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Volumn 25, Issue 5, 2014, Pages 533-541

Tyrosine phosphorylation in Toll-like receptor signaling

Author keywords

EGFR; Protein tyrosine kinases; Src; TLR; Tyrosine phosphorylation

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; MYELOID DIFFERENTIATION FACTOR 88; PROTEIN TYROSINE KINASE; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 5; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 1; TYROSINE;

EID: 84908339164     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.06.002     Document Type: Short Survey
Times cited : (77)

References (90)
  • 1
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B., Nicolas E., Michaut L., Reichhart J.M., Hoffmann J.A. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996, 86:973-983.
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 2
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
    • Kawai T., Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol 2010, 11:373-384.
    • (2010) Nat Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 3
    • 77249160271 scopus 로고    scopus 로고
    • Localisation and trafficking of Toll-like receptors: an important mode of regulation
    • McGettrick A.F., O'Neill L.A. Localisation and trafficking of Toll-like receptors: an important mode of regulation. Curr Opin Immunol 2010, 22:20-27.
    • (2010) Curr Opin Immunol , vol.22 , pp. 20-27
    • McGettrick, A.F.1    O'Neill, L.A.2
  • 4
    • 69149104309 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in immune cells: direct and indirect effects on Toll-like receptor-induced proinflammatory cytokine production
    • Johnson P., Cross J.L. Tyrosine phosphorylation in immune cells: direct and indirect effects on Toll-like receptor-induced proinflammatory cytokine production. Crit Rev Immunol 2009, 29:347-367.
    • (2009) Crit Rev Immunol , vol.29 , pp. 347-367
    • Johnson, P.1    Cross, J.L.2
  • 5
    • 79956300649 scopus 로고    scopus 로고
    • Toll-like receptors and their crosstalk with other innate receptors in infection and immunity
    • Kawai T., Akira S. Toll-like receptors and their crosstalk with other innate receptors in infection and immunity. Immunity 2011, 34:637-650.
    • (2011) Immunity , vol.34 , pp. 637-650
    • Kawai, T.1    Akira, S.2
  • 6
    • 27744526784 scopus 로고    scopus 로고
    • TLR3 and TLR7 are targeted to the same intracellular compartments by distinct regulatory elements
    • Nishiya T., Kajita E., Miwa S., Defranco A.L. TLR3 and TLR7 are targeted to the same intracellular compartments by distinct regulatory elements. J Biol Chem 2005, 280:37107-37117.
    • (2005) J Biol Chem , vol.280 , pp. 37107-37117
    • Nishiya, T.1    Kajita, E.2    Miwa, S.3    Defranco, A.L.4
  • 7
    • 40749098665 scopus 로고    scopus 로고
    • UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes
    • Kim Y.M., Brinkmann M.M., Paquet M.E., Ploegh H.L. UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes. Nature 2008, 452:234-238.
    • (2008) Nature , vol.452 , pp. 234-238
    • Kim, Y.M.1    Brinkmann, M.M.2    Paquet, M.E.3    Ploegh, H.L.4
  • 9
    • 84865571191 scopus 로고    scopus 로고
    • TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance-forming modification
    • Oldenburg M., Kruger A., Ferstl R., Kaufmann A., Nees G., Sigmund A., et al. TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance-forming modification. Science 2012, 337:1111-1115.
    • (2012) Science , vol.337 , pp. 1111-1115
    • Oldenburg, M.1    Kruger, A.2    Ferstl, R.3    Kaufmann, A.4    Nees, G.5    Sigmund, A.6
  • 10
    • 33845868493 scopus 로고    scopus 로고
    • S100 proteins expressed in phagocytes: a novel group of damage-associated molecular pattern molecules
    • Foell D., Wittkowski H., Vogl T., Roth J. S100 proteins expressed in phagocytes: a novel group of damage-associated molecular pattern molecules. J Leukoc Biol 2007, 81:28-37.
    • (2007) J Leukoc Biol , vol.81 , pp. 28-37
    • Foell, D.1    Wittkowski, H.2    Vogl, T.3    Roth, J.4
  • 11
    • 34247236200 scopus 로고    scopus 로고
    • Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE
    • Tian J., Avalos A.M., Mao S.Y., Chen B., Senthil K., Wu H., et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nat Immunol 2007, 8:487-496.
    • (2007) Nat Immunol , vol.8 , pp. 487-496
    • Tian, J.1    Avalos, A.M.2    Mao, S.Y.3    Chen, B.4    Senthil, K.5    Wu, H.6
  • 12
    • 36548999695 scopus 로고    scopus 로고
    • HMGB1 release induced by liver ischemia involves Toll-like receptor 4 dependent reactive oxygen species production and calcium-mediated signaling
    • Tsung A., Klune J.R., Zhang X., Jeyabalan G., Cao Z., Peng X., et al. HMGB1 release induced by liver ischemia involves Toll-like receptor 4 dependent reactive oxygen species production and calcium-mediated signaling. J Exp Med 2007, 204:2913-2923.
    • (2007) J Exp Med , vol.204 , pp. 2913-2923
    • Tsung, A.1    Klune, J.R.2    Zhang, X.3    Jeyabalan, G.4    Cao, Z.5    Peng, X.6
  • 13
    • 84901828348 scopus 로고    scopus 로고
    • S100A1 is released from ischemic cardiomyocytes and signals myocardial damage via Toll-like receptor 4
    • Rohde D., Schon C., Boerries M., Didrihsone I., Ritterhoff J., Kubatzky K.F., et al. S100A1 is released from ischemic cardiomyocytes and signals myocardial damage via Toll-like receptor 4. EMBO Mol Med 2014, 6:778-794.
