메뉴 건너뛰기




Volumn 53, Issue , 1999, Pages 155-187

The induction of apoptosis by bacterial pathogens

Author keywords

Bacteria; Effectors; Infections; Toxins; Virulence

Indexed keywords

APOPTOSIS; BACTERIAL INFECTION; CELL DEATH; HOST RESISTANCE; IMMUNOCOMPETENT CELL; INFLAMMATION; PRIORITY JOURNAL; REVIEW; TREATMENT OUTCOME; VIRULENCE;

EID: 0032724044     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.53.1.155     Document Type: Review
Times cited : (346)

References (263)
  • 1
    • 0027189548 scopus 로고
    • Growth rate paradox of Salmonella typhimurium within macrophages
    • Abshire K, Neidhardt F. 1993. Growth rate paradox of Salmonella typhimurium within macrophages. J. Bacteriol. 175:3744-48
    • (1993) J. Bacteriol. , vol.175 , pp. 3744-3748
    • Abshire, K.1    Neidhardt, F.2
  • 2
    • 0022342760 scopus 로고
    • Minimal requirements for exocytosis: A study using PC12 cell permeabilized with staphylococcal alpha-toxin
    • Ahnert-Hilger G, Bhakdi S, Gratzl M. 1985. Minimal requirements for exocytosis: a study using PC12 cell permeabilized with staphylococcal alpha-toxin. J. Biol. Chem. 260:12730-34
    • (1985) J. Biol. Chem. , vol.260 , pp. 12730-12734
    • Ahnert-Hilger, G.1    Bhakdi, S.2    Gratzl, M.3
  • 3
  • 4
    • 0030802038 scopus 로고    scopus 로고
    • Rho proteins: Targets for bacterial toxins
    • Aktories K. 1997. Rho proteins: targets for bacterial toxins. Trends Microbiol. 7:282-88
    • (1997) Trends Microbiol. , vol.7 , pp. 282-288
    • Aktories, K.1
  • 5
    • 0030473860 scopus 로고    scopus 로고
    • Bacterial pathogens in plants: Life up against the wall
    • Alfano JR, Collmer A. 1996. Bacterial pathogens in plants: life up against the wall. Plant Cell 8:1683-98
    • (1996) Plant Cell , vol.8 , pp. 1683-1698
    • Alfano, J.R.1    Collmer, A.2
  • 7
    • 0028117273 scopus 로고
    • Salmonella stimulate macrophage macropinocytosis and persist within spacious phagosomes
    • Alpuche-Aranda CM, Racoosin EL, Swanson JA, Miller SI. 1994. Salmonella stimulate macrophage macropinocytosis and persist within spacious phagosomes. J. Exp. Med. 179:601-8
    • (1994) J. Exp. Med. , vol.179 , pp. 601-608
    • Alpuche-Aranda, C.M.1    Racoosin, E.L.2    Swanson, J.A.3    Miller, S.I.4
  • 8
    • 0028949289 scopus 로고
    • Characterization of Pseudomonas aeruginosa-induced MDCK cell injury: Glycosylation defective host cells are resistant to bacterial killing
    • Apodaca G, Bomsel M, Lindstedt R, Engel J, Frank D, et al. 1995. Characterization of Pseudomonas aeruginosa-induced MDCK cell injury: glycosylation defective host cells are resistant to bacterial killing. Infect. Immun. 63:1541-51
    • (1995) Infect. Immun. , vol.63 , pp. 1541-1551
    • Apodaca, G.1    Bomsel, M.2    Lindstedt, R.3    Engel, J.4    Frank, D.5
  • 10
    • 0027525167 scopus 로고
    • Adhesion of Bordetella pertussis to eukaryotic cells requires a time-dependent export and maturation of filamentous hemagglutinin
    • Arico B, Nuti S, Scarlato V, Rappuoli R. 1993. Adhesion of Bordetella pertussis to eukaryotic cells requires a time-dependent export and maturation of filamentous hemagglutinin. Proc. Natl. Acad. Sci. USA 90:9204-8
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9204-9208
    • Arico, B.1    Nuti, S.2    Scarlato, V.3    Rappuoli, R.4
  • 11
    • 0029929118 scopus 로고    scopus 로고
    • In vivo activation of Y cell induction into the primed phenotype and programmed cell death by staphylococcal enterotoxin B
    • Aroeira L, Moreno M, Martinez C. 1996. In vivo activation of Y cell induction into the primed phenotype and programmed cell death by staphylococcal enterotoxin B. Scand. J. Immunol. 43:545-50
    • (1996) Scand. J. Immunol. , vol.43 , pp. 545-550
    • Aroeira, L.1    Moreno, M.2    Martinez, C.3
  • 12
    • 0001401761 scopus 로고
    • Involvement of plasma membrane calcium influx in bacterial induction of the K+/H+ and hypersensitive responses in tobacco
    • Atkinson MM, Keppler LD, Oralandi EW, Baker JC, Mischki CF. 1990. Involvement of plasma membrane calcium influx in bacterial induction of the K+/H+ and hypersensitive responses in tobacco. Plant Physiol. 92:215-21
    • (1990) Plant Physiol. , vol.92 , pp. 215-221
    • Atkinson, M.M.1    Keppler, L.D.2    Oralandi, E.W.3    Baker, J.C.4    Mischki, C.F.5
  • 13
    • 0030013337 scopus 로고    scopus 로고
    • Transcriptional activation by p53, but not induction of the p21 gene, is essential for oncogene-mediated apoptosis
    • Attardi LD, Lowe SW, Brugarolas J, Jacks T. 1996. Transcriptional activation by p53, but not induction of the p21 gene, is essential for oncogene-mediated apoptosis. EMBO J. 15:3693-701
    • (1996) EMBO J. , vol.15 , pp. 3693-3701
    • Attardi, L.D.1    Lowe, S.W.2    Brugarolas, J.3    Jacks, T.4
  • 14
    • 0027054511 scopus 로고
    • In vivo neutralization of tumor necrosis factor alpha and interferon-gamma abrogates resistance to Yersinia enterocolitica infection in mice
    • Autenrieth IB, Heesemann J. 1992. In vivo neutralization of tumor necrosis factor alpha and interferon-gamma abrogates resistance to Yersinia enterocolitica infection in mice. Med. Microbiol. Immunol. 181:333-38
    • (1992) Med. Microbiol. Immunol. , vol.181 , pp. 333-338
    • Autenrieth, I.B.1    Heesemann, J.2
  • 15
    • 0028174061 scopus 로고
    • Function and activation of NF-kB in the immune system
    • Baeuerle P, Henkel T. 1994. Function and activation of NF-kB in the immune system. Annu. Rev. Immunol. 12:141-79
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.1    Henkel, T.2
  • 18
    • 0021934042 scopus 로고
    • Cloning the chromosomal breakpoint of t(14;18) human lymphomas: Clustering around JH on chromosome 14 and near a transcriptional unit on 18
    • Bakhshi A, Jensen JP, Goldman P, Wright JJ, McBride OW, Epstein AL, Korsmeyer SJ. 1985. Cloning the chromosomal breakpoint of t(14;18) human lymphomas: clustering around JH on chromosome 14 and near a transcriptional unit on 18. Cell 41: 899-906
    • (1985) Cell , vol.41 , pp. 899-906
    • Bakhshi, A.1    Jensen, J.P.2    Goldman, P.3    Wright, J.J.4    McBride, O.W.5    Epstein, A.L.6    Korsmeyer, S.J.7
  • 19
    • 0032167519 scopus 로고    scopus 로고
    • Pathogenic Mycobacterium tuberculosis evades apoptosis of host macrophages by release of TNF-R2, resulting in inactivation of TNF-a
    • Balcewicz-Sablinska MK, Keane J, Kornfeld H, Remold HG. 1998. Pathogenic Mycobacterium tuberculosis evades apoptosis of host macrophages by release of TNF-R2, resulting in inactivation of TNF-a. J. Immunol. 161:2636-41
    • (1998) J. Immunol. , vol.161 , pp. 2636-2641
    • Balcewicz-Sablinska, M.K.1    Keane, J.2    Kornfeld, H.3    Remold, H.G.4
  • 20
    • 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: 4075-81
    • (1997) Infect. Immun. , vol.65 , pp. 4075-4081
    • Barsig, J.1    Kaufmann, S.H.2
  • 21
    • 0031976003 scopus 로고    scopus 로고
    • Intracellular Staphylococcus aureus escapes the endosome and induces apoptosis in epithelial cells
    • Bayles KW, Wesson CA, Liou LE, Fox LK, Bohach GA, Trumble WR. 1998. Intracellular Staphylococcus aureus escapes the endosome and induces apoptosis in epithelial cells. Infect. Immun. 66:336-42
    • (1998) Infect. Immun. , vol.66 , pp. 336-342
    • Bayles, K.W.1    Wesson, C.A.2    Liou, L.E.3    Fox, L.K.4    Bohach, G.A.5    Trumble, W.R.6
  • 22
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kB in preventing TNFa-induced cell death
    • Beg AA, Baltimore D. 1996. An essential role for NF-kB in preventing TNFa-induced cell death. Science 274:782-84
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 23
    • 0029021898 scopus 로고
    • Mathematical analysis of activation thresholds in enzyme-catalyzed positive feedbacks: Application to the feedbacks of blood coagulation
    • Beltrami E, Jesty J. 1995. Mathematical analysis of activation thresholds in enzyme-catalyzed positive feedbacks: application to the feedbacks of blood coagulation. Proc. Natl. Acad. Sci. USA 92:8744-48
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8744-8748
    • Beltrami, E.1    Jesty, J.2
  • 24
    • 0030476449 scopus 로고    scopus 로고
    • Plant disease resistance genes: Function meets structure
    • Bent AF. 1996. Plant disease resistance genes: function meets structure. Plant Cell 8:1757-71
    • (1996) Plant Cell , vol.8 , pp. 1757-1771
    • Bent, A.F.1
  • 25
    • 0028923946 scopus 로고
    • Bacterial evasion of host immune defense: Yersinia enterocolitica encodes a suppressor for tumor necrosis factor alpha expression
    • Beuscher HU, Rödel F, Forsberg Å, Röllinghoff M. 1995. Bacterial evasion of host immune defense: Yersinia enterocolitica encodes a suppressor for tumor necrosis factor alpha expression. Infect. Immun. 63:1270-77
    • (1995) Infect. Immun. , vol.63 , pp. 1270-1277
    • Beuscher, H.U.1    Rödel, F.2    Forsberg, Å.3    Röllinghoff, M.4
  • 27
    • 0029043658 scopus 로고
    • Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach
    • Blaser MJ, Perez-Perez GI, Kleanthous H, Cover TL, Peek RM, et al. 1995. Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach. Cancer Res. 55:2111-15
    • (1995) Cancer Res. , vol.55 , pp. 2111-2115
    • Blaser, M.J.1    Perez-Perez, G.I.2    Kleanthous, H.3    Cover, T.L.4    Peek, R.M.5
  • 29
    • 0031899661 scopus 로고    scopus 로고
    • Role of YopP in suppression of tumor necrosis factor alpha release by macrophages during Yersinia infection
    • Boland A, Cornelis GR. 1998. Role of YopP in suppression of tumor necrosis factor alpha release by macrophages during Yersinia infection. Infect. Immun. 66:1878-84
    • (1998) Infect. Immun. , vol.66 , pp. 1878-1884
    • Boland, A.1    Cornelis, G.R.2
  • 30
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-l- and TNF receptor-induced cell death
    • Boldin MP, Goncharov TM, Goltsev YV, Wallach D. 1996. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-l- and TNF receptor-induced cell death. Cell 85:803-15
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 31
    • 0028985261 scopus 로고
    • Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APOI prompts signaling for TNF and Fas/APOI effects
    • Boldin MP, Mett IL, Vafolomeev EE, Chumakov I, Shemer-Avni Y, Camonis JH, Wallach D. 1995. Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APOI prompts signaling for TNF and Fas/APOI effects. J. Biol. Chem. 270:387-91
    • (1995) J. Biol. Chem. , vol.270 , pp. 387-391
    • Boldin, M.P.1    Mett, I.L.2    Vafolomeev, E.E.3    Chumakov, I.4    Shemer-Avni, Y.5    Camonis, J.H.6    Wallach, D.7
  • 32
    • 0028812606 scopus 로고
    • Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins
    • Boyd JM, Gallo GJ, Elangovan B, Houghton AB, Malstrom S, Avery BJ, et al. 1995. Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. Oncogene 11:1921-28
