메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Ficolin-2 Defends against Virulent Mycobacteria Tuberculosis Infection In Vivo, and Its Insufficiency Is Associated with Infection in Humans

Author keywords

[No Author keywords available]

Indexed keywords

FICOLIN 2; GAMMA INTERFERON; GLYCOLIPID; INTERLEUKIN 17; INTERLEUKIN 6; NITRIC OXIDE; RECOMBINANT PROTEIN; STREPTOMYCIN; STRESS ACTIVATED PROTEIN KINASE; TUBERCULOSTATIC AGENT; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84883647779     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073859     Document Type: Article
Times cited : (58)

References (44)
  • 1
    • 56149108209 scopus 로고    scopus 로고
    • Extensively drug-resistant tuberculosis in the United States, 1993-2007
    • doi:10.1001/jama.300.18.2153
    • Shah NS, Pratt R, Armstrong L, Robison V, Castro KG, et al. (2008) Extensively drug-resistant tuberculosis in the United States, 1993-2007. JAMA 300: 2153-2160. doi:10.1001/jama.300.18.2153. PubMed: 19001626.
    • (2008) JAMA , vol.300 , pp. 2153-2160
    • Shah, N.S.1    Pratt, R.2    Armstrong, L.3    Robison, V.4    Castro, K.G.5
  • 2
    • 57349100353 scopus 로고    scopus 로고
    • Recurrent tuberculosis in HIV-infected patients in Rio de Janeiro, Brazil
    • doi:10.1097/QAD.0b013e328311ac4e
    • Golub JE, Durovni B, King BS, Cavalacante SC, Pacheco AG, et al. (2008) Recurrent tuberculosis in HIV-infected patients in Rio de Janeiro, Brazil. AIDS 22: 2527-2533. doi:10.1097/QAD.0b013e328311ac4e. PubMed: 19005276.
    • (2008) AIDS , vol.22 , pp. 2527-2533
    • Golub, J.E.1    Durovni, B.2    King, B.S.3    Cavalacante, S.C.4    Pacheco, A.G.5
  • 3
    • 0036584407 scopus 로고    scopus 로고
    • Evolution of the lectin-complement pathway and its role in innate immunity
    • doi:10.1038/nri800
    • Fujita T, (2002) Evolution of the lectin-complement pathway and its role in innate immunity. Nat Rev Immunol 2: 346-353. doi:10.1038/nri800. PubMed: 12033740.
    • (2002) Nat Rev Immunol , vol.2 , pp. 346-353
    • Fujita, T.1
  • 4
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway--its role in innate immunity and evolution
    • doi:10.1111/j.0105-2896.2004.0123.x
    • Fujita T, Matsushita M, Endo Y, (2004) The lectin-complement pathway--its role in innate immunity and evolution. Immunol Rev 198: 185-202. doi:10.1111/j.0105-2896.2004.0123.x. PubMed: 15199963.
    • (2004) Immunol Rev , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 5
    • 0030587494 scopus 로고    scopus 로고
    • Cloning and characterization of the human lectin P35 gene and its related gene
    • doi:10.1006/geno.1996.0497
    • Endo Y, Sato Y, Matsushita M, Fujita T, (1996) Cloning and characterization of the human lectin P35 gene and its related gene. Genomics 36: 515-521. doi:10.1006/geno.1996.0497. PubMed: 8884275.
    • (1996) Genomics , vol.36 , pp. 515-521
    • Endo, Y.1    Sato, Y.2    Matsushita, M.3    Fujita, T.4
  • 6
    • 18344409247 scopus 로고    scopus 로고
    • Human L-ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain
    • doi:10.1016/S0014-5793(98)00267-1
    • Le Y, Lee SH, Kon OL, Lu J, (1998) Human L-ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain. FEBS Lett 425: 367-370. doi:10.1016/S0014-5793(98)00267-1. PubMed: 9559681.