    • (2014) EMBO Mol Med , vol.6 , pp. 778-794
    • Rohde, D.1    Schon, C.2    Boerries, M.3    Didrihsone, I.4    Ritterhoff, J.5    Kubatzky, K.F.6
  • 14
    • 68849085894 scopus 로고    scopus 로고
    • A cell biological view of Toll-like receptor function: regulation through compartmentalization
    • Barton G.M., Kagan J.C. A cell biological view of Toll-like receptor function: regulation through compartmentalization. Nat Rev Immunol 2009, 9:535-542.
    • (2009) Nat Rev Immunol , vol.9 , pp. 535-542
    • Barton, G.M.1    Kagan, J.C.2
  • 15
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill L.A., Bowie A.G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat Rev Immunol 2007, 7:353-364.
    • (2007) Nat Rev Immunol , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 16
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway
    • Yamamoto M., Sato S., Hemmi H., Hoshino K., Kaisho T., Sanjo H., et al. Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway. Science 2003, 301:640-643.
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Hoshino, K.4    Kaisho, T.5    Sanjo, H.6
  • 18
    • 17144404177 scopus 로고    scopus 로고
    • IRF-7 is the master regulator of type-I interferon-dependent immune responses
    • Honda K., Yanai H., Negishi H., Asagiri M., Sato M., Mizutani T., et al. IRF-7 is the master regulator of type-I interferon-dependent immune responses. Nature 2005, 434:772-777.
    • (2005) Nature , vol.434 , pp. 772-777
    • Honda, K.1    Yanai, H.2    Negishi, H.3    Asagiri, M.4    Sato, M.5    Mizutani, T.6
  • 19
    • 33645841633 scopus 로고    scopus 로고
    • IkappaB kinase-alpha is critical for interferon-alpha production induced by Toll-like receptors 7 and 9
    • Hoshino K., Sugiyama T., Matsumoto M., Tanaka T., Saito M., Hemmi H., et al. IkappaB kinase-alpha is critical for interferon-alpha production induced by Toll-like receptors 7 and 9. Nature 2006, 440:949-953.
    • (2006) Nature , vol.440 , pp. 949-953
    • Hoshino, K.1    Sugiyama, T.2    Matsumoto, M.3    Tanaka, T.4    Saito, M.5    Hemmi, H.6
  • 20
    • 0037799886 scopus 로고    scopus 로고
    • Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex
    • Jiang Z., Johnson H.J., Nie H., Qin J., Bird T.A., Li X. Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex. J Biol Chem 2003, 278:10952-10956.
    • (2003) J Biol Chem , vol.278 , pp. 10952-10956
    • Jiang, Z.1    Johnson, H.J.2    Nie, H.3    Qin, J.4    Bird, T.A.5    Li, X.6
  • 21
    • 0031893220 scopus 로고    scopus 로고
    • Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation
    • Lin R., Heylbroeck C., Pitha P.M., Hiscott J. Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation. Mol Cell Biol 1998, 18:2986-2996.
    • (1998) Mol Cell Biol , vol.18 , pp. 2986-2996
    • Lin, R.1    Heylbroeck, C.2    Pitha, P.M.3    Hiscott, J.4
  • 22
    • 34447499052 scopus 로고    scopus 로고
    • Triggering the innate antiviral response through IRF-3 activation
    • Hiscott J. Triggering the innate antiviral response through IRF-3 activation. J Biol Chem 2007, 282:15325-15329.
    • (2007) J Biol Chem , vol.282 , pp. 15325-15329
    • Hiscott, J.1
  • 23
    • 77952566304 scopus 로고    scopus 로고
    • The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway
    • Yang P., An H., Liu X., Wen M., Zheng Y., Rui Y., et al. The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway. Nat Immunol 2010, 11:487-494.
    • (2010) Nat Immunol , vol.11 , pp. 487-494
    • Yang, P.1    An, H.2    Liu, X.3    Wen, M.4    Zheng, Y.5    Rui, Y.6
  • 24
    • 84880081839 scopus 로고    scopus 로고
    • Inhibition of viral pathogenesis and promotion of the septic shock response to bacterial infection by IRF-3 are regulated by the acetylation and phosphorylation of its coactivators
    • Chattopadhyay S., Fensterl V., Zhang Y., Veleeparambil M., Wetzel J.L., Sen G.C. Inhibition of viral pathogenesis and promotion of the septic shock response to bacterial infection by IRF-3 are regulated by the acetylation and phosphorylation of its coactivators. mBio 2013, 4.
    • (2013) mBio , pp. 4
    • Chattopadhyay, S.1    Fensterl, V.2    Zhang, Y.3    Veleeparambil, M.4    Wetzel, J.L.5    Sen, G.C.6
  • 25
    • 0242556891 scopus 로고    scopus 로고
    • Toll-like receptors: balancing host resistance with immune tolerance
    • Pasare C., Medzhitov R. Toll-like receptors: balancing host resistance with immune tolerance. Curr Opin Immunol 2003, 15:677-682.
    • (2003) Curr Opin Immunol , vol.15 , pp. 677-682
    • Pasare, C.1    Medzhitov, R.2
  • 27
    • 84862068459 scopus 로고    scopus 로고
    • Genetic variation in Toll-like receptors and disease susceptibility
    • Netea M.G., Wijmenga C., O'Neill L.A. Genetic variation in Toll-like receptors and disease susceptibility. Nat Immunol 2012, 13:535-542.
    • (2012) Nat Immunol , vol.13 , pp. 535-542
    • Netea, M.G.1    Wijmenga, C.2    O'Neill, L.A.3
  • 29
    • 79551686422 scopus 로고    scopus 로고
    • Oncogenically active MYD88 mutations in human lymphoma
    • Ngo V.N., Young R.M., Schmitz R., Jhavar S., Xiao W., Lim K.H., et al. Oncogenically active MYD88 mutations in human lymphoma. Nature 2011, 470:115-119.
