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Volumn 7, Issue 2, 2011, Pages

DC-SIGN mediated sphingomyelinase-activation and ceramide generation is essential for enhancement of viral uptake in dendritic cells

Author keywords

[No Author keywords available]

Indexed keywords

CD150 ANTIGEN; CD209 ANTIGEN; CERAMIDE; MANNAN; MITOGEN ACTIVATED PROTEIN KINASE; RAF PROTEIN; SPHINGOMYELIN PHOSPHODIESTERASE; CELL ADHESION MOLECULE; CELL SURFACE RECEPTOR; DC-SPECIFIC ICAM-3 GRABBING NONINTEGRIN; LECTIN; LEUKOCYTE ANTIGEN; MESSENGER RNA; SMALL INTERFERING RNA; VIRUS RECEPTOR;

EID: 79952206109     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1001290     Document Type: Article
Times cited : (85)

References (68)
  • 1
    • 70049116988 scopus 로고    scopus 로고
    • Influence of dendritic cells on viral pathogenicity
    • Freer G, Matteucci D, (2009) Influence of dendritic cells on viral pathogenicity. PLoS Pathog 5: e1000384.
    • (2009) PLoS Pathog , vol.5
    • Freer, G.1    Matteucci, D.2
  • 5
    • 33646162168 scopus 로고    scopus 로고
    • SLAM family receptors and SAP-related adaptors: matters arising
    • Veillette A, Cruz-Munoz ME, Zhong MC, (2006) SLAM family receptors and SAP-related adaptors: matters arising. Trends Immunol 27: 228-234.
    • (2006) Trends Immunol , vol.27 , pp. 228-234
    • Veillette, A.1    Cruz-Munoz, M.E.2    Zhong, M.C.3
  • 6
    • 37349049260 scopus 로고    scopus 로고
    • Predominant infection of CD150+ lymphocytes and dendritic cells during measles virus infection of macaques
    • de Swart RL, Ludlow M, de Witte L, Yanagi Y, van Amerongen G, et al. (2007) Predominant infection of CD150+ lymphocytes and dendritic cells during measles virus infection of macaques. PLoS Pathog 3: e178.
    • (2007) PLoS Pathog , vol.3
    • de Swart, R.L.1    Ludlow, M.2    de Witte, L.3    Yanagi, Y.4    van Amerongen, G.5
  • 7
    • 0035881677 scopus 로고    scopus 로고
    • Signaling lymphocytic activation molecule is expressed on mature CD83+ dendritic cells and is up-regulated by IL-1 beta
    • Kruse M, Meinl E, Henning G, Kuhnt C, Berchtold S, et al. (2001) Signaling lymphocytic activation molecule is expressed on mature CD83+ dendritic cells and is up-regulated by IL-1 beta. J Immunol 167: 1989-1995.
    • (2001) J Immunol , vol.167 , pp. 1989-1995
    • Kruse, M.1    Meinl, E.2    Henning, G.3    Kuhnt, C.4    Berchtold, S.5
  • 8
    • 45749114494 scopus 로고    scopus 로고
    • Receptor interactions, tropism, and mechanisms involved in morbillivirus-induced immunomodulation
    • Schneider-Schaulies J, Schneider-Schaulies S, (2008) Receptor interactions, tropism, and mechanisms involved in morbillivirus-induced immunomodulation. Adv Virus Res 71: 173-205.
    • (2008) Adv Virus Res , vol.71 , pp. 173-205
    • Schneider-Schaulies, J.1    Schneider-Schaulies, S.2
  • 10
    • 43049084813 scopus 로고    scopus 로고
    • DC-SIGN and CD150 have distinct roles in transmission of measles virus from dendritic cells to T-lymphocytes
    • de Witte L, de Vries RD, van der Vlist M, Yuksel S, Litjens M, et al. (2008) DC-SIGN and CD150 have distinct roles in transmission of measles virus from dendritic cells to T-lymphocytes. PLoS Pathog 4: e1000049.
    • (2008) PLoS Pathog , vol.4
    • de Witte, L.1    de Vries, R.D.2    van der Vlist, M.3    Yuksel, S.4    Litjens, M.5
  • 11
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-κB
    • Gringhuis SI, den Dunnen J, Litjens M, van Het Hof B, van Kooyk Y, et al. (2007) C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-κB. Immunity 26: 605-616.
