메뉴 건너뛰기




Volumn 77, Issue 10, 2009, Pages 4327-4336

CA-074Me protection against anthrax lethal toxin

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRAX TOXIN; CA 074ME; CATHEPSIN B; CATHEPSIN B INHIBITOR; CRYOPYRIN; INTERLEUKIN 1BETA CONVERTING ENZYME; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR NLRP 1B; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 70349413073     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00730-09     Document Type: Article
Times cited : (76)

References (64)
  • 1
    • 4444224022 scopus 로고    scopus 로고
    • Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway
    • DOI 10.1083/jcb.200312072
    • Abrami, L., M. Lindsay, R. G. Parton, S. H. Leppla, and F. G. van der Goot. 2004. Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway. J. Cell Biol. 166:645-651. (Pubitemid 39181002)
    • (2004) Journal of Cell Biology , vol.166 , Issue.5 , pp. 645-651
    • Abrami, L.1    Lindsay, M.2    Parton, R.G.3    Leppla, S.H.4    Van Der Goot, F.G.5
  • 2
    • 33645318478 scopus 로고    scopus 로고
    • Mitochondrial impairment is a critical event in anthrax lethal toxin-induced cytolysis of murine macrophages
    • Alileche, A., R. C. Squires, S. M. Muehlbauer, M. P. Lisanti, and J. Brojatsch. 2006. Mitochondrial impairment is a critical event in anthrax lethal toxin-induced cytolysis of murine macrophages. Cell Cycle 5:100-106.
    • (2006) Cell Cycle , vol.5 , pp. 100-106
    • Alileche, A.1    Squires, R.C.2    Muehlbauer, S.M.3    Lisanti, M.P.4    Brojatsch, J.5
  • 3
    • 3042800587 scopus 로고    scopus 로고
    • Phospholipases C and A2 control lysosome-mediated IL-1β secretion: Implications for inflammatory processes
    • Andrei, C., P. Margiocco, A. Poggi, L. V. Lotti, M. R. Torrisi, and A. Rubartelli. 2004. Phospholipases C and A2 control lysosome-mediated IL-1β secretion: implications for inflammatory processes. Proc. Natl. Acad. Sci. USA 101:9745-9750.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9745-9750
    • Andrei, C.1    Margiocco, P.2    Poggi, A.3    Lotti, L.V.4    Torrisi, M.R.5    Rubartelli, A.6
  • 5
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere, N., H. K. Lorenzo, S. Carmona, M. Laforge, F. Harper, C. Dumont, and A. Senik. 2003. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 278:31401-31411.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 6
    • 77956833281 scopus 로고
    • Intracellular Proteolysis
    • A. Neuberger and K. Brocklehurst (ed.), Elsevier, Amsterdam, The Netherlands.
    • Bohley, P. 1987. Intracellular Proteolysis, p. 307-332. In A. Neuberger and K. Brocklehurst (ed.), New comprehensive biochemistry, vol.16. Elsevier, Amsterdam, The Netherlands.
    • (1987) New Comprehensive Biochemistry , vol.16 , pp. 307-332
    • Bohley, P.1
  • 7
    • 54949137644 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization in cell death
    • Boya, P., and G. Kroemer. 2008. Lysosomal membrane permeabilization in cell death. Oncogene 27:6434-6451.
    • (2008) Oncogene , vol.27 , pp. 6434-6451
    • Boya, P.1    Kroemer, G.2
  • 8
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden, E. D., and W. F. Dietrich. 2006. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat. Genet. 38:240-244.
    • (2006) Nat. Genet. , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 9
    • 0030757986 scopus 로고    scopus 로고
    • Photooxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • Brunk, U. T., H. Dalen, K. Roberg, and H. B. Hellquist. 1997. Photooxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic. Biol. Med. 23:616-626.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 12
    • 41949127121 scopus 로고    scopus 로고
    • Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
    • Fink, S. L., T. Bergsbaken, and B. T. Cookson. 2008. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Proc. Natl. Acad. Sci. USA 105:4312-4317.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4312-4317
    • Fink, S.L.1    Bergsbaken, T.2    Cookson, B.T.3
  • 14
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: A caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • Franchi, L., T. Eigenbrod, R. Munoz-Planillo, and G. Nunez. 2009. The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nat. Immunol. 10:241-247.
