메뉴 건너뛰기




Volumn 15, Issue 8, 2016, Pages 1728-1742

An Evolutionarily Conserved PLC-PKD-TFEB Pathway for Host Defense

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS ELEGANS PROTEIN; PHOSPHOLIPASE C; PROTEIN DKF 1; PROTEIN EGL 30; PROTEIN GALPHAQ; PROTEIN KINASE C ALPHA; PROTEIN KINASE D; PROTEIN PLC 1; PROTEIN TFEB; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; PROTEIN KINASE C;

EID: 84966600317     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2016.04.052     Document Type: Article
Times cited : (47)

References (73)
  • 2
    • 0030480576 scopus 로고    scopus 로고
    • The antiviral, antitumoural xanthate D609 is a competitive inhibitor of phosphatidylcholine-specific phospholipase C
    • Amtmann E. The antiviral, antitumoural xanthate D609 is a competitive inhibitor of phosphatidylcholine-specific phospholipase C. Drugs Exp. Clin. Res. 1996, 22:287-294.
    • (1996) Drugs Exp. Clin. Res. , vol.22 , pp. 287-294
    • Amtmann, E.1
  • 6
    • 0034746792 scopus 로고    scopus 로고
    • Protein kinase Cepsilon is required for macrophage activation and defense against bacterial infection
    • Castrillo A., Pennington D.J., Otto F., Parker P.J., Owen M.J., Boscá L. Protein kinase Cepsilon is required for macrophage activation and defense against bacterial infection. J. Exp. Med. 2001, 194:1231-1242.
    • (2001) J. Exp. Med. , vol.194 , pp. 1231-1242
    • Castrillo, A.1    Pennington, D.J.2    Otto, F.3    Parker, P.J.4    Owen, M.J.5    Boscá, L.6
  • 8
    • 84859573948 scopus 로고    scopus 로고
    • PKD is a kinase of Vps34 that mediates ROS-induced autophagy downstream of DAPk
    • Eisenberg-Lerner A., Kimchi A. PKD is a kinase of Vps34 that mediates ROS-induced autophagy downstream of DAPk. Cell Death Differ. 2012, 19:788-797.
    • (2012) Cell Death Differ. , vol.19 , pp. 788-797
    • Eisenberg-Lerner, A.1    Kimchi, A.2
  • 9
    • 33745868293 scopus 로고    scopus 로고
    • Characterization of a novel protein kinase D: Caenorhabditis elegans DKF-1 is activated by translocation-phosphorylation and regulates movement and growth in vivo
    • Feng H., Ren M., Wu S.-L., Hall D.H., Rubin C.S. Characterization of a novel protein kinase D: Caenorhabditis elegans DKF-1 is activated by translocation-phosphorylation and regulates movement and growth in vivo. J. Biol. Chem. 2006, 281:17801-17814.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17801-17814
    • Feng, H.1    Ren, M.2    Wu, S.-L.3    Hall, D.H.4    Rubin, C.S.5
  • 10
    • 35748950144 scopus 로고    scopus 로고
    • Properties, regulation, and in vivo functions of a novel protein kinase D: Caenorhabditis elegans DKF-2 links diacylglycerol second messenger to the regulation of stress responses and life span
    • Feng H., Ren M., Chen L., Rubin C.S. Properties, regulation, and in vivo functions of a novel protein kinase D: Caenorhabditis elegans DKF-2 links diacylglycerol second messenger to the regulation of stress responses and life span. J. Biol. Chem. 2007, 282:31273-31288.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31273-31288
    • Feng, H.1    Ren, M.2    Chen, L.3    Rubin, C.S.4
  • 12
    • 79961026124 scopus 로고    scopus 로고
    • Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology
    • Fu Y., Rubin C.S. Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology. EMBO Rep. 2011, 12:785-796.
    • (2011) EMBO Rep. , vol.12 , pp. 785-796
    • Fu, Y.1    Rubin, C.S.2
  • 13
    • 84862862332 scopus 로고    scopus 로고
    • Epithelial antimicrobial defence of the skin and intestine
    • Gallo R.L., Hooper L.V. Epithelial antimicrobial defence of the skin and intestine. Nat. Rev. Immunol. 2012, 12:503-516.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 503-516
    • Gallo, R.L.1    Hooper, L.V.2
  • 14
    • 0030603158 scopus 로고    scopus 로고
    • Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase c isoenzymes
    • Gschwendt M., Dieterich S., Rennecke J., Kittstein W., Mueller H.J., Johannes F.J. Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase c isoenzymes. FEBS Lett. 1996, 392:77-80.