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.I.1    den Dunnen, J.2    Litjens, M.3    van Het Hof, B.4    van Kooyk, Y.5
  • 12
    • 0141519281 scopus 로고    scopus 로고
    • Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a pathogen receptor with broad specificity
    • Geijtenbeek TB, van Kooyk Y, (2003) Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a pathogen receptor with broad specificity. APMIS 111: 698-714.
    • (2003) APMIS , vol.111 , pp. 698-714
    • Geijtenbeek, T.B.1    van Kooyk, Y.2
  • 13
    • 0141688292 scopus 로고    scopus 로고
    • DC-SIGN: escape mechanism for pathogens
    • van Kooyk Y, Geijtenbeek TB, (2003) DC-SIGN: escape mechanism for pathogens. Nat Rev Immunol 3: 697-709.
    • (2003) Nat Rev Immunol , vol.3 , pp. 697-709
    • van Kooyk, Y.1    Geijtenbeek, T.B.2
  • 15
    • 67649781789 scopus 로고    scopus 로고
    • Endogenous ligands for C-type lectin receptors: the true regulators of immune homeostasis
    • Garcia-Vallejo JJ, van Kooyk Y, (2009) Endogenous ligands for C-type lectin receptors: the true regulators of immune homeostasis. Immunol Rev 230: 22-37.
    • (2009) Immunol Rev , vol.230 , pp. 22-37
    • Garcia-Vallejo, J.J.1    van Kooyk, Y.2
  • 16
    • 42149114525 scopus 로고    scopus 로고
    • Distribution and lateral mobility of DC-SIGN on immature dendritic cells-implications for pathogen uptake
    • Neumann AK, Thompson NL, Jacobson K, (2008) Distribution and lateral mobility of DC-SIGN on immature dendritic cells-implications for pathogen uptake. J Cell Sci 121: 634-643.
    • (2008) J Cell Sci , vol.121 , pp. 634-643
    • Neumann, A.K.1    Thompson, N.L.2    Jacobson, K.3
  • 17
    • 0347122962 scopus 로고    scopus 로고
    • Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
    • Cambi A, de Lange F, van Maarseveen NM, Nijhuis M, Joosten B, et al. (2004) Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells. J Cell Biol 164: 145-155.
    • (2004) J Cell Biol , vol.164 , pp. 145-155
    • Cambi, A.1    de Lange, F.2    van Maarseveen, N.M.3    Nijhuis, M.4    Joosten, B.5
  • 18
    • 34248228113 scopus 로고    scopus 로고
    • Ligand-conjugated quantum dots monitor antigen uptake and processing by dendritic cells
    • Cambi A, Lidke DS, Arndt-Jovin DJ, Figdor CG, Jovin TM, (2007) Ligand-conjugated quantum dots monitor antigen uptake and processing by dendritic cells. Nano Lett 7: 970-977.
    • (2007) Nano Lett , vol.7 , pp. 970-977
    • Cambi, A.1    Lidke, D.S.2    Arndt-Jovin, D.J.3    Figdor, C.G.4    Jovin, T.M.5
  • 19
    • 34447569554 scopus 로고    scopus 로고
    • Nanoscale organization of the pathogen receptor DC-SIGN mapped by single-molecule high-resolution fluorescence microscopy
    • de Bakker BI, de Lange F, Cambi A, Korterik JP, van Dijk EM, et al. (2007) Nanoscale organization of the pathogen receptor DC-SIGN mapped by single-molecule high-resolution fluorescence microscopy. Chemphyschem 8: 1473-1480.
    • (2007) Chemphyschem , vol.8 , pp. 1473-1480
    • de Bakker, B.I.1    de Lange, F.2    Cambi, A.3    Korterik, J.P.4    van Dijk, E.M.5
  • 21
    • 70349201241 scopus 로고    scopus 로고
    • Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to Mycobacterium tuberculosis, HIV-1 and Helicobacter pylori
    • Gringhuis SI, den Dunnen J, Litjens M, van der Vlist M, Geijtenbeek TB, (2009) Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to Mycobacterium tuberculosis, HIV-1 and Helicobacter pylori. Nat Immunol 10: 1081-1088.
