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Volumn 98, Issue 3, 2013, Pages 457-468

Development of cellular signaling pathway inhibitors as new antivirals against influenza

Author keywords

Antiviral therapy; Cellular drug targets; Influenza virus; Resistance; Signaling pathways

Indexed keywords

1 (1 CYANO 1 METHYLETHYL) 3 METHYL 8 (3 QUINOLINYL)IMIDAZO[4,5 C]QUINOLIN 2(1H,3H) ONE; 1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 12 (2 CYANOETHYL) 6,7,12,13 TETRAHYDRO 13 METHYL 5 OXOINDOLO[2,3 A]PYRROLO[3,4 C]CARBAZOLE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 (2 CHLORO 4 IODOANILINO) N CYCLOPROPYLMETHOXY 3,4 DIFLUOROBENZAMIDE; ACETYLSALICYLIC ACID; AMANTADINE; ANTIVIRUS AGENT; AZD 8330; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CL 1040; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYSINE ACETYLSALICYLATE; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; N (2,3 DIHYDROXYPROPOXY) 3,4 DIFLUORO 2 (2 FLUORO 4 IODOANILINO)BENZAMIDE; OSELTAMIVIR; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN KINASE C; RAF PROTEIN; RDEA 119; SC 75741; SELUMETINIB; UNCLASSIFIED DRUG; VL 01;

EID: 84877613064     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2013.04.008     Document Type: Review
Times cited : (86)

References (107)
  • 1
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 2004, 5:417-421.
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 2
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat. Rev. Cancer 2004, 4:349-360.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 3
    • 2642551603 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor Velcade (Bortezomib)
    • Adams J., Kauffman M. Development of the proteasome inhibitor Velcade (Bortezomib). Cancer Invest. 2004, 22:304-311.
    • (2004) Cancer Invest. , vol.22 , pp. 304-311
    • Adams, J.1    Kauffman, M.2
  • 8
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G., Karin M. The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 2004, 25:280-288.
    • (2004) Trends Immunol. , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 9
    • 79953794385 scopus 로고    scopus 로고
    • Fine tuning of protein kinase C (PKC) isoforms in cancer: shortening the distance from the laboratory to the bedside
    • Bosco R., Melloni E., Celeghini C., Rimondi E., Vaccarezza M., Zauli G. Fine tuning of protein kinase C (PKC) isoforms in cancer: shortening the distance from the laboratory to the bedside. Mini Rev. Med. Chem. 2011, 11:185-199.
    • (2011) Mini Rev. Med. Chem. , vol.11 , pp. 185-199
    • Bosco, R.1    Melloni, E.2    Celeghini, C.3    Rimondi, E.4    Vaccarezza, M.5    Zauli, G.6
  • 10
    • 84877924495 scopus 로고    scopus 로고
    • Dissecting bortezomib: development, application, adverse effects and future direction
    • 2012 Nov 2. [Epub ahead of print].
    • Cao, B., Li, J., Mao, X., 2012. Dissecting bortezomib: development, application, adverse effects and future direction. Curr. Pharm. Des. 2012 Nov 2. [Epub ahead of print].
    • (2012) Curr. Pharm. Des.
    • Cao, B.1    Li, J.2    Mao, X.3
  • 11
    • 51849084360 scopus 로고    scopus 로고
    • The PTEN-PI3K pathway: of feedbacks and cross-talks
    • Carracedo A., Pandolfi P.P. The PTEN-PI3K pathway: of feedbacks and cross-talks. Oncogene 2008, 27:5527-5541.
    • (2008) Oncogene , vol.27 , pp. 5527-5541
    • Carracedo, A.1    Pandolfi, P.P.2
  • 12
    • 79960055459 scopus 로고    scopus 로고
    • RAS interaction with PI3K: more than just another effector pathway
    • Castellano E., Downward J. RAS interaction with PI3K: more than just another effector pathway. Genes Cancer 2011, 2:261-274.
    • (2011) Genes Cancer , vol.2 , pp. 261-274
    • Castellano, E.1    Downward, J.2
  • 20
    • 80052782091 scopus 로고    scopus 로고
    • Antiviral activity of the MEK-inhibitor U0126 against pandemic H1N1v and highly pathogenic avian influenza virus in vitro and in vivo
    • Droebner K., Pleschka S., Ludwig S., Planz O. Antiviral activity of the MEK-inhibitor U0126 against pandemic H1N1v and highly pathogenic avian influenza virus in vitro and in vivo. Antiviral Res.. 2011, 92:195-203.
