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Volumn 13, Issue 7, 2011, Pages 1026-1043

Pore-forming toxins induce multiple cellular responses promoting survival

Author keywords

[No Author keywords available]

Indexed keywords

AEROLYSIN; LISTERIOLYSIN O; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38;

EID: 79959273057     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2011.01600.x     Document Type: Article
Times cited : (131)

References (65)
  • 2
    • 0032498627 scopus 로고    scopus 로고
    • A pore-forming toxin interact with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum
    • Abrami, L., Fivaz, M., Glauser, P.-E., Parton, R.G., and van der Goot, F.G. (1998b) A pore-forming toxin interact with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. J Cell Biol 140: 525-540.
    • (1998) J Cell Biol , vol.140 , pp. 525-540
    • Abrami, L.1    Fivaz, M.2    Glauser, P.-E.3    Parton, R.G.4    van der Goot, F.G.5
  • 3
    • 0034176550 scopus 로고    scopus 로고
    • Adventures of a pore-forming toxin at the target cell surface
    • Abrami, L., Fivaz, M., and van Der Goot, F.G. (2000) Adventures of a pore-forming toxin at the target cell surface. Trends Microbiol 8: 168-172.
    • (2000) Trends Microbiol , vol.8 , pp. 168-172
    • Abrami, L.1    Fivaz, M.2    van Der Goot, F.G.3
  • 4
    • 77951229401 scopus 로고    scopus 로고
    • Phosphatase-dependent regulation of epithelial mitogen-activated protein kinase responses to toxin-induced membrane pores
    • Aguilar, J.L., Kulkarni, R., Randis, T.M., Soman, S., Kikuchi, A., Yin, Y., and Ratner, A.J. (2009) Phosphatase-dependent regulation of epithelial mitogen-activated protein kinase responses to toxin-induced membrane pores. PLoS ONE 4: e8076.
    • (2009) PLoS ONE , vol.4
    • Aguilar, J.L.1    Kulkarni, R.2    Randis, T.M.3    Soman, S.4    Kikuchi, A.5    Yin, Y.6    Ratner, A.J.7
  • 5
    • 33846829776 scopus 로고    scopus 로고
    • Pore-forming toxins and cellular non-immune defenses (CNIDs)
    • Aroian, R., and van der Goot, F.G. (2007) Pore-forming toxins and cellular non-immune defenses (CNIDs). Curr Opin Microbiol 10: 57-61.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 57-61
    • Aroian, R.1    van der Goot, F.G.2
  • 6
    • 77952954544 scopus 로고    scopus 로고
    • Lipid droplets: a dynamic organelle moves into focus
    • Beller, M., Thiel, K., Thul, P.J., and Jackle, H. (2009) Lipid droplets: a dynamic organelle moves into focus. FEBS Lett 584: 2176-2182.
    • (2009) FEBS Lett , vol.584 , pp. 2176-2182
    • Beller, M.1    Thiel, K.2    Thul, P.J.3    Jackle, H.4
  • 7
    • 74549201550 scopus 로고    scopus 로고
    • Hypoxia and the hypoxic response pathway protect against pore-forming toxins in C. elegans
    • Bellier, A., Chen, C.S., Kao, C.Y., Cinar, H.N., and Aroian, R.V. (2009) Hypoxia and the hypoxic response pathway protect against pore-forming toxins in C. elegans. PLoS Pathog 5: e1000689.
    • (2009) PLoS Pathog , vol.5
    • Bellier, A.1    Chen, C.S.2    Kao, C.Y.3    Cinar, H.N.4    Aroian, R.V.5
  • 8
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • Bhakdi, S., and Tranum-Jensen, J. (1991) Alpha-toxin of Staphylococcus aureus. Microbiol Rev 55: 733-751.
    • (1991) Microbiol Rev , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 9
    • 55449127739 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo
    • Bischof, L.J., Kao, C.Y., Los, F.C., Gonzalez, M.R., Shen, Z., Briggs, S.P., etal. (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    Briggs, S.P.6
  • 11
    • 0025004421 scopus 로고
    • Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida
    • Buckley, J.T. (1990) Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida. Biochem Cell Biol 68: 221-224.
