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Volumn 384, Issue 1, 2009, Pages 135-143

Activation of p38 MAPK by feline infectious peritonitis virus regulates pro-inflammatory cytokine production in primary blood-derived feline mononuclear cells

Author keywords

Cytokine; Feline coronavirus; Feline infectious peritonitis; IL 1 beta; p38 MAPK; TNF alpha

Indexed keywords

CYTOKINE; INTERLEUKIN 1BETA; INTERLEUKIN 6; MITOGEN ACTIVATED PROTEIN KINASE P38; TUMOR NECROSIS FACTOR ALPHA;

EID: 58549087344     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2008.11.006     Document Type: Article
Times cited : (45)

References (55)
  • 1
    • 0033982336 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases
    • Adamson A.L., Darr D., Holley-Guthrie E., Johnson R.A., Mauser A., Swenson J., and Kenney S. Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases. J. Virol. 74 3 (2000) 1224-1233
    • (2000) J. Virol. , vol.74 , Issue.3 , pp. 1224-1233
    • Adamson, A.L.1    Darr, D.2    Holley-Guthrie, E.3    Johnson, R.A.4    Mauser, A.5    Swenson, J.6    Kenney, S.7
  • 2
    • 0036109516 scopus 로고    scopus 로고
    • Murine coronavirus replication-induced p38 mitogen-activated protein kinase activation promotes interleukin-6 production and virus replication in cultured cells
    • Banerjee S., Narayanan K., Mizutani T., and Makino S. Murine coronavirus replication-induced p38 mitogen-activated protein kinase activation promotes interleukin-6 production and virus replication in cultured cells. J. Virol. 76 12 (2002) 5937-5948
    • (2002) J. Virol. , vol.76 , Issue.12 , pp. 5937-5948
    • Banerjee, S.1    Narayanan, K.2    Mizutani, T.3    Makino, S.4
  • 3
  • 5
    • 0032571569 scopus 로고    scopus 로고
    • TRAF2 plays a dual role in NF-kappaB-dependent gene activation by mediating the TNF-induced activation of p38 MAPK and IkappaB kinase pathways
    • Carpentier I., Declercq W., Malinin N.L., Wallach D., Fiers W., and Beyaert R. TRAF2 plays a dual role in NF-kappaB-dependent gene activation by mediating the TNF-induced activation of p38 MAPK and IkappaB kinase pathways. FEBS Lett. 425 2 (1998) 195-198
    • (1998) FEBS Lett. , vol.425 , Issue.2 , pp. 195-198
    • Carpentier, I.1    Declercq, W.2    Malinin, N.L.3    Wallach, D.4    Fiers, W.5    Beyaert, R.6
  • 6
    • 33645229326 scopus 로고    scopus 로고
    • The avian coronavirus infectious bronchitis virus undergoes direct low-pH-dependent fusion activation during entry into host cells
    • Chu V., McElroy L.J., Chu V., Bauman B.E., and Whittaker G.R. The avian coronavirus infectious bronchitis virus undergoes direct low-pH-dependent fusion activation during entry into host cells. J. Virol. 80 7 (2006) 3180-3188
    • (2006) J. Virol. , vol.80 , Issue.7 , pp. 3180-3188
    • Chu, V.1    McElroy, L.J.2    Chu, V.3    Bauman, B.E.4    Whittaker, G.R.5
  • 7
    • 0344154638 scopus 로고    scopus 로고
    • In vivo cytokine response to experimental feline infectious peritonitis virus infection
    • Dean G., Olivry T., Stanton C., and Pedersen N.C. In vivo cytokine response to experimental feline infectious peritonitis virus infection. Vet. Microbiol. 97 1-2 (2003) 1-12
    • (2003) Vet. Microbiol. , vol.97 , Issue.1-2 , pp. 1-12