    • (2011) Antiviral Res.. , vol.92 , pp. 195-203
    • Droebner, K.1    Pleschka, S.2    Ludwig, S.3    Planz, O.4
  • 21
    • 77956029025 scopus 로고    scopus 로고
    • The clinically approved proteasome inhibitor PS-341 efficiently blocks influenza A virus and vesicular stomatitis virus propagation by establishing an antiviral state
    • Dudek S.E., Luig C., Pauli E.K., Schubert U., Ludwig S. The clinically approved proteasome inhibitor PS-341 efficiently blocks influenza A virus and vesicular stomatitis virus propagation by establishing an antiviral state. J. Virol. 2010, 84:9439-9451.
    • (2010) J. Virol. , vol.84 , pp. 9439-9451
    • Dudek, S.E.1    Luig, C.2    Pauli, E.K.3    Schubert, U.4    Ludwig, S.5
  • 22
    • 65549130101 scopus 로고    scopus 로고
    • A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway
    • Ehrhardt C., Ludwig S. A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway. Cell Microbiol. 2009, 11:863-871.
    • (2009) Cell Microbiol. , vol.11 , pp. 863-871
    • Ehrhardt, C.1    Ludwig, S.2
  • 23
    • 33745753573 scopus 로고    scopus 로고
    • Bivalent role of the phosphatidylinositol-3-kinase (PI3K) during influenza virus infection and host cell defence
    • Ehrhardt C., Marjuki H., Wolff T., Nurnberg B., Planz O., Pleschka S., Ludwig S. Bivalent role of the phosphatidylinositol-3-kinase (PI3K) during influenza virus infection and host cell defence. Cell Microbiol. 2006, 8:1336-1348.
    • (2006) Cell Microbiol. , vol.8 , pp. 1336-1348
    • Ehrhardt, C.1    Marjuki, H.2    Wolff, T.3    Nurnberg, B.4    Planz, O.5    Pleschka, S.6    Ludwig, S.7
  • 24
    • 33947381763 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses
    • Ehrhardt C., Wolff T., Pleschka S., Planz O., Beermann W., Bode J.G., Schmolke M., Ludwig S. Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses. J. Virol. 2007, 81:3058-3067.
    • (2007) J. Virol. , vol.81 , pp. 3058-3067
    • Ehrhardt, C.1    Wolff, T.2    Pleschka, S.3    Planz, O.4    Beermann, W.5    Bode, J.G.6    Schmolke, M.7    Ludwig, S.8
  • 26
    • 33749180269 scopus 로고    scopus 로고
    • Clustering of raft-associated proteins in the external membrane leaflet modulates internal leaflet H-ras diffusion and signaling
    • Eisenberg S., Shvartsman D.E., Ehrlich M., Henis Y.I. Clustering of raft-associated proteins in the external membrane leaflet modulates internal leaflet H-ras diffusion and signaling. Mol. Cell Biol. 2006, 26:7190-7200.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 7190-7200
    • Eisenberg, S.1    Shvartsman, D.E.2    Ehrlich, M.3    Henis, Y.I.4
  • 27
    • 0034722379 scopus 로고    scopus 로고
    • Caspases disrupt the nuclear-cytoplasmic barrier
    • Faleiro L., Lazebnik Y. Caspases disrupt the nuclear-cytoplasmic barrier. J. Cell Biol. 2000, 151:951-959.
    • (2000) J. Cell Biol. , vol.151 , pp. 951-959
    • Faleiro, L.1    Lazebnik, Y.2
  • 28
    • 77949464718 scopus 로고    scopus 로고
    • From basic research to clinical development of MEK1/2 inhibitors for cancer therapy
    • Fremin C., Meloche S. From basic research to clinical development of MEK1/2 inhibitors for cancer therapy. J. Hematol. Oncol. 2010, 3:8.
