immune response in Drosophila. EMBO J. 21, 2568\u20132579 (2002)","journal-title":"EMBO J."},{"key":"BFnature02021_CR61","doi-asserted-by":"publisher","first-page":"756","DOI":"10.1038\/414756a","volume":"414","author":"T Michel","year":"2001","unstructured":"Michel, T., Reichhart, J. M., Hoffmann, J. A. & Royet, J. Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature 414, 756\u2013759 (2001)","journal-title":"Nature"},{"key":"BFnature02021_CR62","unstructured":"Gobert, V. et al. Toll activation during bacterial infection in Drosophila requires the concomitant function of two distinct blood-borne recognition proteins. Science (submitted)"},{"key":"BFnature02021_CR63","doi-asserted-by":"publisher","first-page":"13854","DOI":"10.1074\/jbc.271.23.13854","volume":"271","author":"H Yoshida","year":"1996","unstructured":"Yoshida, H., Kinoshita, K. & Ashida, M. Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J. Biol. Chem. 271, 13854\u201313860 (1996)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR64","doi-asserted-by":"publisher","first-page":"7888","DOI":"10.1073\/pnas.93.15.7888","volume":"93","author":"WJ Lee","year":"1996","unstructured":"Lee, W. J., Lee, J. D., Kravchenko, V. V., Ulevitch, R. J. & Brey, P. T. Purification and molecular cloning of an inducible Gram-negative bacteria-binding protein from the silkworm, Bombyx mori. Proc. Natl Acad. Sci. USA 93, 7888\u20137893 (1996)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR65","doi-asserted-by":"publisher","first-page":"10078","DOI":"10.1073\/pnas.95.17.10078","volume":"95","author":"D Kang","year":"1998","unstructured":"Kang, D., Liu, G., Lundstrom, A., Gelius, E. & Steiner, H. A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc. Natl Acad. Sci. USA 95, 10078\u201310082 (1998)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR66","doi-asserted-by":"publisher","first-page":"11854","DOI":"10.1074\/jbc.274.17.11854","volume":"274","author":"M Ochiai","year":"1999","unstructured":"Ochiai, M. & Ashida, M. A pattern recognition protein for peptidoglycan. Cloning the cDNA and the gene of the silkworm, Bombyx mori. J. Biol. Chem. 274, 11854\u201311858 (1999)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR67","doi-asserted-by":"publisher","first-page":"13772","DOI":"10.1073\/pnas.97.25.13772","volume":"97","author":"T Werner","year":"2000","unstructured":"Werner, T. et al. A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proc. Natl Acad. Sci. USA 97, 13772\u201313777 (2000)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR68","doi-asserted-by":"publisher","first-page":"4995","DOI":"10.1074\/jbc.275.7.4995","volume":"275","author":"M Ochiai","year":"2000","unstructured":"Ochiai, M. & Ashida, M. A pattern-recognition protein for \u03b2-1,3-glucan. The binding domain and the cDNA cloning of \u03b2-1,3-glucan recognition protein from the silkworm, Bombyx mori. J. Biol. Chem. 275, 4995\u20135002 (2000)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR69","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1126\/science.1072391","volume":"297","author":"P Ligoxygakis","year":"2002","unstructured":"Ligoxygakis, P., Pelte, N., Hoffmann, J. A. & Reichhart, J. M. Activation of Drosophila Toll during fungal infection by a blood serine protease. Science 297, 114\u2013116 (2002)","journal-title":"Science"},{"key":"BFnature02021_CR70","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1038\/nature734","volume":"416","author":"M Gottar","year":"2002","unstructured":"Gottar, M. et al. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 416, 640\u2013644 (2002)","journal-title":"Nature"},{"key":"BFnature02021_CR71","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1126\/science.1070216","volume":"296","author":"KM Choe","year":"2002","unstructured":"Choe, K. M., Werner, T., Stoven, S., Hultmark, D. & Anderson, K. V. Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science 296, 359\u2013362 (2002)","journal-title":"Science"},{"key":"BFnature02021_CR72","doi-asserted-by":"publisher","first-page":"644","DOI":"10.1038\/nature735","volume":"416","author":"M Ramet","year":"2002","unstructured":"Ramet, M., Manfruelli, P., Pearson, A., Mathey-Prevot, B. & Ezekowitz, R. A. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 416, 644\u2013648 (2002)","journal-title":"Nature"},{"key":"BFnature02021_CR73","doi-asserted-by":"publisher","first-page":"13705","DOI":"10.1073\/pnas.212301199","volume":"99","author":"A Takehana","year":"2002","unstructured":"Takehana, A. 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. USA 99, 13705\u201313710 (2002)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR74","doi-asserted-by":"publisher","first-page":"4034","DOI":"10.1073\/pnas.91.9.4034","volume":"91","author":"X Cheng","year":"1994","unstructured":"Cheng, X., Zhang, X., Pflugrath, J. W. & Studier, F. W. