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Volumn 67, Issue , 2017, Pages 139-152

ST2 from rainbow trout quenches TLR signalling, localises at the nuclear membrane and allows the nuclear translocation of MYD88

Author keywords

CHSE 214; Evolution; HEK 293; Interleukin 1 receptor like 1; Oncorhynchus mykiss; TIR domain; Toll like receptor signalling

Indexed keywords

AMINO ACID; GREEN FLUORESCENT PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR; MESSENGER RNA; MYELOID DIFFERENTIATION FACTOR 88; PROTEIN ST2; SERUM AMYLOID A; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG; FISH PROTEIN; IL1RL1 PROTEIN, HUMAN; INTERLEUKIN 1 RECEPTOR LIKE 1 PROTEIN; PROTEIN BINDING;

EID: 85000716029     PISSN: 0145305X     EISSN: 18790089     Source Type: Journal    
DOI: 10.1016/j.dci.2016.10.009     Document Type: Article
Times cited : (10)

References (69)
  • 1
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., Uematsu, S., Takeuchi, O., Pathogen recognition and innate immunity. Cell 124 (2006), 783–801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 3
    • 80052294520 scopus 로고    scopus 로고
    • In silico approach to inhibition of signaling pathways of toll-like receptors 2 and 4 by ST2L
    • Basith, S., Manavalan, B., Govindaraj, R.G., Choi, S., In silico approach to inhibition of signaling pathways of toll-like receptors 2 and 4 by ST2L. PLoS One, 6, 2011.
    • (2011) PLoS One , vol.6
    • Basith, S.1    Manavalan, B.2    Govindaraj, R.G.3    Choi, S.4
  • 4
    • 0028204189 scopus 로고
    • Alternative promoter usage of the fos-responsive gene Fit-1 generates messenger-rna isoforms coding for either secreted or membrane-bound proteins related to the Il-1 receptor
    • Bergers, G., Reikerstorfer, A., Braselmann, S., Graninger, P., Busslinger, M., Alternative promoter usage of the fos-responsive gene Fit-1 generates messenger-rna isoforms coding for either secreted or membrane-bound proteins related to the Il-1 receptor. Embo J. 13 (1994), 1176–1188.
    • (1994) Embo J. , vol.13 , pp. 1176-1188
    • Bergers, G.1    Reikerstorfer, A.2    Braselmann, S.3    Graninger, P.4    Busslinger, M.5
  • 5
    • 0036453721 scopus 로고    scopus 로고
    • Evolution of the TIR, tolls and TLRs: functional inferences from computational biology
    • Beutler, B., Rehli, M., Evolution of the TIR, tolls and TLRs: functional inferences from computational biology. Curr. Top. Microbiol. Immunol. 270 (2002), 1–21.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.270 , pp. 1-21
    • Beutler, B.1    Rehli, M.2
  • 6
    • 84892866814 scopus 로고    scopus 로고
    • The interleukin-1 receptor family
    • Boraschi, D., Tagliabue, A., The interleukin-1 receptor family. Semin. Immunol. 25 (2013), 394–407.
    • (2013) Semin. Immunol. , vol.25 , pp. 394-407
    • Boraschi, D.1    Tagliabue, A.2
  • 7
    • 84907200607 scopus 로고    scopus 로고
    • Creatine metabolism differs between mammals and rainbow trout (Oncorhynchus mykiss)
    • Borchel, A., Verleih, M., Rebl, A., Kühn, C., Goldammer, T., Creatine metabolism differs between mammals and rainbow trout (Oncorhynchus mykiss). Springerplus, 3, 2014, 510.
    • (2014) Springerplus , vol.3 , pp. 510
    • Borchel, A.1    Verleih, M.2    Rebl, A.3    Kühn, C.4    Goldammer, T.5
  • 8
    • 37449021983 scopus 로고    scopus 로고
    • Detection and quantitation of infectious pancreatic necrosis virus by real-time reverse transcriptase-polymerase chain reaction using lethal and non-lethal tissue sampling
    • Bowers, R.M., Lapatra, S.E., Dhar, A.K., Detection and quantitation of infectious pancreatic necrosis virus by real-time reverse transcriptase-polymerase chain reaction using lethal and non-lethal tissue sampling. J. Virol. Methods 147 (2008), 226–234.
