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Volumn 21, Issue 11, 2009, Pages 1239-1249

Recombinant YopJ induces apoptosis in murine peritoneal macrophages in vitro : Involvement of mitochondrial death pathway

Author keywords

Cell death; RYopJ; Yersinia

Indexed keywords

CASPASE; CASPASE 3; CASPASE 8; CELL PROTEIN; CYTOCHALASIN B; CYTOCHROME C; LIPOCORTIN 5; MATRIX METALLOPROTEINASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BID; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN J;

EID: 71049166694     PISSN: 09538178     EISSN: 14602377     Source Type: Journal    
DOI: 10.1093/intimm/dxp086     Document Type: Article
Times cited : (5)

References (52)
  • 2
    • 0031002852 scopus 로고    scopus 로고
    • Yersinia enterocolitica: The charisma continues
    • Bottone, E. J. 1997. Yersinia enterocolitica: The charisma continues. Clin. Microbiol. Rev. 10:257.
    • (1997) Clin. Microbiol. Rev , vol.10 , pp. 257
    • Bottone, E.J.1
  • 3
    • 0025781733 scopus 로고
    • Factors promoting acute and chronic diseases caused by yersiniae
    • Brubaker, R. R. 1991. Factors promoting acute and chronic diseases caused by yersiniae. Clin. Microbiol. Rev. 4:309.
    • (1991) Clin. Microbiol. Rev , vol.4 , pp. 309
    • Brubaker, R.R.1
  • 5
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R. and Wolf-Watz, H. 1997. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23:861.
    • (1997) Mol. Microbiol , vol.23 , pp. 861
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 6
    • 0036322385 scopus 로고    scopus 로고
    • Yersinia type III secretion: Send in the effectors
    • Cornelis, G. R. 2002. Yersinia type III secretion: Send in the effectors. J. Cell Biol. 158:401.
    • (2002) J. Cell Biol , vol.158 , pp. 401
    • Cornelis, G.R.1
  • 7
    • 0030913232 scopus 로고    scopus 로고
    • Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • Black, D. S. and Bliska, J. B. 1997. Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 16:2730.
    • (1997) EMBO J , vol.16 , pp. 2730
    • Black, D.S.1    Bliska, J.B.2
  • 8
    • 0030978909 scopus 로고    scopus 로고
    • The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
    • Persson, C., Carballeira, N., Wolf-Watz, H. and Fallman, M. 1997. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 16: 2307.
    • (1997) EMBO J , vol.16 , pp. 2307
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fallman, M.4
  • 9
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth, K., Palmer, L. E., Bao, Z. Q. et al. 1999. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science 285:1920.
    • (1999) Science , vol.285 , pp. 1920
    • Orth, K.1    Palmer, L.E.2    Bao, Z.Q.3
  • 10
    • 0031775572 scopus 로고    scopus 로고
    • The yopJ locus is required for Yersinia-mediated inhibition of NF-kappaB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity
    • Schesser, K., Spiik, A. K., Dukuzumuremyi, J. M., Neurath, M. F., Pettersson, S. and Wolf-Watz, H. 1998. The yopJ locus is required for Yersinia-mediated inhibition of NF-kappaB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity. Mol. Microbiol. 28:1067.
    • (1998) Mol. Microbiol , vol.28 , pp. 1067
    • Schesser, K.1    Spiik, A.K.2    Dukuzumuremyi, J.M.3    Neurath, M.F.4    Pettersson, S.5    Wolf-Watz, H.6
  • 11
    • 0030780833 scopus 로고    scopus 로고
    • Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis
    • Ruckdeschel, K., Roggenkamp, A., Lafont, V., Mangeat, P., Heesemann, J. and Rouot, B. 1997. Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis. Infect. Immun. 65:4813.