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc. Natl Acad. Sci. USA 91, 4034\u20134038 (1994)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature02021_CR75","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1016\/S0022-2836(03)00185-2","volume":"327","author":"E Liepinsh","year":"2003","unstructured":"Liepinsh, E., Genereux, C., Dehareng, D., Joris, B. & Otting, G. NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains. J. Mol. Biol. 327, 833\u2013842 (2003)","journal-title":"J. Mol. Biol."},{"key":"BFnature02021_CR76","doi-asserted-by":"publisher","first-page":"7059","DOI":"10.1074\/jbc.M208900200","volume":"278","author":"P Mellroth","year":"2003","unstructured":"Mellroth, P., Karlsson, J. & Steiner, H. A scavenger function for a Drosophila peptidoglycan recognition protein. J. Biol. Chem. 278, 7059\u20137064 (2003)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR77","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1038\/ni952","volume":"4","author":"MS Kim","year":"2003","unstructured":"Kim, M. S., Byun, M. & Oh, B. H. Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nature Immunol. 4, 787\u2013793 (2003)","journal-title":"Nature Immunol."},{"key":"BFnature02021_CR78","doi-asserted-by":"publisher","first-page":"478","DOI":"10.1038\/ni922","volume":"4","author":"F Leulier","year":"2003","unstructured":"Leulier, F. et al. The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nature Immunol. 4, 478\u2013484 (2003)","journal-title":"Nature Immunol."},{"key":"BFnature02021_CR79","doi-asserted-by":"publisher","first-page":"34686","DOI":"10.1074\/jbc.M105566200","volume":"276","author":"C Liu","year":"2001","unstructured":"Liu, C., Xu, Z., Gupta, D. & Dziarski, R. Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J. Biol. Chem. 276, 34686\u201334694 (2001)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR80","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1182\/blood-2002-12-3853","volume":"102","author":"R Dziarski","year":"2003","unstructured":"Dziarski, R., Platt, K. A., Gelius, E., Steiner, H. & Gupta, D. Defect in neutrophil killing and increased susceptibility to infection with non-pathogenic Gram-positive bacteria in peptidoglycan recognition protein-S (PGRP-S)-deficient mice. Blood 102, 689\u2013697 (2003)","journal-title":"Blood"},{"key":"BFnature02021_CR81","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1016\/S1074-7613(00)80119-3","volume":"11","author":"O Takeuchi","year":"1999","unstructured":"Takeuchi, O. et al. Differential roles of TLR2 and TLR4 in recognition of Gram-negative and Gram-positive bacterial cell wall components. Immunity 11, 443\u2013451 (1999)","journal-title":"Immunity"},{"key":"BFnature02021_CR82","doi-asserted-by":"publisher","first-page":"41701","DOI":"10.1074\/jbc.M206473200","volume":"277","author":"O Gutierrez","year":"2002","unstructured":"Gutierrez, O. et al. Induction of Nod2 in myelomonocytic and intestinal epithelial cells via nuclear factor-\u03baB activation. J. Biol. Chem. 277, 41701\u201341705 (2002)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR83","doi-asserted-by":"publisher","first-page":"1584","DOI":"10.1126\/science.1084677","volume":"300","author":"SE Girardin","year":"2003","unstructured":"Girardin, S. E. et al. Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 300, 1584\u20131587 (2003)","journal-title":"Science"},{"key":"BFnature02021_CR84","doi-asserted-by":"publisher","first-page":"29731","DOI":"10.1074\/jbc.M000184200","volume":"275","author":"MN Becker","year":"2000","unstructured":"Becker, M. N., Diamond, G., Verghese, M. W. & Randell, S. H. CD14-dependent lipopolysaccharide-induced \u03b2-defensin-2 expression in human tracheobronchial epithelium. J. Biol. Chem. 275, 29731\u201329736 (2000)","journal-title":"J. Biol. Chem."},{"key":"BFnature02021_CR85","doi-asserted-by":"publisher","first-page":"575","DOI":"10.4049\/jimmunol.170.1.575","volume":"170","author":"L Liu","year":"2003","unstructured":"Liu, L., Roberts, A. A. & Ganz, T. By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide. J. Immunol. 170, 575\u2013580 (2003)","journal-title":"J. Immunol."}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nature02021.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature02021","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature02021.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T18:18:19Z","timestamp":1684433899000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature02021"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,11]]},"references-count":85,"journal-issue":{"issue":"6962","published-print":{"date-parts":[[2003,11]]}},"alternative-id":["BFnature02021"],"URL":"https:\/\/doi.org\/10.1038\/nature02021","relation":{},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,11]]}}}