    • (2008) J. Virol. Methods , vol.147 , pp. 226-234
    • Bowers, R.M.1    Lapatra, S.E.2    Dhar, A.K.3
  • 9
    • 84942023609 scopus 로고    scopus 로고
    • Structurally diverse genes encode Tlr2 in rainbow trout: the conserved receptor cannot be stimulated by classical ligands to activate NF-κB in vitro
    • Brietzke, A., Arnemo, M., Gjøen, T., Rebl, H., Korytář, T., Goldammer, T., Rebl, A., Seyfert, H.-M., Structurally diverse genes encode Tlr2 in rainbow trout: the conserved receptor cannot be stimulated by classical ligands to activate NF-κB in vitro. Dev. Comp. Immunol. 54 (2016), 75–88.
    • (2016) Dev. Comp. Immunol. , vol.54 , pp. 75-88
    • Brietzke, A.1    Arnemo, M.2    Gjøen, T.3    Rebl, H.4    Korytář, T.5    Goldammer, T.6    Rebl, A.7    Seyfert, H.-M.8
  • 10
    • 84891146679 scopus 로고    scopus 로고
    • Characterization of the interleukin 1 receptor-associated kinase 4 (IRAK4)-encoding gene in salmonid fish: the functional copy is rearranged in Oncorhynchus mykiss and that factor can impair TLR signaling in mammalian cells
    • Brietzke, A., Goldammer, T., Rebl, H., Korytář, T., Köllner, B., Yang, W., Rebl, A., Seyfert, H.-M., Characterization of the interleukin 1 receptor-associated kinase 4 (IRAK4)-encoding gene in salmonid fish: the functional copy is rearranged in Oncorhynchus mykiss and that factor can impair TLR signaling in mammalian cells. Fish. Shellfish Immunol. 36 (2014), 206–214.
    • (2014) Fish. Shellfish Immunol. , vol.36 , pp. 206-214
    • Brietzke, A.1    Goldammer, T.2    Rebl, H.3    Korytář, T.4    Köllner, B.5    Yang, W.6    Rebl, A.7    Seyfert, H.-M.8
  • 12
    • 0037147298 scopus 로고    scopus 로고
    • Characterization of signaling pathways activated by the interleukin 1 (IL-1) receptor homologue T1/ST2-A Role for Jun N-terminal kinase in IL-4 induction
    • Brint, E.K., Fitzgerald, K.A., Smith, P., Coyle, A.J., Gutierrez-Ramos, J.C., Fallon, P.G., O'Neill, L.A.J., Characterization of signaling pathways activated by the interleukin 1 (IL-1) receptor homologue T1/ST2-A Role for Jun N-terminal kinase in IL-4 induction. J. Biol. Chem. 277 (2002), 49205–49211.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49205-49211
    • Brint, E.K.1    Fitzgerald, K.A.2    Smith, P.3    Coyle, A.J.4    Gutierrez-Ramos, J.C.5    Fallon, P.G.6    O'Neill, L.A.J.7
  • 13
    • 2942721674 scopus 로고    scopus 로고
    • ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance
    • Brint, E.K., Xu, D., Liu, H., Dunne, A., McKenzie, A.N., O'Neill, L.A., Liew, F.Y., ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance. Nat. Immunol. 5 (2004), 373–379.
    • (2004) Nat. Immunol. , vol.5 , pp. 373-379
    • Brint, E.K.1    Xu, D.2    Liu, H.3    Dunne, A.4    McKenzie, A.N.5    O'Neill, L.A.6    Liew, F.Y.7
  • 14
    • 0033775615 scopus 로고    scopus 로고
    • Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assays
    • Bustin, S.A., Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assays. J. Mol. Endocrinol. 25 (2000), 169–193.
    • (2000) J. Mol. Endocrinol. , vol.25 , pp. 169-193
    • Bustin, S.A.1
  • 16
    • 84949627341 scopus 로고    scopus 로고
    • Toll-like receptors: activation, signaling and transcriptional modulation
    • De Nardo, D., Toll-like receptors: activation, signaling and transcriptional modulation. Cytokine 74 (2015), 181–189.