    • (1997) Infect. Immun , vol.65 , pp. 4813
    • Ruckdeschel, K.1    Roggenkamp, A.2    Lafont, V.3    Mangeat, P.4    Heesemann, J.5    Rouot, B.6
  • 12
    • 0030985415 scopus 로고    scopus 로고
    • Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death
    • Monack, D. M., Mecsas, J., Ghori, N. and Falkow, S. 1997. Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death. Proc. Natl Acad. Sci. USA 94:10385.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10385
    • Monack, D.M.1    Mecsas, J.2    Ghori, N.3    Falkow, S.4
  • 13
    • 0030730859 scopus 로고    scopus 로고
    • Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms and involving YopP, presumably acting as an effector protein
    • Mills, S. D., Boland, A., Sory, M. P. et al. 1997. Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms and involving YopP, presumably acting as an effector protein. Proc. Natl Acad. Sci. USA 94:12638.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12638
    • Mills, S.D.1    Boland, A.2    Sory, M.P.3
  • 14
    • 20444413447 scopus 로고    scopus 로고
    • Inhibition of MAPK and NF-κB pathways is necessary for rapid apoptosis in macrophages infected with Yersinia
    • Zhang, Y., Ting, A. T., Marcu, K. B. and Bliska, J. B. 2005. Inhibition of MAPK and NF-κB pathways is necessary for rapid apoptosis in macrophages infected with Yersinia. J. Immunol. 174:7939.
    • (2005) J. Immunol , vol.174 , pp. 7939
    • Zhang, Y.1    Ting, A.T.2    Marcu, K.B.3    Bliska, J.B.4
  • 15
    • 0031744367 scopus 로고    scopus 로고
    • Yersinia induced apoptosis in vivo aids in the establishment of a systemic infection of mice
    • Monack, D. M., Mecsas, J., Bouley, D. and Falkow, S. 1998. Yersinia induced apoptosis in vivo aids in the establishment of a systemic infection of mice. J. Exp. Med. 188:2127.
    • (1998) J. Exp. Med , vol.188 , pp. 2127
    • Monack, D.M.1    Mecsas, J.2    Bouley, D.3    Falkow, S.4
  • 16
    • 0034711403 scopus 로고    scopus 로고
    • Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease
    • Orth, K., Xu, Z., Mudgett, M. B. et al. 2000. Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. Science 290:1594.
    • (2000) Science , vol.290 , pp. 1594
    • Orth, K.1    Xu, Z.2    Mudgett, M.B.3
  • 17
    • 9244251566 scopus 로고    scopus 로고
    • Yersinia enterocolitica induces apoptosis and inhibits surface molecule expression and cytokine production in murine dendritic cells
    • Erfurth, S. E., Grobner, S., Kramer, U. et al. 2004. Yersinia enterocolitica induces apoptosis and inhibits surface molecule expression and cytokine production in murine dendritic cells. Infect. Immun. 72:7045.
    • (2004) Infect. Immun , vol.72 , pp. 7045
    • Erfurth, S.E.1    Grobner, S.2    Kramer, U.3
  • 18
    • 0141923688 scopus 로고    scopus 로고
    • A dominant role of Toll-like receptor 4 in the signaling of apoptosis in bacteria-faced macrophages
    • Haase, R., Kirschning, C. J., Sing, A. et al. 2003. A dominant role of Toll-like receptor 4 in the signaling of apoptosis in bacteria-faced macrophages. J. Immunol. 171:4294.
    • (2003) J. Immunol , vol.171 , pp. 4294
    • Haase, R.1    Kirschning, C.J.2    Sing, A.3
  • 19
    • 29144435082 scopus 로고    scopus 로고
    • Yersinia outer protein P suppresses TGF-beta-activated kinase-1 activity to impair innate immune signaling in Yersinia enterocolitica-infected cells
    • Haase, R., Richter, K., Pfaffinger, G., Courtois, G. and Ruckdeschel, K. 2005. Yersinia outer protein P suppresses TGF-beta-activated kinase-1 activity to impair innate immune signaling in Yersinia enterocolitica-infected cells. J. Immunol. 175:8209.
    • (2005) J. Immunol , vol.175 , pp. 8209
    • Haase, R.1    Richter, K.2    Pfaffinger, G.3    Courtois, G.4    Ruckdeschel, K.5
  • 20
    • 27944471038 scopus 로고    scopus 로고
    • Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation
    • Zhou, H., Monack, D. M., Kayagaki, N. et al. 2005. Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation. J. Exp. Med. 202:1327.