    • (2010) J. Hematol. Oncol. , vol.3 , pp. 8
    • Fremin, C.1    Meloche, S.2
  • 29
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-kappaB: players, pathways, perspectives
    • Gilmore T.D. Introduction to NF-kappaB: players, pathways, perspectives. Oncogene 2006, 25:6680-6684.
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 30
    • 84859946812 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB signaling as a strategy in disease therapy
    • Gilmore T.D., Garbati M.R. Inhibition of NF-kappaB signaling as a strategy in disease therapy. Curr. Top. Microbiol. Immunol. 2011, 349:245-263.
    • (2011) Curr. Top. Microbiol. Immunol. , vol.349 , pp. 245-263
    • Gilmore, T.D.1    Garbati, M.R.2
  • 31
    • 33750446341 scopus 로고    scopus 로고
    • Inhibitors of NF-kappaB signaling: 785 and counting
    • Gilmore T.D., Herscovitch M. Inhibitors of NF-kappaB signaling: 785 and counting. Oncogene 2006, 25:6887-6899.
    • (2006) Oncogene , vol.25 , pp. 6887-6899
    • Gilmore, T.D.1    Herscovitch, M.2
  • 32
    • 33845389394 scopus 로고    scopus 로고
    • Reye's syndrome: the case for a causal link with aspirin
    • Glasgow J.F. Reye's syndrome: the case for a causal link with aspirin. Drug Safety 2006, 29:1111-1121.
    • (2006) Drug Safety , vol.29 , pp. 1111-1121
    • Glasgow, J.F.1
  • 35
    • 84876003945 scopus 로고    scopus 로고
    • Combination of MEK inhibitors and oseltamivir leads to synergistic antiviral effects after influenza A virus infection in vitro
    • Haasbach E., Hartmayer C., Planz O. Combination of MEK inhibitors and oseltamivir leads to synergistic antiviral effects after influenza A virus infection in vitro. Antiviral Res.. 2013, 98:319-324.
    • (2013) Antiviral Res.. , vol.98 , pp. 319-324
    • Haasbach, E.1    Hartmayer, C.2    Planz, O.3
  • 37
    • 33750448661 scopus 로고    scopus 로고
    • Transcriptional regulation via the NF-kappaB signaling module
    • Hoffmann A., Natoli G., Ghosh G. Transcriptional regulation via the NF-kappaB signaling module. Oncogene 2006, 25:6706-6716.
    • (2006) Oncogene , vol.25 , pp. 6706-6716
    • Hoffmann, A.1    Natoli, G.2    Ghosh, G.3
  • 38
    • 53249140699 scopus 로고    scopus 로고
    • Modulation of influenza virus replication by alteration of sodium ion transport and protein kinase C activity
    • Hoffmann H.H., Palese P., Shaw M.L. Modulation of influenza virus replication by alteration of sodium ion transport and protein kinase C activity. Antiviral Res.. 2008, 80:124-134.
    • (2008) Antiviral Res.. , vol.80 , pp. 124-134
    • Hoffmann, H.H.1    Palese, P.2    Shaw, M.L.3
  • 39
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: the complexity of targeted inhibitors
    • Hynes N.E., Lane H.A. ERBB receptors and cancer: the complexity of targeted inhibitors. Nat. Rev. Cancer 2005, 5:341-354.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 42
    • 0031808369 scopus 로고    scopus 로고
    • Mediation by NF-kappa B of cytokine induced expression of intercellular adhesion molecule 1 (ICAM-1) in an intestinal epithelial cell line, a process blocked by proteasome inhibitors
    • Jobin C., Hellerbrand C., Licato L.L., Brenner D.A., Sartor R.B. Mediation by NF-kappa B of cytokine induced expression of intercellular adhesion molecule 1 (ICAM-1) in an intestinal epithelial cell line, a process blocked by proteasome inhibitors. Gut 1998, 42:779-787.