    • (1996) FEBS Lett. , vol.392 , pp. 77-80
    • Gschwendt, M.1    Dieterich, S.2    Rennecke, J.3    Kittstein, W.4    Mueller, H.J.5    Johannes, F.J.6
  • 15
    • 81355136036 scopus 로고    scopus 로고
    • Automated analysis of time-lapse imaging of nuclear translocation by retrospective strategy and its application to STAT1 in HeLa cells
    • Han F., Liang P., Wang F., Zeng L., Zhang B. Automated analysis of time-lapse imaging of nuclear translocation by retrospective strategy and its application to STAT1 in HeLa cells. PLoS ONE 2011, 6:e27454.
    • (2011) PLoS ONE , vol.6 , pp. e27454
    • Han, F.1    Liang, P.2    Wang, F.3    Zeng, L.4    Zhang, B.5
  • 17
    • 84855263820 scopus 로고    scopus 로고
    • Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1 activity via p38 MAPK signaling during infection in C. elegans
    • Hoeven Rv., McCallum K.C., Cruz M.R., Garsin D.A. Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1 activity via p38 MAPK signaling during infection in C. elegans. PLoS Pathog. 2011, 7:e1002453.
    • (2011) PLoS Pathog. , vol.7 , pp. e1002453
    • Hoeven, R.1    McCallum, K.C.2    Cruz, M.R.3    Garsin, D.A.4
  • 18
    • 24044537290 scopus 로고    scopus 로고
    • Renal carcinoma-associated transcription factors TFE3 and TFEB are leukemia inhibitory factor-responsive transcription activators of E-cadherin
    • Huan C., Sashital D., Hailemariam T., Kelly M.L., Roman C.A.J. Renal carcinoma-associated transcription factors TFE3 and TFEB are leukemia inhibitory factor-responsive transcription activators of E-cadherin. J. Biol. Chem. 2005, 280:30225-30235.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30225-30235
    • Huan, C.1    Sashital, D.2    Hailemariam, T.3    Kelly, M.L.4    Roman, C.A.J.5
  • 19
    • 56249116997 scopus 로고    scopus 로고
    • Role for beta-catenin and HOX transcription factors in Caenorhabditis elegans and mammalian host epithelial-pathogen interactions
    • Irazoqui J.E., Ng A., Xavier R.J., Ausubel F.M. Role for beta-catenin and HOX transcription factors in Caenorhabditis elegans and mammalian host epithelial-pathogen interactions. Proc. Natl. Acad. Sci. USA 2008, 105:17469-17474.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17469-17474
    • Irazoqui, J.E.1    Ng, A.2    Xavier, R.J.3    Ausubel, F.M.4
  • 20
    • 8944246315 scopus 로고    scopus 로고
    • (S)-13-[(dimethylamino)methyl]-10,11,14,15-tetrahydro-4,9:16, 21-dimetheno-1H, 13H-dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecene-1,3(2H)-d ione (LY333531) and related analogues: isozyme selective inhibitors of protein kinase C β
    • Jirousek M.R., Gillig J.R., Gonzalez C.M., Heath W.F., McDonald J.H., Neel D.A., Rito C.J., Singh U., Stramm L.E., Melikian-Badalian A., et al. (S)-13-[(dimethylamino)methyl]-10,11,14,15-tetrahydro-4,9:16, 21-dimetheno-1H, 13H-dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecene-1,3(2H)-d ione (LY333531) and related analogues: isozyme selective inhibitors of protein kinase C β. J. Med. Chem. 1996, 39:2664-2671.