    • (2011) Nature , vol.470 , pp. 115-119
    • Ngo, V.N.1    Young, R.M.2    Schmitz, R.3    Jhavar, S.4    Xiao, W.5    Lim, K.H.6
  • 30
    • 0034891984 scopus 로고    scopus 로고
    • Detection of Toll-like receptor 2 (TLR2) mutation in the lepromatous leprosy patients
    • Kang T.J., Chae G.T. Detection of Toll-like receptor 2 (TLR2) mutation in the lepromatous leprosy patients. FEMS Immunol Med Microbiol 2001, 31:53-58.
    • (2001) FEMS Immunol Med Microbiol , vol.31 , pp. 53-58
    • Kang, T.J.1    Chae, G.T.2
  • 31
    • 1042269515 scopus 로고    scopus 로고
    • The Arg753GLn polymorphism of the human Toll-like receptor 2 gene in tuberculosis disease
    • Ogus A.C., Yoldas B., Ozdemir T., Uguz A., Olcen S., Keser I., et al. The Arg753GLn polymorphism of the human Toll-like receptor 2 gene in tuberculosis disease. Eur Respir J 2004, 23:219-223.
    • (2004) Eur Respir J , vol.23 , pp. 219-223
    • Ogus, A.C.1    Yoldas, B.2    Ozdemir, T.3    Uguz, A.4    Olcen, S.5    Keser, I.6
  • 32
    • 84868316949 scopus 로고    scopus 로고
    • R753Q polymorphism inhibits Toll-like receptor (TLR) 2 tyrosine phosphorylation, dimerization with TLR6, and recruitment of myeloid differentiation primary response protein 88
    • Xiong Y., Song C., Snyder G.A., Sundberg E.J., Medvedev A.E. R753Q polymorphism inhibits Toll-like receptor (TLR) 2 tyrosine phosphorylation, dimerization with TLR6, and recruitment of myeloid differentiation primary response protein 88. J Biol Chem 2012, 287:38327-38337.
    • (2012) J Biol Chem , vol.287 , pp. 38327-38337
    • Xiong, Y.1    Song, C.2    Snyder, G.A.3    Sundberg, E.J.4    Medvedev, A.E.5
  • 33
    • 34047098731 scopus 로고    scopus 로고
    • A Mal functional variant is associated with protection against invasive pneumococcal disease, bacteremia, malaria and tuberculosis
    • Khor C.C., Chapman S.J., Vannberg F.O., Dunne A., Murphy C., Ling E.Y., et al. A Mal functional variant is associated with protection against invasive pneumococcal disease, bacteremia, malaria and tuberculosis. Nat Genet 2007, 39:523-528.
    • (2007) Nat Genet , vol.39 , pp. 523-528
    • Khor, C.C.1    Chapman, S.J.2    Vannberg, F.O.3    Dunne, A.4    Murphy, C.5    Ling, E.Y.6
  • 34
    • 34948904198 scopus 로고    scopus 로고
    • Selective predisposition to bacterial infections in IRAK-4-deficient children: IRAK-4-dependent TLRs are otherwise redundant in protective immunity
    • Ku C.L., von Bernuth H., Picard C., Zhang S.Y., Chang H.H., Yang K., et al. Selective predisposition to bacterial infections in IRAK-4-deficient children: IRAK-4-dependent TLRs are otherwise redundant in protective immunity. J Exp Med 2007, 204:2407-2422.
    • (2007) J Exp Med , vol.204 , pp. 2407-2422
    • Ku, C.L.1    von Bernuth, H.2    Picard, C.3    Zhang, S.Y.4    Chang, H.H.5    Yang, K.6
  • 35
    • 34548699323 scopus 로고    scopus 로고
    • TLR3 deficiency in patients with herpes simplex encephalitis
    • Zhang S.Y., Jouanguy E., Ugolini S., Smahi A., Elain G., Romero P., et al. TLR3 deficiency in patients with herpes simplex encephalitis. Science 2007, 317:1522-1527.
    • (2007) Science , vol.317 , pp. 1522-1527
    • Zhang, S.Y.1    Jouanguy, E.2    Ugolini, S.3    Smahi, A.4    Elain, G.5    Romero, P.6
  • 36
  • 37
    • 77954995650 scopus 로고    scopus 로고
    • Toll-like receptor 3 regulates angiogenesis and apoptosis in prostate cancer cell lines through hypoxia-inducible factor 1 alpha
    • Paone A., Galli R., Gabellini C., Lukashev D., Starace D., Gorlach A., et al. Toll-like receptor 3 regulates angiogenesis and apoptosis in prostate cancer cell lines through hypoxia-inducible factor 1 alpha. Neoplasia 2010, 12:539-549.
    • (2010) Neoplasia , vol.12 , pp. 539-549
    • Paone, A.1    Galli, R.2    Gabellini, C.3    Lukashev, D.4    Starace, D.5    Gorlach, A.6
  • 38
    • 54849148000 scopus 로고    scopus 로고
    • Toll-like receptor 3 and geographic atrophy in age-related macular degeneration
    • Yang Z., Stratton C., Francis P.J., Kleinman M.E., Tan P.L., Gibbs D., et al. Toll-like receptor 3 and geographic atrophy in age-related macular degeneration. N Engl J Med 2008, 359:1456-1463.
    • (2008) N Engl J Med , vol.359 , pp. 1456-1463
    • Yang, Z.1    Stratton, C.2    Francis, P.J.3    Kleinman, M.E.4    Tan, P.L.5    Gibbs, D.6
  • 39
    • 0034084438 scopus 로고    scopus 로고
    • TLR4 mutations are associated with endotoxin hyporesponsiveness in humans
    • Arbour N.C., Lorenz E., Schutte B.C., Zabner J., Kline J.N., Jones M., et al. TLR4 mutations are associated with endotoxin hyporesponsiveness in humans. Nat Genet 2000, 25:187-191.