    • Dean, G.1    Olivry, T.2    Stanton, C.3    Pedersen, N.C.4
  • 8
    • 33645014111 scopus 로고    scopus 로고
    • Rhinoviral infections activate p38MAP-kinases via membrane rafts and RhoA
    • Dumitru C.A., Dreschers S., and Gulbins E. Rhinoviral infections activate p38MAP-kinases via membrane rafts and RhoA. Cell. Physiol. Biochem. 17 3-4 (2006) 159-166
    • (2006) Cell. Physiol. Biochem. , vol.17 , Issue.3-4 , pp. 159-166
    • Dumitru, C.A.1    Dreschers, S.2    Gulbins, E.3
  • 9
    • 0036058267 scopus 로고    scopus 로고
    • Hepatitis C virus core protein induces cell proliferation and activates ERK, JNK, and p38 MAP kinases together with the MAP kinase phosphatase MKP-1 in a HepG2 Tet-Off cell line
    • Erhardt A., Hassan M., Heintges T., and Häussinger D. Hepatitis C virus core protein induces cell proliferation and activates ERK, JNK, and p38 MAP kinases together with the MAP kinase phosphatase MKP-1 in a HepG2 Tet-Off cell line. Virology 292 2 (2002) 272-284
    • (2002) Virology , vol.292 , Issue.2 , pp. 272-284
    • Erhardt, A.1    Hassan, M.2    Heintges, T.3    Häussinger, D.4
  • 10
    • 0347951396 scopus 로고    scopus 로고
    • Monocyte/macrophage-derived CC chemokines and their modulation by HIV-1 and cytokines: a complex network of interactions influencing viral replication and AIDS pathogenesis
    • Fantuzzi L., Belardelli F., and Gessani S. Monocyte/macrophage-derived CC chemokines and their modulation by HIV-1 and cytokines: a complex network of interactions influencing viral replication and AIDS pathogenesis. 74 5 (2003) 719-725
    • (2003) 74 , vol.5 , pp. 719-725
    • Fantuzzi, L.1    Belardelli, F.2    Gessani, S.3
  • 12
    • 0037223402 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts
    • Frevel M.A., Bakheet T., Silva A.M., Hissong J.G., Khabar K.S., and Williams B.R. p38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts. Mol. Cell. Biol. 23 2 (2003) 425-436
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.2 , pp. 425-436
    • Frevel, M.A.1    Bakheet, T.2    Silva, A.M.3    Hissong, J.G.4    Khabar, K.S.5    Williams, B.R.6
  • 13
    • 0034327287 scopus 로고    scopus 로고
    • Role of p38 mitogen-activated protein kinase in rhinovirus-induced cytokine production by bronchial epithelial cells
    • Griego S.D., Weston C.B., Adams J.L., Tal-Singer R., and Dillon S.B. Role of p38 mitogen-activated protein kinase in rhinovirus-induced cytokine production by bronchial epithelial cells. J. Immunol. 165 9 (2000) 5211-5220
    • (2000) J. Immunol. , vol.165 , Issue.9 , pp. 5211-5220
    • Griego, S.D.1    Weston, C.B.2    Adams, J.L.3    Tal-Singer, R.4    Dillon, S.B.5
  • 15
    • 33748747144 scopus 로고    scopus 로고
    • Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components
    • Head B., Patel H.H., Roth D.M., Murray F., Swaney J.S., Niesman I.R., Farquhar M.G., and Insel P.A. Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components. J. Biol. Chem. 281 36 (2006) 26391-26399
    • (2006) J. Biol. Chem. , vol.281 , Issue.36 , pp. 26391-26399
    • Head, B.1    Patel, H.H.2    Roth, D.M.3    Murray, F.4    Swaney, J.S.5    Niesman, I.R.6    Farquhar, M.G.7    Insel, P.A.8
  • 16
    • 33750333125 scopus 로고    scopus 로고