    • (1990) Biochem Cell Biol , vol.68 , pp. 221-224
    • Buckley, J.T.1
  • 12
    • 0019580931 scopus 로고
    • Purification and some properties of the hemolytic toxin aerolysin
    • Buckley, J.T., Halasa, L.N., Lund, K.D., and MacIntyre, S. (1981) Purification and some properties of the hemolytic toxin aerolysin. Can J Biochem 59: 430-435.
    • (1981) Can J Biochem , vol.59 , pp. 430-435
    • Buckley, J.T.1    Halasa, L.N.2    Lund, K.D.3    MacIntyre, S.4
  • 13
    • 51449085299 scopus 로고    scopus 로고
    • The role of autophagy in mammalian development: cell makeover rather than cell death
    • Cecconi, F., and Levine, B. (2008) The role of autophagy in mammalian development: cell makeover rather than cell death. Dev Cell 15: 344-357.
    • (2008) Dev Cell , vol.15 , pp. 344-357
    • Cecconi, F.1    Levine, B.2
  • 14
    • 0034058065 scopus 로고    scopus 로고
    • The cytotoxic enterotoxin of Aeromonas hydrophila induces proinflammatory cytokine production and activates arachidonic acid metabolism in macrophages
    • Chopra, A.K., Xu, X., Ribardo, D., Gonzalez, M., Kuhl, K., Peterson, J.W., and Houston, C.W. (2000) The cytotoxic enterotoxin of Aeromonas hydrophila induces proinflammatory cytokine production and activates arachidonic acid metabolism in macrophages. Infect Immun 68: 2808-2818.
    • (2000) Infect Immun , vol.68 , pp. 2808-2818
    • Chopra, A.K.1    Xu, X.2    Ribardo, D.3    Gonzalez, M.4    Kuhl, K.5    Peterson, J.W.6    Houston, C.W.7
  • 15
    • 33947719749 scopus 로고    scopus 로고
    • eIF2alpha phosphorylation bidirectionally regulates the switch from short- to long-term synaptic plasticity and memory
    • Costa-Mattioli, M., Gobert, D., Stern, E., Gamache, K., Colina, R., Cuello, C., etal. (2007) eIF2alpha phosphorylation bidirectionally regulates the switch from short- to long-term synaptic plasticity and memory. Cell 129: 195-206.
    • (2007) Cell , vol.129 , pp. 195-206
    • Costa-Mattioli, M.1    Gobert, D.2    Stern, E.3    Gamache, K.4    Colina, R.5    Cuello, C.6
  • 16
    • 77956397771 scopus 로고    scopus 로고
    • Inflammasome activation by adenylate cyclase toxin directs Th17 responses and protection against Bordetella pertussis
    • Dunne, A., Ross, P.J., Pospisilova, E., Masin, J., Meaney, A., Sutton, C.E., etal. (2010) Inflammasome activation by adenylate cyclase toxin directs Th17 responses and protection against Bordetella pertussis. J Immunol 185: 1711-1719.
    • (2010) J Immunol , vol.185 , pp. 1711-1719
    • Dunne, A.1    Ross, P.J.2    Pospisilova, E.3    Masin, J.4    Meaney, A.5    Sutton, C.E.6
  • 17
    • 77955973704 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins
    • Gilbert, R.J. (2010) Cholesterol-dependent cytolysins. Adv Exp Med Biol 677: 56-66.
    • (2010) Adv Exp Med Biol , vol.677 , pp. 56-66
    • Gilbert, R.J.1
  • 18
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: towards a molecular definition
    • Golstein, P., and Kroemer, G. (2007) Cell death by necrosis: towards a molecular definition. Trends Biochem Sci 32: 37-43.
    • (2007) Trends Biochem Sci , vol.32 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 21
    • 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., and van der Goot, F.G. (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
  • 23
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense
    • Hadders, M.A., Beringer, D.X., and Gros, P. (2007) Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Science 317: 1552-1554.
    • (2007) Science , vol.317 , pp. 1552-1554
    • Hadders, M.A.1    Beringer, D.X.2    Gros, P.3
  • 25
    • 0021688655 scopus 로고
    • Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells
    • Hann, S.R., and Eisenman, R.N. (1984) Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells. Mol Cell Biol 4: 2486-2497.