    • (2000) Nat Genet , vol.25 , pp. 187-191
    • Arbour, N.C.1    Lorenz, E.2    Schutte, B.C.3    Zabner, J.4    Kline, J.N.5    Jones, M.6
  • 40
    • 0037071251 scopus 로고    scopus 로고
    • Relevance of mutations in the TLR4 receptor in patients with Gram-negative septic shock
    • Lorenz E., Mira J.P., Frees K.L., Schwartz D.A. Relevance of mutations in the TLR4 receptor in patients with Gram-negative septic shock. Arch Intern Med 2002, 162:1028-1032.
    • (2002) Arch Intern Med , vol.162 , pp. 1028-1032
    • Lorenz, E.1    Mira, J.P.2    Frees, K.L.3    Schwartz, D.A.4
  • 42
    • 84885129586 scopus 로고    scopus 로고
    • IFIT2 is an effector protein of type I IFN-mediated amplification of lipopolysaccharide (LPS)-induced TNF-alpha secretion and LPS-induced endotoxin shock
    • Siegfried A., Berchtold S., Manncke B., Deuschle E., Reber J., Ott T., et al. IFIT2 is an effector protein of type I IFN-mediated amplification of lipopolysaccharide (LPS)-induced TNF-alpha secretion and LPS-induced endotoxin shock. J Immunol 2013, 191:3913-3921.
    • (2013) J Immunol , vol.191 , pp. 3913-3921
    • Siegfried, A.1    Berchtold, S.2    Manncke, B.3    Deuschle, E.4    Reber, J.5    Ott, T.6
  • 43
    • 0034445697 scopus 로고    scopus 로고
    • Differential alteration in intestinal epithelial cell expression of Toll-like receptor 3 (TLR3) and TLR4 in inflammatory bowel disease
    • Cario E., Podolsky D.K. Differential alteration in intestinal epithelial cell expression of Toll-like receptor 3 (TLR3) and TLR4 in inflammatory bowel disease. Infect Immun 2000, 68:7010-7017.
    • (2000) Infect Immun , vol.68 , pp. 7010-7017
    • Cario, E.1    Podolsky, D.K.2
  • 44
    • 84883214806 scopus 로고    scopus 로고
    • Toll-like receptor 4 mediates retinal ischemia/reperfusion injury through nuclear factor-kappaB and spleen tyrosine kinase activation
    • Ishizuka F., Shimazawa M., Inoue Y., Nakano Y., Ogishima H., Nakamura S., et al. Toll-like receptor 4 mediates retinal ischemia/reperfusion injury through nuclear factor-kappaB and spleen tyrosine kinase activation. Invest Ophthalmol Vis Sci 2013, 54:5807-5816.
    • (2013) Invest Ophthalmol Vis Sci , vol.54 , pp. 5807-5816
    • Ishizuka, F.1    Shimazawa, M.2    Inoue, Y.3    Nakano, Y.4    Ogishima, H.5    Nakamura, S.6
  • 45
    • 84866735326 scopus 로고    scopus 로고
    • TLR7 and TLR9 in SLE: when sensing self goes wrong
    • Celhar T., Magalhaes R., Fairhurst A.M. TLR7 and TLR9 in SLE: when sensing self goes wrong. Immunol Res 2012, 53:58-77.
    • (2012) Immunol Res , vol.53 , pp. 58-77
    • Celhar, T.1    Magalhaes, R.2    Fairhurst, A.M.3
  • 47
    • 33746545577 scopus 로고    scopus 로고
    • Toll-like receptor 3 associates with c-Src tyrosine kinase on endosomes to initiate antiviral signaling
    • Johnsen I.B., Nguyen T.T., Ringdal M., Tryggestad A.M., Bakke O., Lien E., et al. Toll-like receptor 3 associates with c-Src tyrosine kinase on endosomes to initiate antiviral signaling. EMBO J 2006, 25:3335-3346.
    • (2006) EMBO J , vol.25 , pp. 3335-3346
    • Johnsen, I.B.1    Nguyen, T.T.2    Ringdal, M.3    Tryggestad, A.M.4    Bakke, O.5    Lien, E.6
  • 48
    • 0038701608 scopus 로고    scopus 로고
    • Double-stranded RNA signaling by Toll-like receptor 3 requires specific tyrosine residues in its cytoplasmic domain
    • Sarkar S.N., Smith H.L., Rowe T.M., Sen G.C. Double-stranded RNA signaling by Toll-like receptor 3 requires specific tyrosine residues in its cytoplasmic domain. J Biol Chem 2003, 278:4393-4396.
    • (2003) J Biol Chem , vol.278 , pp. 4393-4396
    • Sarkar, S.N.1    Smith, H.L.2    Rowe, T.M.3    Sen, G.C.4
  • 49
    • 7544225495 scopus 로고    scopus 로고
    • Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling
    • Sarkar S.N., Peters K.L., Elco C.P., Sakamoto S., Pal S., Sen G.C. Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling. Nat Struct Mol Biol 2004, 11:1060-1067.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1060-1067
    • Sarkar, S.N.1    Peters, K.L.2    Elco, C.P.3    Sakamoto, S.4    Pal, S.5    Sen, G.C.6
  • 50
    • 33947520687 scopus 로고    scopus 로고
    • Two tyrosine residues of Toll-like receptor 3 trigger different steps of NF-kappa B activation
    • Sarkar S.N., Elco C.P., Peters K.L., Chattopadhyay S., Sen G.C. Two tyrosine residues of Toll-like receptor 3 trigger different steps of NF-kappa B activation. J Biol Chem 2007, 282:3423-3427.