    • (1996) J. Med. Chem. , vol.39 , pp. 2664-2671
    • Jirousek, M.R.1    Gillig, J.R.2    Gonzalez, C.M.3    Heath, W.F.4    McDonald, J.H.5    Neel, D.A.6    Rito, C.J.7    Singh, U.8    Stramm, L.E.9    Melikian-Badalian, A.10
  • 21
    • 0029745535 scopus 로고    scopus 로고
    • A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function
    • Johnson J.A., Gray M.O., Chen C.H., Mochly-Rosen D. A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function. J. Biol. Chem. 1996, 271:24962-24966.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24962-24966
    • Johnson, J.A.1    Gray, M.O.2    Chen, C.H.3    Mochly-Rosen, D.4
  • 25
    • 77956384716 scopus 로고    scopus 로고
    • Systemic and cell intrinsic roles of Gqalpha signaling in the regulation of innate immunity, oxidative stress, and longevity in Caenorhabditis elegans
    • Kawli T., Wu C., Tan M.-W.W. Systemic and cell intrinsic roles of Gqalpha signaling in the regulation of innate immunity, oxidative stress, and longevity in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 2010, 107:13788-13793.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13788-13793
    • Kawli, T.1    Wu, C.2    Tan, M.-W.W.3
  • 26
    • 77951895550 scopus 로고    scopus 로고
    • Protein kinase D1 is essential for the proinflammatory response induced by hypersensitivity pneumonitis-causing thermophilic actinomycetes Saccharopolyspora rectivirgula
    • Kim Y.-I., Park J.-E., Brand D.D., Fitzpatrick E.A., Yi A.-K. Protein kinase D1 is essential for the proinflammatory response induced by hypersensitivity pneumonitis-causing thermophilic actinomycetes Saccharopolyspora rectivirgula. J. Immunol. 2010, 184:3145-3156.
    • (2010) J. Immunol. , vol.184 , pp. 3145-3156
    • Kim, Y.-I.1    Park, J.-E.2    Brand, D.D.3    Fitzpatrick, E.A.4    Yi, A.-K.5
  • 27
    • 84878500403 scopus 로고    scopus 로고
    • Filamin and phospholipase C-ε are required for calcium signaling in the Caenorhabditis elegans spermatheca
    • Kovacevic I., Orozco J.M., Cram E.J. Filamin and phospholipase C-ε are required for calcium signaling in the Caenorhabditis elegans spermatheca. PLoS Genet. 2013, 9:e1003510.
    • (2013) PLoS Genet. , vol.9 , pp. e1003510
    • Kovacevic, I.1    Orozco, J.M.2    Cram, E.J.3
  • 28
    • 84881357155 scopus 로고    scopus 로고
    • Concentration memory-dependent synaptic plasticity of a taste circuit regulates salt concentration chemotaxis in Caenorhabditis elegans
    • Kunitomo H., Sato H., Iwata R., Satoh Y., Ohno H., Yamada K., Iino Y. Concentration memory-dependent synaptic plasticity of a taste circuit regulates salt concentration chemotaxis in Caenorhabditis elegans. Nat. Commun. 2013, 4:2210.
    • (2013) Nat. Commun. , vol.4 , pp. 2210
    • Kunitomo, H.1    Sato, H.2    Iwata, R.3    Satoh, Y.4    Ohno, H.5    Yamada, K.6    Iino, Y.7
  • 29
    • 84921491493 scopus 로고    scopus 로고
    • Protein kinase d inhibitors uncouple phosphorylation from activity by promoting agonist-dependent activation loop phosphorylation
    • Kunkel M.T., Newton A.C. Protein kinase d inhibitors uncouple phosphorylation from activity by promoting agonist-dependent activation loop phosphorylation. Chem. Biol. 2015, 22:98-106.
    • (2015) Chem. Biol. , vol.22 , pp. 98-106
    • Kunkel, M.T.1    Newton, A.C.2
  • 31
    • 0034283687 scopus 로고    scopus 로고
    • Differential requirement for classic and novel PKC isoforms in respiratory burst and phagocytosis in RAW 264.7 cells
    • Larsen E.C., DiGennaro J.A., Saito N., Mehta S., Loegering D.J., Mazurkiewicz J.E., Lennartz M.R. Differential requirement for classic and novel PKC isoforms in respiratory burst and phagocytosis in RAW 264.7 cells. J. Immunol. 2000, 165:2809-2817.