    • (2009) Nat. Immunol. , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Munoz-Planillo, R.3    Nunez, G.4
  • 15
    • 0027470890 scopus 로고
    • Characterization of macrophage sensitivity and resistance to anthrax lethal toxin
    • Friedlander, A. M., R. Bhatnagar, S. H. Leppla, L. Johnson, and Y. Singh. 1993. Characterization of macrophage sensitivity and resistance to anthrax lethal toxin. Infect. Immun. 61:245-252.
    • (1993) Infect. Immun. , vol.61 , pp. 245-252
    • Friedlander, A.M.1    Bhatnagar, R.2    Leppla, S.H.3    Johnson, L.4    Singh, Y.5
  • 17
    • 0035980006 scopus 로고    scopus 로고
    • Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone
    • Gray, J., M. M. Haran, K. Schneider, S. Vesce, A. M. Ray, D. Owen, I. R. White, P. Cutler, and J. B. Davis. 2001. Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone. J. Biol. Chem. 276:32750-32755.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32750-32755
    • Gray, J.1    Haran, M.M.2    Schneider, K.3    Vesce, S.4    Ray, A.M.5    Owen, D.6    White, I.R.7    Cutler, P.8    Davis, J.B.9
  • 20
    • 0028535825 scopus 로고
    • Role of macrophage oxidative burst in the action of anthrax lethal toxin
    • Hanna, P. C., B. A. Kruskal, R. A. Ezekowitz, B. R. Bloom, and R. J. Collier. 1994. Role of macrophage oxidative burst in the action of anthrax lethal toxin. Mol. Med. 1:7-18.
    • (1994) Mol. Med. , vol.1 , pp. 7-18
    • Hanna, P.C.1    Kruskal, B.A.2    Ezekowitz, R.A.3    Bloom, B.R.4    Collier, R.J.5
  • 21
    • 0042914359 scopus 로고    scopus 로고
    • Critical role for cathepsin B in mediating caspase-1-dependent interleukin-18 maturation and caspase-1-independent necrosis triggered by the microbial toxin nigericin
    • DOI 10.1038/sj.cdd.4401264
    • Hentze, H., X. Y. Lin, M. S. Choi, and A. G. Porter. 2003. Critical role for cathepsin B in mediating caspase-1-dependent interleukin-18 maturation and caspase-1-independent necrosis triggered by the microbial toxin nigericin. Cell Death Differ. 10:956-968. (Pubitemid 37069473)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.9 , pp. 956-968
    • Hentze, H.1    Lin, X.Y.2    Choi, M.S.K.3    Porter, A.G.4
  • 23
    • 0037031926 scopus 로고    scopus 로고
    • Identification of calcium-independent phospholipase A2 (iPLA2) β, and not iPLA2γ, as the mediator of arginine vasopressin-induced arachidonic acid release in A-10 smooth muscle cells: Enantioselective mechanism-based discrimination of mammalian iPLA2s
    • Jenkins, C. M., X. Han, D. J. Mancuso, and R. W. Gross. 2002. Identification of calcium-independent phospholipase A2 (iPLA2) β, and not iPLA2γ, as the mediator of arginine vasopressin-induced arachidonic acid release in A-10 smooth muscle cells: enantioselective mechanism-based discrimination of mammalian iPLA2s. J. Biol. Chem. 277:32807-32814.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32807-32814
    • Jenkins, C.M.1    Han, X.2    Mancuso, D.J.3    Gross, R.W.4
  • 26
    • 70349412578 scopus 로고
    • Structure, function, and regulation of endogenous thiol proteinase inhibitor
    • N. Katunuma, H. Umezawa, and H. Holzer (ed.), Japan Scientific Societies Press, Tokyo, Japan.
    • Katunuma, N., N. Wakamatsu, K. Takio, K. Titani, and E. Kominami. 1983. Structure, function, and regulation of endogenous thiol proteinase inhibitor, p. 135-145. In N. Katunuma, H. Umezawa, and H. Holzer (ed.), Proteinase inhibitors: medical and biological aspects. Japan Scientific Societies Press, Tokyo, Japan.
    • (1983) Proteinase Inhibitors: Medical and Biological Aspects , pp. 135-145
    • Katunuma, N.1    Wakamatsu, N.2    Takio, K.3    Titani, K.4    Kominami, E.5
  • 27
    • 0001891521 scopus 로고
    • Chemistry of lysosomal proteases
    • H. Glanmann and J. Ballard (ed.), Academic Press, London, England.