    • (2007) J Biol Chem , vol.282 , pp. 3423-3427
    • Sarkar, S.N.1    Elco, C.P.2    Peters, K.L.3    Chattopadhyay, S.4    Sen, G.C.5
  • 51
    • 84897415714 scopus 로고    scopus 로고
    • The inducible nitric-oxide synthase (iNOS)/Src axis mediates Toll-like receptor 3 tyrosine 759 phosphorylation and enhances its signal transduction, leading to interferon-beta synthesis in macrophages
    • Hsieh M.Y., Chang M.Y., Chen Y.J., Li Y.K., Chuang T.H., Yu G.Y., et al. The inducible nitric-oxide synthase (iNOS)/Src axis mediates Toll-like receptor 3 tyrosine 759 phosphorylation and enhances its signal transduction, leading to interferon-beta synthesis in macrophages. J Biol Chem 2014, 289:9208-9220.
    • (2014) J Biol Chem , vol.289 , pp. 9208-9220
    • Hsieh, M.Y.1    Chang, M.Y.2    Chen, Y.J.3    Li, Y.K.4    Chuang, T.H.5    Yu, G.Y.6
  • 52
    • 84859564599 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase phosphorylates Toll-like receptor 3 to initiate antiviral response
    • Lee K.G., Xu S., Kang Z.H., Huo J., Huang M., Liu D., et al. Bruton's tyrosine kinase phosphorylates Toll-like receptor 3 to initiate antiviral response. Proc Natl Acad Sci U S A 2012, 109:5791-5796.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5791-5796
    • Lee, K.G.1    Xu, S.2    Kang, Z.H.3    Huo, J.4    Huang, M.5    Liu, D.6
  • 53
  • 54
    • 81055129630 scopus 로고    scopus 로고
    • CD14 controls the LPS-induced endocytosis of Toll-like receptor 4
    • Zanoni I., Ostuni R., Marek L.R., Barresi S., Barbalat R., Barton G.M., et al. CD14 controls the LPS-induced endocytosis of Toll-like receptor 4. Cell 2011, 147:868-880.
    • (2011) Cell , vol.147 , pp. 868-880
    • Zanoni, I.1    Ostuni, R.2    Marek, L.R.3    Barresi, S.4    Barbalat, R.5    Barton, G.M.6
  • 55
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • Yamamoto M., Sato S., Hemmi H., Uematsu S., Hoshino K., Kaisho T., et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat Immunol 2003, 4:1144-1150.
    • (2003) Nat Immunol , vol.4 , pp. 1144-1150
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Uematsu, S.4    Hoshino, K.5    Kaisho, T.6
  • 56
    • 40949134086 scopus 로고    scopus 로고
    • TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta
    • Kagan J.C., Su T., Horng T., Chow A., Akira S., Medzhitov R. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta. Nat Immunol 2008, 9:361-368.
    • (2008) Nat Immunol , vol.9 , pp. 361-368
    • Kagan, J.C.1    Su, T.2    Horng, T.3    Chow, A.4    Akira, S.5    Medzhitov, R.6
  • 57
    • 0037378954 scopus 로고    scopus 로고
    • Involvement of protein tyrosine kinase in Toll-like receptor 4-mediated NF-kappa B activation in human peripheral blood monocytes
    • Chen L.Y., Zuraw B.L., Zhao M., Liu F.T., Huang S., Pan Z.K. Involvement of protein tyrosine kinase in Toll-like receptor 4-mediated NF-kappa B activation in human peripheral blood monocytes. Am J Physiol Lung Cell Mol Physiol 2003, 284:L607-L613.
    • (2003) Am J Physiol Lung Cell Mol Physiol , vol.284 , pp. L607-L613
    • Chen, L.Y.1    Zuraw, B.L.2    Zhao, M.3    Liu, F.T.4    Huang, S.5    Pan, Z.K.6
  • 58
    • 35548985405 scopus 로고    scopus 로고
    • Chemical inhibition of Src family kinases affects major LPS-activated pathways in primary human macrophages
    • Smolinska M.J., Horwood N.J., Page T.H., Smallie T., Foxwell B.M. Chemical inhibition of Src family kinases affects major LPS-activated pathways in primary human macrophages. Mol Immunol 2008, 45:990-1000.
    • (2008) Mol Immunol , vol.45 , pp. 990-1000
    • Smolinska, M.J.1    Horwood, N.J.2    Page, T.H.3    Smallie, T.4    Foxwell, B.M.5
  • 59
    • 34447525018 scopus 로고    scopus 로고
    • Role of TLR4 tyrosine phosphorylation in signal transduction and endotoxin tolerance
    • Medvedev A.E., Piao W., Shoenfelt J., Rhee S.H., Chen H., Basu S., et al. Role of TLR4 tyrosine phosphorylation in signal transduction and endotoxin tolerance. J Biol Chem 2007, 282:16042-16053.
    • (2007) J Biol Chem , vol.282 , pp. 16042-16053
    • Medvedev, A.E.1    Piao, W.2    Shoenfelt, J.3    Rhee, S.H.4    Chen, H.5    Basu, S.6
  • 60
    • 84863912331 scopus 로고    scopus 로고
    • Lyn kinase controls TLR4-dependent IKK and MAPK activation modulating the activity of TRAF-6/TAK-1 protein complex in mast cells
    • Avila M., Martinez-Juarez A., Ibarra-Sanchez A., Gonzalez-Espinosa C. Lyn kinase controls TLR4-dependent IKK and MAPK activation modulating the activity of TRAF-6/TAK-1 protein complex in mast cells. Innate Immun 2012, 18:648-660.