    • (2015) Cytokine , vol.74 , pp. 181-189
    • De Nardo, D.1
  • 17
    • 80155142138 scopus 로고    scopus 로고
    • Evolution of the TIR domain-containing adaptors in humans: swinging between constraint and adaptation
    • Fornarino, S., Laval, G., Barreiro, L.B., Manry, J., Vasseur, E., Quintana-Murci, L., Evolution of the TIR domain-containing adaptors in humans: swinging between constraint and adaptation. Mol. Biol. Evol. 28 (2011), 3087–3097.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 3087-3097
    • Fornarino, S.1    Laval, G.2    Barreiro, L.B.3    Manry, J.4    Vasseur, E.5    Quintana-Murci, L.6
  • 18
    • 84941805448 scopus 로고    scopus 로고
    • A structural view of negative regulation of the toll-like receptor-mediated inflammatory pathway
    • Guven-Maiorov, E., Keskin, O., Gursoy, A., Nussinov, R., A structural view of negative regulation of the toll-like receptor-mediated inflammatory pathway. Biophys. J. 109 (2015), 1214–1226.
    • (2015) Biophys. J. , vol.109 , pp. 1214-1226
    • Guven-Maiorov, E.1    Keskin, O.2    Gursoy, A.3    Nussinov, R.4
  • 19
    • 84939824619 scopus 로고    scopus 로고
    • The architecture of the TIR domain signalosome in the toll-like Receptor-4 signaling pathway
    • Guven-Maiorov, E., Keskin, O., Gursoy, A., VanWaes, C., Chen, Z., Tsai, C.-J., Nussinov, R., The architecture of the TIR domain signalosome in the toll-like Receptor-4 signaling pathway. Sci. Rep., 5, 2015, 13128.
    • (2015) Sci. Rep. , vol.5 , pp. 13128
    • Guven-Maiorov, E.1    Keskin, O.2    Gursoy, A.3    VanWaes, C.4    Chen, Z.5    Tsai, C.-J.6    Nussinov, R.7
  • 21
    • 34548825396 scopus 로고    scopus 로고
    • Soluble ST2 blocks interleukin-33 signaling in allergic airway inflammation
    • Hayakawa, H., Hayakawa, M., Kume, A., Tominaga, S., Soluble ST2 blocks interleukin-33 signaling in allergic airway inflammation. J. Biol. Chem. 282 (2007), 26369–26380.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26369-26380
    • Hayakawa, H.1    Hayakawa, M.2    Kume, A.3    Tominaga, S.4
  • 22
    • 79651473582 scopus 로고    scopus 로고
    • NF-κB in immunobiology
    • Hayden, M.S., Ghosh, S., NF-κB in immunobiology. Cell. Res. 21 (2011), 223–244.
    • (2011) Cell. Res. , vol.21 , pp. 223-244
    • Hayden, M.S.1    Ghosh, S.2
  • 23
    • 84926663837 scopus 로고    scopus 로고
    • Tree of life reveals clock-like speciation and diversification
    • Hedges, S.B., Marin, J., Suleski, M., Paymer, M., Kumar, S., Tree of life reveals clock-like speciation and diversification. Mol. Biol. Evol. 32 (2015), 835–845.
    • (2015) Mol. Biol. Evol. , vol.32 , pp. 835-845
    • Hedges, S.B.1    Marin, J.2    Suleski, M.3    Paymer, M.4    Kumar, S.5
  • 24
    • 82755176785 scopus 로고    scopus 로고
    • MyD88 interacts with interferon regulatory factor (IRF) 3 and IRF7 in Atlantic salmon (Salmo salar): transgenic SsMyD88 modulates the IRF-induced type I interferon response and accumulates in aggresomes
    • Iliev, D.B., Sobhkhez, M., Fremmerlid, K., Jørgensen, J.B., MyD88 interacts with interferon regulatory factor (IRF) 3 and IRF7 in Atlantic salmon (Salmo salar): transgenic SsMyD88 modulates the IRF-induced type I interferon response and accumulates in aggresomes. J. Biol. Chem. 286 (2011), 42715–42724.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42715-42724
    • Iliev, D.B.1    Sobhkhez, M.2    Fremmerlid, K.3    Jørgensen, J.B.4
  • 25
    • 9244222725 scopus 로고    scopus 로고
    • Molecular cloning of the chicken ST2 gene and a novel variant form of the ST2 gene product, ST2LV. Biochim. Biophys
    • Iwahana, H., Hayakawa, M., Kuroiwa, K., Tago, K., Yanagisawa, K., Noji, S., Tominaga, S., Molecular cloning of the chicken ST2 gene and a novel variant form of the ST2 gene product, ST2LV. Biochim. Biophys. Acta-Gene Struct. Expr. 1681 (2004), 1–14.