    • (1998) FEBS Lett , vol.425 , pp. 367-370
    • Le, Y.1    Lee, S.H.2    Kon, O.L.3    Lu, J.4
  • 7
    • 0032516814 scopus 로고    scopus 로고
    • Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family
    • doi:10.1074/jbc.273.33.20721
    • Sugimoto R, Yae Y, Akaiwa M, Kitajima S, Shibata Y, et al. (1998) Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family. J Biol Chem 273: 20721-20727. doi:10.1074/jbc.273.33.20721. PubMed: 9694814.
    • (1998) J Biol Chem , vol.273 , pp. 20721-20727
    • Sugimoto, R.1    Yae, Y.2    Akaiwa, M.3    Kitajima, S.4    Shibata, Y.5
  • 8
    • 23844486704 scopus 로고    scopus 로고
    • Human M-ficolin is a secretory protein that activates the lectin complement pathway
    • Liu Y, Endo Y, Iwaki D, Nakata M, Matsushita M, et al. (2005) Human M-ficolin is a secretory protein that activates the lectin complement pathway. J Immunol 175: 3150-3156. PubMed: 16116205.
    • (2005) J Immunol , vol.175 , pp. 3150-3156
    • Liu, Y.1    Endo, Y.2    Iwaki, D.3    Nakata, M.4    Matsushita, M.5
  • 9
    • 34548038427 scopus 로고    scopus 로고
    • Identification of a functionally relevant signal peptide of mouse ficolin A
    • doi:10.5483/BMBRep.2007.40.4.532
    • Kwon S, Kim MS, Kim D, Lee KW, Choi SY, et al. (2007) Identification of a functionally relevant signal peptide of mouse ficolin A. J Biochem Mol Biol 40: 532-538. doi:10.5483/BMBRep.2007.40.4.532. PubMed: 17669269.
    • (2007) J Biochem Mol Biol , vol.40 , pp. 532-538
    • Kwon, S.1    Kim, M.S.2    Kim, D.3    Lee, K.W.4    Choi, S.Y.5
  • 10
    • 4744376266 scopus 로고    scopus 로고
    • Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human
    • Endo Y, Liu Y, Kanno K, Takahashi M, Matsushita M, et al. (2004) Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human pp. L/M-ficolins. Genomics 84: 737-744.
    • (2004) Genomics , vol.84 , pp. 737-744
    • Endo, Y.1    Liu, Y.2    Kanno, K.3    Takahashi, M.4    Matsushita, M.5
  • 11
    • 27644539147 scopus 로고    scopus 로고
    • Binding of porcine ficolin-alpha to lipopolysaccharides from Gram-negative bacteria and lipoteichoic acids from Gram-positive bacteria
    • doi:10.1016/j.dci.2005.04.002
    • Nahid AM, Sugii S, (2006) Binding of porcine ficolin-alpha to lipopolysaccharides from Gram-negative bacteria and lipoteichoic acids from Gram-positive bacteria. Dev Comp Immunol 30: 335-343. doi:10.1016/j.dci.2005.04.002. PubMed: 15964070.
    • (2006) Dev Comp Immunol , vol.30 , pp. 335-343
    • Nahid, A.M.1    Sugii, S.2
  • 12
    • 0034570757 scopus 로고    scopus 로고
    • Opsonic function and concentration of human serum ficolin/P35
    • Taira S, Kodama N, Matsushita M, Fujita T, (2000) Opsonic function and concentration of human serum ficolin/P35. Fukushima J Med Sci 46: 13-23. PubMed: 11446374.
    • (2000) Fukushima J Med Sci , vol.46 , pp. 13-23
    • Taira, S.1    Kodama, N.2    Matsushita, M.3    Fujita, T.4
  • 13
    • 10844272309 scopus 로고    scopus 로고
    • Role of L-ficolin/mannose-binding lectin-associated serine protease complexes in the opsonophagocytosis of type III group B streptococci
    • Aoyagi Y, Adderson EE, Min JG, Matsushita M, Fujita T, et al. (2005) Role of L-ficolin/mannose-binding lectin-associated serine protease complexes in the opsonophagocytosis of type III group B streptococci. J Immunol 174: 418-425. PubMed: 15611266.