    • (2005) J. Exp. Med , vol.202 , pp. 1327
    • Zhou, H.1    Monack, D.M.2    Kayagaki, N.3
  • 21
    • 33747794347 scopus 로고    scopus 로고
    • Thiefes, A., Wolf, A., Doerrie, A. et al. 2006. The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway. EMBO Rep. 7:838.
    • Thiefes, A., Wolf, A., Doerrie, A. et al. 2006. The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway. EMBO Rep. 7:838.
  • 22
    • 0035253695 scopus 로고    scopus 로고
    • Yersinia outer protein P of Yersinia enterocolitica simultaneously blocks the nuclear factor-kappa B pathway and exploits lipopolysaccharide signaling to trigger apoptosis in macrophages
    • Ruckdeschel, K., Mannel, O., Richter, K. et al. 2001. Yersinia outer protein P of Yersinia enterocolitica simultaneously blocks the nuclear factor-kappa B pathway and exploits lipopolysaccharide signaling to trigger apoptosis in macrophages. J. Immunol. 166:1823.
    • (2001) J. Immunol , vol.166 , pp. 1823
    • Ruckdeschel, K.1    Mannel, O.2    Richter, K.3
  • 23
    • 33845480946 scopus 로고    scopus 로고
    • Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling
    • Mittal, R., Peak-Chew, S. Y. and McMahon, H. T. 2006. Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling. Proc. Natl Acad. Sci. USA 103:18574.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18574
    • Mittal, R.1    Peak-Chew, S.Y.2    McMahon, H.T.3
  • 24
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • Mukherjee, S., Keitany, G., Li, Y. et al. 2006. Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312:1211.
    • (2006) Science , vol.312 , pp. 1211
    • Mukherjee, S.1    Keitany, G.2    Li, Y.3
  • 25
    • 0033009890 scopus 로고    scopus 로고
    • The central effectors of cell death in the immune system
    • Rathmell, J. C. and Thompson, C. B. 1999. The central effectors of cell death in the immune system. Annu. Rev. Immunol. 17:781.
    • (1999) Annu. Rev. Immunol , vol.17 , pp. 781
    • Rathmell, J.C.1    Thompson, C.B.2
  • 26
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M. O. 2000. The biochemistry of apoptosis. Nature 407:770.
    • (2000) Nature , vol.407 , pp. 770
    • Hengartner, M.O.1
  • 27
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • Fischer, U., Janicke, R. U. and Schulze-Osthoff, K. 2003. Many cuts to ruin: A comprehensive update of caspase substrates. Cell Death Differ. 10:76.
    • (2003) Cell Death Differ , vol.10 , pp. 76
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 28
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist, M. and Jaattela, M. 2001. Four deaths and a funeral: From caspases to alternative mechanisms. Nat. Rev. Mol. Cell Biol. 2:589.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 589
    • Leist, M.1    Jaattela, M.2
  • 29
    • 0035211935 scopus 로고    scopus 로고
    • Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis
    • Rudner, J., Lepple-Wienhues, A., Budach, W. et al. 2001. Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis. J. Cell Sci. 114:4161.
    • (2001) J. Cell Sci , vol.114 , pp. 4161
    • Rudner, J.1    Lepple-Wienhues, A.2    Budach, W.3
  • 30
    • 0242412240 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins induce lymphocyte apoptosis by activating the mitochondrial apoptosis pathway independent of external death receptor signaling
    • Nencioni, A., Lauber, K., Grunebach, F. et al. 2003. Cyclopentenone prostaglandins induce lymphocyte apoptosis by activating the mitochondrial apoptosis pathway independent of external death receptor signaling. J. Immunol. 171:5148.
    • (2003) J. Immunol , vol.171 , pp. 5148
    • Nencioni, A.1    Lauber, K.2    Grunebach, F.3
  • 32
    • 0037305877 scopus 로고    scopus 로고
    • Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation
    • Leverkus, M., Sprick, M. R., Wachter, T. et al. 2003. Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation. Mol. Cell. Biol. 23:777.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 777
    • Leverkus, M.1    Sprick, M.R.2    Wachter, T.3
  • 33
    • 20044381271 scopus 로고    scopus 로고
    • A central role for Bid in granzyme B-induced apoptosis
    • Waterhouse, N. J., Sedelies, K. A., Browne, K. A. et al. 2005. A central role for Bid in granzyme B-induced apoptosis. J. Biol. Chem. 280:4476.