    • (1995) Oncogene , vol.11 , pp. 1921-1928
    • Boyd, J.M.1    Gallo, G.J.2    Elangovan, B.3    Houghton, A.B.4    Malstrom, S.5    Avery, B.J.6
  • 33
    • 0029614765 scopus 로고
    • Neural apoptosis
    • Bredesen DE. 1995. Neural apoptosis. Ann. Neurol. 38:839-51
    • (1995) Ann. Neurol. , vol.38 , pp. 839-851
    • Bredesen, D.E.1
  • 34
    • 0028889656 scopus 로고
    • Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1
    • Brinkmann U, Brinkmann E, Gallo M, Pastan I. 1995. Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1. Proc. Natl. Acad. Sci. USA 92:10427-31
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10427-10431
    • Brinkmann, U.1    Brinkmann, E.2    Gallo, M.3    Pastan, I.4
  • 35
    • 0029953768 scopus 로고    scopus 로고
    • Role of CAS, a human homologue to the yeast chromosome segregation gene CSE1, in toxin and tumor necrosis factor mediated apoptosis
    • Brinkmann U, Brinkmann E, Gallo M, Scherf U, Pastan I. 1996. Role of CAS, a human homologue to the yeast chromosome segregation gene CSE1, in toxin and tumor necrosis factor mediated apoptosis. Biochemistry 35:6891-99
    • (1996) Biochemistry , vol.35 , pp. 6891-6899
    • Brinkmann, U.1    Brinkmann, E.2    Gallo, M.3    Scherf, U.4    Pastan, I.5
  • 36
    • 0024593717 scopus 로고
    • Intracellular survival of wild-type Salmonella typhimurium and macrophage-sensitive mutants in diverse populations of macrophages
    • Buchmeier N, Heffron F. 1989. Intracellular survival of wild-type Salmonella typhimurium and macrophage-sensitive mutants in diverse populations of macrophages, Infect. Immun. 57:1-7
    • (1989) Infect. Immun. , vol.57 , pp. 1-7
    • Buchmeier, N.1    Heffron, F.2
  • 37
    • 0021739258 scopus 로고
    • Escherichia coli alpha hemolysin: Characteristics and probable role in pathogenicity
    • Cavalieri S, Bohach G, Snyder I. 1984. Escherichia coli alpha hemolysin: characteristics and probable role in pathogenicity. Microbiol. Rev. 48:326-43
    • (1984) Microbiol. Rev. , vol.48 , pp. 326-343
    • Cavalieri, S.1    Bohach, G.2    Snyder, I.3
  • 38
    • 0024458557 scopus 로고
    • Internucleosomal DNA cleavage precedes diphtheria toxin induced cytolysis
    • Chang M, Bramhal J, Graves S, Bonavida B, Wisnieski B. 1989. Internucleosomal DNA cleavage precedes diphtheria toxin induced cytolysis. J. Biol. Chem. 264:15261-67
    • (1989) J. Biol. Chem. , vol.264 , pp. 15261-15267
    • Chang, M.1    Bramhal, J.2    Graves, S.3    Bonavida, B.4    Wisnieski, B.5
  • 39
    • 0024380924 scopus 로고
    • Second cytotoxic pathway of diphtheria toxin suggested by nuclease activity
    • Chang M, Baldwin R, Bruce C, Wisnieski B. 1989. Second cytotoxic pathway of diphtheria toxin suggested by nuclease activity. Science 246:1165-68
    • (1989) Science , vol.246 , pp. 1165-1168
    • Chang, M.1    Baldwin, R.2    Bruce, C.3    Wisnieski, B.4
  • 40
    • 0025282524 scopus 로고
    • Comparison of the intoxication pathways on tumor necrosis factor and diphtheria toxin
    • Chang M, Wisnieski B. 1990. Comparison of the intoxication pathways on tumor necrosis factor and diphtheria toxin. Infect. Immun. 58:2644-50
    • (1990) Infect. Immun. , vol.58 , pp. 2644-2650
    • Chang, M.1    Wisnieski, B.2
  • 41
    • 0031876318 scopus 로고    scopus 로고
    • mcl-I is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling pathway and is one component of the GM-CSF viability response
    • Chao JR, Wang JM, Lee SF, Peng HW, Lin YH, Chou CH, et al. 1998. mcl-I is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling pathway and is one component of the GM-CSF viability response. Mol. Cell. Biol. 18:4883-98
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4883-4898
    • Chao, J.R.1    Wang, J.M.2    Lee, S.F.3    Peng, H.W.4    Lin, Y.H.5    Chou, C.H.6
  • 42
    • 0031581082 scopus 로고    scopus 로고
    • Apoptosis in gastric epithelial cells is induced by Helicobacter pylori and accompanied by increased expression of BAK
    • Chen G, Sordillo EM, Ramey WG, Reidy J, Holt PR, et al. 1997. Apoptosis in gastric epithelial cells is induced by Helicobacter pylori and accompanied by increased expression of BAK. Biochem. Biophys. Res. Commun. 239:626-32
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 626-632
    • Chen, G.1    Sordillo, E.M.2    Ramey, W.G.3    Reidy, J.4    Holt, P.R.5
  • 43
    • 0029818081 scopus 로고    scopus 로고
    • Salmonella spp. are cytotoxic for cultured macrophages
    • Chen LM, Kaniga K, Galan JE. 1996. Salmonella spp. are cytotoxic for cultured macrophages. Mol. Microbiol. 21:1101-15
    • (1996) Mol. Microbiol. , vol.21 , pp. 1101-1115
    • Chen, L.M.1    Kaniga, K.2    Galan, J.E.3
  • 44
    • 0029738195 scopus 로고    scopus 로고
    • A bacterial invasin induces macrophage apoptosis by directly binding ICE
    • Chen Y, Smith MR, Thirumalai K, Zychlinsky A. 1996. A bacterial invasin induces macrophage apoptosis by directly binding ICE. EMBO J. 15:3853-60
    • (1996) EMBO J. , vol.15 , pp. 3853-3860
    • Chen, Y.1    Smith, M.R.2    Thirumalai, K.3    Zychlinsky, A.4
  • 45
    • 0028605175 scopus 로고
    • Apoptosis induced by bacterial pathogens
    • Chen Y, Zychlinsky A. 1994. Apoptosis induced by bacterial pathogens. Microb. Pathog. 17:203-12
    • (1994) Microb. Pathog. , vol.17 , pp. 203-212
    • Chen, Y.1    Zychlinsky, A.2
  • 46
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM, 1995. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81:505-12
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 48
    • 0030249877 scopus 로고    scopus 로고
    • The involvement of an ATP gated ion channel, P2X1, in thymocyte apoptosis
    • Chvatchko Y, Valera S, Aubry J, Renno T, Buell G, et al. 1996. The involvement of an ATP gated ion channel, P2X1, in thymocyte apoptosis. Immunity 5:275-83
    • (1996) Immunity , vol.5 , pp. 275-283
    • Chvatchko, Y.1    Valera, S.2    Aubry, J.3    Renno, T.4    Buell, G.5
  • 49
    • 0022971142 scopus 로고
    • Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation
    • Cleary ML, Smith SD, Sklar J. 1986. Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation. Cell 47:19-28
    • (1986) Cell , vol.47 , pp. 19-28
    • Cleary, M.L.1    Smith, S.D.2    Sklar, J.3
  • 50
    • 0032516101 scopus 로고    scopus 로고
    • NF-kB-dependent inhibition of apoptosis is essential for host cell survival during Rickettsia rickettsii infection
    • Clifton DR, Goss RA, Sahni SK, van Antwerp D, Baggs RB, et al. 1998. NF-kB-dependent inhibition of apoptosis is essential for host cell survival during Rickettsia rickettsii infection. Proc. Natl. Acad. Sci. USA 95:4646-51
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4646-4651
    • Clifton, D.R.1    Goss, R.A.2    Sahni, S.K.3    Van Antwerp, D.4    Baggs, R.B.5
  • 51
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis G, Wolf-Watz H. 1997. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23:861-67
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.1    Wolf-Watz, H.2
  • 52
    • 0026643058 scopus 로고
    • Helicobacter pylori and gastroduodenal disease
    • Cover TL, Blaser MJ. 1992. Helicobacter pylori and gastroduodenal disease. Annu. Rev. Med. 43:135-45
    • (1992) Annu. Rev. Med. , vol.43 , pp. 135-145
    • Cover, T.L.1    Blaser, M.J.2
  • 53
    • 0030809535 scopus 로고    scopus 로고
    • Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly
    • Cover TL, Hanson PI, Heuser JE. 1997. Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly. J. Cell. Biol. 138:759-69
    • (1997) J. Cell. Biol. , vol.138 , pp. 759-769
    • Cover, T.L.1    Hanson, P.I.2    Heuser, J.E.3
  • 54
    • 0023546916 scopus 로고
    • Cell death in granulomata: The role of apoptosis
    • Cree I, Nurbhai S, Milne G, Beck J. 1987. Cell death in granulomata: the role of apoptosis. J. Clin. Pathol. 40:1314-19
    • (1987) J. Clin. Pathol. , vol.40 , pp. 1314-1319
    • Cree, I.1    Nurbhai, S.2    Milne, G.3    Beck, J.4
  • 55
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns V, Yuan J. 1998. Proteases to die for. Genes Dev. 12:1551-70
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 56
    • 0027531699 scopus 로고
    • Thymic and peripheral apoptosis of antigen-specific T cells might cooperate in establishing self tolerance
    • D'Adamio L, Awad K, Rcinherz E. 1993. Thymic and peripheral apoptosis of antigen-specific T cells might cooperate in establishing self tolerance. Euro. J. Immunol. 23:747-53
    • (1993) Euro. J. Immunol. , vol.23 , pp. 747-753
    • D'Adamio, L.1    Awad, K.2    Rcinherz, E.3
  • 57
    • 0027998238 scopus 로고
    • The enigmatic avirulence genes of phytopathogenic bacteria
    • Dangel JL. 1994. The enigmatic avirulence genes of phytopathogenic bacteria. Curr. Top. Microbiol. Immunol. 192:99-118
    • (1994) Curr. Top. Microbiol. Immunol. , vol.192 , pp. 99-118
    • Dangel, J.L.1
  • 58
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, Masters S, Fu H, et al. 1997. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery, Cell 91:231-41
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5
  • 59
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez G. 1997, Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278:687-89
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 60
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IkB kinase that activates the transcription factor NF-kB
    • DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E, Karin M. 1997. A cytokine-responsive IkB kinase that activates the transcription factor NF-kB. Nature 388:548-54
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 61
    • 0025345957 scopus 로고
    • Secretion of tissue-type plasminogen activator and plasminogen activator inhibitor by Rickettsia conorii- and Rickettsia rickettsii-infected cultured endothelial cells
    • Drancourt M, Alessi M-C, Levy P-Y, Juhan-Vague I, Raoult D. 1990. Secretion of tissue-type plasminogen activator and plasminogen activator inhibitor by Rickettsia conorii- and Rickettsia rickettsii-infected cultured endothelial cells. Infect. Immun. 58:2459-63
    • (1990) Infect. Immun. , vol.58 , pp. 2459-2463
    • Drancourt, M.1    Alessi, M.-C.2    Levy, P.-Y.3    Juhan-Vague, I.4    Raoult, D.5
  • 62
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, et al. 1998. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391:43-50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5
  • 63
    • 0029036647 scopus 로고
    • Fas ligand mediated cytotoxicity is directly responsible for apoptosis of normal CD4+ T cells responding to a bacterial superantigen
    • Ettinger R, Panka D, Wang J, Stanger B, Ju S, Rothstein A. 1995. Fas ligand mediated cytotoxicity is directly responsible for apoptosis of normal CD4+ T cells responding to a bacterial superantigen. J. Immunol. 154:4320-28
    • (1995) J. Immunol. , vol.154 , pp. 4320-4328