    • (2004) Acta-Gene Struct. Expr. , vol.1681 , pp. 1-14
    • Iwahana, H.1    Hayakawa, M.2    Kuroiwa, K.3    Tago, K.4    Yanagisawa, K.5    Noji, S.6    Tominaga, S.7
  • 26
    • 0033198885 scopus 로고    scopus 로고
    • Different promoter usage and multiple transcription initiation sites of the interleukin-1 receptor-related human ST2 gene in UT-7 and TM12 cells
    • Iwahana, H., Yanagisawa, K., Ito-Kosaka, A., Kuroiwa, K., Tago, K., Komatsu, N., Katashima, R., Itakura, M., Tominaga, S., Different promoter usage and multiple transcription initiation sites of the interleukin-1 receptor-related human ST2 gene in UT-7 and TM12 cells. Eur. J. Biochem. 264 (1999), 397–406.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 397-406
    • Iwahana, H.1    Yanagisawa, K.2    Ito-Kosaka, A.3    Kuroiwa, K.4    Tago, K.5    Komatsu, N.6    Katashima, R.7    Itakura, M.8    Tominaga, S.9
  • 27
    • 0032566336 scopus 로고    scopus 로고
    • Ultrastructural distribution of the death-domain-containing MyD88 protein in HeLa cells
    • Jaunin, F., Burns, K., Tschopp, J., Martin, T.E., Fakan, S., Ultrastructural distribution of the death-domain-containing MyD88 protein in HeLa cells. Exp. Cell. Res. 243 (1998), 67–75.
    • (1998) Exp. Cell. Res. , vol.243 , pp. 67-75
    • Jaunin, F.1    Burns, K.2    Tschopp, J.3    Martin, T.E.4    Fakan, S.5
  • 28
    • 0019390307 scopus 로고
    • Nuclear lamina assembly, synthesis and disaggregation during the cell cycle in synchronized HeLa cells
    • Jost, E., Johnson, R.T., Nuclear lamina assembly, synthesis and disaggregation during the cell cycle in synchronized HeLa cells. J. Cell. Sci. 47 (1981), 25–53.
    • (1981) J. Cell. Sci. , vol.47 , pp. 25-53
    • Jost, E.1    Johnson, R.T.2
  • 29
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls toll-like receptor signaling
    • Kagan, J.C., Medzhitov, R., Phosphoinositide-mediated adaptor recruitment controls toll-like receptor signaling. Cell 125 (2006), 943–955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 30
    • 53249113212 scopus 로고    scopus 로고
    • The IL-33/ST2 pathway: therapeutic target and novel biomarker
    • Kakkar, R., Lee, R.T., The IL-33/ST2 pathway: therapeutic target and novel biomarker. Nat. Rev. Drug Discov. 7 (2008), 827–840.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 827-840
    • Kakkar, R.1    Lee, R.T.2
  • 31
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin, M., Lin, A., NF-kappaB at the crossroads of life and death. Nat. Immunol. 3 (2002), 221–227.
    • (2002) Nat. Immunol. , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 32
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-kappab by toll-like receptors
    • Kawai, T., Akira, S., Signaling to NF-kappab by toll-like receptors. Trends Mol. Med. 13 (2007), 460–469.
    • (2007) Trends Mol. Med. , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 34
    • 79251611112 scopus 로고    scopus 로고
    • Activation of MyD88 signaling upon staphylococcal enterotoxin binding to MHC class II molecules
    • Kissner, T.L., Ruthel, G., Alam, S., Ulrich, R.G., Fernandez, S., Saikh, K.U., Activation of MyD88 signaling upon staphylococcal enterotoxin binding to MHC class II molecules. PLoS One, 6, 2011, e15985.
    • (2011) PLoS One , vol.6 , pp. e15985
    • Kissner, T.L.1    Ruthel, G.2    Alam, S.3    Ulrich, R.G.4    Fernandez, S.5    Saikh, K.U.6
  • 35
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor-mediated immune responses
    • Liew, F.Y., Xu, D., Brint, E.K., O'Neill, L.A., Negative regulation of toll-like receptor-mediated immune responses. Nat. Rev. Immunol. 5 (2005), 446–458.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 446-458
    • Liew, F.Y.1    Xu, D.2    Brint, E.K.3    O'Neill, L.A.4
  • 36
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signaling
    • Lin, S.C., Lo, Y.C., Wu, H., Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signaling. Nature 465 (2010), 885–890.
