메뉴 건너뛰기




Volumn 8, Issue 7, 2012, Pages 32-

Membrane damage during Listeria monocytogenes infection triggers a caspase-7 dependent cytoprotective response

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 7; LISTERIOLYSIN O; MYELOID DIFFERENTIATION FACTOR 88; BACTERIAL TOXIN; CYTOSKELETON PROTEIN; HEAT SHOCK PROTEIN; HEMOLYSIN; HLYA PROTEIN, LISTERIA MONOCYTOGENES; INTERLEUKIN 1BETA CONVERTING ENZYME; MYD88 PROTEIN, MOUSE; PYCARD PROTEIN, MOUSE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK2 PROTEIN, MOUSE; VIRULENCE FACTOR;

EID: 84864629840     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002628     Document Type: Article
Times cited : (35)

References (60)
  • 2
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy DA, Jacks PS, Hinrichs DJ, (1988) Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med 167: 1459-1471.
    • (1988) J Exp Med , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 3
    • 0030846035 scopus 로고    scopus 로고
    • The mechanism of cell death in Listeria monocytogenes-infected murine macrophages is distinct from apoptosis
    • Barsig J, Kaufmann SH, (1997) The mechanism of cell death in Listeria monocytogenes-infected murine macrophages is distinct from apoptosis. Infect Immun 65: 4075-4081.
    • (1997) Infect Immun , vol.65 , pp. 4075-4081
    • Barsig, J.1    Kaufmann, S.H.2
  • 4
    • 33645553471 scopus 로고    scopus 로고
    • Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles
    • Shaughnessy LM, Hoppe AD, Christensen KA, Swanson JA, (2006) Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles. Cell Microbiol 8: 781-792.
    • (2006) Cell Microbiol , vol.8 , pp. 781-792
    • Shaughnessy, L.M.1    Hoppe, A.D.2    Christensen, K.A.3    Swanson, J.A.4
  • 5
    • 0344851711 scopus 로고    scopus 로고
    • Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses
    • Glomski IJ, Decatur AL, Portnoy DA, (2003) Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses. Infect Immun 71: 6754-6765.
    • (2003) Infect Immun , vol.71 , pp. 6754-6765
    • Glomski, I.J.1    Decatur, A.L.2    Portnoy, D.A.3
  • 6
    • 0037128936 scopus 로고    scopus 로고
    • The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells
    • Glomski IJ, Gedde MM, Tsang AW, Swanson JA, Portnoy DA, (2002) The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells. J Cell Biol 156: 1029-1038.
    • (2002) J Cell Biol , vol.156 , pp. 1029-1038
    • Glomski, I.J.1    Gedde, M.M.2    Tsang, A.W.3    Swanson, J.A.4    Portnoy, D.A.5
  • 7
    • 33644819006 scopus 로고    scopus 로고
    • Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: role of the PEST-like sequence
    • Schnupf P, Portnoy DA, Decatur AL, (2006) Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: role of the PEST-like sequence. Cell Microbiol 8: 353-364.
    • (2006) Cell Microbiol , vol.8 , pp. 353-364
    • Schnupf, P.1    Portnoy, D.A.2    Decatur, A.L.3
  • 8
    • 1842588607 scopus 로고    scopus 로고
    • Toll-like receptor 2 is required for optimal control of Listeria monocytogenes infection
    • Torres D, Barrier M, Bihl F, Quesniaux VJ, Maillet I, et al. (2004) Toll-like receptor 2 is required for optimal control of Listeria monocytogenes infection. Infect Immun 72: 2131-2139.
    • (2004) Infect Immun , vol.72 , pp. 2131-2139
    • Torres, D.1    Barrier, M.2    Bihl, F.3    Quesniaux, V.J.4    Maillet, I.5
  • 9
    • 34250888664 scopus 로고    scopus 로고
    • Nod1/RICK and TLR signaling regulate chemokine and antimicrobial innate immune responses in mesothelial cells
    • Park JH, Kim YG, Shaw M, Kanneganti TD, Fujimoto Y, et al. (2007) Nod1/RICK and TLR signaling regulate chemokine and antimicrobial innate immune responses in mesothelial cells. J Immunol 179: 514-521.