    • (2012) Innate Immun , vol.18 , pp. 648-660
    • Avila, M.1    Martinez-Juarez, A.2    Ibarra-Sanchez, A.3    Gonzalez-Espinosa, C.4
  • 61
    • 0037492123 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is a Toll/interleukin-1 receptor domain-binding protein that participates in nuclear factor kappaB activation by Toll-like receptor 4
    • Jefferies C.A., Doyle S., Brunner C., Dunne A., Brint E., Wietek C., et al. Bruton's tyrosine kinase is a Toll/interleukin-1 receptor domain-binding protein that participates in nuclear factor kappaB activation by Toll-like receptor 4. J Biol Chem 2003, 278:26258-26264.
    • (2003) J Biol Chem , vol.278 , pp. 26258-26264
    • Jefferies, C.A.1    Doyle, S.2    Brunner, C.3    Dunne, A.4    Brint, E.5    Wietek, C.6
  • 62
    • 84867304046 scopus 로고    scopus 로고
    • The SYK side of TLR4: signalling mechanisms in response to LPS and minimally oxidized LDL
    • Miller Y.I., Choi S.H., Wiesner P., Bae Y.S. The SYK side of TLR4: signalling mechanisms in response to LPS and minimally oxidized LDL. Br J Pharmacol 2012, 167:990-999.
    • (2012) Br J Pharmacol , vol.167 , pp. 990-999
    • Miller, Y.I.1    Choi, S.H.2    Wiesner, P.3    Bae, Y.S.4
  • 63
    • 84884224192 scopus 로고    scopus 로고
    • The tyrosine kinase Syk differentially regulates Toll-like receptor signaling downstream of the adaptor molecules TRAF6 and TRAF3
    • Lin Y.C., Huang D.Y., Chu C.L., Lin Y.L., Lin W.W. The tyrosine kinase Syk differentially regulates Toll-like receptor signaling downstream of the adaptor molecules TRAF6 and TRAF3. Sci Signal 2013, 6:ra71.
    • (2013) Sci Signal , vol.6 , pp. ra71
    • Lin, Y.C.1    Huang, D.Y.2    Chu, C.L.3    Lin, Y.L.4    Lin, W.W.5
  • 64
    • 84893358098 scopus 로고    scopus 로고
    • Activation of the epidermal growth factor receptor in macrophages regulates cytokine production and experimental colitis
    • Lu N., Wang L., Cao H., Liu L., Van Kaer L., Washington M.K., et al. Activation of the epidermal growth factor receptor in macrophages regulates cytokine production and experimental colitis. J Immunol 2014, 192:1013-1023.
    • (2014) J Immunol , vol.192 , pp. 1013-1023
    • Lu, N.1    Wang, L.2    Cao, H.3    Liu, L.4    Van Kaer, L.5    Washington, M.K.6
  • 65
    • 0034577944 scopus 로고    scopus 로고
    • Toll-like receptor 2-mediated NF-kappa B activation requires a Rac1-dependent pathway
    • Arbibe L., Mira J.P., Teusch N., Kline L., Guha M., Mackman N., et al. Toll-like receptor 2-mediated NF-kappa B activation requires a Rac1-dependent pathway. Nat Immunol 2000, 1:533-540.
    • (2000) Nat Immunol , vol.1 , pp. 533-540
    • Arbibe, L.1    Mira, J.P.2    Teusch, N.3    Kline, L.4    Guha, M.5    Mackman, N.6
  • 66
    • 77955888865 scopus 로고    scopus 로고
    • TLR2 ligands induce cardioprotection against ischaemia/reperfusion injury through a PI3K/Akt-dependent mechanism
    • Ha T., Hu Y., Liu L., Lu C., McMullen J.R., Kelley J., et al. TLR2 ligands induce cardioprotection against ischaemia/reperfusion injury through a PI3K/Akt-dependent mechanism. Cardiovasc Res 2010, 87:694-703.
    • (2010) Cardiovasc Res , vol.87 , pp. 694-703
    • Ha, T.1    Hu, Y.2    Liu, L.3    Lu, C.4    McMullen, J.R.5    Kelley, J.6
  • 67
    • 33644844972 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is required for TLR2 and TLR4-induced TNF, but not IL-6, production
    • Horwood N.J., Page T.H., McDaid J.P., Palmer C.D., Campbell J., Mahon T., et al. Bruton's tyrosine kinase is required for TLR2 and TLR4-induced TNF, but not IL-6, production. J Immunol 2006, 176:3635-3641.
    • (2006) J Immunol , vol.176 , pp. 3635-3641
    • Horwood, N.J.1    Page, T.H.2    McDaid, J.P.3    Palmer, C.D.4    Campbell, J.5    Mahon, T.6
  • 68
    • 33845450196 scopus 로고    scopus 로고
    • A phosphorylation site in the Toll-like receptor 5 TIR domain is required for inflammatory signalling in response to flagellin
    • Ivison S.M., Khan M.A., Graham N.R., Bernales C.Q., Kaleem A., Tirling C.O., et al. A phosphorylation site in the Toll-like receptor 5 TIR domain is required for inflammatory signalling in response to flagellin. Biochem Biophys Res Commun 2007, 352:936-941.
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 936-941
    • Ivison, S.M.1    Khan, M.A.2    Graham, N.R.3    Bernales, C.Q.4    Kaleem, A.5    Tirling, C.O.6
  • 69
    • 38149021578 scopus 로고    scopus 로고
    • The covalent modification and regulation of TLR8 in HEK-293 cells stimulated with imidazoquinoline agonists
    • Rajagopal R., Waller A.S., Mendoza J.D., Wightman P.D. The covalent modification and regulation of TLR8 in HEK-293 cells stimulated with imidazoquinoline agonists. Biochem J 2008, 409:275-287.