    • Ettinger, R.1    Panka, D.2    Wang, J.3    Stanger, B.4    Ju, S.5    Rothstein, A.6
  • 64
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • Evan G, Littlewood T. 1998. A matter of life and cell death. Science 281:1317-22
    • (1998) Science , vol.281 , pp. 1317-1322
    • Evan, G.1    Littlewood, T.2
  • 66
    • 0030926081 scopus 로고    scopus 로고
    • Temporal effect of tumor necrossis factor-a on murine macrophages infected with Mycobacterium avium
    • Eviks IS, Emerson CL. 1997. Temporal effect of tumor necrossis factor-a on murine macrophages infected with Mycobacterium avium. Infect. Immun. 65:2100-6
    • (1997) Infect. Immun. , vol.65 , pp. 2100-2106
    • Eviks, I.S.1    Emerson, C.L.2
  • 68
    • 0032536526 scopus 로고    scopus 로고
    • Inhibition of apoptosis in Chlamydia-infected cells: Blockade of mitochondrial cytochrome c release and caspase activation
    • Fan T, Lu H, Hu H, Shi L, McClarty GA, et al. 1998. Inhibition of apoptosis in Chlamydia-infected cells: blockade of mitochondrial cytochrome c release and caspase activation. J. Exp. Med. 187:487-96
    • (1998) J. Exp. Med. , vol.187 , pp. 487-496
    • Fan, T.1    Lu, H.2    Hu, H.3    Shi, L.4    McClarty, G.A.5
  • 69
    • 0032543222 scopus 로고    scopus 로고
    • The effect of Class 11 major histocompatibility complex expression on adherence of Helicobacter pylori and induction of apoptosis in gastric epithelial cells: A mechanism for T helper cell type l-mediated damage
    • Fan XJ, Crowe SE, Behar S, Gunasena H, Ye G, Haeberle H, et al. 1998. The effect of Class 11 major histocompatibility complex expression on adherence of Helicobacter pylori and induction of apoptosis in gastric epithelial cells: a mechanism for T helper cell type l-mediated damage. J. Exp. Med. 187:1659-69
    • (1998) J. Exp. Med. , vol.187 , pp. 1659-1669
    • Fan, X.J.1    Crowe, S.E.2    Behar, S.3    Gunasena, H.4    Ye, G.5    Haeberle, H.6
  • 70
    • 0030063866 scopus 로고    scopus 로고
    • Immunopathology of tuberculosis: Roles of macrophages and monocytes
    • Fenton MJ, Vermeulen MW. 1996. Immunopathology of tuberculosis: roles of macrophages and monocytes. Infect. Immun. 64:683-90
    • (1996) Infect. Immun. , vol.64 , pp. 683-690
    • Fenton, M.J.1    Vermeulen, M.W.2
  • 72
  • 73
    • 0028251878 scopus 로고
    • Superantigens produced by infectious pathogens: Molecular mechanism of action and biological significance
    • Fleischer B. 1994. Superantigens produced by infectious pathogens: molecular mechanism of action and biological significance. Int. J. Clin. Lab. Res. 24:193-37
    • (1994) Int. J. Clin. Lab. Res. , vol.24 , pp. 193-237
    • Fleischer, B.1
  • 74
    • 0031133280 scopus 로고    scopus 로고
    • Programmed cell death of Mycobacterium avium serovar 4-infected macrophages prevents the mycobacteria from spreading and induces mycobacterial growth inhibition by freshly added, uninfected macrophages
    • Fratazzi C, Arbeit R, Carini C, Remold H. 1997. Programmed cell death of Mycobacterium avium serovar 4-infected macrophages prevents the mycobacteria from spreading and induces mycobacterial growth inhibition by freshly added, uninfected macrophages. J. Immunol. 158:432-37
    • (1997) J. Immunol. , vol.158 , pp. 432-437
    • Fratazzi, C.1    Arbeit, R.2    Carini, C.3    Remold, H.4
  • 75
    • 0028213094 scopus 로고
    • Differential in vivo effects of a superantigen and an antibody targeted to the same T cell receptor
    • Gonzalo J, Baixeras E, Garcia A, Chandy A, Rooijen N, et al. 1994. Differential in vivo effects of a superantigen and an antibody targeted to the same T cell receptor. J. Immunol. 152:1597-8
    • (1994) J. Immunol. , vol.152 , pp. 1597-1598
    • Gonzalo, J.1    Baixeras, E.2    Garcia, A.3    Chandy, A.4    Rooijen, N.5
  • 76
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. 1998. Mitochondria and apoptosis. Science 281:1309-12
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 77
    • 0028988541 scopus 로고
    • Interleukin-1β converting enzyme requires oligomerization for activity of processed forms in vivo
    • Gu Y, Wu J, Faucheu C, Lalanne JL, Diu A, et al. 1995. Interleukin-1β converting enzyme requires oligomerization for activity of processed forms in vivo. EMBO J. 14:1923-31
    • (1995) EMBO J. , vol.14 , pp. 1923-1931
    • Gu, Y.1    Wu, J.2    Faucheu, C.3    Lalanne, J.L.4    Diu, A.5
  • 78
    • 0032036424 scopus 로고    scopus 로고
    • Role of adenylate cyclase-hemolysin in alveolar macrophage apoptosis during Bordetella pertussis infection in vivo
    • Gueirard P, Druilhe A, Pretolani M, Guiso N. 1998. Role of adenylate cyclase-hemolysin in alveolar macrophage apoptosis during Bordetella pertussis infection in vivo. Infect. Immun. 66:1718-25
    • (1998) Infect. Immun. , vol.66 , pp. 1718-1725
    • Gueirard, P.1    Druilhe, A.2    Pretolani, M.3    Guiso, N.4
  • 79
    • 0031035693 scopus 로고    scopus 로고
    • Bcl2 is the guardian of microtubule integrity
    • Haldar S, Basu A, Croce CM. 1997. Bcl2 is the guardian of microtubule integrity, Cancer Res. 57:229-33
    • (1997) Cancer Res. , vol.57 , pp. 229-233
    • Haldar, S.1    Basu, A.2    Croce, C.M.3
  • 80
    • 0029790857 scopus 로고    scopus 로고
    • Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K
    • Han J, Sabbatini P, White E. 1996. Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K. Mol. Cell. Biol. 16:5857-64
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5857-5864
    • Han, J.1    Sabbatini, P.2    White, E.3
  • 81
    • 0024592135 scopus 로고
    • Immunohistochemical and electron microscopic study of the interaction of Yersinia enterocolitica serotype 08 with intestinal mucosa during experimental enteritis
    • Hanski C, Kutscchka H, Schmoranzer H, Naumann M, Stallmach A, et al. 1989. Immunohistochemical and electron microscopic study of the interaction of Yersinia enterocolitica serotype 08 with intestinal mucosa during experimental enteritis. Infect. Immun. 57:673-78
    • (1989) Infect. Immun. , vol.57 , pp. 673-678
    • Hanski, C.1    Kutscchka, H.2    Schmoranzer, H.3    Naumann, M.4    Stallmach, A.5
  • 82
    • 0030886017 scopus 로고    scopus 로고
    • A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria
    • Hardt W, Galan J. 1997. A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria. Proc. Natl. Acad. Sci. USA 94: 9887-92
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9887-9892
    • Hardt, W.1    Galan, J.2
  • 83
    • 0028288277 scopus 로고
    • C elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner MO, Horvitz HR. 1994. C elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell 76:665-76
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 84
    • 0029051014 scopus 로고
    • Functional conservation of the Salmonella and Shigella effectors of entry into epithelial cells
    • Hermant D, Menard R, Arricau N, Parsot C, Popoff MY, 1995. Functional conservation of the Salmonella and Shigella effectors of entry into epithelial cells. Mol. Microbiol. 17:781-89
    • (1995) Mol. Microbiol. , vol.17 , pp. 781-789
    • Hermant, D.1    Menard, R.2    Arricau, N.3    Parsot, C.4    Popoff, M.Y.5
  • 86
    • 15644374367 scopus 로고    scopus 로고
    • Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB
    • Hilbi H, Moss J, Hersh D, Chen Y, Arondel J, et al. 1998. Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB. J. Biol. Chem. 273:32895-900
    • (1998) J. Biol. Chem. , vol.273 , pp. 32895-32900
    • Hilbi, H.1    Moss, J.2    Hersh, D.3    Chen, Y.4    Arondel, J.5
  • 87
    • 0025947639 scopus 로고
    • Staphylococcal alpha-toxin: Dual mechanism of binding to target cells
    • Hildebrand A, Roth M, Bhakdi S. 1991. Staphylococcal alpha-toxin: dual mechanism of binding to target cells. J. Biol. Chem. 266:17195-200
    • (1991) J. Biol. Chem. , vol.266 , pp. 17195-17200
    • Hildebrand, A.1    Roth, M.2    Bhakdi, S.3
  • 89
    • 0029007194 scopus 로고
    • Virulence plasmid-encoded YopK is essential for Yersinia pseudotuberculosis to cause systemic infection in mice
    • Holmstrom A, Rosqvist R, Wolf-Watz H, Forsberg A. 1995. Virulence plasmid-encoded YopK is essential for Yersinia pseudotuberculosis to cause systemic infection in mice. Infect. Immun. 63:2269-76
    • (1995) Infect. Immun. , vol.63 , pp. 2269-2276
    • Holmstrom, A.1    Rosqvist, R.2    Wolf-Watz, H.3    Forsberg, A.4
  • 90
    • 0018885613 scopus 로고
    • Legionnaires' disease bacterium (Legionella pneumophila) multiplies intracellularly in human monocytes
    • Horowitz MA, Silverstein SC. 1980. Legionnaires' disease bacterium (Legionella pneumophila) multiplies intracellularly in human monocytes. J. Clin. Invest. 66:441-50
    • (1980) J. Clin. Invest. , vol.66 , pp. 441-450
    • Horowitz, M.A.1    Silverstein, S.C.2
  • 91
    • 0020591330 scopus 로고
    • The legionnaires' disease bacterium (Legionella pneumophila) inhibits lysosome-phagosome fusion in human monocytes
    • Horwitz MA. 1983. The legionnaires' disease bacterium (Legionella pneumophila) inhibits lysosome-phagosome fusion in human monocytes, J. Exp. Med. 158:1319-31
    • (1983) J. Exp. Med. , vol.158 , pp. 1319-1331
    • Horwitz, M.A.1
  • 92
    • 0021346850 scopus 로고
    • Phagocytosis of the legionnaires' disease bacterium (Legionella pneumophila) occurs by a novel mechanism: Engulfment with a pseudopod coil
    • Horwitz MA. 1984. Phagocytosis of the legionnaires' disease bacterium (Legionella pneumophila) occurs by a novel mechanism: engulfment with a pseudopod coil. Cell 36:27-33
    • (1984) Cell , vol.36 , pp. 27-33
    • Horwitz, M.A.1
  • 93
    • 0030877189 scopus 로고    scopus 로고
    • Type III secretion genes identify a putative virulence locus of Chlamydia
    • Hsia R-C, Pannekeok Y, Ingerowski E, Bavoil PM. 1997. Type III secretion genes identify a putative virulence locus of Chlamydia. Mol. Microbiol. 25:351-59
    • (1997) Mol. Microbiol. , vol.25 , pp. 351-359
    • Hsia, R.-C.1    Pannekeok, Y.2    Ingerowski, E.3    Bavoil, P.M.4
  • 94
    • 0024346776 scopus 로고
    • Pathogenesis and immunity in murine salmonellosis
    • Hsu H. 1989. Pathogenesis and immunity in murine salmonellosis. Microbiol. Rev. 53:390-409
    • (1989) Microbiol. Rev. , vol.53 , pp. 390-409
    • Hsu, H.1
  • 95
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV. 1996. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4:387-96
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 96
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H, Shu HB, Pan MG, Goeddel DV. 1996. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84:299-308
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 97
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kB activation
    • Hsu H, Xiong J, Goeddel DV. 1995. The TNF receptor 1-associated protein TRADD signals cell death and NF-kB activation. Cell 81:495-504
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 98