    • (1998) Gut , vol.42 , pp. 779-787
    • Jobin, C.1    Hellerbrand, C.2    Licato, L.L.3    Brenner, D.A.4    Sartor, R.B.5
  • 43
    • 33744832401 scopus 로고    scopus 로고
    • United States food and drug administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy
    • Kane R.C., Farrell A.T., Sridhara R., Pazdur R. United States food and drug administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy. Clin. Cancer Res. 2006, 12:2955-2960.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 2955-2960
    • Kane, R.C.1    Farrell, A.T.2    Sridhara, R.3    Pazdur, R.4
  • 44
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
    • Karin M., Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu. Rev. Immunol. 2000, 18:621-663.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 45
    • 49649115096 scopus 로고    scopus 로고
    • Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina
    • Kramer A., Liashkovich I., Oberleithner H., Ludwig S., Mazur I., Shahin V. Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina. Proc. Natl. Acad. Sci. USA 2008, 105:11236-11241.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11236-11241
    • Kramer, A.1    Liashkovich, I.2    Oberleithner, H.3    Ludwig, S.4    Mazur, I.5    Shahin, V.6
  • 46
    • 53749106185 scopus 로고    scopus 로고
    • NF-kappaB signaling differentially regulates influenza virus RNA synthesis
    • Kumar N., Xin Z.T., Liang Y., Ly H. NF-kappaB signaling differentially regulates influenza virus RNA synthesis. J. Virol. 2008, 82:9880-9889.
    • (2008) J. Virol. , vol.82 , pp. 9880-9889
    • Kumar, N.1    Xin, Z.T.2    Liang, Y.3    Ly, H.4
  • 47
    • 84865676740 scopus 로고    scopus 로고
    • PI3 kinase inhibitors in the clinic: an update
    • Kurtz J.E., Ray-Coquard I. PI3 kinase inhibitors in the clinic: an update. Anticancer Res 2012, 32:2463-2470.
    • (2012) Anticancer Res , vol.32 , pp. 2463-2470
    • Kurtz, J.E.1    Ray-Coquard, I.2
  • 50
    • 67249156976 scopus 로고    scopus 로고
    • Targeting cell signalling pathways to fight the flu: towards a paradigm change in anti-influenza therapy
    • Ludwig S. Targeting cell signalling pathways to fight the flu: towards a paradigm change in anti-influenza therapy. J. Antimicrob. Chemother. 2009, 64:1-4.
    • (2009) J. Antimicrob. Chemother. , vol.64 , pp. 1-4
    • Ludwig, S.1
  • 51
    • 54049111798 scopus 로고    scopus 로고
    • Influenza viruses and the NF-kappaB signaling pathway - towards a novel concept of antiviral therapy
    • Ludwig S., Planz O. Influenza viruses and the NF-kappaB signaling pathway - towards a novel concept of antiviral therapy. Biol. Chem. 2008, 389:1307-1312.
    • (2008) Biol. Chem. , vol.389 , pp. 1307-1312
    • Ludwig, S.1    Planz, O.2
  • 52
    • 0037295292 scopus 로고    scopus 로고
    • Influenza-virus-induced signaling cascades: targets for antiviral therapy?
    • Ludwig S., Planz O., Pleschka S., Wolff T. Influenza-virus-induced signaling cascades: targets for antiviral therapy?. Trends Mol. Med. 2003, 9:46-52.
    • (2003) Trends Mol. Med. , vol.9 , pp. 46-52
    • Ludwig, S.1    Planz, O.2    Pleschka, S.3    Wolff, T.4
  • 53
  • 54
    • 33644825268 scopus 로고    scopus 로고
    • Ringing the alarm bells: signalling and apoptosis in influenza virus infected cells
    • Ludwig S., Pleschka S., Planz O., Wolff T. Ringing the alarm bells: signalling and apoptosis in influenza virus infected cells. Cell Microbiol. 2006, 8:375-386.
    • (2006) Cell Microbiol. , vol.8 , pp. 375-386
    • Ludwig, S.1    Pleschka, S.2    Planz, O.3    Wolff, T.4
  • 55
    • 78049525017 scopus 로고    scopus 로고
    • Proteasome inhibition in vivo promotes survival in a lethal murine model of severe acute respiratory syndrome
    • Ma X.Z., Bartczak A., Zhang J., Khattar R., Chen L., Liu M.F., Edwards A., Levy G., McGilvray I.D. Proteasome inhibition in vivo promotes survival in a lethal murine model of severe acute respiratory syndrome. J. Virol. 2010, 84:12419-12428.