    • (2009) Nat Immunol , vol.10 , pp. 1081-1088
    • Gringhuis, S.I.1    den Dunnen, J.2    Litjens, M.3    van der Vlist, M.4    Geijtenbeek, T.B.5
  • 22
    • 34249088361 scopus 로고    scopus 로고
    • Activation of the lectin DC-SIGN induces an immature dendritic cell phenotype triggering Rho-GTPase activity required for HIV-1 replication
    • Hodges A, Sharrocks K, Edelmann M, Baban D, Moris A, et al. (2007) Activation of the lectin DC-SIGN induces an immature dendritic cell phenotype triggering Rho-GTPase activity required for HIV-1 replication. Nat Immunol 8: 569-577.
    • (2007) Nat Immunol , vol.8 , pp. 569-577
    • Hodges, A.1    Sharrocks, K.2    Edelmann, M.3    Baban, D.4    Moris, A.5
  • 23
    • 3042788418 scopus 로고    scopus 로고
    • Hepatitis C virus targets DC-SIGN and L-SIGN to escape lysosomal degradation
    • Ludwig IS, Lekkerkerker AN, Depla E, Bosman F, Musters RJ, et al. (2004) Hepatitis C virus targets DC-SIGN and L-SIGN to escape lysosomal degradation. J Virol 78: 8322-8332.
    • (2004) J Virol , vol.78 , pp. 8322-8332
    • Ludwig, I.S.1    Lekkerkerker, A.N.2    Depla, E.3    Bosman, F.4    Musters, R.J.5
  • 24
    • 38049086957 scopus 로고    scopus 로고
    • Distinct roles for DC-SIGN+-dendritic cells and Langerhans cells in HIV-1 transmission
    • de Witte L, Nabatov A, Geijtenbeek TB, (2008) Distinct roles for DC-SIGN+-dendritic cells and Langerhans cells in HIV-1 transmission. Trends Mol Med 14: 12-19.
    • (2008) Trends Mol Med , vol.14 , pp. 12-19
    • de Witte, L.1    Nabatov, A.2    Geijtenbeek, T.B.3
  • 25
    • 38449102893 scopus 로고    scopus 로고
    • Analysis of the interaction of Ebola virus glycoprotein with DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) and its homologue DC-SIGNR
    • Marzi A, Moller P, Hanna SL, Harrer T, Eisemann J, et al. (2007) Analysis of the interaction of Ebola virus glycoprotein with DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) and its homologue DC-SIGNR. J Infect Dis 196: S237-246.
    • (2007) J Infect Dis , vol.196
    • Marzi, A.1    Moller, P.2    Hanna, S.L.3    Harrer, T.4    Eisemann, J.5
  • 26
    • 0033974782 scopus 로고    scopus 로고
    • Ceramide in the eukaryotic stress response
    • Hannun YA, Luberto C, (2000) Ceramide in the eukaryotic stress response. Trends Cell Biol 10: 73-80.
    • (2000) Trends Cell Biol , vol.10 , pp. 73-80
    • Hannun, Y.A.1    Luberto, C.2
  • 27
    • 58149204290 scopus 로고    scopus 로고
    • Ceramide-enriched membrane domains-Structure and function
    • Zhang Y, Li X, Becker KA, Gulbins E, (2009) Ceramide-enriched membrane domains-Structure and function. Biochim Biophys Acta 1788: 178-83.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 178-183
    • Zhang, Y.1    Li, X.2    Becker, K.A.3    Gulbins, E.4
  • 28
    • 34250742501 scopus 로고    scopus 로고
    • Biological aspects of ceramide-enriched membrane domains
    • Grassme H, Riethmuller J, Gulbins E, (2007) Biological aspects of ceramide-enriched membrane domains. Prog Lipid Res 46: 161-170.
    • (2007) Prog Lipid Res , vol.46 , pp. 161-170
    • Grassme, H.1    Riethmuller, J.2    Gulbins, E.3
  • 30
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: lessons from sphingolipids
    • Hannun YA, Obeid LM, (2008) Principles of bioactive lipid signalling: lessons from sphingolipids. Nat Rev Mol Cell Biol 9: 139-150.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 32
    • 0037201939 scopus 로고    scopus 로고
    • Sphingomyelinases: enzymology and membrane activity
    • Goni FM, Alonso A, (2002) Sphingomyelinases: enzymology and membrane activity. FEBS Lett 531: 38-46.
    • (2002) FEBS Lett , vol.531 , pp. 38-46
    • Goni, F.M.1    Alonso, A.2
  • 33
    • 68349131603 scopus 로고    scopus 로고
    • A ceramide-binding C1 domain mediates kinase suppressor of ras membrane translocation
    • Yin X, Zafrullah M, Lee H, Haimovitz-Friedman A, Fuks Z, et al. (2009) A ceramide-binding C1 domain mediates kinase suppressor of ras membrane translocation. Cell Physiol Biochem 24: 219-230.