    • (2000) J. Immunol. , vol.165 , pp. 2809-2817
    • Larsen, E.C.1    DiGennaro, J.A.2    Saito, N.3    Mehta, S.4    Loegering, D.J.5    Mazurkiewicz, J.E.6    Lennartz, M.R.7
  • 33
    • 61849108279 scopus 로고    scopus 로고
    • Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: Impact of alternative halogenated privileged structures for PLD1 specificity
    • Lewis J.A., Scott S.A., Lavieri R., Buck J.R., Selvy P.E., Stoops S.L., Armstrong M.D., Brown H.A., Lindsley C.W. Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: Impact of alternative halogenated privileged structures for PLD1 specificity. Bioorg. Med. Chem. Lett. 2009, 19:1916-1920.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1916-1920
    • Lewis, J.A.1    Scott, S.A.2    Lavieri, R.3    Buck, J.R.4    Selvy, P.E.5    Stoops, S.L.6    Armstrong, M.D.7    Brown, H.A.8    Lindsley, C.W.9
  • 34
    • 0031792203 scopus 로고    scopus 로고
    • Distinct PKC isoforms mediate the activation of cPLA2 and adenylyl cyclase by phorbol ester in RAW264.7 macrophages
    • Lin W.W., Chen B.C. Distinct PKC isoforms mediate the activation of cPLA2 and adenylyl cyclase by phorbol ester in RAW264.7 macrophages. Br. J. Pharmacol. 1998, 125:1601-1609.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 1601-1609
    • Lin, W.W.1    Chen, B.C.2
  • 35
    • 38549135536 scopus 로고    scopus 로고
    • Genomic overview of protein kinases
    • Manning G. Genomic overview of protein kinases. WormBook 2005, 1-19.
    • (2005) WormBook , pp. 1-19
    • Manning, G.1
  • 36
    • 84864874958 scopus 로고    scopus 로고
    • MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
    • Martina J.A., Chen Y., Gucek M., Puertollano R. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 2012, 8:903-914.
    • (2012) Autophagy , vol.8 , pp. 903-914
    • Martina, J.A.1    Chen, Y.2    Gucek, M.3    Puertollano, R.4
  • 38
    • 84860903825 scopus 로고    scopus 로고
    • Behavioral and immune responses to infection require Gαq- RhoA signaling in C. elegans
    • McMullan R., Anderson A., Nurrish S. Behavioral and immune responses to infection require Gαq- RhoA signaling in C. elegans. PLoS Pathog. 2012, 8:e1002530.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002530
    • McMullan, R.1    Anderson, A.2    Nurrish, S.3
  • 40
    • 70349443224 scopus 로고    scopus 로고
    • Transcriptional control of the inflammatory response
    • Medzhitov R., Horng T. Transcriptional control of the inflammatory response. Nat. Rev. Immunol. 2009, 9:692-703.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 692-703
    • Medzhitov, R.1    Horng, T.2
  • 42
    • 84926631409 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of cytotoxic T cells to reveal protein kinase d 2 regulated networks
    • Navarro M.N., Goebel J., Hukelmann J.L., Cantrell D.A. Quantitative phosphoproteomics of cytotoxic T cells to reveal protein kinase d 2 regulated networks. Mol. Cell. Proteomics 2014, 13:3544-3557.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3544-3557
    • Navarro, M.N.1    Goebel, J.2    Hukelmann, J.L.3    Cantrell, D.A.4
  • 43
    • 84878533962 scopus 로고    scopus 로고
    • MXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to nutrient availability
    • O'Rourke E.J., Ruvkun G. MXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to nutrient availability. Nat. Cell Biol. 2013, 15:668-676.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 668-676
    • O'Rourke, E.J.1    Ruvkun, G.2
  • 44
    • 80052716148 scopus 로고    scopus 로고
    • Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways
    • Palmieri M., Impey S., Kang H., di Ronza A., Pelz C., Sardiello M., Ballabio A. Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways. Hum. Mol. Genet. 2011, 20:3852-3866.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 3852-3866
    • Palmieri, M.1    Impey, S.2    Kang, H.3    di Ronza, A.4    Pelz, C.5    Sardiello, M.6    Ballabio, A.7
  • 45
    • 49649096410 scopus 로고    scopus 로고
    • Protein kinase D1: a new component in TLR9 signaling
    • Park J.-E., Kim Y.-I., Yi A.-K. Protein kinase D1: a new component in TLR9 signaling. J. Immunol. 2008, 181:2044-2055.
    • (2008) J. Immunol. , vol.181 , pp. 2044-2055
    • Park, J.-E.1    Kim, Y.-I.2    Yi, A.-K.3
  • 46
    • 77950274021 scopus 로고    scopus 로고
    • Protein kinase D1 is essential for MyD88-dependent TLR signaling pathway
    • Park J.-E., Kim Y.-I., Yi A.-K. Protein kinase D1 is essential for MyD88-dependent TLR signaling pathway. J. Immunol. 2009, 182:6316-6327.