    • Rotavirus activates JNK and p38 signaling pathways in intestinal cells, leading to AP-1-driven transcriptional responses and enhanced virus replication
    • Holloway G., and Coulson B.S. Rotavirus activates JNK and p38 signaling pathways in intestinal cells, leading to AP-1-driven transcriptional responses and enhanced virus replication. J. Virol. 80 21 (2006) 10624-10633
    • (2006) J. Virol. , vol.80 , Issue.21 , pp. 10624-10633
    • Holloway, G.1    Coulson, B.S.2
  • 17
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu H., Xiong J., and Goeddel D.V. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell 81 4 (1995) 495-504
    • (1995) Cell , vol.81 , Issue.4 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 18
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H., Shu H.B., Pan M.G., and Goeddel D.V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84 2 (1996) 299-308
    • (1996) Cell , vol.84 , Issue.2 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 19
    • 7244231301 scopus 로고    scopus 로고
    • MAP kinases and cell migration
    • Huang C., Jacobson K., and Schaller M.D. MAP kinases and cell migration. J. Cell. Sci. 117 20 (2004) 4619-4628
    • (2004) J. Cell. Sci. , vol.117 , Issue.20 , pp. 4619-4628
    • Huang, C.1    Jacobson, K.2    Schaller, M.D.3
  • 20
    • 0036029868 scopus 로고    scopus 로고
    • The role of monocytes and macrophages in the pathogenesis of HIV-1 infection
    • Kedzierska K., and Crowe S. The role of monocytes and macrophages in the pathogenesis of HIV-1 infection. Curr. Med. Chem. 9 21 (2002) 1893-1903
    • (2002) Curr. Med. Chem. , vol.9 , Issue.21 , pp. 1893-1903
    • Kedzierska, K.1    Crowe, S.2
  • 21
    • 1842633818 scopus 로고    scopus 로고
    • Disease outcome and cytokine responses in cats immunized with an avirulent feline infectious peritonitis virus (FIPV)-UCD1 and challenge-exposed with virulent FIPV-UCD8
    • Kiss I., Poland A.M., and Pedersen N.C. Disease outcome and cytokine responses in cats immunized with an avirulent feline infectious peritonitis virus (FIPV)-UCD1 and challenge-exposed with virulent FIPV-UCD8. J. Feline Med. Surg. 6 2 (2004) 89-97
    • (2004) J. Feline Med. Surg. , vol.6 , Issue.2 , pp. 89-97
    • Kiss, I.1    Poland, A.M.2    Pedersen, N.C.3
  • 22
    • 0142026209 scopus 로고    scopus 로고
    • p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases
    • Kumar S., Boehm J., and Lee J.C. p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases. Nat. Rev. Drug Discov. 2 9 (2003) 717-726
    • (2003) Nat. Rev. Drug Discov. , vol.2 , Issue.9 , pp. 717-726
    • Kumar, S.1    Boehm, J.2    Lee, J.C.3
  • 24
    • 25644440748 scopus 로고    scopus 로고
    • HIV-1 gp120-induced TNF-{alpha} production by primary human macrophages is mediated by phosphatidylinositol-3 (PI-3) kinase and mitogen-activated protein (MAP) kinase pathways
    • Lee C., Tomkowicz B., Freedman B.D., and Collman R.G. HIV-1 gp120-induced TNF-{alpha} production by primary human macrophages is mediated by phosphatidylinositol-3 (PI-3) kinase and mitogen-activated protein (MAP) kinase pathways. J. Leukoc. Biol. 78 4 (2005) 1016-1023
    • (2005) J. Leukoc. Biol. , vol.78 , Issue.4 , pp. 1016-1023
    • Lee, C.1    Tomkowicz, B.2    Freedman, B.D.3    Collman, R.G.4
  • 25