    • (2005) J. Biol. Chem , vol.280 , pp. 4476
    • Waterhouse, N.J.1    Sedelies, K.A.2    Browne, K.A.3
  • 34
    • 38949116573 scopus 로고    scopus 로고
    • Structural requirements for Yersinia YopJ inhibition of MAP kinase pathways
    • Hao, Y.-H., Wang, Y., Burdette, D. et al. 2008. Structural requirements for Yersinia YopJ inhibition of MAP kinase pathways. PLoS ONE 3:e1375.
    • (2008) PLoS ONE , vol.3
    • Hao, Y.-H.1    Wang, Y.2    Burdette, D.3
  • 35
  • 36
    • 0021564388 scopus 로고
    • The cell biology of macrophage activation
    • Adam, D. O. and Hamilton, T. A. 1984. The cell biology of macrophage activation. Annu. Rev. Immun. 2:283.
    • (1984) Annu. Rev. Immun , vol.2 , pp. 283
    • Adam, D.O.1    Hamilton, T.A.2
  • 37
    • 0023907091 scopus 로고
    • Macrophage-mediated tumoricidal activity: Mechanisms of activation and cytotoxicity
    • Drysdale, B. E., Agarwal, S. and Shin, H. S. 1988. Macrophage-mediated tumoricidal activity: Mechanisms of activation and cytotoxicity. Prog. Allergy 40:111.
    • (1988) Prog. Allergy , vol.40 , pp. 111
    • Drysdale, B.E.1    Agarwal, S.2    Shin, H.S.3
  • 38
    • 0344643405 scopus 로고    scopus 로고
    • The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through Toll-like receptor-2
    • Lopez, M., Sly, L. M., Luu, Y., Young, D., Cooper, H. and Reiner, N. E. 2003. The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through Toll-like receptor-2. J. Immunol. 170:2409.
    • (2003) J. Immunol , vol.170 , pp. 2409
    • Lopez, M.1    Sly, L.M.2    Luu, Y.3    Young, D.4    Cooper, H.5    Reiner, N.E.6
  • 39
    • 34248671986 scopus 로고    scopus 로고
    • The ESAT-6 protein of Mycobacterium tuberculosis induces apoptosis of macrophages by activating the caspase expression
    • Derrick, S. C. and Morris, S. L. 2007. The ESAT-6 protein of Mycobacterium tuberculosis induces apoptosis of macrophages by activating the caspase expression. Cell. Microbiol. 9:1547.
    • (2007) Cell. Microbiol , vol.9 , pp. 1547
    • Derrick, S.C.1    Morris, S.L.2
  • 40
    • 33644816989 scopus 로고    scopus 로고
    • Virulence markers of LCR plasmid in Indian isolates of Yersinia pestis
    • Khushiramani, R., Tuteja, U., Shukla, J., Panikkar, A. and Batra, H. V. 2006. Virulence markers of LCR plasmid in Indian isolates of Yersinia pestis. APMIS 114:15.
    • (2006) APMIS , vol.114 , pp. 15
    • Khushiramani, R.1    Tuteja, U.2    Shukla, J.3    Panikkar, A.4    Batra, H.V.5
  • 41
    • 0035662338 scopus 로고    scopus 로고
    • Regulation of nitric oxide production by murine peritoneal macrophages treated in vitro with chemokine monocyte chemoattractant protein 1
    • Biswas, S. K., Sodhi, A. and Paul, S. 2001. Regulation of nitric oxide production by murine peritoneal macrophages treated in vitro with chemokine monocyte chemoattractant protein 1. Nitric Oxide 5:566.
    • (2001) Nitric Oxide , vol.5 , pp. 566
    • Biswas, S.K.1    Sodhi, A.2    Paul, S.3
  • 42
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. 1983. Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. J. Immunol. Methods 65:55.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55
    • Mosmann, T.1
  • 43
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi, C., Poderoso, J. J. and Boveris, A. 1998. Production of nitric oxide by mitochondria. J. Biol. Chem. 273:11038.