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-l and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y, Benedict MA, Wu D, Inohara N, Nunez G. 1998. Bcl-XL interacts with Apaf-l and inhibits Apaf-1-dependent caspase-9 activation. Proc. Natl. Acad. Sci. USA 95:4386-91
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nunez, G.5
  • 99
    • 0032481346 scopus 로고    scopus 로고
    • The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4
    • Huang DC, Adams JM, Cory S. 1998. The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. EMBO J. 17:1029-39
    • (1998) EMBO J. , vol.17 , pp. 1029-1039
    • Huang, D.C.1    Adams, J.M.2    Cory, S.3
  • 100
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck CJ. 1998. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62:379-433
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 101
    • 0028215798 scopus 로고
    • Cytotoxicity of extracellular Legionella pneumophila
    • Husmann LK, Johnson W. 1994. Cytotoxicity of extracellular Legionella pneumophila. Infect. Immun. 62:2111-14
    • (1994) Infect. Immun. , vol.62 , pp. 2111-2114
    • Husmann, L.K.1    Johnson, W.2
  • 102
    • 0023654013 scopus 로고
    • Interaction of the alpha-toxin of S. aureus with the liposome membrane
    • Ikigae H, Nakae T. 1987. Interaction of the alpha-toxin of S. aureus with the liposome membrane. J. Biol. Chem. 262:2156-60
    • (1987) J. Biol. Chem. , vol.262 , pp. 2156-2160
    • Ikigae, H.1    Nakae, T.2
  • 103
    • 1842417077 scopus 로고    scopus 로고
    • Human Bak induces cell death in Schizosaccharomyces pombe with morphological changes similar to those with apoptosis in mammalian cells
    • Ink B, Zornig M, Baum B, Hajibagheri N, James C, et al. 1997. Human Bak induces cell death in Schizosaccharomyces pombe with morphological changes similar to those with apoptosis in mammalian cells. Mol. Cell. Biol. 17:2468-74
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2468-2474
    • Ink, B.1    Zornig, M.2    Baum, B.3    Hajibagheri, N.4    James, C.5
  • 105
    • 0031037985 scopus 로고    scopus 로고
    • In situ characterization of inflammatory responses in the rectal mucosae of patients with shigellosis
    • Islam D, Veress B, Bardhan PK, Lindberg AA, Christensson B. 1997. In situ characterization of inflammatory responses in the rectal mucosae of patients with shigellosis. Infect. Immun. 65:735-49
    • (1997) Infect. Immun. , vol.65 , pp. 735-749
    • Islam, D.1    Veress, B.2    Bardhan, P.K.3    Lindberg, A.A.4    Christensson, B.5
  • 106
    • 0030959304 scopus 로고    scopus 로고
    • Bcl-2 phosphorylation required for anti-apoptosis function
    • Ito T, Dens X, Cart B, May WS. 1997. Bcl-2 phosphorylation required for anti-apoptosis function. J. Biol. Chem. 272:11671-73
    • (1997) J. Biol. Chem. , vol.272 , pp. 11671-11673
    • Ito, T.1    Dens, X.2    Cart, B.3    May, W.S.4
  • 108
    • 0024806727 scopus 로고
    • Antigen induced apoptosis in developing T cells: A mechanism for negative selection of the T cell repertoire
    • Jenkinson E, Kingston R, Smith C, Williams G, Owen J. 1989. Antigen induced apoptosis in developing T cells: a mechanism for negative selection of the T cell repertoire. Eur. J. Immunol. 19:2175-77
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2175-2177
    • Jenkinson, E.1    Kingston, R.2    Smith, C.3    Williams, G.4    Owen, J.5
  • 109
    • 0026706266 scopus 로고
    • The involvement of protein kinase C in activation-induced cell death in T-cell hybridoma
    • Jin LW, Inaba K, Saitoh T. 1992. The involvement of protein kinase C in activation-induced cell death in T-cell hybridoma. Cell. Immunol. 144:217-27
    • (1992) Cell. Immunol. , vol.144 , pp. 217-227
    • Jin, L.W.1    Inaba, K.2    Saitoh, T.3
  • 110
    • 0028324930 scopus 로고
    • Novel path to apoptosis small transmembrane pores created by staphylococcal alpha toxin T lymphocytes evokes internucleosomal degradation
    • Jonas D, Walev I, Berger T, Liebetrau M, Palmer M, Bhakdi S. 1994. Novel path to apoptosis small transmembrane pores created by staphylococcal alpha toxin T lymphocytes evokes internucleosomal degradation. Infect. Immun. 62:1304-12
    • (1994) Infect. Immun. , vol.62 , pp. 1304-1312
    • Jonas, D.1    Walev, I.2    Berger, T.3    Liebetrau, M.4    Palmer, M.5    Bhakdi, S.6
  • 111
    • 0028214086 scopus 로고
    • Salmonella typhimurium initiates murine infection by penetrating and destroying the specialized epithelial M cells of Peyer's patches
    • Jones B, Ghouri N, Falkow S. 1994. Salmonella typhimurium initiates murine infection by penetrating and destroying the specialized epithelial M cells of Peyer's patches. J. Exp. Med. 180:15-23
    • (1994) J. Exp. Med. , vol.180 , pp. 15-23
    • Jones, B.1    Ghouri, N.2    Falkow, S.3
  • 115
    • 0026677151 scopus 로고
    • Life and death of a superantigen reactive human CD4+ T cell clone: Staphylococcal enterotoxins induce death by apoptosis but simultaneously trigger a proliferative response in the presence of HLA-DR+ antigen presenting cells
    • Kabelitz D, Wesselborg S. 1992. Life and death of a superantigen reactive human CD4+ T cell clone: staphylococcal enterotoxins induce death by apoptosis but simultaneously trigger a proliferative response in the presence of HLA-DR+ antigen presenting cells. Int. Immunol. 4:1381-88
    • (1992) Int. Immunol. , vol.4 , pp. 1381-1388
    • Kabelitz, D.1    Wesselborg, S.2
  • 117
    • 0029059332 scopus 로고
    • Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells
    • Kaniga K, Tucker SC, Trollinger D, Galen JE. 1995. Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells. J. Bacteriol. 177:3965-71
    • (1995) J. Bacteriol. , vol.177 , pp. 3965-3971
    • Kaniga, K.1    Tucker, S.C.2    Trollinger, D.3    Galen, J.E.4
  • 118
    • 0026068601 scopus 로고
    • Programmed cell death and extrathymic reduction of Vb8+ CD4+ T cells in mice tolerant to Staphylococcus aureus enterotoxin B
    • Kawabe Y, Ochi A. 1991. Programmed cell death and extrathymic reduction of Vb8+ CD4+ T cells in mice tolerant to Staphylococcus aureus enterotoxin B. Nature 349:245-48
    • (1991) Nature , vol.349 , pp. 245-248
    • Kawabe, Y.1    Ochi, A.2
  • 120
    • 0025639083 scopus 로고
    • Gene-for-gene complementarity in plant pathogen interactions
    • Keen NT. 1990. Gene-for-gene complementarity in plant pathogen interactions. Annu. Rev. Genet. 24:447-63
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 447-463
    • Keen, N.T.1
  • 121
    • 0022996068 scopus 로고
    • Morphologic evaluation of the effects of Shiga toxin and E. coli Shiga like toxin on the rabbit intestine
    • Keenan K, Dharpnack D, Formal S, O'Brien A. 1986. Morphologic evaluation of the effects of Shiga toxin and E. coli Shiga like toxin on the rabbit intestine. Am. J. Pathol. 125:69-80
    • (1986) Am. J. Pathol. , vol.125 , pp. 69-80
    • Keenan, K.1    Dharpnack, D.2    Formal, S.3    O'Brien, A.4
  • 122
    • 0028812868 scopus 로고
    • Induction of macrophage apoptosis by Bordetella pertussis adenylate cyclase-hemolysin
    • Khelef N, Guiso N. 1995. Induction of macrophage apoptosis by Bordetella pertussis adenylate cyclase-hemolysin. FEMS Microbiol. Lett. 134:27-32
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 27-32
    • Khelef, N.1    Guiso, N.2
  • 123
    • 0026831206 scopus 로고
    • Both adenylate cyclase and hemolytic activities are required by Bordetella pertussis to initiate infection
    • Khelef N, Sakamoto H, Guiso N, 1992. Both adenylate cyclase and hemolytic activities are required by Bordetella pertussis to initiate infection. Microb. Pathog. 12:227-35
    • (1992) Microb. Pathog. , vol.12 , pp. 227-235
    • Khelef, N.1    Sakamoto, H.2    Guiso, N.3
  • 124
    • 0027374664 scopus 로고
    • Bordetella pertussis induces apoptosis in macrophages: Role of adenylate cyclase-hemolysin
    • Khelef N, Zychlinsky A, Guiso N. 1993. Bordetella pertussis induces apoptosis in macrophages: role of adenylate cyclase-hemolysin. Infect. Immun. 61:4064-71
    • (1993) Infect. Immun. , vol.61 , pp. 4064-4071
    • Khelef, N.1    Zychlinsky, A.2    Guiso, N.3
  • 126
    • 0030731701 scopus 로고    scopus 로고
    • Effects of mycobacteria on regulation of apoptosis in mononuclear phagocytes
    • Klinger K, Tchou-Wong K-M, Brändli O, Aston C, Kim R, et al. 1997. Effects of mycobacteria on regulation of apoptosis in mononuclear phagocytes. Infect. Immun. 65:5272-78
    • (1997) Infect. Immun. , vol.65 , pp. 5272-5278
    • Klinger, K.1    Tchou-Wong, K.-M.2    Brändli, O.3    Aston, C.4    Kim, R.5
  • 127
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132-36
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 128
    • 0027265538 scopus 로고
    • DNA fragmentation and cytolysis in U937 cells treated with diphtheria toxin or other inhibitors of protein synthesis
    • Kochi S, Collier J. 1993. DNA fragmentation and cytolysis in U937 cells treated with diphtheria toxin or other inhibitors of protein synthesis. Exp. Cell Res. 208:296-302
    • (1993) Exp. Cell Res. , vol.208 , pp. 296-302
    • Kochi, S.1    Collier, J.2
  • 129
    • 0023645535 scopus 로고
    • Highly frequent single amino acid substitution in mammalian EF-2 results in expression of resistance to EF-2 ADP-ribosylating toxins
    • Kohno K, Uchida T. 1987. Highly frequent single amino acid substitution in mammalian EF-2 results in expression of resistance to EF-2 ADP-ribosylating toxins. J. Biol. Chem. 262:12298-305
    • (1987) J. Biol. Chem. , vol.262 , pp. 12298-12305
    • Kohno, K.1    Uchida, T.2
  • 131
    • 0030820875 scopus 로고    scopus 로고
    • Caspase-3-generated fragment of gelsolin: Effector of morphological change in apoptosis
    • Kothakota S, Azuma T, Reinhard C, Klippel A, Tang J, Chu K, et al. 1997. Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis. Science 278:294-98
    • (1997) Science , vol.278 , pp. 294-298
    • Kothakota, S.1    Azuma, T.2    Reinhard, C.3    Klippel, A.4    Tang, J.5    Chu, K.6
  • 132
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2
    • Kozopas KM, Yang T, Buchan HL, Zhou P, Craig RW. 1993. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc. Natl. Acad. Sci. USA 90:3516-20
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 133
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. 1997. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat. Med. 3:614-20
    • (1997) Nat. Med. , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 134
    • 0030586563 scopus 로고    scopus 로고
    • Implantation of IL-2 containing osmotic pump prolongs the survivor of superantigen reactive T cells expanded in mice injected with bacterial superantigen
    • Kuroda K, Yagi J, Imanishi K, Yen X, Li X, et al. 1996. Implantation of IL-2 containing osmotic pump prolongs the survivor of superantigen reactive T cells expanded in mice injected with bacterial superantigen. J. Immunol. 157:1422-31