    • (2009) Cell Physiol Biochem , vol.24 , pp. 219-230
    • Yin, X.1    Zafrullah, M.2    Lee, H.3    Haimovitz-Friedman, A.4    Fuks, Z.5
  • 35
    • 0037401894 scopus 로고    scopus 로고
    • Intracellular signal transduction pathways activated by ceramide and its metabolites
    • Ruvolo PP, (2003) Intracellular signal transduction pathways activated by ceramide and its metabolites. Pharmacol Res 47: 383-392.
    • (2003) Pharmacol Res , vol.47 , pp. 383-392
    • Ruvolo, P.P.1
  • 36
    • 0343742670 scopus 로고    scopus 로고
    • Kinase suppressor of Ras is ceramide-activated protein kinase
    • Zhang Y, Yao B, Delikat S, Bayoumy S, Lin XH, et al. (1997) Kinase suppressor of Ras is ceramide-activated protein kinase. Cell 89: 63-72.
    • (1997) Cell , vol.89 , pp. 63-72
    • Zhang, Y.1    Yao, B.2    Delikat, S.3    Bayoumy, S.4    Lin, X.H.5
  • 37
    • 0035116903 scopus 로고    scopus 로고
    • Kinase suppressor of ras is necessary for tumor necrosis factor alpha activation of extracellular signal-regulated kinase/mitogen-activated protein kinase in intestinal epithelial cells
    • Yan F, Polk DB, (2001) Kinase suppressor of ras is necessary for tumor necrosis factor alpha activation of extracellular signal-regulated kinase/mitogen-activated protein kinase in intestinal epithelial cells. Cancer Res 61: 963-969.
    • (2001) Cancer Res , vol.61 , pp. 963-969
    • Yan, F.1    Polk, D.B.2
  • 38
    • 58149292279 scopus 로고    scopus 로고
    • Ceramide-enriched membrane domains in infectious biology and development
    • Becker KA, Gellhaus A, Winterhager E, Gulbins E, (2008) Ceramide-enriched membrane domains in infectious biology and development. Subcell Biochem 49: 523-538.
    • (2008) Subcell Biochem , vol.49 , pp. 523-538
    • Becker, K.A.1    Gellhaus, A.2    Winterhager, E.3    Gulbins, E.4
  • 40
    • 41649103930 scopus 로고    scopus 로고
    • Fusogenicity of membranes: the impact of acid sphingomyelinase on innate immune responses
    • Utermohlen O, Herz J, Schramm M, Kronke M, (2008) Fusogenicity of membranes: the impact of acid sphingomyelinase on innate immune responses. Immunobiology 213: 307-314.
    • (2008) Immunobiology , vol.213 , pp. 307-314
    • Utermohlen, O.1    Herz, J.2    Schramm, M.3    Kronke, M.4
  • 41
    • 33646577823 scopus 로고    scopus 로고
    • DC-SIGN ligation on dendritic cells results in ERK and PI3K activation and modulates cytokine production
    • Caparros E, Munoz P, Sierra-Filardi E, Serrano-Gomez D, Puig-Kroger A, et al. (2006) DC-SIGN ligation on dendritic cells results in ERK and PI3K activation and modulates cytokine production. Blood 107: 3950-3958.
    • (2006) Blood , vol.107 , pp. 3950-3958
    • Caparros, E.1    Munoz, P.2    Sierra-Filardi, E.3    Serrano-Gomez, D.4    Puig-Kroger, A.5
  • 42
    • 0033590083 scopus 로고    scopus 로고
    • Phosphatidylserine exposure during apoptosis is a cell-type-specific event and does not correlate with plasma membrane phospholipid scramblase expression
    • Fadeel B, Gleiss B, Hogstrand K, Chandra J, Wiedmer T, et al. (1999) Phosphatidylserine exposure during apoptosis is a cell-type-specific event and does not correlate with plasma membrane phospholipid scramblase expression. Biochem Biophys Res Commun 266: 504-511.