    • (2010) J. Virol. , vol.84 , pp. 12419-12428
    • Ma, X.Z.1    Bartczak, A.2    Zhang, J.3    Khattar, R.4    Chen, L.5    Liu, M.F.6    Edwards, A.7    Levy, G.8    McGilvray, I.D.9
  • 57
    • 67649224477 scopus 로고    scopus 로고
    • Influenza A virus proteins PB1 and NS1 are subject to functionally important phosphorylation by protein kinase C
    • Mahmoudian S., Auerochs S., Grone M., Marschall M. Influenza A virus proteins PB1 and NS1 are subject to functionally important phosphorylation by protein kinase C. J. Gen. Virol. 2009, 90:1392-1397.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1392-1397
    • Mahmoudian, S.1    Auerochs, S.2    Grone, M.3    Marschall, M.4
  • 58
    • 79952109693 scopus 로고    scopus 로고
    • From the bench to the bed side: PI3K pathway inhibitors in clinical development
    • Maira S.M., Finan P., Garcia-Echeverria C. From the bench to the bed side: PI3K pathway inhibitors in clinical development. Curr. Top. Microbiol. Immunol. 2010, 347:209-239.
    • (2010) Curr. Top. Microbiol. Immunol. , vol.347 , pp. 209-239
    • Maira, S.M.1    Finan, P.2    Garcia-Echeverria, C.3
  • 59
    • 33745186230 scopus 로고    scopus 로고
    • Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling
    • Marjuki H., Alam M.I., Ehrhardt C., Wagner R., Planz O., Klenk H.D., Ludwig S., Pleschka S. Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling. J. Biol. Chem. 2006, 281:16707-16715.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16707-16715
    • Marjuki, H.1    Alam, M.I.2    Ehrhardt, C.3    Wagner, R.4    Planz, O.5    Klenk, H.D.6    Ludwig, S.7    Pleschka, S.8
  • 60
    • 38849122079 scopus 로고    scopus 로고
    • Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade
    • Marjuki H., Yen H.L., Franks J., Webster R.G., Pleschka S., Hoffmann E. Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade. Virol. J. 2007, 4:134.
    • (2007) Virol. J. , vol.4 , pp. 134
    • Marjuki, H.1    Yen, H.L.2    Franks, J.3    Webster, R.G.4    Pleschka, S.5    Hoffmann, E.6
  • 63
    • 0042235524 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in influenza virus induction of prostaglandin E2 from arachidonic acid in bronchial epithelial cells
    • Mizumura K., Hashimoto S., Maruoka S., Gon Y., Kitamura N., Matsumoto K., Hayashi S., Shimizu K., Horie T. Role of mitogen-activated protein kinases in influenza virus induction of prostaglandin E2 from arachidonic acid in bronchial epithelial cells. Clin. Exp. Allergy 2003, 33:1244-1251.
    • (2003) Clin. Exp. Allergy , vol.33 , pp. 1244-1251
    • Mizumura, K.1    Hashimoto, S.2    Maruoka, S.3    Gon, Y.4    Kitamura, N.5    Matsumoto, K.6    Hayashi, S.7    Shimizu, K.8    Horie, T.9
  • 64
    • 77955980932 scopus 로고    scopus 로고
    • The TCR-mediated signaling pathways that control the direction of helper T cell differentiation
    • Nakayama T., Yamashita M. The TCR-mediated signaling pathways that control the direction of helper T cell differentiation. Semin. Immunol. 2010, 22:303-309.
    • (2010) Semin. Immunol. , vol.22 , pp. 303-309
    • Nakayama, T.1    Yamashita, M.2
  • 68
    • 0036258055 scopus 로고    scopus 로고
    • Is aspirin a cause of Reye's syndrome? A case against
    • Orlowski J.P., Hanhan U.A., Fiallos M.R. Is aspirin a cause of Reye's syndrome? A case against. Drug Safety 2002, 25:225-231.
    • (2002) Drug Safety , vol.25 , pp. 225-231
    • Orlowski, J.P.1    Hanhan, U.A.2    Fiallos, M.R.3
  • 70
    • 0038710633 scopus 로고    scopus 로고
    • Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant
    • Ott D.E., Coren L.V., Chertova E.N., Gagliardi T.D., Nagashima K., Sowder R.C., Poon D.T., Gorelick R.J. Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant. J. Virol 2003, 77:5547-5556.