    • (1996) J. Immunol. , vol.157 , pp. 1422-1431
    • Kuroda, K.1    Yagi, J.2    Imanishi, K.3    Yen, X.4    Li, X.5
  • 135
    • 0000843289 scopus 로고
    • Epithelial cell penetration as an essential step in the pathogenesis of bacillary dysentery
    • LaBrec EH, Schneider H, Magnani TJ, Formal SB. 1964. Epithelial cell penetration as an essential step in the pathogenesis of bacillary dysentery. J. Bacteriol. 88:1503-18
    • (1964) J. Bacteriol. , vol.88 , pp. 1503-1518
    • LaBrec, E.H.1    Schneider, H.2    Magnani, T.J.3    Formal, S.B.4
  • 137
    • 15444347280 scopus 로고    scopus 로고
    • RTX Toxins recognize a b2 integrin on the surface of human target cells
    • Lally ET, Kieba IR, Sato A, Green CL, Rosenbloom J, et al. 1997. RTX Toxins recognize a b2 integrin on the surface of human target cells. J. Biol. Chem. 272:30463-69
    • (1997) J. Biol. Chem. , vol.272 , pp. 30463-30469
    • Lally, E.T.1    Kieba, I.R.2    Sato, A.3    Green, C.L.4    Rosenbloom, J.5
  • 138
    • 0027955308 scopus 로고
    • Plant disease resistance genes in signal perception and transduction
    • Lamb CJ. 1994. Plant disease resistance genes in signal perception and transduction. Cell 76:419-22
    • (1994) Cell , vol.76 , pp. 419-422
    • Lamb, C.J.1
  • 140
    • 0026586710 scopus 로고
    • Localization of diphtheria toxin nuclease activity to fragment A
    • Lessnick S, Lyczak J, Bruce C, Lewis D, Kim P, et al. 1992. Localization of diphtheria toxin nuclease activity to fragment A. J. Bacteriol. 174:2032-38
    • (1992) J. Bacteriol. , vol.174 , pp. 2032-2038
    • Lessnick, S.1    Lyczak, J.2    Bruce, C.3    Lewis, D.4    Kim, P.5
  • 141
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79:583-93
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 142
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-l/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, et al. 1997. Cytochrome c and dATP-dependent formation of Apaf-l/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-89
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1
  • 143
    • 0024436208 scopus 로고
    • Molecular cloning and characterization of a hemolysin gene from Actinobacillus (Haemophilus) pleuropneumoniae
    • Lian CJ, Rosendal S, Macinnes JI. 1989. Molecular cloning and characterization of a hemolysin gene from Actinobacillus (Haemophilus) pleuropneumoniae. Infect. Immun. 57:3377-82
    • (1989) Infect. Immun. , vol.57 , pp. 3377-3382
    • Lian, C.J.1    Rosendal, S.2    Macinnes, J.I.3
  • 144
    • 0027326012 scopus 로고
    • Characterization of Al, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2
    • Lin EY, Orlofsky A, Berger MS, Prystowsky MB. 1993. Characterization of Al, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2. J. Immunol. 151:1979-88
    • (1993) J. Immunol. , vol.151 , pp. 1979-1988
    • Lin, E.Y.1    Orlofsky, A.2    Berger, M.S.3    Prystowsky, M.B.4
  • 145
    • 0029145912 scopus 로고
    • Changes of protein kinase C subspecies in staphylococcal enterotoxin B induced thymocyte apotosis
    • Lin Y, Kao S, Jan M, Cheng M, Wing L, et al. 1995. Changes of protein kinase C subspecies in staphylococcal enterotoxin B induced thymocyte apotosis. Biochem. Biophy. Res. Commun. 213:1132-39
    • (1995) Biochem. Biophy. Res. Commun. , vol.213 , pp. 1132-1139
    • Lin, Y.1    Kao, S.2    Jan, M.3    Cheng, M.4    Wing, L.5
  • 146
    • 0026631856 scopus 로고
    • In vivo induction of apoptosis in immature thymocytes by staphylococcal enterotoxin B
    • Lin Y, Lei H, Low TLK, Shen CL, Chou LJ, Jan MS. 1992. In vivo induction of apoptosis in immature thymocytes by staphylococcal enterotoxin B. J. Immunol. 149:1156-63
    • (1992) J. Immunol. , vol.149 , pp. 1156-1163
    • Lin, Y.1    Lei, H.2    Low, T.L.K.3    Shen, C.L.4    Chou, L.J.5    Jan, M.S.6
  • 147
    • 0029978844 scopus 로고    scopus 로고
    • Macrophage killing is an essential virulence mechanism of Salmonella typhimurium
    • Lindgren SW, Stojilkovic I, Heffron F. 1996. Macrophage killing is an essential virulence mechanism of Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 93:4197-201
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4197-4201
    • Lindgren, S.W.1    Stojilkovic, I.2    Heffron, F.3
  • 148
    • 0032563202 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 is a marker of M phase events and not a determinant of apoptosis
    • Ling YH, Tornos C, Perez-Soler R. 1998. Phosphorylation of Bcl-2 is a marker of M phase events and not a determinant of apoptosis. J. Biol, Chem. 273:18984-91
    • (1998) J. Biol. Chem. , vol.273 , pp. 18984-18991
    • Ling, Y.H.1    Tornos, C.2    Perez-Soler, R.3
  • 149
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. 1996. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147-57
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 150
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X, Zou H, Slaughter C, Wang X. 1997. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-84
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 151
    • 0029898566 scopus 로고    scopus 로고
    • Oligomeric and subunit structure of the Helicobacter priori vacuolating cytotoxin
    • Lupetti P, Heuser JE, Manetti R, Massari P, Lanzavecchia S, et al. 1996. Oligomeric and subunit structure of the Helicobacter priori vacuolating cytotoxin. J. Cell. Biol. 133:801-6
    • (1996) J. Cell. Biol. , vol.133 , pp. 801-806
    • Lupetti, P.1    Heuser, J.E.2    Manetti, R.3    Massari, P.4    Lanzavecchia, S.5
  • 152
    • 0025874073 scopus 로고
    • Lethal effects of Actinobacillus actinomycetemcomitans leukotoxin on human T lymphocytes
    • Magan D, Taichman N, Lally E, Wahl S. 1991. Lethal effects of Actinobacillus actinomycetemcomitans leukotoxin on human T lymphocytes. Infect. Immun. 59:3267-72
    • (1991) Infect. Immun. , vol.59 , pp. 3267-3272
    • Magan, D.1    Taichman, N.2    Lally, E.3    Wahl, S.4
  • 153
    • 0032425435 scopus 로고    scopus 로고
    • Effect of Clostridium difficile toxin A on human colonic lamina propria cells: Early loss of macrophages followed by T-cell apoptosis
    • Mahida YR, Galvin A, Makh S, Hyde S, Sanfilippo L, et al. 1998. Effect of Clostridium difficile toxin A on human colonic lamina propria cells: early loss of macrophages followed by T-cell apoptosis. Infect. Immun. 66:5462-69
    • (1998) Infect. Immun. , vol.66 , pp. 5462-5469
    • Mahida, Y.R.1    Galvin, A.2    Makh, S.3    Hyde, S.4    Sanfilippo, L.5
  • 154
    • 0029868433 scopus 로고    scopus 로고
    • Effect of Clostridium difficile toxin A on human intestinal epithelial cells: Induction of interleukin 8 production and apoptosis after cell detachment
    • Mahida YR, Makh S, Hyde S, Gray T, Borriello SP. 1996. Effect of Clostridium difficile toxin A on human intestinal epithelial cells: induction of interleukin 8 production and apoptosis after cell detachment. Gut 38:337-47
    • (1996) Gut , vol.38 , pp. 337-347
    • Mahida, Y.R.1    Makh, S.2    Hyde, S.3    Gray, T.4    Borriello, S.P.5
  • 155
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-kB induction by TNF, CD95 and IL-1
    • Malinin NL, Boldin MP, Kovalenko AV, Wallach D. 1997. MAP3K-related kinase involved in NF-kB induction by TNF, CD95 and IL-1. Nature 385:540-44
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 156
    • 0027366926 scopus 로고
    • Apoptosis induced in Burkitt's lymphoma cells via Gb3/CD77, a glycolipid antigen
    • Mangeney M, Lingwood C, Taga S, Caillou B, Tursz T, Wiels J. 1993. Apoptosis induced in Burkitt's lymphoma cells via Gb3/CD77, a glycolipid antigen. Cancer Res. 53:5314-19
    • (1993) Cancer Res. , vol.53 , pp. 5314-5319
    • Mangeney, M.1    Lingwood, C.2    Taga, S.3    Caillou, B.4    Tursz, T.5    Wiels, J.6
  • 157
    • 8944241770 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase, nitrotyrosine, and apoptosis in Helicobacter pylori gastritis: Effect of antibiotics and antioxidants
    • Mannick E, Bravo L, Zarama G, Realpe J, Zhang X, et al. 1996. Inducible nitric oxide synthase, nitrotyrosine, and apoptosis in Helicobacter pylori gastritis: effect of antibiotics and antioxidants. Cancer Res. 56:3238-43
    • (1996) Cancer Res. , vol.56 , pp. 3238-3243
    • Mannick, E.1    Bravo, L.2    Zarama, G.3    Realpe, J.4    Zhang, X.5
  • 158
    • 0021259505 scopus 로고
    • Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration
    • Marshall BJ, Warren JR. 1984. Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration. Lancet 8390:1311-15
    • (1984) Lancet , vol.8390 , pp. 1311-1315
    • Marshall, B.J.1    Warren, J.R.2
  • 160
    • 15644381250 scopus 로고    scopus 로고
    • Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress-activated protein kinases in the presence of the constitutively active GTP-binding protein Racl
    • Maundrell K, Antonsson B, Magnenat E, Camps M, Muda M, Chabert C, et al. 1997. Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress-activated protein kinases in the presence of the constitutively active GTP-binding protein Racl. J. Biol. Chem. 272:25238-42
    • (1997) J. Biol. Chem. , vol.272 , pp. 25238-25242
    • Maundrell, K.1    Antonsson, B.2    Magnenat, E.3    Camps, M.4    Muda, M.5    Chabert, C.6
  • 161
    • 0022504362 scopus 로고
    • Ionic channel formed by Staphylococcus aureus alphatoxin voltage dependent inhibition by divalent and trivalent cations
    • Menestrina G. 1986. Ionic channel formed by Staphylococcus aureus alphatoxin voltage dependent inhibition by divalent and trivalent cations. J. Membr Biol. 19:177-90
    • (1986) J. Membr. Biol. , vol.19 , pp. 177-190
    • Menestrina, G.1
  • 162
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: Cytokine-activated IkB kinases essential for NF-kB activation
    • Mercurio F, Zhu H, Murray BW, Shevchenko A, Bennett BL, Li J, et al. 1997. IKK-1 and IKK-2: cytokine-activated IkB kinases essential for NF-kB activation. Science 278:860-66
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.1    Zhu, H.2    Murray, B.W.3    Shevchenko, A.4    Bennett, B.L.5    Li, J.6
  • 163
    • 0030730859 scopus 로고    scopus 로고
    • Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms involving YopP, presumably acting as an effector protein
    • Mills S, Boland A, Sory MP, Van Der Smissen P, Kerbourch C, et al. 1997. Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms involving YopP, presumably acting as an effector protein. Proc. Natl. Acad. Sci. USA 94:12638-43
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12638-12643
    • Mills, S.1    Boland, A.2    Sory, M.P.3    Van Der Smissen, P.4    Kerbourch, C.5
  • 164
    • 0028136987 scopus 로고
    • Apoptosis, but not necrosis, of infected monocytes coupled with killing of intracellular Bacillus Calmette-Guerin