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 37
    • 84864018937 scopus 로고    scopus 로고
    • Deletion of the ST2 proximal promoter disrupts fibroblast-specific expression but does not reduce the amount of soluble ST2 in circulation
    • Lipsky, B.P., Toy, D.Y., Swart, D.A., Smithgall, M.D., Smith, D., Deletion of the ST2 proximal promoter disrupts fibroblast-specific expression but does not reduce the amount of soluble ST2 in circulation. Eur. J. Immunol. 42 (2012), 1863–1869.
    • (2012) Eur. J. Immunol. , vol.42 , pp. 1863-1869
    • Lipsky, B.P.1    Toy, D.Y.2    Swart, D.A.3    Smithgall, M.D.4    Smith, D.5
  • 38
    • 77954750715 scopus 로고    scopus 로고
    • ST2 negatively regulates TLR2 signaling, but is not required for bacterial lipoprotein-induced tolerance
    • Liu, J., Buckley, J.M., Redmond, H.P., Wang, J.H., ST2 negatively regulates TLR2 signaling, but is not required for bacterial lipoprotein-induced tolerance. J. Immunol. 184 (2010), 5802–5808.
    • (2010) J. Immunol. , vol.184 , pp. 5802-5808
    • Liu, J.1    Buckley, J.M.2    Redmond, H.P.3    Wang, J.H.4
  • 40
    • 84930260934 scopus 로고    scopus 로고
    • New dog and new tricks: evolving roles for IL-33 in type 2 immunity
    • Lott, J.M., Sumpter, T.L., Turnquist, H.R., New dog and new tricks: evolving roles for IL-33 in type 2 immunity. J. Leukoc. Biol. 97 (2015), 1037–1048.
    • (2015) J. Leukoc. Biol. , vol.97 , pp. 1037-1048
    • Lott, J.M.1    Sumpter, T.L.2    Turnquist, H.R.3
  • 42
    • 34250842580 scopus 로고    scopus 로고
    • Distinct roles of TIR and non-TIR regions in the subcellular localization and signaling properties of MyD88
    • Nishiya, T., Kajita, E., Horinouchi, T., Nishimoto, A., Miwa, S., Distinct roles of TIR and non-TIR regions in the subcellular localization and signaling properties of MyD88. FEBS Lett. 581 (2007), 3223–3229.
    • (2007) FEBS Lett. , vol.581 , pp. 3223-3229
    • Nishiya, T.1    Kajita, E.2    Horinouchi, T.3    Nishimoto, A.4    Miwa, S.5
  • 43
    • 55149105005 scopus 로고    scopus 로고
    • The interleukin-1 receptor/Toll-like receptor superfamily: 10 years of progress
    • 10–18
    • O'Neill, L.A., The interleukin-1 receptor/Toll-like receptor superfamily: 10 years of progress. Immunol. Rev. 226 (2008), 10–18 10–18.
    • (2008) Immunol. Rev. , vol.226 , pp. 10-18
    • O'Neill, L.A.1
  • 44
    • 0034075754 scopus 로고    scopus 로고
    • The IL-I receptor/toll-like receptor superfamily: crucial receptors for inflammation and host defense
    • O'Neill, L.A.J., Dinarello, C.A., The IL-I receptor/toll-like receptor superfamily: crucial receptors for inflammation and host defense. Immunol. Today 21 (2000), 206–209.
    • (2000) Immunol. Today , vol.21 , pp. 206-209
    • O'Neill, L.A.J.1    Dinarello, C.A.2
  • 46
    • 84900502291 scopus 로고    scopus 로고
    • The IL-1 family in fish: swimming through the muddy waters of inflammasome evolution
    • Ogryzko, N.V., Renshaw, S.A., Wilson, H.L., The IL-1 family in fish: swimming through the muddy waters of inflammasome evolution. Dev. Comp. Immunol. 46 (2014), 53–62.