    • (2008) Biochem J , vol.409 , pp. 275-287
    • Rajagopal, R.1    Waller, A.S.2    Mendoza, J.D.3    Wightman, P.D.4
  • 70
    • 45549085993 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase separately regulates NFkappaB p65RelA activation and cytokine interleukin (IL)-10/IL-12 production in TLR9-stimulated B Cells
    • Lee K.G., Xu S., Wong E.T., Tergaonkar V., Lam K.P. Bruton's tyrosine kinase separately regulates NFkappaB p65RelA activation and cytokine interleukin (IL)-10/IL-12 production in TLR9-stimulated B Cells. J Biol Chem 2008, 283:11189-11198.
    • (2008) J Biol Chem , vol.283 , pp. 11189-11198
    • Lee, K.G.1    Xu, S.2    Wong, E.T.3    Tergaonkar, V.4    Lam, K.P.5
  • 71
    • 37549021148 scopus 로고    scopus 로고
    • Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine kinase
    • Doyle S.L., Jefferies C.A., Feighery C., O'Neill L.A. Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine kinase. J Biol Chem 2007, 282:36953-36960.
    • (2007) J Biol Chem , vol.282 , pp. 36953-36960
    • Doyle, S.L.1    Jefferies, C.A.2    Feighery, C.3    O'Neill, L.A.4
  • 72
    • 33645281948 scopus 로고    scopus 로고
    • CpG-induced tyrosine phosphorylation occurs via a TLR9-independent mechanism and is required for cytokine secretion
    • Sanjuan M.A., Rao N., Lai K.T., Gu Y., Sun S., Fuchs A., et al. CpG-induced tyrosine phosphorylation occurs via a TLR9-independent mechanism and is required for cytokine secretion. J Cell Biol 2006, 172:1057-1068.
    • (2006) J Cell Biol , vol.172 , pp. 1057-1068
    • Sanjuan, M.A.1    Rao, N.2    Lai, K.T.3    Gu, Y.4    Sun, S.5    Fuchs, A.6
  • 73
    • 84856020199 scopus 로고    scopus 로고
    • Cutting edge: a TLR9 cytoplasmic tyrosine motif is selectively required for proinflammatory cytokine production
    • Chockalingam A., Rose W.A., Hasan M., Ju C.H., Leifer C.A. Cutting edge: a TLR9 cytoplasmic tyrosine motif is selectively required for proinflammatory cytokine production. J Immunol 2012, 188:527-530.
    • (2012) J Immunol , vol.188 , pp. 527-530
    • Chockalingam, A.1    Rose, W.A.2    Hasan, M.3    Ju, C.H.4    Leifer, C.A.5
  • 74
    • 80054756987 scopus 로고    scopus 로고
    • Myeloid differentiation factor-2 interacts with Lyn kinase and is tyrosine phosphorylated following lipopolysaccharide-induced activation of the TLR4 signaling pathway
    • Gray P., Dagvadorj J., Michelsen K.S., Brikos C., Rentsendorj A., Town T., et al. Myeloid differentiation factor-2 interacts with Lyn kinase and is tyrosine phosphorylated following lipopolysaccharide-induced activation of the TLR4 signaling pathway. J Immunol 2011, 187:4331-4337.
    • (2011) J Immunol , vol.187 , pp. 4331-4337
    • Gray, P.1    Dagvadorj, J.2    Michelsen, K.S.3    Brikos, C.4    Rentsendorj, A.5    Town, T.6
  • 75
    • 41249084567 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of MyD88 adapter-like (Mal) is critical for signal transduction and blocked in endotoxin tolerance
    • Piao W., Song C., Chen H., Wahl L.M., Fitzgerald K.A., O'Neill L.A., et al. Tyrosine phosphorylation of MyD88 adapter-like (Mal) is critical for signal transduction and blocked in endotoxin tolerance. J Biol Chem 2008, 283:3109-3119.
    • (2008) J Biol Chem , vol.283 , pp. 3109-3119
    • Piao, W.1    Song, C.2    Chen, H.3    Wahl, L.M.4    Fitzgerald, K.A.5    O'Neill, L.A.6
  • 76
    • 33744543517 scopus 로고    scopus 로고
    • MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction
    • Gray P., Dunne A., Brikos C., Jefferies C.A., Doyle S.L., O'Neill L.A. MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction. J Biol Chem 2006, 281:10489-10495.
    • (2006) J Biol Chem , vol.281 , pp. 10489-10495
    • Gray, P.1    Dunne, A.2    Brikos, C.3    Jefferies, C.A.4    Doyle, S.L.5    O'Neill, L.A.6
  • 77
    • 31344467156 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation
    • Mansell A., Smith R., Doyle S.L., Gray P., Fenner J.E., Crack P.J., et al. Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation. Nat Immunol 2006, 7:148-155.
    • (2006) Nat Immunol , vol.7 , pp. 148-155
    • Mansell, A.1    Smith, R.2    Doyle, S.L.3    Gray, P.4    Fenner, J.E.5    Crack, P.J.6
  • 78
    • 77954946392 scopus 로고    scopus 로고
    • Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b
    • Han C., Jin J., Xu S., Liu H., Li N., Cao X. Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b. Nat Immunol 2010, 11:734-742.
    • (2010) Nat Immunol , vol.11 , pp. 734-742
    • Han, C.1    Jin, J.2    Xu, S.3    Liu, H.4    Li, N.5    Cao, X.6
  • 79
    • 84890363675 scopus 로고    scopus 로고
    • Caveolin-1 Tyr14 phosphorylation induces interaction with TLR4 in endothelial cells and mediates MyD88-dependent signaling and sepsis-induced lung inflammation
    • Jiao H., Zhang Y., Yan Z., Wang Z.G., Liu G., Minshall R.D., et al. Caveolin-1 Tyr14 phosphorylation induces interaction with TLR4 in endothelial cells and mediates MyD88-dependent signaling and sepsis-induced lung inflammation. J Immunol 2013, 191:6191-6199.