    • Molloy A, Laochumroonvorapong P, Kaplan G. 1994. Apoptosis, but not necrosis, of infected monocytes coupled with killing of intracellular Bacillus Calmette-Guerin. J. Exp. Med. 180:1499-509
    • (1994) J. Exp. Med. , vol.180 , pp. 1499-1509
    • Molloy, A.1    Laochumroonvorapong, P.2    Kaplan, G.3
  • 166
    • 0030985415 scopus 로고    scopus 로고
    • Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death
    • Monack D, Mecsas J, Ghori N, Falkow S. 1997. Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death. Proc. Natl. Acad. Sci. USA 94:10385-90
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10385-10390
    • Monack, D.1    Mecsas, J.2    Ghori, N.3    Falkow, S.4
  • 167
    • 0031744367 scopus 로고    scopus 로고
    • Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice
    • Monack DM, Mecsas J, Bouley D, Falkow S. 1998. Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice. J. Exp. Med. 188:2127-37
    • (1998) J. Exp. Med. , vol.188 , pp. 2127-2137
    • Monack, D.M.1    Mecsas, J.2    Bouley, D.3    Falkow, S.4
  • 168
    • 0026670960 scopus 로고
    • Diphtheria toxin and Pseudomonas A toxin mediated apoptosis
    • Morimoto H, Bonavida S. 1992. Diphtheria toxin and Pseudomonas A toxin mediated apoptosis. J. Immunol. 149:2089-94
    • (1992) J. Immunol. , vol.149 , pp. 2089-2094
    • Morimoto, H.1    Bonavida, S.2
  • 169
    • 0029987967 scopus 로고    scopus 로고
    • Induction of gastric epithelial apoptosis by Helicobacter pylori
    • Moss S, Calam J, Agarwal B, Wang S, Holt P. 1996. Induction of gastric epithelial apoptosis by Helicobacter pylori. Gut 38:498-501
    • (1996) Gut , vol.38 , pp. 498-501
    • Moss, S.1    Calam, J.2    Agarwal, B.3    Wang, S.4    Holt, P.5
  • 170
    • 0028922885 scopus 로고
    • Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice
    • Motoyama N, Wang F, Roth KA, Sawa H, Nakayama K, Nakayama K, et al. 1995. Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice. Science 267:1506-10
    • (1995) Science , vol.267 , pp. 1506-1510
    • Motoyama, N.1    Wang, F.2    Roth, K.A.3    Sawa, H.4    Nakayama, K.5    Nakayama, K.6
  • 171
    • 0025979037 scopus 로고
    • Interaction of chlamydiae and host cells in vitro
    • Moulder JW. 1991. Interaction of chlamydiae and host cells in vitro. Microbiol. Rev. 55:143-90
    • (1991) Microbiol. Rev. , vol.55 , pp. 143-190
    • Moulder, J.W.1
  • 172
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • Muchmore SW, Sorrier M, Liang H, Meadows RP, Harlan JE, Yoon HS, et al. 1996. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature 381:335-41
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sorrier, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5    Yoon, H.S.6
  • 173
    • 0029844198 scopus 로고    scopus 로고
    • Evidence for apoptosis of human macrophage-like HL-60 cells by Legionella pneumophila infection
    • Müller A, Hacker J, Brand BC. 1996. Evidence for apoptosis of human macrophage-like HL-60 cells by Legionella pneumophila infection. Infect. Immun. 64:4900-6
    • (1996) Infect. Immun. , vol.64 , pp. 4900-4906
    • Müller, A.1    Hacker, J.2    Brand, B.C.3
  • 174
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICF/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, et al. 1996. FLICE, a novel FADD-homologous ICF/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85:817-27
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3    O'Rourke, K.4    Shevchenko, A.5    Ni, J.6
  • 176
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. 1997. Apoptosis by death factor. Cell 88:355-65
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 177
    • 0027534069 scopus 로고
    • Association between virulence of Yersinia pestis and suppression of gamma interferon and tumor necrosis factor alpha
    • Nakajima R, Brubaker RR. 1993. Association between virulence of Yersinia pestis and suppression of gamma interferon and tumor necrosis factor alpha, Infect. Immun. 61:23-31
    • (1993) Infect. Immun. , vol.61 , pp. 23-31
    • Nakajima, R.1    Brubaker, R.R.2
  • 178
    • 0029021978 scopus 로고
    • Suppression of cytokines in mice by A-V antigen fusion peptide and restoration of synthesis by active immunization
    • Nakajima R, Motin VL, Brubaker RR. 1995. Suppression of cytokines in mice by A-V antigen fusion peptide and restoration of synthesis by active immunization. Infect. Immun. 63:3021-29
    • (1995) Infect. Immun. , vol.63 , pp. 3021-3029
    • Nakajima, R.1    Motin, V.L.2    Brubaker, R.R.3
  • 179
    • 0031013545 scopus 로고    scopus 로고
    • Activation of SAPK/JNK by TNF receptor l through a noncytotoxic TRAF2-dependent pathway
    • Natoli G, Costanzo A, Ianni A, Templeton DJ, Woodgett JR, et al. 1997. Activation of SAPK/JNK by TNF receptor l through a noncytotoxic TRAF2-dependent pathway. Science 275:200-3
    • (1997) Science , vol.275 , pp. 200-203
    • Natoli, G.1    Costanzo, A.2    Ianni, A.3    Templeton, D.J.4    Woodgett, J.R.5
  • 180
    • 0028019746 scopus 로고
    • Cell-free apoptosis in Xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria
    • Newmeyer DD, Farschon DM, Reed JC. 1994. Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell 79:353-64
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1    Farschon, D.M.2    Reed, J.C.3
  • 182
    • 0027967403 scopus 로고
    • High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes Triggers multiple defense responses
    • Nürnberger T, Nennsteil D, Jabs T, Sacks WR, Hahlbrock K, Schell D. 1994. High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes Triggers multiple defense responses. Cell 78:449-60
    • (1994) Cell , vol.78 , pp. 449-460
    • Nürnberger, T.1    Nennsteil, D.2    Jabs, T.3    Sacks, W.R.4    Hahlbrock, K.5    Schell, D.6
  • 183
    • 0001350946 scopus 로고    scopus 로고
    • Organization of diphtheria toxin T domain in bilayers: A site directed spin labeling study
    • Oh K, Zhan H, Cui C, Hideg K, Collier R, Hubbel W. 1996. Organization of diphtheria toxin T domain in bilayers: a site directed spin labeling study. Science 273:810-12
    • (1996) Science , vol.273 , pp. 810-812
    • Oh, K.1    Zhan, H.2    Cui, C.3    Hideg, K.4    Collier, R.5    Hubbel, W.6
  • 184
    • 0032532304 scopus 로고    scopus 로고
    • Apoptosis of epithelial cells and macrophages due to infection with the obligate intracellular pathogen Chlamydia
    • Ojcius DM, Souque P, Perfettini J-L, Dautry-Varsat A. 1998. Apoptosis of epithelial cells and macrophages due to infection with the obligate intracellular pathogen Chlamydia. J. Immunol. 161:4220-26
    • (1998) J. Immunol. , vol.161 , pp. 4220-4226
    • Ojcius, D.M.1    Souque, P.2    Perfettini, J.-L.3    Dautry-Varsat, A.4
  • 185
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Millman CL, Korsmeyer SJ. 1993. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609-19
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Millman, C.L.2    Korsmeyer, S.J.3
  • 186
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • Orth K, Chinnaiyan AM, Garg M, Froelich CJ, Dixit VM. 1996. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 271:16443-46
    • (1996) J. Biol. Chem. , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 187
    • 13144253096 scopus 로고    scopus 로고
    • The m2 form of the Helicobacter pylori cytotoxin has cell type-specific vacuolating activity
    • Pagliaccia C, Bernard M, Lupetti P, Ji X, Burroni D, et al. 1998. The m2 form of the Helicobacter pylori cytotoxin has cell type-specific vacuolating activity. Proc. Natl. Acad. Sci. USA 95:10212-17
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10212-10217
    • Pagliaccia, C.1    Bernard, M.2    Lupetti, P.3    Ji, X.4    Burroni, D.5
  • 188
    • 0031780201 scopus 로고    scopus 로고
    • YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-a production and downregulation of the MAP kinases p38 and JNK
    • Palmer LE, Hobble S, Galan JE, Bliska J. 1998. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-a production and downregulation of the MAP kinases p38 and JNK. Mol. Microbiol. 27:953-65
    • (1998) Mol. Microbiol. , vol.27 , pp. 953-965
    • Palmer, L.E.1    Hobble, S.2    Galan, J.E.3    Bliska, J.4
  • 189
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan G, O'Rourke K, Dixit VM. 1998. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J. Biol. Chem. 273: 5841-45
    • (1998) J. Biol. Chem. , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 190
    • 1842331503 scopus 로고    scopus 로고
    • Helicobacter pylori cagA+ strains and dissociation of gastrointestinal epithelial cell proliferation from apoptosis
    • Peek RM Jr, Moss SF, Tham KT, Perez-Perez GI, Wang S, et al. 1997. Helicobacter pylori cagA+ strains and dissociation of gastrointestinal epithelial cell proliferation from apoptosis. J. Natl. Cancer Inst. 89:863-68
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 863-868
    • Peek R.M., Jr.1    Moss, S.F.2    Tham, K.T.3    Perez-Perez, G.I.4    Wang, S.5
  • 191
    • 0029095837 scopus 로고
    • PhoP/PhoQ transcriptional repression of Salmonella typhimurium invasion genes: Evidence fora role in protein secretion
    • Pegues DA, Hantman MJ, Behlau I, Miller SI. 1995. PhoP/PhoQ transcriptional repression of Salmonella typhimurium invasion genes: evidence fora role in protein secretion. Mol. Microbiol. 17:169-81
    • (1995) Mol. Microbiol. , vol.17 , pp. 169-181
    • Pegues, D.A.1    Hantman, M.J.2    Behlau, I.3    Miller, S.I.4
  • 192
  • 193
    • 0027529133 scopus 로고
    • Saccharomyces cerevisiae elongation factor 2
    • Phan L, Perentesis J, Bodley J. 1993. Saccharomyces cerevisiae elongation factor 2. J. Biol. Chem. 268:8665-68
    • (1993) J. Biol. Chem. , vol.268 , pp. 8665-8668
    • Phan, L.1    Perentesis, J.2    Bodley, J.3
  • 194
    • 0026587933 scopus 로고
    • Molecular determinants of Listeria monocytogenes pathogenesis
    • Portnoy D, Chakraborty T, Goebel W, Crossart P. 1992. Molecular determinants of Listeria monocytogenes pathogenesis. Infect. Immun. 60:1263-67
    • (1992) Infect. Immun. , vol.60 , pp. 1263-1267
    • Portnoy, D.1    Chakraborty, T.2    Goebel, W.3    Crossart, P.4
  • 195
    • 0032497567 scopus 로고    scopus 로고
    • Caspases and programmed cell death in the hypersensitive response of plants to pathogens
    • Pozo O, Lam E. 1998. Caspases and programmed cell death in the hypersensitive response of plants to pathogens Curr. Biol. 8:1129-32
    • (1998) Curr. Biol. , vol.8 , pp. 1129-1132
    • Pozo, O.1    Lam, E.2
  • 196
    • 0002380868 scopus 로고    scopus 로고
    • The molecular basis of pathogenicity
    • ed. KB Crossley, GL Archer, New York: Churchill Livingstone
    • Projan SJ, Novick RP. 1997. The molecular basis of pathogenicity. In The Staphylococci in Human Disease, ed. KB Crossley, GL Archer, pp. 55-81. New York: Churchill Livingstone
    • (1997) The Staphylococci in Human Disease , pp. 55-81