    • (2003) J. Virol , vol.77 , pp. 5547-5556
    • Ott, D.E.1    Coren, L.V.2    Chertova, E.N.3    Gagliardi, T.D.4    Nagashima, K.5    Sowder, R.C.6    Poon, D.T.7    Gorelick, R.J.8
  • 71
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-kappaB transcription factors
    • Pahl H.L. Activators and target genes of Rel/NF-kappaB transcription factors. Oncogene 1999, 18:6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 72
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994, 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 74
    • 57149092384 scopus 로고    scopus 로고
    • Influenza A virus inhibits type I IFN signaling via NF-kappaB-dependent induction of SOCS-3 expression
    • Pauli E.K., Schmolke M., Wolff T., Viemann D., Roth J., Bode J.G., Ludwig S. Influenza A virus inhibits type I IFN signaling via NF-kappaB-dependent induction of SOCS-3 expression. PLoS Pathog. 2008, 4:e1000196.
    • (2008) PLoS Pathog. , vol.4
    • Pauli, E.K.1    Schmolke, M.2    Wolff, T.3    Viemann, D.4    Roth, J.5    Bode, J.G.6    Ludwig, S.7
  • 75
    • 33750457370 scopus 로고    scopus 로고
    • Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
    • Perkins N.D. Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway. Oncogene 2006, 25:6717-6730.
    • (2006) Oncogene , vol.25 , pp. 6717-6730
    • Perkins, N.D.1
  • 76
    • 80052696801 scopus 로고    scopus 로고
    • Inhibition of influenza virus-induced NF-kappaB and Raf/MEK/ERK activation can reduce both virus titers and cytokine expression simultaneously in vitro and in vivo
    • Pinto R., Herold S., Cakarova L., Hoegner K., Lohmeyer J., Planz O., Pleschka S. Inhibition of influenza virus-induced NF-kappaB and Raf/MEK/ERK activation can reduce both virus titers and cytokine expression simultaneously in vitro and in vivo. Antiviral Res. 2011, 92:45-56.
    • (2011) Antiviral Res. , vol.92 , pp. 45-56
    • Pinto, R.1    Herold, S.2    Cakarova, L.3    Hoegner, K.4    Lohmeyer, J.5    Planz, O.6    Pleschka, S.7
  • 77
    • 0035027950 scopus 로고    scopus 로고
    • MEK-specific inhibitor U0126 blocks spread of Borna disease virus in cultured cells
    • Planz O., Pleschka S., Ludwig S. MEK-specific inhibitor U0126 blocks spread of Borna disease virus in cultured cells. J. Virol. 2001, 75:4871-4877.
    • (2001) J. Virol. , vol.75 , pp. 4871-4877
    • Planz, O.1    Pleschka, S.2    Ludwig, S.3
  • 78
    • 54049131196 scopus 로고    scopus 로고
    • RNA viruses and the mitogenic Raf/MEK/ERK signal transduction cascade
    • Pleschka S. RNA viruses and the mitogenic Raf/MEK/ERK signal transduction cascade. Biol. Chem. 2008, 389:1273-1282.
    • (2008) Biol. Chem. , vol.389 , pp. 1273-1282
    • Pleschka, S.1
  • 79
  • 82
    • 84866156494 scopus 로고    scopus 로고
    • The NS1 protein of influenza A virus blocks RIG-I-mediated activation of the noncanonical NF-kappaB pathway and p52/RelB-dependent gene expression in lung epithelial cells
    • Ruckle A., Haasbach E., Julkunen I., Planz O., Ehrhardt C., Ludwig S. The NS1 protein of influenza A virus blocks RIG-I-mediated activation of the noncanonical NF-kappaB pathway and p52/RelB-dependent gene expression in lung epithelial cells. J. Virol. 2012, 86:10211-10217.
    • (2012) J. Virol. , vol.86 , pp. 10211-10217
    • Ruckle, A.1    Haasbach, E.2    Julkunen, I.3    Planz, O.4    Ehrhardt, C.5    Ludwig, S.6
  • 85
    • 33750443289 scopus 로고    scopus 로고
    • IkappaB kinase complexes: gateways to NF-kappaB activation and transcription
    • Scheidereit C. IkappaB kinase complexes: gateways to NF-kappaB activation and transcription. Oncogene 2006, 25:6685-6705.