    • (2007) J Immunol , vol.179 , pp. 514-521
    • Park, J.H.1    Kim, Y.G.2    Shaw, M.3    Kanneganti, T.D.4    Fujimoto, Y.5
  • 10
    • 1342305252 scopus 로고    scopus 로고
    • Characterization of flagellin expression and its role in Listeria monocytogenes infection and immunity
    • Way SS, Thompson LJ, Lopes JE, Hajjar AM, Kollmann TR, et al. (2004) Characterization of flagellin expression and its role in Listeria monocytogenes infection and immunity. Cell Microbiol 6: 235-242.
    • (2004) Cell Microbiol , vol.6 , pp. 235-242
    • Way, S.S.1    Thompson, L.J.2    Lopes, J.E.3    Hajjar, A.M.4    Kollmann, T.R.5
  • 11
    • 0035953543 scopus 로고    scopus 로고
    • The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5
    • Hayashi F, Smith KD, Ozinsky A, Hawn TR, Yi EC, et al. (2001) The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 410: 1099-1103.
    • (2001) Nature , vol.410 , pp. 1099-1103
    • Hayashi, F.1    Smith, K.D.2    Ozinsky, A.3    Hawn, T.R.4    Yi, E.C.5
  • 12
    • 39149094587 scopus 로고    scopus 로고
    • The cytosolic sensors Nod1 and Nod2 are critical for bacterial recognition and host defense after exposure to Toll-like receptor ligands
    • Kim YG, Park JH, Shaw MH, Franchi L, Inohara N, et al. (2008) The cytosolic sensors Nod1 and Nod2 are critical for bacterial recognition and host defense after exposure to Toll-like receptor ligands. Immunity 28: 246-257.
    • (2008) Immunity , vol.28 , pp. 246-257
    • Kim, Y.G.1    Park, J.H.2    Shaw, M.H.3    Franchi, L.4    Inohara, N.5
  • 13
    • 16244362671 scopus 로고    scopus 로고
    • Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells
    • Fink SL, Cookson BT, (2005) Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect Immun 73: 1907-1916.
    • (2005) Infect Immun , vol.73 , pp. 1907-1916
    • Fink, S.L.1    Cookson, B.T.2
  • 14
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello CA, (1996) Biologic basis for interleukin-1 in disease. Blood 87: 2095-2147.
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 15
    • 0032607876 scopus 로고    scopus 로고
    • IL-18: A TH1-inducing, proinflammatory cytokine and new member of the IL-1 family
    • Dinarello CA, (1999) IL-18: A TH1-inducing, proinflammatory cytokine and new member of the IL-1 family. J Allergy Clin Immunol 103: 11-24.
    • (1999) J Allergy Clin Immunol , vol.103 , pp. 11-24
    • Dinarello, C.A.1
  • 16
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, et al. (1992) A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356: 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5
  • 17
    • 47249095738 scopus 로고    scopus 로고
    • Multiple Nod-like receptors activate caspase 1 during Listeria monocytogenes infection
    • Warren SE, Mao DP, Rodriguez AE, Miao EA, Aderem A, (2008) Multiple Nod-like receptors activate caspase 1 during Listeria monocytogenes infection. J Immunol 180: 7558-7564.
    • (2008) J Immunol , vol.180 , pp. 7558-7564
    • Warren, S.E.1    Mao, D.P.2    Rodriguez, A.E.3    Miao, E.A.4    Aderem, A.5
  • 18
    • 77957578665 scopus 로고    scopus 로고
    • Involvement of the AIM2, NLRC4, and NLRP3 inflammasomes in caspase-1 activation by Listeria monocytogenes
    • Wu J, Fernandes-Alnemri T, Alnemri ES, (2010) Involvement of the AIM2, NLRC4, and NLRP3 inflammasomes in caspase-1 activation by Listeria monocytogenes. J Clin Immunol 30: 693-702.
    • (2010) J Clin Immunol , vol.30 , pp. 693-702
    • Wu, J.1    Fernandes-Alnemri, T.2    Alnemri, E.S.3
  • 19
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam VA, Jiang Z, Waggoner SN, Sharma S, Cole LE, et al. (2010) The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol 11: 395-402.