    • (1999) Biochem Biophys Res Commun , vol.266 , pp. 504-511
    • Fadeel, B.1    Gleiss, B.2    Hogstrand, K.3    Chandra, J.4    Wiedmer, T.5
  • 43
    • 69249154681 scopus 로고    scopus 로고
    • The C-type lectin DC-SIGN internalizes soluble antigens and HIV-1 virions via a clathrin-dependent mechanism
    • Cambi A, Beeren I, Joosten B, Fransen JA, Figdor CG, (2009) The C-type lectin DC-SIGN internalizes soluble antigens and HIV-1 virions via a clathrin-dependent mechanism. Eur J Immunol 39: 1923-1928.
    • (2009) Eur J Immunol , vol.39 , pp. 1923-1928
    • Cambi, A.1    Beeren, I.2    Joosten, B.3    Fransen, J.A.4    Figdor, C.G.5
  • 44
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek TB, Kwon DS, Torensma R, van Vliet SJ, van Duijnhoven GC, et al. (2000) DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 100: 587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3    van Vliet, S.J.4    van Duijnhoven, G.C.5
  • 45
    • 0038407687 scopus 로고    scopus 로고
    • DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission
    • Geijtenbeek TB, van Kooyk Y, (2003) DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission. Curr Top Microbiol Immunol 276: 31-54.
    • (2003) Curr Top Microbiol Immunol , vol.276 , pp. 31-54
    • Geijtenbeek, T.B.1    van Kooyk, Y.2
  • 46
    • 18744366087 scopus 로고    scopus 로고
    • Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection
    • Halary F, Amara A, Lortat-Jacob H, Messerle M, Delaunay T, et al. (2002) Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection. Immunity 17: 653-664.
    • (2002) Immunity , vol.17 , pp. 653-664
    • Halary, F.1    Amara, A.2    Lortat-Jacob, H.3    Messerle, M.4    Delaunay, T.5
  • 47
    • 0029951162 scopus 로고    scopus 로고
    • Ceramide-binding and activation defines protein kinase c-Raf as a ceramide-activated protein kinase
    • Huwiler A, Brunner J, Hummel R, Vervoordeldonk M, Stabel S, et al. (1996) Ceramide-binding and activation defines protein kinase c-Raf as a ceramide-activated protein kinase. Proc Natl Acad Sci U S A 93: 6959-6963.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6959-6963
    • Huwiler, A.1    Brunner, J.2    Hummel, R.3    Vervoordeldonk, M.4    Stabel, S.5
  • 48
    • 0028838235 scopus 로고
    • Phosphorylation of Raf by ceramide-activated protein kinase
    • Yao B, Zhang Y, Delikat S, Mathias S, Basu S, et al. (1995) Phosphorylation of Raf by ceramide-activated protein kinase. Nature 378: 307-310.
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3    Mathias, S.4    Basu, S.5
  • 49
    • 77954232042 scopus 로고    scopus 로고
    • Studies on the role of acid sphingomyelinase and ceramide in the regulation of TACE activity and TNFα secretion in macrophages
    • Rozenova KA, Deevska GM, Karakashian AA, Nikolova-Karakashian MN, (2010) Studies on the role of acid sphingomyelinase and ceramide in the regulation of TACE activity and TNFα secretion in macrophages. J Biol Chem 285: 21103-13.
    • (2010) J Biol Chem , vol.285 , pp. 21103-21113
    • Rozenova, K.A.1    Deevska, G.M.2    Karakashian, A.A.3    Nikolova-Karakashian, M.N.4
  • 50
    • 73449145722 scopus 로고    scopus 로고
    • Induction of membrane ceramides: a novel strategy to interfere with T lymphocyte cytoskeletal reorganisation in viral immunosuppression
    • Gassert E, Avota E, Harms H, Krohne G, Gulbins E, et al. (2009) Induction of membrane ceramides: a novel strategy to interfere with T lymphocyte cytoskeletal reorganisation in viral immunosuppression. PLoS Pathog 5: e1000623.
    • (2009) PLoS Pathog , vol.5
    • Gassert, E.1    Avota, E.2    Harms, H.3    Krohne, G.4    Gulbins, E.5
  • 51
    • 0027461121 scopus 로고
    • Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta
    • Mathias S, Younes A, Kan CC, Orlow I, Joseph C, et al. (1993) Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta. Science 259: 519-522.
    • (1993) Science , vol.259 , pp. 519-522
    • Mathias, S.1    Younes, A.2    Kan, C.C.3    Orlow, I.4    Joseph, C.5
  • 52
    • 0030595340 scopus 로고    scopus 로고
    • FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase
    • Adam-Klages S, Adam D, Wiegmann K, Struve S, Kolanus W, et al. (1996) FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase. Cell 86: 937-947.