    • (1984) Mol Cell Biol , vol.4 , pp. 2486-2497
    • Hann, S.R.1    Eisenman, R.N.2
  • 26
    • 77952302993 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin family of gram-positive bacterial toxins
    • Heuck, A.P., Moe, P.C., and Johnson, B.B. (2010) The cholesterol-dependent cytolysin family of gram-positive bacterial toxins. Subcell Biochem 51: 551-577.
    • (2010) Subcell Biochem , vol.51 , pp. 551-577
    • Heuck, A.P.1    Moe, P.C.2    Johnson, B.B.3
  • 27
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik, M., and Sonenberg, N. (2005) Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6: 318-327.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 29
    • 33646166722 scopus 로고    scopus 로고
    • Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O
    • Husmann, M., Dersch, K., Bobkiewicz, W., Beckmann, E., Veerachato, G., and Bhakdi, S. (2006) Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O. Biochem Biophys Res Commun 344: 1128-1134.
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 1128-1134
    • Husmann, M.1    Dersch, K.2    Bobkiewicz, W.3    Beckmann, E.4    Veerachato, G.5    Bhakdi, S.6
  • 30
    • 58149479324 scopus 로고    scopus 로고
    • Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis
    • Husmann, M., Beckmann, E., Boller, K., Kloft, N., Tenzer, S., Bobkiewicz, W., etal. (2009) Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis. FEBS Lett 583: 337-344.
    • (2009) FEBS Lett , vol.583 , pp. 337-344
    • Husmann, M.1    Beckmann, E.2    Boller, K.3    Kloft, N.4    Tenzer, S.5    Bobkiewicz, W.6
  • 31
    • 32544443056 scopus 로고    scopus 로고
    • A rivet model for channel formation by aerolysin-like pore-forming toxins
    • Iacovache, I., Paumard, P., Scheib, H., Lesieur, C., Sakai, N., Matile, S., etal. (2006) A rivet model for channel formation by aerolysin-like pore-forming toxins. EMBO J 25: 457-466.
    • (2006) EMBO J , vol.25 , pp. 457-466
    • Iacovache, I.1    Paumard, P.2    Scheib, H.3    Lesieur, C.4    Sakai, N.5    Matile, S.6
  • 32
    • 45449117125 scopus 로고    scopus 로고
    • Pore formation: an ancient yet complex form of attack
    • Iacovache, I., van der Goot, F.G., and Pernot, L. (2008) Pore formation: an ancient yet complex form of attack. Biochim Biophys Acta 1778: 1611-1623.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1611-1623
    • Iacovache, I.1    van der Goot, F.G.2    Pernot, L.3
  • 34
    • 0030972879 scopus 로고    scopus 로고
    • Triacsin C blocks de novo synthesis of glycerolipids and cholesterol esters but not recycling of fatty acid into phospholipid: evidence for functionally separate pools of acyl-CoA
    • Igal, R.A., Wang, P., and Coleman, R.A. (1997) Triacsin C blocks de novo synthesis of glycerolipids and cholesterol esters but not recycling of fatty acid into phospholipid: evidence for functionally separate pools of acyl-CoA. Biochem J 324 (Part 2): 529-534.
    • (1997) Biochem J , vol.324 , Issue.PART 2 , pp. 529-534
    • Igal, R.A.1    Wang, P.2    Coleman, R.A.3
  • 35
    • 70049117142 scopus 로고    scopus 로고
    • Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum
    • Kennedy, C.L., Smith, D.J., Lyras, D., Chakravorty, A., and Rood, J.I. (2009) Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum. PLoS Pathog 5: e1000516.
    • (2009) PLoS Pathog , vol.5
    • Kennedy, C.L.1    Smith, D.J.2    Lyras, D.3    Chakravorty, A.4    Rood, J.I.5
  • 36
    • 77749260612 scopus 로고    scopus 로고
    • Pyroptosis - a cell death modality of its kind?
    • Kepp, O., Galluzzi, L., Zitvogel, L., and Kroemer, G. (2010) Pyroptosis - a cell death modality of its kind? Eur J Immunol 40: 627-630.