    • (2010) Nat Immunol , vol.11 , pp. 395-402
    • Rathinam, V.A.1    Jiang, Z.2    Waggoner, S.N.3    Sharma, S.4    Cole, L.E.5
  • 20
    • 77955294800 scopus 로고    scopus 로고
    • Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol
    • Sauer JD, Witte CE, Zemansky J, Hanson B, Lauer P, et al. (2010) Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol. Cell Host Microbe 7: 412-419.
    • (2010) Cell Host Microbe , vol.7 , pp. 412-419
    • Sauer, J.D.1    Witte, C.E.2    Zemansky, J.3    Hanson, B.4    Lauer, P.5
  • 22
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L, Abrami L, Girardin S, Tschopp J, van der Goot FG, (2006) Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126: 1135-1145.
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    van der Goot, F.G.5
  • 24
    • 0141817959 scopus 로고    scopus 로고
    • Human caspase-7 activity and regulation by its N-terminal peptide
    • Denault JB, Salvesen GS, (2003) Human caspase-7 activity and regulation by its N-terminal peptide. J Biol Chem 278: 34042-34050.
    • (2003) J Biol Chem , vol.278 , pp. 34042-34050
    • Denault, J.B.1    Salvesen, G.S.2
  • 25
    • 32444434664 scopus 로고    scopus 로고
    • Caspases 3 and 7: key mediators of mitochondrial events of apoptosis
    • Lakhani SA, Masud A, Kuida K, Porter GA Jr, Booth CJ, et al. (2006) Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science 311: 847-851.
    • (2006) Science , vol.311 , pp. 847-851
    • Lakhani, S.A.1    Masud, A.2    Kuida, K.3    Porter Jr., G.A.4    Booth, C.J.5
  • 26
    • 0030044324 scopus 로고    scopus 로고
    • ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
    • Duan H, Chinnaiyan AM, Hudson PL, Wing JP, He WW, et al. (1996) ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. J Biolo Chem 271: 1621-1625.
    • (1996) J Biolo Chem , vol.271 , pp. 1621-1625
    • Duan, H.1    Chinnaiyan, A.M.2    Hudson, P.L.3    Wing, J.P.4    He, W.W.5
  • 27
    • 60149085396 scopus 로고    scopus 로고
    • The many roles of FAS receptor signaling in the immune system
    • Strasser A, Jost PJ, Nagata S, (2009) The many roles of FAS receptor signaling in the immune system. Immunity 30: 180-192.
    • (2009) Immunity , vol.30 , pp. 180-192
    • Strasser, A.1    Jost, P.J.2    Nagata, S.3
  • 28
    • 66349093381 scopus 로고    scopus 로고
    • Caspase-7 activation by the Nlrc4/Ipaf inflammasome restricts Legionella pneumophila infection
    • Akhter A, Gavrilin MA, Frantz L, Washington S, Ditty C, et al. (2009) Caspase-7 activation by the Nlrc4/Ipaf inflammasome restricts Legionella pneumophila infection. PLoS Pathog 5: e1000361.
    • (2009) PLoS Pathog , vol.5
    • Akhter, A.1    Gavrilin, M.A.2    Frantz, L.3    Washington, S.4    Ditty, C.5
  • 30
    • 75149167437 scopus 로고    scopus 로고
    • Proteome-wide Substrate Analysis Indicates Substrate Exclusion as a Mechanism to Generate Caspase-7 Versus Caspase-3 Specificity
    • Demon D, Van Damme P, Vanden Berghe T, Deceuninck A, Van Durme J, et al. (2009) Proteome-wide Substrate Analysis Indicates Substrate Exclusion as a Mechanism to Generate Caspase-7 Versus Caspase-3 Specificity. Mol Cell Proteomics 8: 2700-2714.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2700-2714
    • Demon, D.1    van Damme, P.2    Vanden Berghe, T.3    Deceuninck, A.4    van Durme, J.5
  • 32
    • 0037077283 scopus 로고    scopus 로고
    • The PYRIN-CARD protein ASC is an activating adaptor for caspase-1
    • Srinivasula SM, Poyet JL, Razmara M, Datta P, Zhang Z, et al. (2002) The PYRIN-CARD protein ASC is an activating adaptor for caspase-1. J Biol Chem 277: 21119-21122.