    • (2009) J. Immunol. , vol.182 , pp. 6316-6327
    • Park, J.-E.1    Kim, Y.-I.2    Yi, A.-K.3
  • 48
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 2001, 29:e45.
    • (2001) Nucleic Acids Res. , vol.29 , pp. e45
    • Pfaffl, M.W.1
  • 49
    • 45549095755 scopus 로고    scopus 로고
    • Models of Caenorhabditis elegans infection by bacterial and fungal pathogens
    • Powell J.R., Ausubel F.M. Models of Caenorhabditis elegans infection by bacterial and fungal pathogens. Methods Mol. Biol. 2008, 415:403-427.
    • (2008) Methods Mol. Biol. , vol.415 , pp. 403-427
    • Powell, J.R.1    Ausubel, F.M.2
  • 50
    • 64049100454 scopus 로고    scopus 로고
    • Protein kinase D is an essential regulator of C. elegans innate immunity
    • Ren M., Feng H., Fu Y., Land M., Rubin C.S. Protein kinase D is an essential regulator of C. elegans innate immunity. Immunity 2009, 30:521-532.
    • (2009) Immunity , vol.30 , pp. 521-532
    • Ren, M.1    Feng, H.2    Fu, Y.3    Land, M.4    Rubin, C.S.5
  • 52
    • 79955061032 scopus 로고    scopus 로고
    • Protein kinase D signaling: multiple biological functions in health and disease
    • Rozengurt E. Protein kinase D signaling: multiple biological functions in health and disease. Physiology (Bethesda) 2011, 26:23-33.
    • (2011) Physiology (Bethesda) , vol.26 , pp. 23-33
    • Rozengurt, E.1
  • 53
    • 84931578186 scopus 로고    scopus 로고
    • The transcription factor TFEB acts as a molecular switch that regulates exogenous antigen-presentation pathways
    • advance online publication
    • Samie M., Cresswell P. The transcription factor TFEB acts as a molecular switch that regulates exogenous antigen-presentation pathways. Nat. Immunol. 2015, 16:729-736. advance online publication.
    • (2015) Nat. Immunol. , vol.16 , pp. 729-736
    • Samie, M.1    Cresswell, P.2
  • 58
    • 79951676291 scopus 로고    scopus 로고
    • Systems biology approaches to dissect mammalian innate immunity
    • Shapira S.D., Hacohen N. Systems biology approaches to dissect mammalian innate immunity. Curr. Opin. Immunol. 2011, 23:71-77.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 71-77
    • Shapira, S.D.1    Hacohen, N.2
  • 59
    • 80054767649 scopus 로고    scopus 로고
    • ATP competitive protein kinase C inhibitors demonstrate distinct state-dependent inhibition
    • Smith I.M., Hoshi N. ATP competitive protein kinase C inhibitors demonstrate distinct state-dependent inhibition. PLoS ONE 2011, 6:e26338.
    • (2011) PLoS ONE , vol.6 , pp. e26338
    • Smith, I.M.1    Hoshi, N.2
  • 60
    • 62149152761 scopus 로고    scopus 로고
    • 5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis
    • Su W., Yeku O., Olepu S., Genna A., Park J.-S., Ren H., Du G., Gelb M.H., Morris A.J., Frohman M.A. 5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis. Mol. Pharmacol. 2009, 75:437-446.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 437-446
    • Su, W.1    Yeku, O.2    Olepu, S.3    Genna, A.4    Park, J.-S.5    Ren, H.6    Du, G.7    Gelb, M.H.8    Morris, A.J.9    Frohman, M.A.10
  • 61
    • 0025860413 scopus 로고
    • Activation of the β 1 isozyme of phospholipase C by α subunits of the Gq class of G proteins
    • Taylor S.J., Chae H.Z., Rhee S.G., Exton J.H. Activation of the β 1 isozyme of phospholipase C by α subunits of the Gq class of G proteins. Nature 1991, 350:516-518.
    • (1991) Nature , vol.350 , pp. 516-518
    • Taylor, S.J.1    Chae, H.Z.2    Rhee, S.G.3    Exton, J.H.4
  • 62
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • Timmons L., Court D.L., Fire A. Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 2001, 263:103-112.