    • (2013) J Immunol , vol.191 , pp. 6191-6199
    • Jiao, H.1    Zhang, Y.2    Yan, Z.3    Wang, Z.G.4    Liu, G.5    Minshall, R.D.6
  • 80
    • 84859152282 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the E3 ubiquitin ligase TRIM21 positively regulates interaction with IRF3 and hence TRIM21 activity
    • Stacey K.B., Breen E., Jefferies C.A. Tyrosine phosphorylation of the E3 ubiquitin ligase TRIM21 positively regulates interaction with IRF3 and hence TRIM21 activity. PLoS ONE 2012, 7:e34041.
    • (2012) PLoS ONE , vol.7 , pp. e34041
    • Stacey, K.B.1    Breen, E.2    Jefferies, C.A.3
  • 82
    • 84871119463 scopus 로고    scopus 로고
    • Comment on "epidermal growth factor receptor is essential for Toll-like receptor 3 signaling"
    • Burtness B., Marur S., Bauman J.E., Golemis E.A., Mehra R., Cohen S.J. Comment on "epidermal growth factor receptor is essential for Toll-like receptor 3 signaling". Sci Signal 2012, 5:lc5.
    • (2012) Sci Signal , vol.5 , pp. lc5
    • Burtness, B.1    Marur, S.2    Bauman, J.E.3    Golemis, E.A.4    Mehra, R.5    Cohen, S.J.6
  • 83
    • 57749090358 scopus 로고    scopus 로고
    • Helicobacter pylori protein HP0175 transactivates epidermal growth factor receptor through TLR4 in gastric epithelial cells
    • Basu S., Pathak S.K., Chatterjee G., Pathak S., Basu J., Kundu M. Helicobacter pylori protein HP0175 transactivates epidermal growth factor receptor through TLR4 in gastric epithelial cells. J Biol Chem 2008, 283:32369-32376.
    • (2008) J Biol Chem , vol.283 , pp. 32369-32376
    • Basu, S.1    Pathak, S.K.2    Chatterjee, G.3    Pathak, S.4    Basu, J.5    Kundu, M.6
  • 84
    • 84861663311 scopus 로고    scopus 로고
    • Transactivation of EGFR by LPS induces COX-2 expression in enterocytes
    • McElroy S.J., Hobbs S., Kallen M., Tejera N., Rosen M.J., Grishin A., et al. Transactivation of EGFR by LPS induces COX-2 expression in enterocytes. PLoS ONE 2012, 7:e38373.
    • (2012) PLoS ONE , vol.7 , pp. e38373
    • McElroy, S.J.1    Hobbs, S.2    Kallen, M.3    Tejera, N.4    Rosen, M.J.5    Grishin, A.6
  • 85
    • 11244277091 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and the immune response
    • Mustelin T., Vang T., Bottini N. Protein tyrosine phosphatases and the immune response. Nat Rev Immunol 2005, 5:43-57.
    • (2005) Nat Rev Immunol , vol.5 , pp. 43-57
    • Mustelin, T.1    Vang, T.2    Bottini, N.3
  • 86
    • 33845438110 scopus 로고    scopus 로고
    • SHP-2 phosphatase negatively regulates the TRIF adaptor protein-dependent type I interferon and proinflammatory cytokine production
    • An H., Zhao W., Hou J., Zhang Y., Xie Y., Zheng Y., et al. SHP-2 phosphatase negatively regulates the TRIF adaptor protein-dependent type I interferon and proinflammatory cytokine production. Immunity 2006, 25:919-928.
    • (2006) Immunity , vol.25 , pp. 919-928
    • An, H.1    Zhao, W.2    Hou, J.3    Zhang, Y.4    Xie, Y.5    Zheng, Y.6
  • 87
    • 42449121356 scopus 로고    scopus 로고
    • Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1
    • An H., Hou J., Zhou J., Zhao W., Xu H., Zheng Y., et al. Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1. Nat Immunol 2008, 9:542-550.
    • (2008) Nat Immunol , vol.9 , pp. 542-550
    • An, H.1    Hou, J.2    Zhou, J.3    Zhao, W.4    Xu, H.5    Zheng, Y.6
  • 88
    • 84873552386 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase with proline-glutamine-serine-threonine-rich motifs negatively regulates TLR-triggered innate responses by selectively inhibiting IkappaB kinase beta/NF-kappaB activation
    • Zhang P., Liu X., Li Y., Zhu X., Zhan Z., Meng J., et al. Protein tyrosine phosphatase with proline-glutamine-serine-threonine-rich motifs negatively regulates TLR-triggered innate responses by selectively inhibiting IkappaB kinase beta/NF-kappaB activation. J Immunol 2013, 190:1685-1694.
    • (2013) J Immunol , vol.190 , pp. 1685-1694
    • Zhang, P.1    Liu, X.2    Li, Y.3    Zhu, X.4    Zhan, Z.5    Meng, J.6
  • 89
    • 84861204618 scopus 로고    scopus 로고
    • CEACAM1 negatively regulates IL-1beta production in LPS activated neutrophils by recruiting SHP-1 to a SYK-TLR4-CEACAM1 complex
    • Lu R., Pan H., Shively J.E. CEACAM1 negatively regulates IL-1beta production in LPS activated neutrophils by recruiting SHP-1 to a SYK-TLR4-CEACAM1 complex. PLoS Pathog 2012, 8:e1002597.
    • (2012) PLoS Pathog , vol.8 , pp. e1002597
    • Lu, R.1    Pan, H.2    Shively, J.E.3
  • 90
    • 84867746584 scopus 로고    scopus 로고
    • Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs
    • Yan D., Wang X., Luo L., Cao X., Ge B. Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs. Nat Immunol 2012, 13:1063-1071.
    • (2012) Nat Immunol , vol.13 , pp. 1063-1071
    • Yan, D.1    Wang, X.2    Luo, L.3    Cao, X.4    Ge, B.5


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