    • (2002) J Biol Chem , vol.277 , pp. 21119-21122
    • Srinivasula, S.M.1    Poyet, J.L.2    Razmara, M.3    Datta, P.4    Zhang, Z.5
  • 33
    • 0015522988 scopus 로고
    • Studies on the subunit molecular weight of beef heart lactate dehydrogenase
    • Huston JS, Fish WW, Mann KG, Tanford C, (1972) Studies on the subunit molecular weight of beef heart lactate dehydrogenase. Biochemistry 11: 1609-1612.
    • (1972) Biochemistry , vol.11 , pp. 1609-1612
    • Huston, J.S.1    Fish, W.W.2    Mann, K.G.3    Tanford, C.4
  • 34
    • 0043234285 scopus 로고    scopus 로고
    • Assembly and topography of the prepore complex in cholesterol-dependent cytolysins
    • Heuck AP, Tweten RK, Johnson AE, (2003) Assembly and topography of the prepore complex in cholesterol-dependent cytolysins. J Biol Chem 278: 31218-31225.
    • (2003) J Biol Chem , vol.278 , pp. 31218-31225
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 36
    • 34548490518 scopus 로고    scopus 로고
    • Listeriolysin O: a phagosome-specific lysin
    • Schnupf P, Portnoy DA, (2007) Listeriolysin O: a phagosome-specific lysin. Microbes Infect 9: 1176-1187.
    • (2007) Microbes Infect , vol.9 , pp. 1176-1187
    • Schnupf, P.1    Portnoy, D.A.2
  • 37
    • 44849103483 scopus 로고    scopus 로고
    • IFN-beta increases listeriolysin O-induced membrane permeabilization and death of macrophages
    • Zwaferink H, Stockinger S, Hazemi P, Lemmens-Gruber R, Decker T, (2008) IFN-beta increases listeriolysin O-induced membrane permeabilization and death of macrophages. J Immunol 180: 4116-4123.
    • (2008) J Immunol , vol.180 , pp. 4116-4123
    • Zwaferink, H.1    Stockinger, S.2    Hazemi, P.3    Lemmens-Gruber, R.4    Decker, T.5
  • 38
    • 34147148578 scopus 로고    scopus 로고
    • Sterol and pH interdependence in the binding, oligomerization, and pore formation of Listeriolysin O
    • Bavdek A, Gekara NO, Priselac D, Gutierrez Aguirre I, Darji A, et al. (2007) Sterol and pH interdependence in the binding, oligomerization, and pore formation of Listeriolysin O. Biochemistry 46: 4425-4437.
    • (2007) Biochemistry , vol.46 , pp. 4425-4437
    • Bavdek, A.1    Gekara, N.O.2    Priselac, D.3    Gutierrez Aguirre, I.4    Darji, A.5
  • 39
    • 0028853674 scopus 로고
    • Listeriolysin is processed efficiently into an MHC class I-associated epitope in Listeria monocytogenes-infected cells
    • Villanueva MS, Sijts AJ, Pamer EG, (1995) Listeriolysin is processed efficiently into an MHC class I-associated epitope in Listeria monocytogenes-infected cells. J Immunol 155: 5227-5233.
    • (1995) J Immunol , vol.155 , pp. 5227-5233
    • Villanueva, M.S.1    Sijts, A.J.2    Pamer, E.G.3
  • 40
    • 0036838013 scopus 로고    scopus 로고
    • Inducible control of virulence gene expression in Listeria monocytogenes: temporal requirement of listeriolysin O during intracellular infection
    • Dancz CE, Haraga A, Portnoy DA, Higgins DE, (2002) Inducible control of virulence gene expression in Listeria monocytogenes: temporal requirement of listeriolysin O during intracellular infection. J Bacteriol 184: 5935-5945.
    • (2002) J Bacteriol , vol.184 , pp. 5935-5945
    • Dancz, C.E.1    Haraga, A.2    Portnoy, D.A.3    Higgins, D.E.4
  • 41
    • 0028072474 scopus 로고
    • Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O
    • Jones S, Portnoy DA, (1994) Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O. Infect Immun 62: 5608-5613.
    • (1994) Infect Immun , vol.62 , pp. 5608-5613
    • Jones, S.1    Portnoy, D.A.2
  • 42
    • 0038615855 scopus 로고    scopus 로고
    • Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan
    • Girardin SE, Boneca IG, Carneiro LA, Antignac A, Jehanno M, et al. (2003) Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan. Science 300: 1584-1587.