    • (2005) J Immunol , vol.174 , pp. 418-425
    • Aoyagi, Y.1    Adderson, E.E.2    Min, J.G.3    Matsushita, M.4    Fujita, T.5
  • 14
    • 44649141897 scopus 로고    scopus 로고
    • Recognition of acetylated oligosaccharides by human L-ficolin
    • doi:10.1016/j.imlet.2008.03.014
    • Krarup A, Mitchell DA, Sim RB, (2008) Recognition of acetylated oligosaccharides by human L-ficolin. Immunol Lett 118: 152-156. doi:10.1016/j.imlet.2008.03.014. PubMed: 18486240.
    • (2008) Immunol Lett , vol.118 , pp. 152-156
    • Krarup, A.1    Mitchell, D.A.2    Sim, R.B.3
  • 15
    • 12844264792 scopus 로고    scopus 로고
    • Effect of capsulation of opportunistic pathogenic bacteria on binding of the pattern recognition molecules mannan-binding lectin, L-ficolin, and H-ficolin
    • doi:10.1128/IAI.73.2.1052-1060.2005
    • Krarup A, Sørensen UB, Matsushita M, Jensenius JC, Thiel S, (2005) Effect of capsulation of opportunistic pathogenic bacteria on binding of the pattern recognition molecules mannan-binding lectin, L-ficolin, and H-ficolin. Infect Immun 73: 1052-1060. doi:10.1128/IAI.73.2.1052-1060.2005. PubMed: 15664949.
    • (2005) Infect Immun , vol.73 , pp. 1052-1060
    • Krarup, A.1    Sørensen, U.B.2    Matsushita, M.3    Jensenius, J.C.4    Thiel, S.5
  • 16
    • 41649110643 scopus 로고    scopus 로고
    • Ficolins: novel pattern recognition molecules of the innate immune response
    • doi:10.1016/j.imbio.2007.10.009
    • Runza VL, Schwaeble W, Männel DN, (2008) Ficolins: novel pattern recognition molecules of the innate immune response. Immunobiology 213: 297-306. doi:10.1016/j.imbio.2007.10.009. PubMed: 18406375.
    • (2008) Immunobiology , vol.213 , pp. 297-306
    • Runza, V.L.1    Schwaeble, W.2    Männel, D.N.3
  • 17
    • 84871165182 scopus 로고    scopus 로고
    • Mice defieient in ficolin, a lectin complement pathway recognition molecule, are susceptible to Streptococcus pneumoniae infection
    • Endo Y, Takahashi M, Iwaki D, Ishida Y, Nakazawa N, et al. (2013) Mice defieient in ficolin, a lectin complement pathway recognition molecule, are susceptible to Streptococcus pneumoniae infection. J Immunol 189: 5860-5866.
    • (2013) J Immunol , vol.189 , pp. 5860-5866
    • Endo, Y.1    Takahashi, M.2    Iwaki, D.3    Ishida, Y.4    Nakazawa, N.5
  • 18
    • 80053386669 scopus 로고    scopus 로고
    • Interleukin 24 as a novel potential cytokine immunotherapy for the treatment of Mycobacterium tuberculosis infection
    • doi:10.1016/j.micinf.2011.06.012
    • Ma Y, Chen HD, Wang Y, Wang Q, Li Y, et al. (2011) Interleukin 24 as a novel potential cytokine immunotherapy for the treatment of Mycobacterium tuberculosis infection. Microbes Infect 13: 1099-1110. doi:10.1016/j.micinf.2011.06.012. PubMed: 21787878.
    • (2011) Microbes Infect , vol.13 , pp. 1099-1110
    • Ma, Y.1    Chen, H.D.2    Wang, Y.3    Wang, Q.4    Li, Y.5
  • 19
    • 84862796428 scopus 로고    scopus 로고
    • L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo
    • doi:10.1159/000335670
    • Pan Q, Chen H, Wang F, Jeza VT, Hou W, et al. (2012) L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo. J Innate Immun 4: 312-324. doi:10.1159/000335670. PubMed: 22399010.