    • (1996) Cell , vol.86 , pp. 937-947
    • Adam-Klages, S.1    Adam, D.2    Wiegmann, K.3    Struve, S.4    Kolanus, W.5
  • 53
    • 60249100672 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of measles virus hemagglutinin
    • Hashiguchi T, Maenaka K, Yanagi Y, (2008) X-ray crystallographic analysis of measles virus hemagglutinin. Uirusu 58: 1-10.
    • (2008) Uirusu , vol.58 , pp. 1-10
    • Hashiguchi, T.1    Maenaka, K.2    Yanagi, Y.3
  • 54
    • 0036340341 scopus 로고    scopus 로고
    • Hemagglutinin protein of wild-type measles virus activates toll-like receptor 2 signaling
    • Bieback K, Lien E, Klagge IM, Avota E, Schneider-Schaulies J, et al. (2002) Hemagglutinin protein of wild-type measles virus activates toll-like receptor 2 signaling. J Virol 76: 8729-8736.
    • (2002) J Virol , vol.76 , pp. 8729-8736
    • Bieback, K.1    Lien, E.2    Klagge, I.M.3    Avota, E.4    Schneider-Schaulies, J.5
  • 55
    • 0035201375 scopus 로고    scopus 로고
    • Induction of the measles virus receptor SLAM (CD150) on monocytes
    • Minagawa H, Tanaka K, Ono N, Tatsuo H, Yanagi Y, (2001) Induction of the measles virus receptor SLAM (CD150) on monocytes. J Gen Virol 82: 2913-2917.
    • (2001) J Gen Virol , vol.82 , pp. 2913-2917
    • Minagawa, H.1    Tanaka, K.2    Ono, N.3    Tatsuo, H.4    Yanagi, Y.5
  • 56
    • 4644327020 scopus 로고    scopus 로고
    • Activation of acid sphingomyelinase and its inhibition by the nitric oxide/cyclic guanosine 3′,5′-monophosphate pathway: key events in Escherichia coli-elicited apoptosis of dendritic cells
    • Falcone S, Perrotta C, De Palma C, Pisconti A, Sciorati C, et al. (2004) Activation of acid sphingomyelinase and its inhibition by the nitric oxide/cyclic guanosine 3′,5′-monophosphate pathway: key events in Escherichia coli-elicited apoptosis of dendritic cells. J Immunol 173: 4452-4463.
    • (2004) J Immunol , vol.173 , pp. 4452-4463
    • Falcone, S.1    Perrotta, C.2    De Palma, C.3    Pisconti, A.4    Sciorati, C.5
  • 57
    • 0030442754 scopus 로고    scopus 로고
    • Ceramide inhibits antigen uptake and presentation by dendritic cells
    • Sallusto F, Nicolo C, De Maria R, Corinti S, Testi R, (1996) Ceramide inhibits antigen uptake and presentation by dendritic cells. J Exp Med 184: 2411-2416.
    • (1996) J Exp Med , vol.184 , pp. 2411-2416
    • Sallusto, F.1    Nicolo, C.2    De Maria, R.3    Corinti, S.4    Testi, R.5
  • 58
    • 30144434972 scopus 로고    scopus 로고
    • Ceramide catabolism critically controls survival of human dendritic cells
    • Franchi L, Malisan F, Tomassini B, Testi R, (2006) Ceramide catabolism critically controls survival of human dendritic cells. J Leukoc Biol 79: 166-172.
    • (2006) J Leukoc Biol , vol.79 , pp. 166-172
    • Franchi, L.1    Malisan, F.2    Tomassini, B.3    Testi, R.4
  • 59
    • 0033555928 scopus 로고    scopus 로고
    • Role of ceramide in lipopolysaccharide (LPS)-induced signaling. LPS increases ceramide rather than acting as a structural homolog
    • MacKichan ML, DeFranco AL, (1999) Role of ceramide in lipopolysaccharide (LPS)-induced signaling. LPS increases ceramide rather than acting as a structural homolog. J Biol Chem 274: 1767-1775.