    • 23244461479 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent hyperinduction of tumor necrosis factor alpha expression in response to avian influenza virus H5N1
    • Lee D.C., Cheung C.Y., Law A.H., Mok C.K., Peiris M., and Lau A.S. p38 mitogen-activated protein kinase-dependent hyperinduction of tumor necrosis factor alpha expression in response to avian influenza virus H5N1. J. Virol. 79 16 (2005) 10147-10154
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10147-10154
    • Lee, D.C.1    Cheung, C.Y.2    Law, A.H.3    Mok, C.K.4    Peiris, M.5    Lau, A.S.6
  • 27
    • 34250309177 scopus 로고    scopus 로고
    • Signal transduction in SARS-CoV-infected cells
    • Mizutani T. Signal transduction in SARS-CoV-infected cells. Ann. N. Y. Acad. Sci. 1102 (2007) 86-95
    • (2007) Ann. N. Y. Acad. Sci. , vol.1102 , pp. 86-95
    • Mizutani, T.1
  • 29
    • 2942581447 scopus 로고    scopus 로고
    • Phosphorylation of p38 MAPK and its downstream targets in SARS coronavirus-infected cells
    • Mizutani T., Fukushi S., Saijo M., Kurane I., and Morikawa S. Phosphorylation of p38 MAPK and its downstream targets in SARS coronavirus-infected cells. Biochem. Biophys. Res. Commun. 319 4 (2004) 1228-1234
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , Issue.4 , pp. 1228-1234
    • Mizutani, T.1    Fukushi, S.2    Saijo, M.3    Kurane, I.4    Morikawa, S.5
  • 33
    • 28944455001 scopus 로고    scopus 로고
    • The role of lipid rafts in LPS-induced signaling in a macrophage cell line
    • Olsson S., and Sundler R. The role of lipid rafts in LPS-induced signaling in a macrophage cell line. Mol. Immunol. 43 6 (2006) 607-612
    • (2006) Mol. Immunol. , vol.43 , Issue.6 , pp. 607-612
    • Olsson, S.1    Sundler, R.2
  • 36
    • 0021732942 scopus 로고
    • Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683
    • Pedersen N.C., Evermann J.F., McKeirnan A.J., and Ott R.L. Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683. Am. J. Vet. Res. 45 (1984) 2580-2585
    • (1984) Am. J. Vet. Res. , vol.45 , pp. 2580-2585
    • Pedersen, N.C.1    Evermann, J.F.2    McKeirnan, A.J.3    Ott, R.L.4
  • 38
    • 0035090589 scopus 로고    scopus 로고
    • Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade
    • Pleschka S., Wolff T., Ehrhardt C., Hobom G., Planz O., Rapp U.R., and Ludwig S. Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade. Nat. Cell Biol. 3 3 (2001) 301-305
    • (2001) Nat. Cell Biol. , vol.3 , Issue.3 , pp. 301-305
    • Pleschka, S.1    Wolff, T.2    Ehrhardt, C.3    Hobom, G.4    Planz, O.5    Rapp, U.R.6    Ludwig, S.7
  • 39
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman M., Chen W., and Cobb M.H. Differential regulation and properties of MAPKs. Oncogene 26 22 (2007) 3100-3112
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 40
    • 53549129721 scopus 로고    scopus 로고
    • Regan, A., Shraybman, R., Cohen, R.D., Whittaker, G.W., 2008. Differential role for low pH and cathepsin-mediated cleavage of the viral spike protein during entry of serotype II feline coronaviruses. Vet. Microbiol 132, 235-248.
    • Regan, A., Shraybman, R., Cohen, R.D., Whittaker, G.W., 2008. Differential role for low pH and cathepsin-mediated cleavage of the viral spike protein during entry of serotype II feline coronaviruses. Vet. Microbiol 132, 235-248.