    • (2014) Dev. Comp. Immunol. , vol.46 , pp. 53-62
    • Ogryzko, N.V.1    Renshaw, S.A.2    Wilson, H.L.3
  • 50
    • 81255161674 scopus 로고    scopus 로고
    • MARCH5 gene is duplicated in rainbow trout, but only fish-specific gene copy is up-regulated after VHSV infection
    • Rebl, A., Köbis, J.M., Fischer, U., Takizawa, F., Verleih, M., Wimmers, K., Goldammer, T., MARCH5 gene is duplicated in rainbow trout, but only fish-specific gene copy is up-regulated after VHSV infection. Fish. Shellfish Immunol. 31 (2011), 1041–1050.
    • (2011) Fish. Shellfish Immunol. , vol.31 , pp. 1041-1050
    • Rebl, A.1    Köbis, J.M.2    Fischer, U.3    Takizawa, F.4    Verleih, M.5    Wimmers, K.6    Goldammer, T.7
  • 51
    • 77957865629 scopus 로고    scopus 로고
    • Salmonid Tollip and MyD88 factors can functionally replace their mammalian orthologues in TLR-mediated trout SAA promoter activation
    • Rebl, A., Rebl, H., Liu, S., Goldammer, T., Seyfert, H.-M., Salmonid Tollip and MyD88 factors can functionally replace their mammalian orthologues in TLR-mediated trout SAA promoter activation. Dev. Comp. Immunol. 35 (2011), 81–87.
    • (2011) Dev. Comp. Immunol. , vol.35 , pp. 81-87
    • Rebl, A.1    Rebl, H.2    Liu, S.3    Goldammer, T.4    Seyfert, H.-M.5
  • 53
    • 0028168798 scopus 로고
    • Three NF-kappa B binding sites in the human E-selectin gene required for maximal tumor necrosis factor alpha-induced expression
    • Schindler, U., Baichwal, V.R., Three NF-kappa B binding sites in the human E-selectin gene required for maximal tumor necrosis factor alpha-induced expression. Mol. Cell. Biol. 14 (1994), 5820–5831.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5820-5831
    • Schindler, U.1    Baichwal, V.R.2
  • 55
    • 0036618178 scopus 로고    scopus 로고
    • Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells
    • Shaw, G., Morse, S., Ararat, M., Graham, F.L., Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. FASEB J. 16 (2002), 869–871.
    • (2002) FASEB J. , vol.16 , pp. 869-871
    • Shaw, G.1    Morse, S.2    Ararat, M.3    Graham, F.L.4
  • 56
    • 77955653938 scopus 로고    scopus 로고
    • C/EBP-beta drives expression of the nutritionally regulated promoter IA of the acetyl-CoA carboxylase-alpha gene in cattle
    • Shi, X., Liu, S., Metges, C.C., Seyfert, H.M., C/EBP-beta drives expression of the nutritionally regulated promoter IA of the acetyl-CoA carboxylase-alpha gene in cattle. Biochim. Biophys. Acta-Gene Regul. Mech. 1799 (2010), 561–567.
    • (2010) Biochim. Biophys. Acta-Gene Regul. Mech. , vol.1799 , pp. 561-567
    • Shi, X.1    Liu, S.2    Metges, C.C.3    Seyfert, H.M.4
  • 57
    • 84896722900 scopus 로고    scopus 로고
    • A communication network within the cytoplasmic domain of toll-like receptors has remained conserved during evolution
    • Singh, S., Pandey, K., Rathore, Y.S., Sagar, A., Pattnaik, U.B.K., Ashish, A communication network within the cytoplasmic domain of toll-like receptors has remained conserved during evolution. J. Biomol. Struct. Dyn. 32 (2014), 694–700.
    • (2014) J. Biomol. Struct. Dyn. , vol.32 , pp. 694-700
    • Singh, S.1    Pandey, K.2    Rathore, Y.S.3    Sagar, A.4    Pattnaik, U.B.K.5    Ashish6
  • 58
  • 61
    • 77955053656 scopus 로고    scopus 로고
    • KU812 cells provide a novel in vitro model of the human IL-33/ST2L axis: functional responses and identification of signaling pathways
    • Tare, N., Li, H., Morschauser, A., Cote-Sierra, J., Ju, G., Renzetti, L., Lin, T.-A., KU812 cells provide a novel in vitro model of the human IL-33/ST2L axis: functional responses and identification of signaling pathways. Exp. Cell. Res. 316 (2010), 2527–2537.