    • (2010) Eur J Immunol , vol.40 , pp. 627-630
    • Kepp, O.1    Galluzzi, L.2    Zitvogel, L.3    Kroemer, G.4
  • 37
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky, D.J., Abeliovich, H., Agostinis, P., Agrawal, D.K., Aliev, G., Askew, D.S., etal. (2008) Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4: 151-175.
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5    Askew, D.S.6
  • 40
    • 0032007852 scopus 로고    scopus 로고
    • A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers
    • Korchev, Y.E., Bashford, C.L., Pederzolli, C., Pasternak, C.A., Morgan, P.J., Andrew, P.W., and Mitchell, T.J. (1998) A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers. Biochem J 329 (Part 3): 571-577.
    • (1998) Biochem J , vol.329 , Issue.PART 3 , pp. 571-577
    • Korchev, Y.E.1    Bashford, C.L.2    Pederzolli, C.3    Pasternak, C.A.4    Morgan, P.J.5    Andrew, P.W.6    Mitchell, T.J.7
  • 41
  • 42
    • 0000214972 scopus 로고
    • On the role of intracellular potassium in protein synthesis
    • Lubin, M., and Ennis, H.L. (1964) On the role of intracellular potassium in protein synthesis. Biochim Biophys Acta 80: 614-631.
    • (1964) Biochim Biophys Acta , vol.80 , pp. 614-631
    • Lubin, M.1    Ennis, H.L.2
  • 43
    • 20344402550 scopus 로고    scopus 로고
    • An emergency response team for membrane repair
    • McNeil, P.L., and Kirchhausen, T. (2005) An emergency response team for membrane repair. Nat Rev Mol Cell Biol 6: 499-505.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 499-505
    • McNeil, P.L.1    Kirchhausen, T.2
  • 44
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: repair, prevention, adaptation
    • McNeil, P.L., and Steinhardt, R.A. (2003) Plasma membrane disruption: repair, prevention, adaptation. Annu Rev Cell Dev Biol 19: 697-731.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 45
    • 75149167986 scopus 로고    scopus 로고
    • Alpha-hemolysin is required for the activation of the autophagic pathway in Staphylococcus aureus-infected cells
    • Mestre, M.B., Fader, C.M., Sola, C., and Colombo, M.I. (2010) Alpha-hemolysin is required for the activation of the autophagic pathway in Staphylococcus aureus-infected cells. Autophagy 6: 110-125.
    • (2010) Autophagy , vol.6 , pp. 110-125
    • Mestre, M.B.1    Fader, C.M.2    Sola, C.3    Colombo, M.I.4
  • 46
    • 77649163335 scopus 로고    scopus 로고
    • Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection
    • Meyer-Morse, N., Robbins, J.R., Rae, C.S., Mochegova, S.N., Swanson, M.S., Zhao, Z., etal. (2010) Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection. PLoS ONE 5: e8610.
    • (2010) PLoS ONE , vol.5
    • Meyer-Morse, N.1    Robbins, J.R.2    Rae, C.S.3    Mochegova, S.N.4    Swanson, M.S.5    Zhao, Z.6
  • 47
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima, N., Yamamoto, A., Hatano, M., Kobayashi, Y., Kabeya, Y., Suzuki, K., etal. (2001) Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 152: 657-668.
    • (2001) J Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1    Yamamoto, A.2    Hatano, M.3    Kobayashi, Y.4    Kabeya, Y.5    Suzuki, K.6
  • 48
    • 0033157103 scopus 로고    scopus 로고
    • Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas
    • Nelson, K.L., Brodsky, R.A., and Buckley, J.T. (1999) Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas. Cell Microbiol 1: 69-74.
    • (1999) Cell Microbiol , vol.1 , pp. 69-74
    • Nelson, K.L.1    Brodsky, R.A.2    Buckley, J.T.3
  • 49
    • 79951512773 scopus 로고    scopus 로고
    • Role of MAPK p38 in the cellular responses to pore-forming toxins
    • Porta, H., Cancino-Rodezno, A., Soberon, M., and Bravo, A. (2011) Role of MAPK p38 in the cellular responses to pore-forming toxins. Peptides 32: 601-606.