    • (1998) J. Biol. Chem , vol.273 , pp. 11038
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 44
    • 0032724044 scopus 로고    scopus 로고
    • The induction of apoptosis by bacterial pathogens
    • Weinrauch, Y. and Zychlinsky, A. 1999. The induction of apoptosis by bacterial pathogens. Annu. Rev. Microbiol. 53:155.
    • (1999) Annu. Rev. Microbiol , vol.53 , pp. 155
    • Weinrauch, Y.1    Zychlinsky, A.2
  • 45
    • 0032489918 scopus 로고    scopus 로고
    • Yersinia enterocolitica impairs activation of transcription factor NF-κB: Involvement in the induction of programmed cell death and in the suppression of the macrophage tumor necrosis factor alpha production
    • Ruckdeschel, K., Harb, S., Roggenkamp, A. et al. 1998. Yersinia enterocolitica impairs activation of transcription factor NF-κB: involvement in the induction of programmed cell death and in the suppression of the macrophage tumor necrosis factor alpha production. J. Exp. Med. 187:1069.
    • (1998) J. Exp. Med , vol.187 , pp. 1069
    • Ruckdeschel, K.1    Harb, S.2    Roggenkamp, A.3
  • 46
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioner of apoptosis
    • Cohen, G. M. 1997. Caspases: The executioner of apoptosis. Biochem. J. 326:1.
    • (1997) Biochem. J , vol.326 , pp. 1
    • Cohen, G.M.1
  • 47
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher, S., Osen-Sand, A., Nichols, A. et al. 1999. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J. Cell Biol. 144: 891.
    • (1999) J. Cell Biol , vol.144 , pp. 891
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 48
    • 0035827710 scopus 로고    scopus 로고
    • Yersinia enterocolitica YopP-induced apoptosis of macrophages involves the apoptotic signaling cascade upstream of bid
    • Denecker, G., Declercq, W., Geuijen, C. A. et al. 2001. Yersinia enterocolitica YopP-induced apoptosis of macrophages involves the apoptotic signaling cascade upstream of bid. J. Biol. Chem. 276:19706.
    • (2001) J. Biol. Chem , vol.276 , pp. 19706
    • Denecker, G.1    Declercq, W.2    Geuijen, C.A.3
  • 49
    • 0037372795 scopus 로고    scopus 로고
    • Role of Toll-like receptor signaling in the apoptotic response of macrophages to Yersinia infection
    • Zhang, Y. and Bliska, J. B. 2003. Role of Toll-like receptor signaling in the apoptotic response of macrophages to Yersinia infection. Infect. Immun. 71:1513.
    • (2003) Infect. Immun , vol.71 , pp. 1513
    • Zhang, Y.1    Bliska, J.B.2
  • 50
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross, A., Yin, X. M., Wang, K. et al. 1999. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J. Biol. Chem. 274:1156.
    • (1999) J. Biol. Chem , vol.274 , pp. 1156
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 51
    • 33646882912 scopus 로고    scopus 로고
    • Suppression of Alveolar macrophages apoptosis prolongs survival of rats and mice with pneumocystis pneumonia
    • Lasbury, M. E., Durant, P. J., Ray, C. A., Tschang, D., Schwendener, R. and Lee, C. H. 2006. Suppression of Alveolar macrophages apoptosis prolongs survival of rats and mice with pneumocystis pneumonia. J. Immunol. 176:6443.
    • (2006) J. Immunol , vol.176 , pp. 6443
    • Lasbury, M.E.1    Durant, P.J.2    Ray, C.A.3    Tschang, D.4    Schwendener, R.5    Lee, C.H.6
  • 52
    • 0016298145 scopus 로고
    • Inhibition of phagocytosis and plasma membrane mobility of the cultured macrophages by cytochalasin B
    • Axline, S. G. and Reaven, E. P. 1974. Inhibition of phagocytosis and plasma membrane mobility of the cultured macrophages by cytochalasin B. J. Cell Biol. 62:647.
    • (1974) J. Cell Biol , vol.62 , pp. 647
    • Axline, S.G.1    Reaven, E.P.2


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