    • (2010) Exp. Cell. Res. , vol.316 , pp. 2527-2537
    • Tare, N.1    Li, H.2    Morschauser, A.3    Cote-Sierra, J.4    Ju, G.5    Renzetti, L.6    Lin, T.-A.7
  • 63
    • 0024404517 scopus 로고
    • A putative Protein of A Growth specific cdna from balb C-3T3 cells is highly similar to the extracellular portion of mouse Interleukin-1 receptor
    • Tominaga, S., A putative Protein of A Growth specific cdna from balb C-3T3 cells is highly similar to the extracellular portion of mouse Interleukin-1 receptor. FEBS Lett. 258 (1989), 301–304.
    • (1989) FEBS Lett. , vol.258 , pp. 301-304
    • Tominaga, S.1
  • 64
  • 65
    • 84922334942 scopus 로고    scopus 로고
    • Dual function of IL-33 on proliferation of NIH-3T3 cells
    • Tominaga, S.-I., Tago, K., Tsuda, H., Komine, M., Dual function of IL-33 on proliferation of NIH-3T3 cells. Cytokine 72 (2015), 105–108.
    • (2015) Cytokine , vol.72 , pp. 105-108
    • Tominaga, S.-I.1    Tago, K.2    Tsuda, H.3    Komine, M.4
  • 66
    • 0027509505 scopus 로고
    • Presence of A Novel primary response gene St2L, encoding a product highly similar to the Interleukin-1 receptor Type-1
    • Yanagisawa, K., Takagi, T., Tsukamoto, T., Tetsuka, T., Tominaga, S., Presence of A Novel primary response gene St2L, encoding a product highly similar to the Interleukin-1 receptor Type-1. FEBS Lett. 318 (1993), 83–87.
    • (1993) FEBS Lett. , vol.318 , pp. 83-87
    • Yanagisawa, K.1    Takagi, T.2    Tsukamoto, T.3    Tetsuka, T.4    Tominaga, S.5
  • 67
    • 25644448980 scopus 로고    scopus 로고
    • NF-kappaB factors are essential, but not the switch, for pathogen-related induction of the bovine beta-defensin 5-encoding gene in mammary epithelial cells
    • Yang, W., Molenaar, A., Kurts-Ebert, B., Seyfert, H.M., NF-kappaB factors are essential, but not the switch, for pathogen-related induction of the bovine beta-defensin 5-encoding gene in mammary epithelial cells. Mol. Immunol. 43 (2006), 210–225.
    • (2006) Mol. Immunol. , vol.43 , pp. 210-225
    • Yang, W.1    Molenaar, A.2    Kurts-Ebert, B.3    Seyfert, H.M.4
  • 68
    • 37449013073 scopus 로고    scopus 로고
    • Bovine TLR2 and TLR4 properly transduce signals from Staphylococcus aureus and E. coli, but S. aureus fails to both activate NF-kappaB in mammary epithelial cells and to quickly induce TNFalpha and interleukin-8 (CXCL8) expression in the udder
    • Yang, W., Zerbe, H., Petzl, W., Brunner, R.M., Gunther, J., Draing, C., von, A.S., Schuberth, H.J., Seyfert, H.M., Bovine TLR2 and TLR4 properly transduce signals from Staphylococcus aureus and E. coli, but S. aureus fails to both activate NF-kappaB in mammary epithelial cells and to quickly induce TNFalpha and interleukin-8 (CXCL8) expression in the udder. Mol. Immunol. 45 (2008), 1385–1397.
    • (2008) Mol. Immunol. , vol.45 , pp. 1385-1397
    • Yang, W.1    Zerbe, H.2    Petzl, W.3    Brunner, R.M.4    Gunther, J.5    Draing, C.6    von, A.S.7    Schuberth, H.J.8    Seyfert, H.M.9
  • 69
    • 0034254796 scopus 로고    scopus 로고
    • Role of plasma membrane transporters in muscle metabolism
    • Zorzano, a, Fandos, C., Palacín, M., Role of plasma membrane transporters in muscle metabolism. Biochem. J. 349:Pt 3 (2000), 667–688.
    • (2000) Biochem. J. , vol.349 , pp. 667-688
    • Zorzano, A.1    Fandos, C.2    Palacín, M.3


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