    • Kirschke, H., and A. J. Barrett. 1987. Chemistry of lysosomal proteases, p. 193-238. In H. Glanmann and J. Ballard (ed.), Lysosomes: their role in protein breakdown. Academic Press, London, England.
    • (1987) Lysosomes: Their Role in Protein Breakdown , pp. 193-238
    • Kirschke, H.1    Barrett, A.J.2
  • 28
    • 0033850811 scopus 로고    scopus 로고
    • Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
    • Klemencic, I., A. K. Carmona, M. H. Cezari, M. A. Juliano, L. Juliano, G. Guncar, D. Turk, I. Krizaj, V. Turk, and B. Turk. 2000. Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. Eur. J. Biochem. 267:5404-5412.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5404-5412
    • Klemencic, I.1    Carmona, A.K.2    Cezari, M.H.3    Juliano, M.A.4    Juliano, L.5    Guncar, G.6    Turk, D.7    Krizaj, I.8    Turk, V.9    Turk, B.10
  • 29
    • 55749111567 scopus 로고    scopus 로고
    • Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin
    • Levin, T. C., K. E. Wickliffe, S. H. Leppla, and M. Moayeri. 2008. Heat shock inhibits caspase-1 activity while also preventing its inflammasome- mediated activation by anthrax lethal toxin. Cell. Microbiol. 10:2434-2446.
    • (2008) Cell. Microbiol. , vol.10 , pp. 2434-2446
    • Levin, T.C.1    Wickliffe, K.E.2    Leppla, S.H.3    Moayeri, M.4
  • 30
    • 0036671894 scopus 로고    scopus 로고
    • The Inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • DOI 10.1016/S1097-2765(02)00599-3
    • Martinon, F., K. Burns, and J. Tschopp. 2002. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol. Cell 10:417-426. (Pubitemid 35007355)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 31
    • 9944245491 scopus 로고    scopus 로고
    • Cathepsin B-independent abrogation of cell death by CA-074-OMe upstream of lysosomal breakdown [1]
    • DOI 10.1038/sj.cdd.4401493
    • Mihalik, R., G. Imre, I. Petak, B. Szende, and L. Kopper. 2004. Cathepsin B-independent abrogation of cell death by CA-074-OMe upstream of lysosomal breakdown. Cell Death Differ. 11:1357-1360. (Pubitemid 39591780)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.12 , pp. 1357-1360
    • Mihalik, R.1    Imre, G.2    Petak, I.3    Szende, B.4    Kopper, L.5
  • 32
    • 0036661078 scopus 로고    scopus 로고
    • CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells
    • Montaser, M., G. Lalmanach, and L. Mach. 2002. CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells. Biol. Chem. 383:1305-1308.
    • (2002) Biol. Chem. , vol.383 , pp. 1305-1308
    • Montaser, M.1    Lalmanach, G.2    Mach, L.3
  • 35
    • 62449101446 scopus 로고    scopus 로고
    • Anthrax lethal toxin triggers the formation of a membrane-associated inflammasome complex in murine macrophages
    • Nour, A. M., Y. G. Yeung, L. Santambrogio, E. D. Boyden, E. R. Stanley, and J. Brojatsch. 2009. Anthrax lethal toxin triggers the formation of a membrane-associated inflammasome complex in murine macrophages. Infect. Immun. 77:1262-1271.
    • (2009) Infect. Immun. , vol.77 , pp. 1262-1271
    • Nour, A.M.1    Yeung, Y.G.2    Santambrogio, L.3    Boyden, E.D.4    Stanley, E.R.5    Brojatsch, J.6
  • 36
    • 0034049623 scopus 로고    scopus 로고
    • Optimized production and purification of Bacillus anthracis lethal factor
    • Park, S., and S. H. Leppla. 2000. Optimized production and purification of Bacillus anthracis lethal factor. Protein Expr. Purif. 18:293-302.
    • (2000) Protein Expr. Purif. , vol.18 , pp. 293-302
    • Park, S.1    Leppla, S.H.2
  • 37
    • 0032755353 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNFα
    • Pellizzari, R., C. Guidi-Rontani, G. Vitale, M. Mock, and C. Montecucco. 1999. Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNFα. FEBS Lett. 462:199-204.