    • (2003) Science , vol.300 , pp. 1584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Carneiro, L.A.3    Antignac, A.4    Jehanno, M.5
  • 43
    • 0021022588 scopus 로고
    • Survival of cultured cells after functional and structural disorganization of plasma membrane by bacterial haemolysins and phospholipases
    • Thelestam M, Mollby R, (1983) Survival of cultured cells after functional and structural disorganization of plasma membrane by bacterial haemolysins and phospholipases. Toxicon 21: 805-815.
    • (1983) Toxicon , vol.21 , pp. 805-815
    • Thelestam, M.1    Mollby, R.2
  • 44
    • 0028068011 scopus 로고
    • Recovery of human fibroblasts from attack by the pore-forming alpha-toxin of Staphylococcus aureus
    • Walev I, Palmer M, Martin E, Jonas D, Weller U, et al. (1994) Recovery of human fibroblasts from attack by the pore-forming alpha-toxin of Staphylococcus aureus. Microb Pathog 17: 187-201.
    • (1994) Microb Pathog , vol.17 , pp. 187-201
    • Walev, I.1    Palmer, M.2    Martin, E.3    Jonas, D.4    Weller, U.5
  • 45
    • 0034014595 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: repair of a calcium-impermeable pore in the target cell membrane
    • Valeva A, Walev I, Gerber A, Klein J, Palmer M, et al. (2000) Staphylococcal alpha-toxin: repair of a calcium-impermeable pore in the target cell membrane. Mol Microbiol 36: 467-476.
    • (2000) Mol Microbiol , vol.36 , pp. 467-476
    • Valeva, A.1    Walev, I.2    Gerber, A.3    Klein, J.4    Palmer, M.5
  • 46
    • 0141614012 scopus 로고    scopus 로고
    • Staphylococcus aureus alpha-toxin induces apoptosis in peripheral blood mononuclear cells: role of endogenous tumour necrosis factor-alpha and the mitochondrial death pathway
    • Haslinger B, Strangfeld K, Peters G, Schulze-Osthoff K, Sinha B, (2003) Staphylococcus aureus alpha-toxin induces apoptosis in peripheral blood mononuclear cells: role of endogenous tumour necrosis factor-alpha and the mitochondrial death pathway. Cell Microbiol 5: 729-741.
    • (2003) Cell Microbiol , vol.5 , pp. 729-741
    • Haslinger, B.1    Strangfeld, K.2    Peters, G.3    Schulze-Osthoff, K.4    Sinha, B.5
  • 47
    • 0035969249 scopus 로고    scopus 로고
    • Alpha-Toxin is a mediator of Staphylococcus aureus-induced cell death and activates caspases via the intrinsic death pathway independently of death receptor signaling
    • Bantel H, Sinha B, Domschke W, Peters G, Schulze-Osthoff K, et al. (2001) Alpha-Toxin is a mediator of Staphylococcus aureus-induced cell death and activates caspases via the intrinsic death pathway independently of death receptor signaling. J Cell Biol 155: 637-648.
    • (2001) J Cell Biol , vol.155 , pp. 637-648
    • Bantel, H.1    Sinha, B.2    Domschke, W.3    Peters, G.4    Schulze-Osthoff, K.5
  • 48
    • 0029895343 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins
    • Pai JT, Brown MS, Goldstein JL, (1996) Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins. Proc Natl Acad Sci U S A 93: 5437-5442.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5437-5442
    • Pai, J.T.1    Brown, M.S.2    Goldstein, J.L.3
  • 49
    • 66949153262 scopus 로고    scopus 로고
    • Human caspase 7 is positively controlled by SREBP-1 and SREBP-2
    • Gibot L, Follet J, Metges JP, Auvray P, Simon B, et al. (2009) Human caspase 7 is positively controlled by SREBP-1 and SREBP-2. Biochem J 420: 473-483.
    • (2009) Biochem J , vol.420 , pp. 473-483
    • Gibot, L.1    Follet, J.2    Metges, J.P.3    Auvray, P.4    Simon, B.5
  • 50
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • Wang X, Sato R, Brown MS, Hua X, Goldstein JL, (1994) SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell 77: 53-62.
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 51
    • 77957956726 scopus 로고    scopus 로고
    • Salmonella pathogenesis and processing of secreted effectors by caspase-3
    • Srikanth CV, Wall DM, Maldonado-Contreras A, Shi HN, Zhou D, et al. (2010) Salmonella pathogenesis and processing of secreted effectors by caspase-3. Science 330: 390-393.