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 87
    • 10344258041 scopus 로고    scopus 로고
    • Targeting the mitogen-activated protein kinase cascade to treat cancer
    • Sebolt-Leopold J.S., Herrera R. Targeting the mitogen-activated protein kinase cascade to treat cancer. Nat. Rev. Cancer 2004, 4:937-947.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 937-947
    • Sebolt-Leopold, J.S.1    Herrera, R.2
  • 88
    • 32644456874 scopus 로고    scopus 로고
    • Antiviral innate immunity pathways
    • Seth R.B., Sun L., Chen Z.J. Antiviral innate immunity pathways. Cell Res. 2006, 16:141-147.
    • (2006) Cell Res. , vol.16 , pp. 141-147
    • Seth, R.B.1    Sun, L.2    Chen, Z.J.3
  • 89
    • 0032848467 scopus 로고    scopus 로고
    • Antioxidant properties of aspirin: characterization of the ability of aspirin to inhibit silica-induced lipid peroxidation, DNA damage, NF-kappaB activation, and TNF-alpha production
    • Shi X., Ding M., Dong Z., Chen F., Ye J., Wang S., Leonard S.S., Castranova V., Vallyathan V. Antioxidant properties of aspirin: characterization of the ability of aspirin to inhibit silica-induced lipid peroxidation, DNA damage, NF-kappaB activation, and TNF-alpha production. Mol. Cell Biochem. 1999, 199:93-102.
    • (1999) Mol. Cell Biochem. , vol.199 , pp. 93-102
    • Shi, X.1    Ding, M.2    Dong, Z.3    Chen, F.4    Ye, J.5    Wang, S.6    Leonard, S.S.7    Castranova, V.8    Vallyathan, V.9
  • 90
    • 36349018937 scopus 로고    scopus 로고
    • SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation
    • Shin Y.K., Li Y., Liu Q., Anderson D.H., Babiuk L.A., Zhou Y. SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. J. Virol. 2007, 81:12730-12739.
    • (2007) J. Virol. , vol.81 , pp. 12730-12739
    • Shin, Y.K.1    Li, Y.2    Liu, Q.3    Anderson, D.H.4    Babiuk, L.A.5    Zhou, Y.6
  • 91
    • 33847644660 scopus 로고    scopus 로고
    • Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation
    • Shin Y.K., Liu Q., Tikoo S.K., Babiuk L.A., Zhou Y. Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. J. Gen. Virol. 2007, 88:942-950.
    • (2007) J. Gen. Virol. , vol.88 , pp. 942-950
    • Shin, Y.K.1    Liu, Q.2    Tikoo, S.K.3    Babiuk, L.A.4    Zhou, Y.5
  • 92
    • 0037213578 scopus 로고    scopus 로고
    • Role of protein kinase C betaII in influenza virus entry via late endosomes
    • Sieczkarski S.B., Brown H.A., Whittaker G.R. Role of protein kinase C betaII in influenza virus entry via late endosomes. J. Virol. 2003, 77:460-469.
    • (2003) J. Virol. , vol.77 , pp. 460-469
    • Sieczkarski, S.B.1    Brown, H.A.2    Whittaker, G.R.3
  • 93
    • 82355191581 scopus 로고    scopus 로고
    • Oseltamivir in seasonal, pandemic, and avian influenza: a comprehensive review of 10-years clinical experience
    • Smith J.R., Rayner C.R., Donner B., Wollenhaupt M., Klumpp K., Dutkowski R. Oseltamivir in seasonal, pandemic, and avian influenza: a comprehensive review of 10-years clinical experience. Adv. Ther. 2011, 28:927-959.
    • (2011) Adv. Ther. , vol.28 , pp. 927-959
    • Smith, J.R.1    Rayner, C.R.2    Donner, B.3    Wollenhaupt, M.4    Klumpp, K.5    Dutkowski, R.6
  • 94
    • 46049100809 scopus 로고    scopus 로고
    • Bortezomib: a novel chemotherapeutic agent for hematologic malignancies
    • Utecht K.N., Kolesar J. Bortezomib: a novel chemotherapeutic agent for hematologic malignancies. Am. J. Health Syst. Pharm. 2008, 65:1221-1231.