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3
  • 64
    • 84908336199 scopus 로고    scopus 로고
    • Speculations on the activation of ROS generation in C. elegans innate immune signaling
    • van der Hoeven R., McCallum K.C., Garsin D.A. Speculations on the activation of ROS generation in C. elegans innate immune signaling. Worm 2012, 1:160-163.
    • (2012) Worm , vol.1 , pp. 160-163
    • van der Hoeven, R.1    McCallum, K.C.2    Garsin, D.A.3
  • 65
    • 77951637036 scopus 로고    scopus 로고
    • Imaging type-III secretion reveals dynamics and spatial segregation of Salmonella effectors
    • Van Engelenburg S.B., Palmer A.E. Imaging type-III secretion reveals dynamics and spatial segregation of Salmonella effectors. Nat. Methods 2010, 7:325-330.
    • (2010) Nat. Methods , vol.7 , pp. 325-330
    • Van Engelenburg, S.B.1    Palmer, A.E.2
  • 68
    • 24144434439 scopus 로고    scopus 로고
    • PKC α depletion in RAW264.7 macrophages following microbial/IFNgamma stimulation is PC-PLC-mediated
    • von Knethen A., Brüne B. PKC α depletion in RAW264.7 macrophages following microbial/IFNgamma stimulation is PC-PLC-mediated. Antioxid. Redox Signal. 2005, 7:1217-1222.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1217-1222
    • von Knethen, A.1    Brüne, B.2
  • 69
    • 25844484590 scopus 로고    scopus 로고
    • Protein kinase C-dependent protein kinase D activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor
    • Wong C., Jin Z.-G. Protein kinase C-dependent protein kinase D activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor. J. Biol. Chem. 2005, 280:33262-33269.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33262-33269
    • Wong, C.1    Jin, Z.-G.2
  • 70
    • 84877734323 scopus 로고    scopus 로고
    • Protein kinase C pharmacology: refining the toolbox
    • Wu-Zhang A.X., Newton A.C. Protein kinase C pharmacology: refining the toolbox. Biochem. J. 2013, 452:195-209.
    • (2013) Biochem. J. , vol.452 , pp. 195-209
    • Wu-Zhang, A.X.1    Newton, A.C.2
  • 71
    • 64649085452 scopus 로고    scopus 로고
    • Antifungal innate immunity in C. elegans: PKCdelta links G protein signaling and a conserved p38 MAPK cascade
    • Ziegler K., Kurz C.L., Cypowyj S., Couillault C., Pophillat M., Pujol N., Ewbank J.J. Antifungal innate immunity in C. elegans: PKCdelta links G protein signaling and a conserved p38 MAPK cascade. Cell Host Microbe 2009, 5:341-352.
    • (2009) Cell Host Microbe , vol.5 , pp. 341-352
    • Ziegler, K.1    Kurz, C.L.2    Cypowyj, S.3    Couillault, C.4    Pophillat, M.5    Pujol, N.6    Ewbank, J.J.7
  • 72
    • 84887276664 scopus 로고    scopus 로고
    • The DAF-16/FOXO transcription factor functions as a regulator of epidermal innate immunity
    • Zou C.-G., Tu Q., Niu J., Ji X.-L., Zhang K.-Q. The DAF-16/FOXO transcription factor functions as a regulator of epidermal innate immunity. PLoS Pathog. 2013, 9:e1003660.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003660
    • Zou, C.-G.1    Tu, Q.2    Niu, J.3    Ji, X.-L.4    Zhang, K.-Q.5
  • 73
    • 84906222430 scopus 로고    scopus 로고
    • Activation of a G protein-coupled receptor by its endogenous ligand triggers the innate immune response of Caenorhabditis elegans
    • Zugasti O., Bose N., Squiban B., Belougne J., Kurz C.L., Schroeder F.C., Pujol N., Ewbank J.J. Activation of a G protein-coupled receptor by its endogenous ligand triggers the innate immune response of Caenorhabditis elegans. Nat. Immunol. 2014, 15:833-838.
    • (2014) Nat. Immunol. , vol.15 , pp. 833-838
    • Zugasti, O.1    Bose, N.2    Squiban, B.3    Belougne, J.4    Kurz, C.L.5    Schroeder, F.C.6    Pujol, N.7    Ewbank, J.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.