    • (1999) J Biol Chem , vol.274 , pp. 1767-1775
    • MacKichan, M.L.1    DeFranco, A.L.2
  • 60
    • 22544470314 scopus 로고    scopus 로고
    • Caspase-dependent and -independent activation of acid sphingomyelinase signaling
    • Rotolo JA, Zhang J, Donepudi M, Lee H, Fuks Z, et al. (2005) Caspase-dependent and-independent activation of acid sphingomyelinase signaling. J Biol Chem 280: 26425-26434.
    • (2005) J Biol Chem , vol.280 , pp. 26425-26434
    • Rotolo, J.A.1    Zhang, J.2    Donepudi, M.3    Lee, H.4    Fuks, Z.5
  • 61
    • 0034899667 scopus 로고    scopus 로고
    • The haemagglutinin protein is an important determinant of measles virus tropism for dendritic cells in vitro
    • Ohgimoto S, Ohgimoto K, Niewiesk S, Klagge IM, Pfeuffer J, et al. (2001) The haemagglutinin protein is an important determinant of measles virus tropism for dendritic cells in vitro. J Gen Virol 82: 1835-1844.
    • (2001) J Gen Virol , vol.82 , pp. 1835-1844
    • Ohgimoto, S.1    Ohgimoto, K.2    Niewiesk, S.3    Klagge, I.M.4    Pfeuffer, J.5
  • 62
    • 31444448619 scopus 로고    scopus 로고
    • Fenretinide inhibits HIV infection by promoting viral endocytosis
    • Finnegan CM, Blumenthal R, (2006) Fenretinide inhibits HIV infection by promoting viral endocytosis. Antiviral Res 69: 116-123.
    • (2006) Antiviral Res , vol.69 , pp. 116-123
    • Finnegan, C.M.1    Blumenthal, R.2
  • 63
    • 34248343803 scopus 로고    scopus 로고
    • Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion
    • Finnegan CM, Rawat SS, Cho EH, Guiffre DL, Lockett S, et al. (2007) Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion. J Virol 81: 5294-5304.
    • (2007) J Virol , vol.81 , pp. 5294-5304
    • Finnegan, C.M.1    Rawat, S.S.2    Cho, E.H.3    Guiffre, D.L.4    Lockett, S.5
  • 64
    • 44649176921 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein-mediated fusion and pathogenesis: implications for therapy and vaccine development
    • Jacobs A, Garg H, Viard M, Raviv Y, Puri A, et al. (2008) HIV-1 envelope glycoprotein-mediated fusion and pathogenesis: implications for therapy and vaccine development. Vaccine 26: 3026-3035.
    • (2008) Vaccine , vol.26 , pp. 3026-3035
    • Jacobs, A.1    Garg, H.2    Viard, M.3    Raviv, Y.4    Puri, A.5
  • 65
    • 77956958415 scopus 로고    scopus 로고
    • SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages
    • Berger SB, Romero X, Ma C, Wang G, Faubion WA, et al. (2010) SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages. Nat Immunol 11: 920-927.
    • (2010) Nat Immunol , vol.11 , pp. 920-927
    • Berger, S.B.1    Romero, X.2    Ma, C.3    Wang, G.4    Faubion, W.A.5
  • 67
    • 34548351249 scopus 로고    scopus 로고
    • Fc gamma RII activation induces cell surface ceramide production which participates in the assembly of the receptor signaling complex
    • Korzeniowski M, Shakor AB, Makowska A, Drzewiecka A, Bielawska A, et al. (2007) Fc gamma RII activation induces cell surface ceramide production which participates in the assembly of the receptor signaling complex. Cell Physiol Biochem 20: 347-356.
    • (2007) Cell Physiol Biochem , vol.20 , pp. 347-356
    • Korzeniowski, M.1    Shakor, A.B.2    Makowska, A.3    Drzewiecka, A.4    Bielawska, A.5
  • 68
    • 34147205740 scopus 로고    scopus 로고
    • Role for furin in tumor necrosis factor alpha-induced activation of the matrix metalloproteinase/sphingolipid mitogenic pathway
    • Tellier E, Negre-Salvayre A, Bocquet B, Itohara S, Hannun YA, et al. (2007) Role for furin in tumor necrosis factor alpha-induced activation of the matrix metalloproteinase/sphingolipid mitogenic pathway. Mol Cell Biol 27: 2997-3007.
    • (2007) Mol Cell Biol , vol.27 , pp. 2997-3007
    • Tellier, E.1    Negre-Salvayre, A.2    Bocquet, B.3    Itohara, S.4    Hannun, Y.A.5


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