    • (2008) Am. J. Health Syst. Pharm. , vol.65 , pp. 1221-1231
    • Utecht, K.N.1    Kolesar, J.2
  • 96
    • 84859715410 scopus 로고    scopus 로고
    • A key role for NF-kappaB transcription factor c-Rel in T-lymphocyte-differentiation and effector functions
    • Visekruna A., Volkov A., Steinhoff U. A key role for NF-kappaB transcription factor c-Rel in T-lymphocyte-differentiation and effector functions. Clin. Dev. Immunol. 2012, 2012:239368.
    • (2012) Clin. Dev. Immunol. , vol.2012 , pp. 239368
    • Visekruna, A.1    Volkov, A.2    Steinhoff, U.3
  • 98
    • 33744961633 scopus 로고    scopus 로고
    • NFkappaB negatively regulates interferon-induced gene expression and anti-influenza activity
    • Wei L., Sandbulte M.R., Thomas P.G., Webby R.J., Homayouni R., Pfeffer L.M. NFkappaB negatively regulates interferon-induced gene expression and anti-influenza activity. J. Biol. Chem. 2006, 281:11678-11684.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11678-11684
    • Wei, L.1    Sandbulte, M.R.2    Thomas, P.G.3    Webby, R.J.4    Homayouni, R.5    Pfeffer, L.M.6
  • 99
    • 77956044811 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system affects influenza A virus infection at a postfusion step
    • Widjaja I., de Vries E., Tscherne D.M., Garcia-Sastre A., Rottier P.J., de Haan C.A. Inhibition of the ubiquitin-proteasome system affects influenza A virus infection at a postfusion step. J. Virol. 2010, 84:9625-9631.
    • (2010) J. Virol. , vol.84 , pp. 9625-9631
    • Widjaja, I.1    de Vries, E.2    Tscherne, D.M.3    Garcia-Sastre, A.4    Rottier, P.J.5    de Haan, C.A.6
  • 100
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human
    • Widmann C., Gibson S., Jarpe M.B., Johnson G.L. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 1999, 79:143-180.
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 102
    • 3843130838 scopus 로고    scopus 로고
    • NF-kappaB-dependent induction of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and Fas/FasL is crucial for efficient influenza virus propagation
    • Wurzer W.J., Ehrhardt C., Pleschka S., Berberich-Siebelt F., Wolff T., Walczak H., Planz O., Ludwig S. NF-kappaB-dependent induction of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and Fas/FasL is crucial for efficient influenza virus propagation. J. Biol. Chem. 2004, 279:30931-30937.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30931-30937
    • Wurzer, W.J.1    Ehrhardt, C.2    Pleschka, S.3    Berberich-Siebelt, F.4    Wolff, T.5    Walczak, H.6    Planz, O.7    Ludwig, S.8
  • 104
    • 0032487857 scopus 로고    scopus 로고
    • The anti-inflammatory agents aspirin and salicylate inhibit the activity of I(kappa)B kinase-beta
    • Yin M.J., Yamamoto Y., Gaynor R.B. The anti-inflammatory agents aspirin and salicylate inhibit the activity of I(kappa)B kinase-beta. Nature 1998, 396:77-80.
    • (1998) Nature , vol.396 , pp. 77-80
    • Yin, M.J.1    Yamamoto, Y.2    Gaynor, R.B.3
  • 105
    • 84878956980 scopus 로고    scopus 로고
    • Bortezomib for patients with previously untreated multiple myeloma: a systematic review and meta-analysis of randomized controlled trials
    • 2013 Mar 2. [Epub ahead of print]
    • Zeng Z., Lin J., Chen J. Bortezomib for patients with previously untreated multiple myeloma: a systematic review and meta-analysis of randomized controlled trials. Ann. Hematol. 2013, 23:1-2. 2013 Mar 2. [Epub ahead of print].
    • (2013) Ann. Hematol. , vol.23 , pp. 1-2
    • Zeng, Z.1    Lin, J.2    Chen, J.3
  • 106
    • 34250828457 scopus 로고    scopus 로고
    • Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling
    • Zhirnov O.P., Klenk H.D. Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling. Apoptosis 2007, 12:1419-1432.
    • (2007) Apoptosis , vol.12 , pp. 1419-1432
    • Zhirnov, O.P.1    Klenk, H.D.2


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