    • (2010) Science , vol.330 , pp. 390-393
    • Srikanth, C.V.1    Wall, D.M.2    Maldonado-Contreras, A.3    Shi, H.N.4    Zhou, D.5
  • 52
    • 79952300209 scopus 로고    scopus 로고
    • TLR signaling is required for Salmonella typhimurium virulence
    • Arpaia N, Godec J, Lau L, Sivick KE, McLaughlin LM, et al. (2011) TLR signaling is required for Salmonella typhimurium virulence. Cell 144: 675-688.
    • (2011) Cell , vol.144 , pp. 675-688
    • Arpaia, N.1    Godec, J.2    Lau, L.3    Sivick, K.E.4    McLaughlin, L.M.5
  • 53
    • 77951227176 scopus 로고    scopus 로고
    • Caspase-7 cleavage of Kaposi sarcoma-associated herpesvirus ORF57 confers a cellular function against viral lytic gene expression
    • Majerciak V, Kruhlak M, Dagur PK, McCoy JP Jr, Zheng ZM, (2010) Caspase-7 cleavage of Kaposi sarcoma-associated herpesvirus ORF57 confers a cellular function against viral lytic gene expression. J Biol Chem 285: 11297-11307.
    • (2010) J Biol Chem , vol.285 , pp. 11297-11307
    • Majerciak, V.1    Kruhlak, M.2    Dagur, P.K.3    McCoy Jr., J.P.4    Zheng, Z.M.5
  • 54
    • 67651091732 scopus 로고    scopus 로고
    • Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system
    • Vance RE, Isberg RR, Portnoy DA, (2009) Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system. Cell Host Microbe 6: 10-21.
    • (2009) Cell Host Microbe , vol.6 , pp. 10-21
    • Vance, R.E.1    Isberg, R.R.2    Portnoy, D.A.3
  • 55
    • 40849118150 scopus 로고    scopus 로고
    • Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis
    • Idone V, Tam C, Goss JW, Toomre D, Pypaert M, et al. (2008) Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis. J Cell Biol 180: 905-914.
    • (2008) J Cell Biol , vol.180 , pp. 905-914
    • Idone, V.1    Tam, C.2    Goss, J.W.3    Toomre, D.4    Pypaert, M.5
  • 56
    • 0035853082 scopus 로고    scopus 로고
    • Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O
    • Walev I, Bhakdi SC, Hofmann F, Djonder N, Valeva A, et al. (2001) Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O. Proc Natl Acad Sci U S A 98: 3185-3190.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3185-3190
    • Walev, I.1    Bhakdi, S.C.2    Hofmann, F.3    Djonder, N.4    Valeva, A.5
  • 57
    • 0030850489 scopus 로고    scopus 로고
    • Preclinical studies of streptolysin-O in enhancing antisense oligonucleotide uptake in harvests from chronic myeloid leukaemia patients
    • Broughton CM, Spiller DG, Pender N, Komorovskaya M, Grzybowski J, et al. (1997) Preclinical studies of streptolysin-O in enhancing antisense oligonucleotide uptake in harvests from chronic myeloid leukaemia patients. Leukemia 11: 1435-1441.
    • (1997) Leukemia , vol.11 , pp. 1435-1441
    • Broughton, C.M.1    Spiller, D.G.2    Pender, N.3    Komorovskaya, M.4    Grzybowski, J.5
  • 58
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes
    • Reddy A, Caler EV, Andrews NW, (2001) Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes. Cell 106: 157-169.
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 59
    • 55449127739 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo
    • Bischof LJ, Kao CY, Los FC, Gonzalez MR, Shen Z, et al. (2008) Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo. PLoS Pathog 4: e1000176.
    • (2008) PLoS Pathog , vol.4
    • Bischof, L.J.1    Kao, C.Y.2    Los, F.C.3    Gonzalez, M.R.4    Shen, Z.5
  • 60
    • 0028072474 scopus 로고
    • Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O
    • Jones S, Portnoy DA, (1994) Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O. Infect Immun 62: 5608-5613.
    • (1994) Infect Immun , vol.62 , pp. 5608-5613
    • Jones, S.1    Portnoy, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.