Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling

Innate immune recognition

Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394

Regulation of Cell Survival by Secreted Proneurotrophins

Lee, R., Kermani, P., Teng, K. K., & Hempstead, B. L. (2001) · Science · doi:10.1126/science.1065057 · Cited by 1,670

Discrimination of bacterial lipoproteins by Toll-like receptor 6

Takeuchi, O., Kawai, T., Mühlradt, P. F., Morr, M., Radolf, J. D., Zychlinsky, A., Takeda, K., & Akira, S. (2001) · International Immunology · doi:10.1093/intimm/13.7.933 · Cited by 1,233

Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms

Lemaître, B., Reichhart, J., & Hoffmann, J. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14614 · Cited by 1,044

JPred: a consensus secondary structure prediction server.

Cuff, J. A., Clamp, M. E., Siddiqui, A. S., Finlay, M., & Barton, G. J. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.10.892 · Cited by 1,004

The Toll and Imd pathways are the major regulators of the immune response in Drosophila

Gregorio, E. D., Spellman, P. T., Tzou, P., Rubin, G. M., & Lemaître, B. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2568 · Cited by 936

Use of double-stranded RNA interference in Drosophila cell lines to dissect signal transduction pathways

Clemens, J. C., Worby, C. A., Simonson-Leff, N., Muda, M., Maehama, T., Hemmings, B. A., & Dixon, J. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110149597 · Cited by 843

A CONSERVED SIGNALING PATHWAY: The Drosophila Toll-Dorsal Pathway

Belvin, M. P., & Anderson, K. V. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.393 · Cited by 836 · cited 1×

Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein

Michel, T., Reichhart, J., Hoffmann, J. A., & Royet, J. (2001) · Nature · doi:10.1038/414756a · Cited by 818

Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide.

Lien, E., Means, T., Heine, H., Yoshimura, A., Kusumoto, S., Fukase, K., Fenton, M., Oikawa, M., Qureshi, N., Monks, B., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8541 · Cited by 798

Toll-like receptors: key mediators of microbe detection

Underhill, D. M., & Ozinsky, A. (2002) · Current Opinion in Immunology · doi:10.1016/s0952-7915(01)00304-1 · Cited by 685

Lipopolysaccharide Is in Close Proximity to Each of the Proteins in Its Membrane Receptor Complex

Correia, J. D. S., Soldau, K., Christen, U., Tobias, P. S., & Ulevitch, R. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009164200 · Cited by 649

Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation

Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., & Wilson, I. A. (1999) · Science · doi:10.1126/science.283.5404.987 · Cited by 604

Production of β-defensins by human airway epithelia

Singh, P. K., Jia, H. P., Wiles, K., Hesselberth, J. R., Liu, L., Conway, B. D., Greenberg, E. P., Valore, E. V., Welsh, M. J., Ganz, T., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14961 · Cited by 579

Structures of Glycoprotein Ibα and Its Complex with von Willebrand Factor A1 Domain

Huizinga, E. G., Tsuji, S., Romijn, R. A., Schiphorst, M. E., de Groot, P. G., Sixma, J. J., & Gros, P. (2002) · Science · doi:10.1126/science.107355 · Cited by 545

Toll-like receptors as adjuvant receptors

Kaisho, T., & Akira, S. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(01)00182-3 · Cited by 493

Toll receptors in innate immunity.

Imler, J., & Hoffmann, J. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02004-9 · Cited by 474

Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila.

Levashina, E., Langley, E., Green, C., Gubb, D., Ashburner, M., Hoffmann, J. A., & Reichhart, J. (1999) · Science · doi:10.1126/science.285.5435.1917 · Cited by 469

Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation

Poltorak, A. N., Ricciardi‐Castagnoli, P., Citterio, S., & Beutler, B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040565397 · Cited by 430

Toll-related receptors and the control of antimicrobial peptide expression in Drosophila.

Tauszig, S., Jouanguy, E., Hoffmann, J. A., & Imler, J. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.180130797 · Cited by 429

A genome-wide analysis of immune responses in Drosophila

Irving, P., Troxler, L., Heuer, T. S., Belvin, M. P., Kopczynski, C., Reichhart, J., Hoffmann, J. A., & Hétru, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261573998 · Cited by 397

The Rel Protein DIF Mediates the Antifungal but Not the Antibacterial Host Defense in Drosophila

Rutschmann, S., Jung, A. C., Hétru, C., Reichhart, J., Hoffmann, J. A., & Ferrandon, D. (2000) · Immunity · doi:10.1016/s1074-7613(00)80208-3 · Cited by 377

Two EGF molecules contribute additively to stabilization of the EGFR dimer

Lemmon, M. A., Bu, Z., Ladbury, J. E., Zhou, M., Pinchasi, D., Lax, I., Engelman, D. M., & Schlessinger, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.281 · Cited by 368

Activation of Drosophila Toll During Fungal Infection by a Blood Serine Protease

Ligoxygakis, P., Pelte, N., Hoffmann, J. A., & Reichhart, J. (2002) · Science · doi:10.1126/science.1072391 · Cited by 354

Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-ventral polarity in the Drosophila embryo.