  • 41
    • 0032819499 scopus 로고    scopus 로고
    • The molecular dynamics of feline coronaviruses
    • Rottier P. The molecular dynamics of feline coronaviruses. Vet. Microbiol. 69 1-2 (1999) 117-125
    • (1999) Vet. Microbiol. , vol.69 , Issue.1-2 , pp. 117-125
    • Rottier, P.1
  • 42
    • 27644491880 scopus 로고    scopus 로고
    • Acquisition of macrophage tropism during the pathogenesis of feline infectious peritonitis is determined by mutations in the feline coronavirus spike protein
    • Rottier P., Nakamura K., Schellen P., Volders H., and Haijema B.J. Acquisition of macrophage tropism during the pathogenesis of feline infectious peritonitis is determined by mutations in the feline coronavirus spike protein. J. Virol. 79 22 (2005) 14122-14130
    • (2005) J. Virol. , vol.79 , Issue.22 , pp. 14122-14130
    • Rottier, P.1    Nakamura, K.2    Schellen, P.3    Volders, H.4    Haijema, B.J.5
  • 43
    • 36048939813 scopus 로고    scopus 로고
    • Herpes simplex virus remodels T-cell receptor signaling, resulting in p38-dependent selective synthesis of interleukin-10
    • Sloan D.D., and Jerome K.R. Herpes simplex virus remodels T-cell receptor signaling, resulting in p38-dependent selective synthesis of interleukin-10. J. Virol. 81 22 (2007) 12504-12514
    • (2007) J. Virol. , vol.81 , Issue.22 , pp. 12504-12514
    • Sloan, D.D.1    Jerome, K.R.2
  • 44
    • 0024484373 scopus 로고
    • Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence
    • Stoddart C., and Scott F.W. Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence. J. Virol. 63 1 (1989) 436-440
    • (1989) J. Virol. , vol.63 , Issue.1 , pp. 436-440
    • Stoddart, C.1    Scott, F.W.2
  • 45
    • 34147166070 scopus 로고    scopus 로고
    • The lipid raft proteins flotillins/reggies interact with Galphaq and are involved in Gq-mediated p38 mitogen-activated protein kinase activation through tyrosine kinase
    • Sugawara Y., Nishii H., Takahashi T., Yamauchi J., Mizuno N., Tago K., and Itoh H. The lipid raft proteins flotillins/reggies interact with Galphaq and are involved in Gq-mediated p38 mitogen-activated protein kinase activation through tyrosine kinase. Cell. Signal. 19 6 (2007) 1301-1308
    • (2007) Cell. Signal. , vol.19 , Issue.6 , pp. 1301-1308
    • Sugawara, Y.1    Nishii, H.2    Takahashi, T.3    Yamauchi, J.4    Mizuno, N.5    Tago, K.6    Itoh, H.7
  • 46
    • 33845913769 scopus 로고    scopus 로고
    • A "possible" involvement of TNF-alpha in apoptosis induction in peripheral blood lymphocytes of cats with feline infectious peritonitis
    • Takano T., Hohdatsu T., Hashida Y., Kaneko Y., Tanabe M., and Koyama H. A "possible" involvement of TNF-alpha in apoptosis induction in peripheral blood lymphocytes of cats with feline infectious peritonitis. Vet. Microbiol. 119 2-4 (2007) 121-131
    • (2007) Vet. Microbiol. , vol.119 , Issue.2-4 , pp. 121-131
    • Takano, T.1    Hohdatsu, T.2    Hashida, Y.3    Kaneko, Y.4    Tanabe, M.5    Koyama, H.6
  • 47
    • 34249654148 scopus 로고    scopus 로고
    • TNF-alpha, produced by feline infectious peritonitis virus (FIPV)-infected macrophages, upregulates expression of type II FIPV receptor feline aminopeptidase N in feline macrophages
    • Takano T., Hohdatsu T., Toda A., Tanabe M., and Koyama H. TNF-alpha, produced by feline infectious peritonitis virus (FIPV)-infected macrophages, upregulates expression of type II FIPV receptor feline aminopeptidase N in feline macrophages. Virology 364 1 (2007) 64-72
    • (2007) Virology , vol.364 , Issue.1 , pp. 64-72
    • Takano, T.1    Hohdatsu, T.2    Toda, A.3    Tanabe, M.4    Koyama, H.5
  • 48
    • 0032579804 scopus 로고    scopus 로고
    • Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses
    • Vennema H., Poland A., Foley J., and Pedersen N.C. Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses. Virology 243 1 (1998) 150-157