    • Projan, S.J.1    Novick, R.P.2
  • 198
    • 0031020373 scopus 로고    scopus 로고
    • Secretion of proinflammatory cytokines by epithelial cells in response to Chlamydia infection suggests a central role for epithelial cells in chlamydial pathogenesis
    • Rasmussen SJ, Eckmann L, Quayle AJ, Shen L, Zhang YX, et al. 1997. Secretion of proinflammatory cytokines by epithelial cells in response to Chlamydia infection suggests a central role for epithelial cells in chlamydial pathogenesis. J. Clin. Invest. 99:77
    • (1997) J. Clin. Invest. , vol.99 , pp. 77
    • Rasmussen, S.J.1    Eckmann, L.2    Quayle, A.J.3    Shen, L.4    Zhang, Y.X.5
  • 199
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed J. 1997. Double identity for proteins of the Bcl-2 family. Nature 387:773-76
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.1
  • 201
    • 0009504296 scopus 로고
    • Distinct steps in the penetration of adenylate cyclase toxin of Bordetella pertussis into sheep erythrocytes
    • Rogel A, Hanski E. 1992. Distinct steps in the penetration of adenylate cyclase toxin of Bordetella pertussis into sheep erythrocytes. J. Biol. Chem. 12:232-37
    • (1992) J. Biol. Chem. , vol.12 , pp. 232-237
    • Rogel, A.1    Hanski, E.2
  • 202
    • 0030070367 scopus 로고    scopus 로고
    • Listeria monocytogenes induces apoptosis of infected hepatocytes
    • Rogers H, Callery MD, Deck B, Unanue E. 1996. Listeria monocytogenes induces apoptosis of infected hepatocytes. J. Immunol. 156:679-84
    • (1996) J. Immunol. , vol.156 , pp. 679-684
    • Rogers, H.1    Callery, M.D.2    Deck, B.3    Unanue, E.4
  • 203
    • 0025788249 scopus 로고
    • Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist R, Forsber Å, Wolf-Watz H. 1991. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect. Immun. 59:4562-69
    • (1991) Infect. Immun. , vol.59 , pp. 4562-4569
    • Rosqvist, R.1    Forsber, Å.2    Wolf-Watz, H.3
  • 204
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV. 1995. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83: 1243-52
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 205
    • 0032562704 scopus 로고    scopus 로고
    • Early activation of c-Jun N-terminal kinase and p38 kinase regulate cell survival in response to tumor necrosis factor a
    • Roulston A, Reinhard C, Amiri P, Williams LT. 1998. Early activation of c-Jun N-terminal kinase and p38 kinase regulate cell survival in response to tumor necrosis factor a. J. Biol. Chem. 273: 10232-39
    • (1998) J. Biol. Chem. , vol.273 , pp. 10232-10239
    • Roulston, A.1    Reinhard, C.2    Amiri, P.3    Williams, L.T.4
  • 206
    • 0032489918 scopus 로고    scopus 로고
    • Yersinia enterocolitica impairs activation of transcripton factor NF-kB: Involvement in the induction of cell death and in the suppression of the macrophage tumor necrosis factor a production
    • Ruckdeschel K, Harb S, Roggenkamp A, Hornnef M, Zumbihl R, et al. 1998. Yersinia enterocolitica impairs activation of transcripton factor NF-kB: involvement in the induction of cell death and in the suppression of the macrophage tumor necrosis factor a production. J. Exp. Med. 187:1069-79
    • (1998) J. Exp. Med. , vol.187 , pp. 1069-1079
    • Ruckdeschel, K.1    Harb, S.2    Roggenkamp, A.3    Hornnef, M.4    Zumbihl, R.5
  • 208
    • 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, Rouot B. 1997. Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis. Infect. Immun. 65:4813-21
    • (1997) Infect. Immun. , vol.65 , pp. 4813-4821
    • Ruckdeschel, K.1    Roggenkamp, A.2    Lafont, V.3    Mangeat, P.4    Heesemann, J.5    Rouot, B.6
  • 209
    • 0029143395 scopus 로고
    • Essential role for p53-mediated transcription in ElA-induced apoptosis
    • Sabbatini P, Lin J, Levine AJ, White E. 1995. Essential role for p53-mediated transcription in ElA-induced apoptosis. Genes Dev. 9:2184-92
    • (1995) Genes Dev. , vol.9 , pp. 2184-2192
    • Sabbatini, P.1    Lin, J.2    Levine, A.J.3    White, E.4
  • 210
    • 0026683322 scopus 로고
    • Toxin induced cell lysis: Protection by 3-methyladenine and cycloheximide
    • Sandvig K, Van Deurs B. 1992. Toxin induced cell lysis: protection by 3-methyladenine and cycloheximide. Exp. Cell Res. 200:253-62
    • (1992) Exp. Cell Res. , vol.200 , pp. 253-262
    • Sandvig, K.1    Van Deurs, B.2
  • 211
    • 0029945905 scopus 로고    scopus 로고
    • Infection of rabbit Peyer's patches by Shigella flexneri: Effect of adhesive or invasive phenotypes on follicle-associated epithelium
    • Sansonetti PJ, Arondel J, Cantey JR, Prevost MC, Huerre M. 1996. Infection of rabbit Peyer's patches by Shigella flexneri: effect of adhesive or invasive phenotypes on follicle-associated epithelium. Infect. Immun. 64:2752-64
    • (1996) Infect. Immun. , vol.64 , pp. 2752-2764
    • Sansonetti, P.J.1    Arondel, J.2    Cantey, J.R.3    Prevost, M.C.4    Huerre, M.5
  • 213
    • 0020003681 scopus 로고
    • Involvement of a plasmid in the invasive ability of Shigella flexneri
    • Sansonetti PJ, Kopecko DJ, Formal SB. 1982. Involvement of a plasmid in the invasive ability of Shigella flexneri. Infect. Immun. 35:852-60
    • (1982) Infect. Immun. , vol.35 , pp. 852-860
    • Sansonetti, P.J.1    Kopecko, D.J.2    Formal, S.B.3
  • 214
    • 0030614915 scopus 로고    scopus 로고
    • Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE. 1997. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 275:983-86
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3    Meadows, R.P.4    Harlan, J.E.5
  • 215
    • 0032578625 scopus 로고    scopus 로고
    • The hCSE1/CAS protein is phosphorylated by HeLa extracts and MEK-1: MEK-1 phosphorylation may modulate the intracellular localization of CAS
    • Scherf U, Kalab P, Dasso M, Pastan I, Brinkman U. 1998. The hCSE1/CAS protein is phosphorylated by HeLa extracts and MEK-1: MEK-1 phosphorylation may modulate the intracellular localization of CAS. Biochem. Biophys. Res. Commun. 250:623-28
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 623-628
    • Scherf, U.1    Kalab, P.2    Dasso, M.3    Pastan, I.4    Brinkman, U.5
  • 216
    • 0031775572 scopus 로고    scopus 로고
    • The yopJ locus is required for Yersinia-mediated inhibition of NF-kB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity
    • Schesser K, Splik AK, Dukuzumuremyi JM, Neurath MF, Pettersson S, Wolf-Watz H. 1998. The yopJ locus is required for Yersinia-mediated inhibition of NF-kB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity. Mol. Microbiol. 28:1067-79
    • (1998) Mol. Microbiol. , vol.28 , pp. 1067-1079
    • Schesser, K.1    Splik, A.K.2    Dukuzumuremyi, J.M.3    Neurath, M.F.4    Pettersson, S.5    Wolf-Watz, H.6
  • 217
    • 0027266844 scopus 로고
    • Studies of T-cell deletion and T-cell anergy following in vivo administration of SEB to normal and lupus-prone mice
    • Scott DE, Kisch WJ, Steinberg AD. 1993. Studies of T-cell deletion and T-cell anergy following in vivo administration of SEB to normal and lupus-prone mice. J. Immunol. 150:664
    • (1993) J. Immunol. , vol.150 , pp. 664
    • Scott, D.E.1    Kisch, W.J.2    Steinberg, A.D.3
  • 218
    • 0029942531 scopus 로고    scopus 로고
    • Enteric bacterial toxins: Mechanisms Of action and linkage to intestinal secretion
    • Sears CL, Kaper JB. 1996. Enteric bacterial toxins: mechanisms Of action and linkage to intestinal secretion. Microbiol. Rev.: 167-215
    • (1996) Microbiol. Rev. , pp. 167-215
    • Sears, C.L.1    Kaper, J.B.2
  • 219
    • 0032539674 scopus 로고    scopus 로고
    • Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome
    • Segal G, Purcell M, Shuman HA. 1998. Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome. Proc. Natl. Acad. Sci. USA 95:1669-74
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1669-1674
    • Segal, G.1    Purcell, M.2    Shuman, H.A.3
  • 221
    • 0030032988 scopus 로고    scopus 로고
    • M cells and the pathogenesis of mucosal and systemic infections
    • Siebers A, Finlay BB. 1996. M cells and the pathogenesis of mucosal and systemic infections. Trends Microbiol. 4:22-29
    • (1996) Trends Microbiol. , vol.4 , pp. 22-29
    • Siebers, A.1    Finlay, B.B.2
  • 222
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of nuclear factor-kB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song HY, Regnier CH, Kirschning CJ, Goeddel DV, Rothe M. 1997. Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc. Natl. Acad. Sci. USA 94:9792-96
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9792-9796
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3    Goeddel, D.V.4    Rothe, M.5
  • 223
    • 0028345655 scopus 로고
    • Rickettsia rickettsii infection of cultured human endothelial cells induces tissue factor expression
    • Sporn LA, Haidaris PJ, Shi R-J, Nemerson Y, Silverman DJ, Marder VJ. 1994. Rickettsia rickettsii infection of cultured human endothelial cells induces tissue factor expression. Blood 83:1527-34
    • (1994) Blood , vol.83 , pp. 1527-1534
    • Sporn, L.A.1    Haidaris, P.J.2    Shi, R.-J.3    Nemerson, Y.4    Silverman, D.J.5    Marder, V.J.6
  • 224
    • 0029922228 scopus 로고    scopus 로고
    • Interleukinla production during Rickettsia rickettsii infection of cultured endothelial cells: Potential role in autocrine cell stimulation
    • Sporn LA, Marder VJ. 1996. Interleukinla production during Rickettsia rickettsii infection of cultured endothelial cells: potential role in autocrine cell stimulation. Infect. Immun. 64:1609-13
    • (1996) Infect. Immun. , vol.64 , pp. 1609-1613
    • Sporn, L.A.1    Marder, V.J.2
  • 225
    • 0030979518 scopus 로고    scopus 로고
    • Rickettsia rickettsii infection of cultured human endothelial cells induces NF-kB activation
    • Sporn LA, Sahni SK, Lerner NB, Murder VJ, Silverman DJ, et al. 1997. Rickettsia rickettsii infection of cultured human endothelial cells induces NF-kB activation. Infect. Immun. 65:2786-91
    • (1997) Infect. Immun. , vol.65 , pp. 2786-2791
    • Sporn, L.A.1    Sahni, S.K.2    Lerner, N.B.3    Murder, V.J.4    Silverman, D.J.5
  • 227
    • 0031013334 scopus 로고    scopus 로고
    • Superantigens: Their role in infectious diseases
    • Stevens DL. 1997. Superantigens: their role in infectious diseases, Immunol. Invest. 26:275-81
    • (1997) Immunol. Invest. , vol.26 , pp. 275-281
    • Stevens, D.L.1
  • 228
    • 0029883062 scopus 로고    scopus 로고
    • Pasteurella haemolytica leukotoxin induces bovine leukocytes to undergo morphologic changes with apoptosis in vitro
    • Stevens PK, Cruprynski CJ. 1996. Pasteurella haemolytica leukotoxin induces bovine leukocytes to undergo morphologic changes with apoptosis in vitro. Infect. Immun. 64:2687-94
    • (1996) Infect. Immun. , vol.64 , pp. 2687-2694
    • Stevens, P.K.1    Cruprynski, C.J.2
  • 230
    • 0021912262 scopus 로고