Schneider, D. S., Hudson, K. L., Lin, T. Y., & Anderson, K. V. (1991) · Genes & Development · doi:10.1101/gad.5.5.797 · Cited by 325

Role of Drosophila IKKγ in a Toll-independent antibacterial immune response

Rutschmann, S., Jung, A. C., Zhou, R., Silverman, N. S., Hoffmann, J. A., & Ferrandon, D. (2000) · Nature Immunology · doi:10.1038/79801 · Cited by 280

Toll-like receptors as potential therapeutic targets for multiple diseases

Zuany‐Amorim, C., Hastewell, J. G., & Walker, C. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd914 · Cited by 231

Loopy Proteins Appear Conserved in Evolution

Liu, J., Tan, H., & Rost, B. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00736-2 · Cited by 192

Proteolytic processing of the Drosophila Spätzle protein by Easter generates a dimeric NGF-like molecule with ventralising activity

DeLotto, Y., & DeLotto, R. (1998) · Mechanisms of Development · doi:10.1016/s0925-4773(98)00024-0 · Cited by 187

By IL-1 Signaling, Monocyte-Derived Cells Dramatically Enhance the Epidermal Antimicrobial Response to Lipopolysaccharide

Liu, L., Roberts, A. A., & Ganz, T. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.1.575 · Cited by 184

The pro‐sequence facilitates folding of human nerve growth factor fromEscherichia coliinclusion bodies

Rattenholl, A., Lilie, H., Grossmann, A., Stern, A., Schwarz, E., & Rudolph, R. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02232.x · Cited by 132

The role of Toll-like receptors in host defense against microbial infection

Krutzik, S. R., Sieling, P. A., & Modlin, R. L. (2001) · Current Opinion in Immunology · doi:10.1016/s0952-7915(00)00189-8 · Cited by 131

Signaling of the Cardiotrophin-1 Receptor

Robledo, O., Fourcin, M., Chevalier, S., Guillet, C., Auguste, P., Pouplard-Barthelaix, A., Pennica, D., & Gascan, H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4855 · Cited by 126

The Drosophila Toll‐9 activates a constitutive antimicrobial defense

Ooi, J., Yagi, Y., Hu, X., & Ip, Y. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf004 · Cited by 124

Getting knotted: a model for the structure and activation of Spätzle

Mizuguchi, K., Parker, J. S., Blundell, T. L., & Gay, N. J. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01216-x · Cited by 107

Activation of a protease cascade involved in patterning the Drosophila embryo

LeMosy, E. K., Tan, Y.-Q., & Hashimoto, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081026598 · Cited by 92

Autoproteolysis and feedback in a protease cascade directing Drosophila dorsal–ventral cell fate

Dissing, M., Giordano, H., & DeLotto, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2387 · Cited by 85

Extracellular Toll-Like Receptor 2 Region Containing Ser40-Ile64 but Not Cys30-Ser39 Is Critical for the Recognition ofStaphylococcus aureus Peptidoglycan

Mitsuzawa, H., Wada, I., Sano, H. I., Iwaki, D., Murakami, S., Himi, T., Matsushima, N., & Kuroki, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104177200 · Cited by 58

Constitutive production of human interleukin for DA cells/leukemia inhibitory factor by human tumor cell lines derived from various tissues.

Gascan, H., Anegón, I., Praloran, V., Naulet, J., Godard, A., Soulillou, J., & Jacques, Y. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.7.2592 · Cited by 51

Tehao functions in the Toll pathway in Drosophila melanogaster : possible roles in development and innate immunity

Luo, C., Shen, B., Manley, J. L., & Zheng, L. (2001) · Insect Molecular Biology · doi:10.1046/j.0962-1075.2001.00284.x · Cited by 42

Multiple isoforms of the Drosophila Spätzle protein are encoded by alternatively spliced maternal mRNAs in the precellular blastoderm embryo

DeLotto, Y., Smith, C. L., & DeLotto, R. (2001) · Molecular and General Genetics MGG · doi:10.1007/s004380000350 · Cited by 31

Thermodynamic mixing of molecular states of the epidermal growth factor receptor modulates macroscopic ligand binding affinity

Holbrook, M. R., Slakey, L. L., & GROSS, D. J. (2000) · Biochemical Journal · doi:10.1042/bj3520099 · Cited by 17

Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila

Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,551

The host defense of Drosophila melanogaster.

Lemaître, B., & Hoffmann, J. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141615 · Cited by 3,404

Toll-like receptors in innate immunity

Takeda, K. (2004) · International Immunology · doi:10.1093/intimm/dxh186 · Cited by 3,328

Sterile inflammation: sensing and reacting to damage

Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051

The immune response of Drosophila

Hoffmann, J. A. (2003) · Nature · doi:10.1038/nature02021 · Cited by 1,553

A Twice Tolled Tale

(2003) · Science s STKE · doi:10.1126/stke.2003.194.tw303

Molecular Mechanism That Induces Activation of Spätzle, the Ligand for the Drosophila Toll Receptor

Arnot, C. J., Gay, N., & Gangloff, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.098186 · Cited by 96

Role of the Spätzle Pro-domain in the Generation of an Active Toll Receptor Ligand*

Weber, A., Gangloff, M., Moncrieffe, M., Hyvert, Y., Imler, J., & Gay, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700068200 · Cited by 56

A Spätzle-Processing Enzyme Required for Toll Signaling Activation in Drosophila Innate Immunity

Jang, I.-H., Chosa, N., Kim, S., Nam, H.-J., Lemaître, B., Ochiai, M., Kambris, Z., Brun, S., Hashimoto, C., Ashida, M., et al. (2006) · Developmental Cell · doi:10.1016/j.devcel.2005.11.013 · Cited by 312

Signalling mechanisms of the Toll ectodomain and its extracellular ligand Spätzle

Arnot, C. J. (2010) · OpenGrey (Institut de l'Information Scientifique et Technique)