    • (2012) J Innate Immun , vol.4 , pp. 312-324
    • Pan, Q.1    Chen, H.2    Wang, F.3    Jeza, V.T.4    Hou, W.5
  • 20
    • 56649123422 scopus 로고    scopus 로고
    • Lipoarabinomannan of Mycobacterium: mannose capping by a multifunctional terminal mannosyltransferase
    • doi:10.1073/pnas.0807761105
    • Kaur D, Obregón-Henao A, Pham H, Chatterjee D, Brennan PJ, et al. (2008) Lipoarabinomannan of Mycobacterium: mannose capping by a multifunctional terminal mannosyltransferase. Proc Natl Acad Sci U S A 105: 17973-17977. doi:10.1073/pnas.0807761105. PubMed: 19004785.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17973-17977
    • Kaur, D.1    Obregón-Henao, A.2    Pham, H.3    Chatterjee, D.4    Brennan, P.J.5
  • 21
    • 69949118734 scopus 로고    scopus 로고
    • Specifically binding of L-ficolin to N-glycans of HCV envelope glycoproteins E1 and E2 leads to complement activation
    • doi:10.1038/cmi.2009.32
    • Liu J, Ali MA, Shi Y, Zhao Y, Luo F, et al. (2009) Specifically binding of L-ficolin to N-glycans of HCV envelope glycoproteins E1 and E2 leads to complement activation. Cell Mol Immunol 6: 235-244. doi:10.1038/cmi.2009.32. PubMed: 19728924.
    • (2009) Cell Mol Immunol , vol.6 , pp. 235-244
    • Liu, J.1    Ali, M.A.2    Shi, Y.3    Zhao, Y.4    Luo, F.5
  • 22
    • 0032571113 scopus 로고    scopus 로고
    • Molecular cloning and characterization of mouse ficolin-A
    • doi:10.1006/bbrc.1998.8344
    • Fujimori Y, Harumiya S, Fukumoto Y, Miura Y, Yagasaki K, et al. (1998) Molecular cloning and characterization of mouse ficolin-A. Biochem Biophys Res Commun 244: 796-800. doi:10.1006/bbrc.1998.8344. PubMed: 9535745.
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 796-800
    • Fujimori, Y.1    Harumiya, S.2    Fukumoto, Y.3    Miura, Y.4    Yagasaki, K.5
  • 23
    • 0036147521 scopus 로고    scopus 로고
    • Comparison of Gene Transfer Efficiencies and Gene Expression Levels Achieved with Equine Infectious Anemia Virus- and Human Immunodeficiency Virus Type 1-Derived Lentivirus Vectors
    • doi:10.1128/JVI.76.3.1510-1515.2002
    • O'Rourke JP, Newbound GC, Kohn DB, Olsen JC, Bunnell BA, (2002) Comparison of Gene Transfer Efficiencies and Gene Expression Levels Achieved with Equine Infectious Anemia Virus- and Human Immunodeficiency Virus Type 1-Derived Lentivirus Vectors. J Virol 76: 1510-1515. doi:10.1128/JVI.76.3.1510-1515.2002. PubMed: 11773424.
    • (2002) J Virol , vol.76 , pp. 1510-1515
    • O'Rourke, J.P.1    Newbound, G.C.2    Kohn, D.B.3    Olsen, J.C.4    Bunnell, B.A.5
  • 24
    • 0034699429 scopus 로고    scopus 로고
    • Phagocytosis: measurement by flow cytometry
    • doi:10.1016/S0022-1759(00)00237-4
    • Lehmann AK, Sornes S, Halstensen A, (2000) Phagocytosis: measurement by flow cytometry. J Immunol Methods 243(1-2):: 229-242. doi:10.1016/S0022-1759(00)00237-4. PubMed: 10986417.