    • Staphylococcal alpha toxins stimulate synthesis of prostacyclic cultured endothelial cells from pig pulmonary arteries
    • Suttorp N, Seeger W, Dewein E, Bhakdi S, Roka L. 1985. Staphylococcal alpha toxins stimulate synthesis of prostacyclic cultured endothelial cells from pig pulmonary arteries. Am. J. Physiol. 248:C127-C135
    • (1985) Am. J. Physiol. , vol.248
    • Suttorp, N.1    Seeger, W.2    Dewein, E.3    Bhakdi, S.4    Roka, L.5
  • 231
    • 0023064356 scopus 로고
    • Mechanism of leukotriene generation in polymorphonuclear leukocytes by staphylococcal alpha-toxin
    • Suttorp N, Seeger W, Zucker-Reinmann J, Roka L, and Bhakdi S. 1987. Mechanism of leukotriene generation in polymorphonuclear leukocytes by staphylococcal alpha-toxin. Infect. Immun. 55:104-9
    • (1987) Infect. Immun. , vol.55 , pp. 104-109
    • Suttorp, N.1    Seeger, W.2    Zucker-Reinmann, J.3    Roka, L.4    Bhakdi, S.5
  • 232
    • 0018827360 scopus 로고
    • Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans
    • Taichman N, Dean R, Sanderson C. 1980. Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans. Infect. Immun. 28:258-68
    • (1980) Infect. Immun. , vol.28 , pp. 258-268
    • Taichman, N.1    Dean, R.2    Sanderson, C.3
  • 233
    • 0029758833 scopus 로고    scopus 로고
    • Cleavage of lamin A by Mch2 alpha but not CPP32: Multiple interleukin 1β-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis
    • Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack G, et al. 1996. Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1β-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc. Natl. Acad. Sci. USA 93:8395-400
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8395-8400
    • Takahashi, A.1    Alnemri, E.S.2    Lazebnik, Y.A.3    Fernandes-Alnemri, T.4    Litwack, G.5
  • 234
    • 0025866283 scopus 로고
    • The pathogenic mechanisms of Shiga toxin and the Shiga like toxins
    • Tesh V, O'Brien A. 1991. The pathogenic mechanisms of Shiga toxin and the Shiga like toxins. Mol. Microbiol. 5:1817-22
    • (1991) Mol. Microbiol. , vol.5 , pp. 1817-1822
    • Tesh, V.1    O'Brien, A.2
  • 236
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular parasite, Listeria monocytogenes
    • Tilney L, Portnoy D. 1989. Actin filaments and the growth, movement, and spread of the intracellular parasite, Listeria monocytogenes. J. Cell Biol. 109:1597-8
    • (1989) J. Cell Biol. , vol.109 , pp. 1597-1598
    • Tilney, L.1    Portnoy, D.2
  • 237
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-kB but not Fas/APO-1-initiated apoptosis
    • Ting AT, Pimentel-Muinos FX, Seed B. 1996. RIP mediates tumor necrosis factor receptor 1 activation of NF-kB but not Fas/APO-1-initiated apoptosis. EMBO J. 15:6189-96
    • (1996) EMBO J. , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 238
    • 0018356472 scopus 로고
    • Extraction and partial characterization of a leukotoxin from a plaque derived gram-negative microorganism
    • Tsai C, McArthur W, Baehni P, Hammond B, Taichman N. 1979. Extraction and partial characterization of a leukotoxin from a plaque derived gram-negative microorganism. Infect. Immun. 25:427-39
    • (1979) Infect. Immun. , vol.25 , pp. 427-439
    • Tsai, C.1    McArthur, W.2    Baehni, P.3    Hammond, B.4    Taichman, N.5
  • 239
    • 0021679848 scopus 로고
    • Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation
    • Tsujimoto Y. Finger LR, Yunis J, Nowell PC, Croce CM. 1984. Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation. Science 226:1097-99
    • (1984) Science , vol.226 , pp. 1097-1099
    • Tsujimoto, Y.1    Finger, L.R.2    Yunis, J.3    Nowell, P.C.4    Croce, C.M.5
  • 240
    • 0021802289 scopus 로고
    • Characterization of two adhesins of Bordetella pertussis for human ciliated respiratory-epithelial cells
    • Tuomanen E, Weiss AA. 1985. Characterization of two adhesins of Bordetella pertussis for human ciliated respiratory-epithelial cells. J. Infect. Dis. 152:118-25
    • (1985) J. Infect. Dis. , vol.152 , pp. 118-125
    • Tuomanen, E.1    Weiss, A.A.2
  • 242
    • 0027050145 scopus 로고
    • Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2
    • Vaux DL, Weissman IL, Kim SK. 1992. Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2. Science 258:1955-57
    • (1992) Science , vol.258 , pp. 1955-1957
    • Vaux, D.L.1    Weissman, I.L.2    Kim, S.K.3
  • 243
    • 0027427492 scopus 로고
    • Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
    • Veis DJ, Sorenson CM, Shutter JR. Korsmeyer SJ. 1993. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell 75:229-40
    • (1993) Cell , vol.75 , pp. 229-240
    • Veis, D.J.1    Sorenson, C.M.2    Shutter, J.R.3    Korsmeyer, S.J.4
  • 244
    • 0030980652 scopus 로고    scopus 로고
    • Avirulence genes in plant-pathogenic bacteria: Signals or weapons?
    • Vivian A, Gibbon MJ. 1997. Avirulence genes in plant-pathogenic bacteria: signals or weapons? Microbiology 143:693-4
    • (1997) Microbiology , vol.143 , pp. 693-694
    • Vivian, A.1    Gibbon, M.J.2
  • 245
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-kB
    • Wang CY, Mayo MW, Baldwin AS Jr. 1996. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kB. Science 274:784-87
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin A.S., Jr.3
  • 246
    • 0024495091 scopus 로고
    • Role of M cells in initial antigen uptake and in ulcer formation in rabbit intestinal loop model of shigellosis
    • Wassef JS, Keren DF, Mailloux JL. 1989. Role of M cells in initial antigen uptake and in ulcer formation in rabbit intestinal loop model of shigellosis, Infect. Immun. 57:858-63
    • (1989) Infect. Immun. , vol.57 , pp. 858-863
    • Wassef, J.S.1    Keren, D.F.2    Mailloux, J.L.3
  • 247
    • 0028983364 scopus 로고
    • Selective depletion of Vb-bearing T cells in patients with severe invasive group A streptococcal infection and streptococcal toxic shock syndrome
    • Watanabe-Ohnish R, Low D, McGeer A, Stevens D, Schlievert P, et al. 1995. Selective depletion of Vb-bearing T cells in patients with severe invasive group A streptococcal infection and streptococcal toxic shock syndrome. J. Infect. Dis. 171:78-84
    • (1995) J. Infect. Dis. , vol.171 , pp. 78-84
    • Watanabe-Ohnish, R.1    Low, D.2    McGeer, A.3    Stevens, D.4    Schlievert, P.5
  • 248
    • 0024388753 scopus 로고
    • Lethal infection by Bordetella pertussis in the infant mouse model
    • Weiss AA, Goodwin MS. 1989, Lethal infection by Bordetella pertussis in the infant mouse model. Infect. Immun. 57: 3757-64
    • (1989) Infect. Immun. , vol.57 , pp. 3757-3764
    • Weiss, A.A.1    Goodwin, M.S.2
  • 249
    • 0032441640 scopus 로고    scopus 로고
    • Staphylococcus aureus Agr and Sar global regulators influence internalization and induction of apoptosis
    • Wesson CA, Liou LE, Todd KM, Bohach GA, Trumble WR, Bayles K. 1998. Staphylococcus aureus Agr and Sar global regulators influence internalization and induction of apoptosis. Infect. Immun. 66:5238-43
    • (1998) Infect. Immun. , vol.66 , pp. 5238-5243
    • Wesson, C.A.1    Liou, L.E.2    Todd, K.M.3    Bohach, G.A.4    Trumble, W.R.5    Bayles, K.6
  • 250
    • 0023134272 scopus 로고
    • Expression of adenovirus ElB mutant phenotypes is dependent on the host cell and on synthesis of ElA proteins
    • White E, Stillman B. 1987. Expression of adenovirus ElB mutant phenotypes is dependent on the host cell and on synthesis of ElA proteins. J. Virol. 61:426-35
    • (1987) J. Virol. , vol.61 , pp. 426-435
    • White, E.1    Stillman, B.2
  • 252
    • 0029880987 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
    • Xue D, Shaham S, Horvitz HR. 1996. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev. 1:1073-83
    • (1996) Genes Dev. , vol.1 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 253
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, Kim CN, Ibrado AM, Cai J, et al. 1997. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275:1129-32
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6
  • 254
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of procaspases by oligomerization
    • Yang X, Chang HY, Baltimore D. 1998. Autoproteolytic activation of procaspases by oligomerization. Mol. Cell. 1:319-25
    • (1998) Mol. Cell. , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 255
    • 0025255636 scopus 로고
    • The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death
    • Yuan JY, Horvitz HR. 1990. The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death. Dev. Biol. 138:33-41
    • (1990) Dev. Biol. , vol.138 , pp. 33-41
    • Yuan, J.Y.1    Horvitz, H.R.2
  • 256
    • 0032580361 scopus 로고    scopus 로고
    • Subcellular and submitochondrial mode of action of Bcl-2-like oncoproteins
    • Zamzami N, Brenner C, Marzo I, Susin SA, Kroemer G. 1998. Subcellular and submitochondrial mode of action of Bcl-2-like oncoproteins. Oncogene 16:2265-82
    • (1998) Oncogene , vol.16 , pp. 2265-2282
    • Zamzami, N.1    Brenner, C.2    Marzo, I.3    Susin, S.A.4    Kroemer, G.5
  • 257
    • 0030613551 scopus 로고    scopus 로고
    • The IkB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkB phosphorylation and NF-kB activation
    • Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M. 1997. The IkB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkB phosphorylation and NF-kB activation. Cell 91:243-52
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 258
    • 0029848765 scopus 로고    scopus 로고
    • Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells
    • Zha H, Fisk HA, Yaffe MP, Mahajan N, Herman B, Reed JC. 1996. Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells. Mol. Cell. Biol. 16:6494-508
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6494-6508
    • Zha, H.1    Fisk, H.A.2    Yaffe, M.P.3    Mahajan, N.4    Herman, B.5    Reed, J.C.6
  • 259
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ. 1996. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87:619-28
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 260
    • 0026671268 scopus 로고
    • Defective mainTenance of T cell tolerance to a superantigen in MRL-lpr/lpr mice
    • Zhou T, Bluethmann H, Zhang J, Edwards CK III, Mountz JD. 1992, Defective mainTenance of T cell tolerance to a superantigen in MRL-lpr/lpr mice. J. Exp. Med. 176:1063
    • (1992) J. Exp. Med. , vol.176 , pp. 1063
    • Zhou, T.1    Bluethmann, H.2    Zhang, J.3    Edwards C.K. III4    Mountz, J.D.5
  • 261
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. 1997. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90:405-13
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 262
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky A, Prevost MC, Sansonetti PJ. 1992. Shigella flexneri induces apoptosis in infected macrophages. Nature 358:167-68
    • (1992) Nature , vol.358 , pp. 167-168
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.