    • (1998) Virology , vol.243 , Issue.1 , pp. 150-157
    • Vennema, H.1    Poland, A.2    Foley, J.3    Pedersen, N.C.4
  • 49
    • 8644286664 scopus 로고    scopus 로고
    • Sustained activation of p38 mitogen-activated protein kinase and c-Jun N-terminal kinase pathways by hepatitis B virus X protein mediates apoptosis via induction of Fas/FasL and tumor necrosis factor (TNF) receptor 1/TNF-alpha expression
    • Wang W.H., Grégori G., Hullinger R.L., and Andrisani O.M. Sustained activation of p38 mitogen-activated protein kinase and c-Jun N-terminal kinase pathways by hepatitis B virus X protein mediates apoptosis via induction of Fas/FasL and tumor necrosis factor (TNF) receptor 1/TNF-alpha expression. Mol. Cell. Biol. 24 23 (2004) 10352-10365
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.23 , pp. 10352-10365
    • Wang, W.H.1    Grégori, G.2    Hullinger, R.L.3    Andrisani, O.M.4
  • 50
    • 33750303979 scopus 로고    scopus 로고
    • HSP70 enhances macrophage phagocytosis by interaction with lipid raft-associated TLR-7 and upregulating p38 MAPK and PI3K pathways
    • Wang R., Town T., Gokarn V., Flavell R.A., and Chandawarkar R.Y. HSP70 enhances macrophage phagocytosis by interaction with lipid raft-associated TLR-7 and upregulating p38 MAPK and PI3K pathways. J. Surg. Res. 136 1 (2006) 58-69
    • (2006) J. Surg. Res. , vol.136 , Issue.1 , pp. 58-69
    • Wang, R.1    Town, T.2    Gokarn, V.3    Flavell, R.A.4    Chandawarkar, R.Y.5
  • 51
    • 0019738717 scopus 로고
    • Pathogenesis of feline infectious peritonitis: pathologic changes and immunofluorescence
    • Weiss R., and Scott F.W. Pathogenesis of feline infectious peritonitis: pathologic changes and immunofluorescence. Am. J. Vet. Res. 42 12 (1981) 2036-2048
    • (1981) Am. J. Vet. Res. , vol.42 , Issue.12 , pp. 2036-2048
    • Weiss, R.1    Scott, F.W.2
  • 52
    • 34547196977 scopus 로고    scopus 로고
    • Regulation of gene transcription by mitogen-activated protein kinase signaling pathways
    • Whitmarsh A.J. Regulation of gene transcription by mitogen-activated protein kinase signaling pathways. Biochim. Biophys. Acta 1773 8 (2007) 1285-1298
    • (2007) Biochim. Biophys. Acta , vol.1773 , Issue.8 , pp. 1285-1298
    • Whitmarsh, A.J.1
  • 53
    • 0033561760 scopus 로고    scopus 로고
    • Human cytomegalovirus binding to human monocytes induces immunoregulatory gene expression
    • Yurochko A.D., and Huang E.S. Human cytomegalovirus binding to human monocytes induces immunoregulatory gene expression. J. Immunol. 162 8 (1999) 4806-4816
    • (1999) J. Immunol. , vol.162 , Issue.8 , pp. 4806-4816
    • Yurochko, A.D.1    Huang, E.S.2
  • 54
    • 0033582476 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection stimulates p38/c-Jun N-terminal mitogen-activated protein kinase pathways and activates transcription factor AP-1
    • Zachos G., Clements B., and Conner J. Herpes simplex virus type 1 infection stimulates p38/c-Jun N-terminal mitogen-activated protein kinase pathways and activates transcription factor AP-1. J. Biol. Chem. 274 8 (1999) 5097-5103
    • (1999) J. Biol. Chem. , vol.274 , Issue.8 , pp. 5097-5103
    • Zachos, G.1    Clements, B.2    Conner, J.3
  • 55
    • 38849188633 scopus 로고    scopus 로고
    • Leptin-induced cardiomyocyte hypertrophy involves selective caveolae and RhoA/ROCK-dependent p38 MAPK translocation to nuclei
    • Zeidan A., Javadov S., Chakrabarti S., and Karmazyn M. Leptin-induced cardiomyocyte hypertrophy involves selective caveolae and RhoA/ROCK-dependent p38 MAPK translocation to nuclei. Cardiovasc. Res. 77 1 (2008) 64-72
    • (2008) Cardiovasc. Res. , vol.77 , Issue.1 , pp. 64-72
    • Zeidan, A.1    Javadov, S.2    Chakrabarti, S.3    Karmazyn, M.4


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