    • (2000) J Immunol Methods , vol.243 , pp. 229-242
    • Lehmann, A.K.1    Sornes, S.2    Halstensen, A.3
  • 26
    • 0036435835 scopus 로고    scopus 로고
    • Increased nitric oxide production by neutrophils from patients with chronic granulomatous disease on trimethoprim-sulfamethoxazole
    • doi:10.1016/S1089-8603(02)00110-6
    • Tsuji S, Taniuchi S, Hasui M, Yamamoto A, Kobayashi Y, (2002) Increased nitric oxide production by neutrophils from patients with chronic granulomatous disease on trimethoprim-sulfamethoxazole. Nitric Oxide 7: 283-288. doi:10.1016/S1089-8603(02)00110-6. PubMed: 12446177.
    • (2002) Nitric Oxide , vol.7 , pp. 283-288
    • Tsuji, S.1    Taniuchi, S.2    Hasui, M.3    Yamamoto, A.4    Kobayashi, Y.5
  • 27
    • 84878552360 scopus 로고    scopus 로고
    • PD1-based DNA vaccine amplifies HIV-1 GAG-specific CD8+ T cells in mice
    • doi:10.1172/JCI64704
    • Zhou J, Cheung AK, Tan Z, Wang H, Yu W, et al. (2013) PD1-based DNA vaccine amplifies HIV-1 GAG-specific CD8+ T cells in mice. J Clin Invest 123: 2629-2642. doi:10.1172/JCI64704. PubMed: 23635778.
    • (2013) J Clin Invest , vol.123 , pp. 2629-2642
    • Zhou, J.1    Cheung, A.K.2    Tan, Z.3    Wang, H.4    Yu, W.5
  • 28
    • 0033119812 scopus 로고    scopus 로고
    • P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients
    • doi:10.1016/S0165-2478(98)00147-3
    • Kilpatrick DC, Fujita T, Matsushita M, (1999) P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients. Immunol Lett 67: 109-112. doi:10.1016/S0165-2478(98)00147-3. PubMed: 10232391.
    • (1999) Immunol Lett , vol.67 , pp. 109-112
    • Kilpatrick, D.C.1    Fujita, T.2    Matsushita, M.3
  • 29
    • 84872844989 scopus 로고    scopus 로고
    • Early increased ficolin-2 concentrations are associated with severity of liver inflammation and efficacy of anti-viral therapy in chronic hepatitis C patients
    • doi:10.1111/sji.12014
    • Hu YL, Luo FL, Fu JL, Chen TL, Wu SM, et al. (2013) Early increased ficolin-2 concentrations are associated with severity of liver inflammation and efficacy of anti-viral therapy in chronic hepatitis C patients. Scand J Immunol 77: 144-150. doi:10.1111/sji.12014. PubMed: 23298162.
    • (2013) Scand J Immunol , vol.77 , pp. 144-150
    • Hu, Y.L.1    Luo, F.L.2    Fu, J.L.3    Chen, T.L.4    Wu, S.M.5
  • 30
    • 71649089075 scopus 로고    scopus 로고
    • Natural lysophospholipids reduce Mycobacterium tuberculosis-induced cytotoxicity and induce anti-mycobacterial activity by a phagolysosome maturation-dependent mechanism in A549 type II alveolar epithelial cells
    • doi:10.1111/j.1365-2567.2009.03145.x
    • Greco E, Santucci MB, Sali M, De Angelis FR, Papi M, et al. (2010) Natural lysophospholipids reduce Mycobacterium tuberculosis-induced cytotoxicity and induce anti-mycobacterial activity by a phagolysosome maturation-dependent mechanism in A549 type II alveolar epithelial cells. Immunology 129: 125-132. doi:10.1111/j.1365-2567.2009.03145.x. PubMed: 19878354.
    • (2010) Immunology , vol.129 , pp. 125-132
    • Greco, E.1    Santucci, M.B.2    Sali, M.3    De Angelis, F.R.4    Papi, M.5
  • 31
    • 9644254042 scopus 로고    scopus 로고
    • L-ficolin in children with recurrent respiratory infections
    • doi:10.1111/j.1365-2249.2004.02634.x
    • Atkinson AP, Cedzynski M, Szemraj J, St Swierzko A, Bak-Romaniszyn L, et al. (2004) L-ficolin in children with recurrent respiratory infections. Clin Exp Immunol 138: 517-520. doi:10.1111/j.1365-2249.2004.02634.x. PubMed: 15544630.