    • (1999) FEBS Lett. , vol.462 , pp. 199-204
    • Pellizzari, R.1    Guidi-Rontani, C.2    Vitale, G.3    Mock, M.4    Montecucco, C.5
  • 38
    • 0036234584 scopus 로고    scopus 로고
    • Production, recovery and immunogenicity of the protective antigen from a recombinant strain of Bacillus anthracis
    • Ramirez, D. M., S. H. Leppla, R. Schneerson, and J. Shiloach. 2002. Production, recovery and immunogenicity of the protective antigen from a recombinant strain of Bacillus anthracis. J. Ind. Microbiol. Biotechnol. 28:232-238.
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.28 , pp. 232-238
    • Ramirez, D.M.1    Leppla, S.H.2    Schneerson, R.3    Shiloach, J.4
  • 40
    • 33745760273 scopus 로고    scopus 로고
    • Cytotoxic activity of Bacillus anthracis protective antigen observed in a macrophage cell line overexpressing ANTXR1
    • Salles, I. I., D. E. Voth, S. C. Ward, K. M. Averette, R. K. Tweten, K. A. Bradley, and J. D. Ballard. 2006. Cytotoxic activity of Bacillus anthracis protective antigen observed in a macrophage cell line overexpressing ANTXR1. Cell. Microbiol. 8:1272-1281.
    • (2006) Cell. Microbiol. , vol.8 , pp. 1272-1281
    • Salles, I.I.1    Voth, D.E.2    Ward, S.C.3    Averette, K.M.4    Tweten, R.K.5    Bradley, K.A.6    Ballard, J.D.7
  • 41
    • 0032898735 scopus 로고    scopus 로고
    • Non-specific effects of methyl ketone peptide inhibitors of caspases
    • DOI 10.1016/S0014-5793(98)01640-8, PII S0014579398016408
    • Schotte, P., W. Declercq, H. S. Van, P. Vandenabeele, and R. Beyaert. 1999. Non-specific effects of methyl ketone peptide inhibitors of caspases. FEBS Lett. 442:117-121. (Pubitemid 29065390)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 117-121
    • Schotte, P.1    Declercq, W.2    Van Huffel, S.3    Vandenabeele, P.4    Beyaert, R.5
  • 44
    • 0032587791 scopus 로고    scopus 로고
    • Involvement of phospholipase A2 activation in anthrax lethal toxin-induced cytotoxicity
    • Shin, S., Y. B. Kim, and G. H. Hur. 1999. Involvement of phospholipase A2 activation in anthrax lethal toxin-induced cytotoxicity. Cell Biol. Toxicol. 15:19-29.
    • (1999) Cell Biol. Toxicol. , vol.15 , pp. 19-29
    • Shin, S.1    Kim, Y.B.2    Hur, G.H.3
  • 45
    • 0024392201 scopus 로고
    • Internalization and processing of Bacillus anthracis lethal toxin by toxin-sensitive and -resistant cells
    • Singh, Y., S. H. Leppla, R. Bhatnagar, and A. M. Friedlander. 1989. Internalization and processing of Bacillus anthracis lethal toxin by toxin-sensitive and -resistant cells. J. Biol. Chem. 264:11099-11102.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11099-11102
    • Singh, Y.1    Leppla, S.H.2    Bhatnagar, R.3    Friedlander, A.M.4
  • 46
    • 36349019887 scopus 로고    scopus 로고
    • Proteasomes control caspase-1 activation in anthrax lethal toxin-mediated cell killing
    • Squires, R. C., S. M. Muehlbauer, and J. Brojatsch. 2007. Proteasomes control caspase-1 activation in anthrax lethal toxin-mediated cell killing. J. Biol. Chem. 282:34260-34267.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34260-34267
    • Squires, R.C.1    Muehlbauer, S.M.2    Brojatsch, J.3
  • 48
    • 0025044550 scopus 로고
    • Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells
    • Thiele, D. L., and P. E. Lipsky. 1990. Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. Proc. Natl. Acad. Sci. USA 87:83-87.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 83-87
    • Thiele, D.L.1    Lipsky, P.E.2
  • 51
    • 0031925706 scopus 로고    scopus 로고
    • Internalization of a Bacillus anthracis protective antigen-c-Myc fusion protein mediated by cell surface anti-c-Myc antibodies
    • Varughese, M., A. Chi, A. V. Teixeira, P. J. Nicholls, J. M. Keith, and S. H. Leppla. 1998. Internalization of a Bacillus anthracis protective antigen-c-Myc fusion protein mediated by cell surface anti-c-Myc antibodies. Mol. Med. 4:87-95.