    • (2011) Peptides , vol.32 , pp. 601-606
    • Porta, H.1    Cancino-Rodezno, A.2    Soberon, M.3    Bravo, A.4
  • 51
    • 77951535793 scopus 로고    scopus 로고
    • Listeria monocytogenes impairs SUMOylation for efficient infection
    • Ribet, D., Hamon, M., Gouin, E., Nahori, M.A., Impens, F., Neyret-Kahn, H., etal. (2010) Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 464: 1192-1195.
    • (2010) Nature , vol.464 , pp. 1192-1195
    • Ribet, D.1    Hamon, M.2    Gouin, E.3    Nahori, M.A.4    Impens, F.5    Neyret-Kahn, H.6
  • 52
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D., and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 53
    • 34548666167 scopus 로고    scopus 로고
    • A common fold mediates vertebrate defense and bacterial attack
    • Rosado, C.J., Buckle, A.M., Law, R.H., Butcher, R.E., Kan, W.T., Bird, C.H., etal. (2007) A common fold mediates vertebrate defense and bacterial attack. Science 317: 1548-1551.
    • (2007) Science , vol.317 , pp. 1548-1551
    • Rosado, C.J.1    Buckle, A.M.2    Law, R.H.3    Butcher, R.E.4    Kan, W.T.5    Bird, C.H.6
  • 55
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins
    • Shepard, L.A., Shatursky, O., Johnson, A.E., and Tweten, R.K. (2000) The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins. Biochemistry 39: 10284-10293.
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 57
    • 77953576191 scopus 로고    scopus 로고
    • Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair
    • Tam, C., Idone, V., Devlin, C., Fernandes, M.C., Flannery, A., He, X., etal. (2010) Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair. J Cell Biol 189: 1027-1038.
    • (2010) J Cell Biol , vol.189 , pp. 1027-1038
    • Tam, C.1    Idone, V.2    Devlin, C.3    Fernandes, M.C.4    Flannery, A.5    He, X.6
  • 58
    • 0036771839 scopus 로고    scopus 로고
    • Conversion of a transmembrane to a water-soluble protein complex by a single point mutation
    • Tsitrin, Y., Morton, C.J., El Bez, C., Paumard, P., Velluz, M.C., Adrian, M., etal. (2002) Conversion of a transmembrane to a water-soluble protein complex by a single point mutation. Nat Struct Biol 9: 729-733.
    • (2002) Nat Struct Biol , vol.9 , pp. 729-733
    • Tsitrin, Y.1    Morton, C.J.2    El Bez, C.3    Paumard, P.4    Velluz, M.C.5    Adrian, M.6
  • 60
    • 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., Hohn, B.H., etal. (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    Hohn, B.H.6
  • 61
  • 62
    • 0021826801 scopus 로고
    • Ultrastructure of Saccharomyces cerevisiae strain AG1-7 and its responses to changes in environment
    • Willison, J.H., and Johnston, G.C. (1985) Ultrastructure of Saccharomyces cerevisiae strain AG1-7 and its responses to changes in environment. Can J Microbiol 31: 109-118.
    • (1985) Can J Microbiol , vol.31 , pp. 109-118
    • Willison, J.H.1    Johnston, G.C.2
  • 63
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: core molecular machinery and signaling regulation
    • Yang, Z., and Klionsky, D.J. (2010) Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol 22: 124-131.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 64
    • 39149136542 scopus 로고    scopus 로고
    • Interferons increase cell resistance to Staphylococcal alpha-toxin
    • Yarovinsky, T.O., Monick, M.M., Husmann, M., and Hunninghake, G.W. (2008) Interferons increase cell resistance to Staphylococcal alpha-toxin. Infect Immun 76: 571-577.
    • (2008) Infect Immun , vol.76 , pp. 571-577
    • Yarovinsky, T.O.1    Monick, M.M.2    Husmann, M.3    Hunninghake, G.W.4
  • 65
    • 77952888481 scopus 로고    scopus 로고
    • Systems biology of energy homeostasis in yeast
    • Zhang, J., Vemuri, G., and Nielsen, J. (2010) Systems biology of energy homeostasis in yeast. Curr Opin Microbiol 13: 382-388.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 382-388
    • Zhang, J.1    Vemuri, G.2    Nielsen, J.3


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