    • (2004) Clin Exp Immunol , vol.138 , pp. 517-520
    • Atkinson, A.P.1    Cedzynski, M.2    Szemraj, J.3    St Swierzko, A.4    Bak-Romaniszyn, L.5
  • 32
    • 40849133748 scopus 로고    scopus 로고
    • Functional SNPs in the human ficolin (FCN) genes reveal distinct geographical patterns
    • doi:10.1016/j.molimm.2008.01.003
    • Hummelshøj T, Munthe-Fog L, Madsen HO, Garred P, (2008) Functional SNPs in the human ficolin (FCN) genes reveal distinct geographical patterns. Mol Immunol 45: 2508-2520. doi:10.1016/j.molimm.2008.01.003. PubMed: 18289682.
    • (2008) Mol Immunol , vol.45 , pp. 2508-2520
    • Hummelshøj, T.1    Munthe-Fog, L.2    Madsen, H.O.3    Garred, P.4
  • 33
    • 21244432271 scopus 로고    scopus 로고
    • Polymorphisms in the FCN2 gene determine serum variation and function of Ficolin-2
    • doi:10.1093/hmg/ddi173
    • Hummelshoj T, Munthe-Fog L, Madsen HO, Fujita T, Matsushita M, et al. (2005) Polymorphisms in the FCN2 gene determine serum variation and function of Ficolin-2. Hum Mol Genet 14: 1651-1658. doi:10.1093/hmg/ddi173. PubMed: 15879437.
    • (2005) Hum Mol Genet , vol.14 , pp. 1651-1658
    • Hummelshoj, T.1    Munthe-Fog, L.2    Madsen, H.O.3    Fujita, T.4    Matsushita, M.5
  • 34
    • 84858123873 scopus 로고    scopus 로고
    • Human L-ficolin (ficolin-2) and its clinical significance
    • PubMed: 22500076, PubMed, 22500076
    • Kilpatrick DC, Chalmers JD, (2012) Human L-ficolin (ficolin-2) and its clinical significance. J Biomed Biotechnol,(2012): pp. 138797. PubMed: 22500076.
    • (2012) J Biomed Biotechnol , pp. 138797
    • Kilpatrick, D.C.1    Chalmers, J.D.2
  • 35
    • 59849111369 scopus 로고    scopus 로고
    • Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin
    • Lacroix M, Dumestre-Pérard C, Schoehn G, Houen G, Cesbron JY, et al. (2009) Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin. J Immunol 182: 456-465. PubMed: 19109177.
    • (2009) J Immunol , vol.182 , pp. 456-465
    • Lacroix, M.1    Dumestre-Pérard, C.2    Schoehn, G.3    Houen, G.4    Cesbron, J.Y.5
  • 36
    • 0034679699 scopus 로고    scopus 로고
    • Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. II. Effects on microbial proliferation and host survival in vivo
    • doi:10.1084/jem.192.2.237
    • Mastroeni P, Vazquez-Torres A, Fang FC, Xu Y, Khan S, et al. (2000) Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. II. Effects on microbial proliferation and host survival in vivo. J Exp Med 192: 237-248. doi:10.1084/jem.192.2.237. PubMed: 10899910.
    • (2000) J Exp Med , vol.192 , pp. 237-248
    • Mastroeni, P.1    Vazquez-Torres, A.2    Fang, F.C.3    Xu, Y.4    Khan, S.5
  • 37
    • 84857883847 scopus 로고    scopus 로고
    • Macrophage plasticity and polarization: in vivo veritas
    • Sica A, Mantovani A, (2012) Macrophage plasticity and polarization: in vivo veritas. J Clin Invest 122: 787-795. PubMed: 22378047.