    • (1998) Mol. Med. , vol.4 , pp. 87-95
    • Varughese, M.1    Chi, A.2    Teixeira, A.V.3    Nicholls, P.J.4    Keith, J.M.5    Leppla, S.H.6
  • 52
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • DOI 10.1042/0264-6021:3520739
    • Vitale, G., L. Bernardi, G. Napolitani, M. Mock, and C. Montecucco. 2000. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 352(Pt. 3):739-745. (Pubitemid 32015030)
    • (2000) Biochemical Journal , vol.352 , Issue.3 , pp. 739-745
    • Vitale, G.1    Bernardi, L.2    Napolitani, G.3    Mock, M.4    Montecucco, C.5
  • 53
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale, G., R. Pellizzari, C. Recchi, G. Napolitani, M. Mock, and C. Montecucco. 1998. Anthrax lethal factor cleaves the N terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248:706-711.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 55
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • DOI 10.1016/S0092-8674(00)80943-5
    • Wang, S., M. Miura, Y. K. Jung, H. Zhu, E. Li, and J. Yuan. 1998. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92:501-509. (Pubitemid 28101113)
    • (1998) Cell , vol.92 , Issue.4 , pp. 501-509
    • Wang, S.1    Miura, M.2    Jung, Y.-K.3    Zhu, H.4    Li, E.5    Yuan, J.6
  • 56
    • 0023276349 scopus 로고
    • Differential permeabilization of membranes by saponin treatment of isolated rat hepatocytes. Release of secretory proteins
    • Wassler, M., I. Jonasson, R. Persson, and E. Fries. 1987. Differential permeabilization of membranes by saponin treatment of isolated rat hepatocytes. Release of secretory proteins. Biochem. J. 247:407-415.
    • (1987) Biochem. J. , vol.247 , pp. 407-415
    • Wassler, M.1    Jonasson, I.2    Persson, R.3    Fries, E.4
  • 59
    • 38049119726 scopus 로고    scopus 로고
    • Anthrax lethal toxin-induced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome
    • Wickliffe, K. E., S. H. Leppla, and M. Moayeri. 2008. Anthrax lethal toxin-induced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome. Cell. Microbiol. 10:332-343.
    • (2008) Cell. Microbiol. , vol.10 , pp. 332-343
    • Wickliffe, K.E.1    Leppla, S.H.2    Moayeri, M.3
  • 61
    • 45249089611 scopus 로고    scopus 로고
    • Lysosomal release of cathepsins causes ischemic damage in the rat hippocampal slice and depends on NMDA-mediated calcium influx, arachidonic acid metabolism, and free radical production
    • Windelborn, J. A., and P. Lipton. 2008. Lysosomal release of cathepsins causes ischemic damage in the rat hippocampal slice and depends on NMDA-mediated calcium influx, arachidonic acid metabolism, and free radical production. J. Neurochem. 106:56-69.
    • (2008) J. Neurochem. , vol.106 , pp. 56-69
    • Windelborn, J.A.1    Lipton, P.2
  • 62
    • 50849119416 scopus 로고    scopus 로고
    • The caspase-1 inflammasome: A pilot of innate immune responses
    • Yu, H. B., and B. B. Finlay. 2008. The caspase-1 inflammasome: a pilot of innate immune responses. Cell Host Microbe 4:198-208.
    • (2008) Cell Host Microbe , vol.4 , pp. 198-208
    • Yu, H.B.1    Finlay, B.B.2
  • 63
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao, M., F. Antunes, J. W. Eaton, and U. T. Brunk. 2003. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis. Eur. J. Biochem. 270:3778-3786.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 64
    • 0035861903 scopus 로고    scopus 로고
    • Delayed oxidant-induced cell death involves activation of phospholipase A2
    • DOI 10.1016/S0014-5793(01)03184-2, PII S0014579301031842
    • Zhao, M., U. T. Brunk, and J. W. Eaton. 2001. Delayed oxidant-induced cell death involves activation of phospholipase A2. FEBS Lett. 509:399-404. (Pubitemid 34031968)
    • (2001) FEBS Letters , vol.509 , Issue.3 , pp. 399-404
    • Zhao, M.1    Brunk, U.T.2    Eaton, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.