    • (2012) J Clin Invest , vol.122 , pp. 787-795
    • Sica, A.1    Mantovani, A.2
  • 38
    • 0026354288 scopus 로고
    • Role of gamma interferon and tumor necrosis factor alpha in resistance to Salmonella typhimurium infection
    • Nauciel C, Espinasse-Maes F, (1992) Role of gamma interferon and tumor necrosis factor alpha in resistance to Salmonella typhimurium infection. Infect Immun 60: 450-454. PubMed: 1730475.
    • (1992) Infect Immun , vol.60 , pp. 450-454
    • Nauciel, C.1    Espinasse-Maes, F.2
  • 39
    • 84865425129 scopus 로고    scopus 로고
    • Interferon-γ, tumor necrosis factor, and interleukin-18 cooperate to control growth of Mycobacterium tuberculosis in human macrophages
    • doi:10.1016/j.cyto.2012.06.012
    • Robinson CM, Jung JY, Nau GJ, (2012) Interferon-γ, tumor necrosis factor, and interleukin-18 cooperate to control growth of Mycobacterium tuberculosis in human macrophages. Cytokine 60: 233-241. doi:10.1016/j.cyto.2012.06.012. PubMed: 22749533.
    • (2012) Cytokine , vol.60 , pp. 233-241
    • Robinson, C.M.1    Jung, J.Y.2    Nau, G.J.3
  • 40
    • 58149296036 scopus 로고    scopus 로고
    • Interleukin-17 in host defence against bacterial, mycobacterial and fungal pathogens
    • doi:10.1111/j.1365-2567.2008.03017.x
    • Curtis MM, Way SS, (2009) Interleukin-17 in host defence against bacterial, mycobacterial and fungal pathogens. Immunology 126: 177-185. doi:10.1111/j.1365-2567.2008.03017.x. PubMed: 19125888.
    • (2009) Immunology , vol.126 , pp. 177-185
    • Curtis, M.M.1    Way, S.S.2
  • 41
    • 0142241439 scopus 로고    scopus 로고
    • Innate inhibition of adaptive immunity: Mycobacterium tuberculosis-induced IL-6 inhibits macrophage responses to IFN-gamma
    • Nagabhushanam V, Solache A, Ting LM, Escaron CJ, Zhang JY, et al. (2003) Innate inhibition of adaptive immunity: Mycobacterium tuberculosis-induced IL-6 inhibits macrophage responses to IFN-gamma. J Immunol 171: 4750-4757. PubMed: 14568951.
    • (2003) J Immunol , vol.171 , pp. 4750-4757
    • Nagabhushanam, V.1    Solache, A.2    Ting, L.M.3    Escaron, C.J.4    Zhang, J.Y.5
  • 42
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • Karin M, (1995) The regulation of AP-1 activity by mitogen-activated protein kinases. J Biol Chem 270: 16483-16486. PubMed: 7622446.
    • (1995) J Biol Chem , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 43
    • 0028073283 scopus 로고
    • MAPKs: new JNK expands the group
    • doi:10.1016/0968-0004(94)90132-5
    • Davis RJ, (1994) MAPKs: new JNK expands the group. Trends Biochem Sci 19: 470-473. doi:10.1016/0968-0004(94)90132-5. PubMed: 7855889.
    • (1994) Trends Biochem Sci , vol.19 , pp. 470-473
    • Davis, R.J.1
  • 44
    • 0025095417 scopus 로고
    • The level of mannan-binding protein regulates the binding of complement-derived opsonins to mannan and zymosan at low serum concentrations
    • doi:10.1111/j.1365-2249.1990.tb05170.x
    • Super M, Levinsky RJ, Turner MW, (1990) The level of mannan-binding protein regulates the binding of complement-derived opsonins to mannan and zymosan at low serum concentrations. Clin Exp Immunol 79: 144-150. doi:10.1111/j.1365-2249.1990.tb05170.x. PubMed: 2311294.
    • (1990) Clin Exp Immunol , vol.79 , pp. 144-150
    • Super, M.1    Levinsky, R.J.2    Turner, M.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.