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Volumn 49, Issue , 2016, Pages 493-504

Multifunctional murrel caspase 1, 2, 3, 8 and 9: Conservation, uniqueness and their pathogen-induced expression pattern

Author keywords

Caspase; Epizootic ulcerative syndrome; Innate immunity; Pathogen induced gene expression; Snakehead murrel

Indexed keywords

CASPASE; COMPLEMENTARY DNA; FISH PROTEIN; MESSENGER RNA;

EID: 84955086863     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2016.01.008     Document Type: Article
Times cited : (51)

References (69)
  • 1
    • 0032511880 scopus 로고    scopus 로고
    • Cell suicide for beginners
    • Raff M. Cell suicide for beginners. Nature 1998, 396(6707):119-122. 10.1038/24055.
    • (1998) Nature , vol.396 , Issue.6707 , pp. 119-122
    • Raff, M.1
  • 3
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: a review of programmed cell death
    • Elmore S. Apoptosis: a review of programmed cell death. Toxicol. Pathol. 2007, 35(4):495-516. 10.1080/01926230701320337.
    • (2007) Toxicol. Pathol. , vol.35 , Issue.4 , pp. 495-516
    • Elmore, S.1
  • 5
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: functions and regulation of caspases
    • Chang H.Y., Yang X. Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 2000, 64(4):821-846.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , Issue.4 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 6
    • 0346880485 scopus 로고    scopus 로고
    • The death effector domain protein family
    • Barnhart B.C., Lee J.C., Alappat E.C., Peter M.E. The death effector domain protein family. Oncogene 2003 Nov 24, 22(53):8634-8644.
    • (2003) Oncogene , vol.22 , Issue.53 , pp. 8634-8644
    • Barnhart, B.C.1    Lee, J.C.2    Alappat, E.C.3    Peter, M.E.4
  • 7
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: a searchable database of caspase substrates
    • Lüthi A.U., Martin S.J. The CASBAH: a searchable database of caspase substrates. Cell Death Differ. 2007 Apr, 14(4):641-650.
    • (2007) Cell Death Differ. , vol.14 , Issue.4 , pp. 641-650
    • Lüthi, A.U.1    Martin, S.J.2
  • 8
    • 66449088641 scopus 로고    scopus 로고
    • Pathogen recognition and inflammatory signaling in innate immune defenses
    • Mogensen T.H. Pathogen recognition and inflammatory signaling in innate immune defenses. Clin. Microbiol. Rev. 2009, 22(2):240-273. 10.1128/CMR.00046-08.
    • (2009) Clin. Microbiol. Rev. , vol.22 , Issue.2 , pp. 240-273
    • Mogensen, T.H.1
  • 9
    • 80052179138 scopus 로고    scopus 로고
    • Caspase-1 induced pyroptotic cell death
    • Miao E.A., Rajan J.V., Aderem A. Caspase-1 induced pyroptotic cell death. Immunol. Rev. 2011, 243(1):206-214. 10.1111/j.1600-065X.2011.01044.x.
    • (2011) Immunol. Rev. , vol.243 , Issue.1 , pp. 206-214
    • Miao, E.A.1    Rajan, J.V.2    Aderem, A.3
  • 10
    • 84862908207 scopus 로고    scopus 로고
    • Cell death and infection: a double-edged sword for host and pathogen survival
    • Ashida H., Mimuro H., Ogawa M., et al. Cell death and infection: a double-edged sword for host and pathogen survival. J. Cell Biol. 2011, 195(6):931-942. 10.1083/jcb.201108081.
    • (2011) J. Cell Biol. , vol.195 , Issue.6 , pp. 931-942
    • Ashida, H.1    Mimuro, H.2    Ogawa, M.3
  • 11
  • 12
    • 0034596826 scopus 로고    scopus 로고
    • Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis
    • Jesenberger V., Procyk K.J., Yuan J., Reipert S., Baccarini M. Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis. J. Exp. Med. 2000, 192(7):1035-1046.
    • (2000) J. Exp. Med. , vol.192 , Issue.7 , pp. 1035-1046
    • Jesenberger, V.1    Procyk, K.J.2    Yuan, J.3    Reipert, S.4    Baccarini, M.5
  • 13
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O., Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003, 114:181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 14
    • 0037815277 scopus 로고    scopus 로고
    • Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis
    • Harper N., Hughes M., MacFarlane M., Cohen G.M. Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis. J. Biol. Chem. 2003, 278:25534-25541.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25534-25541
    • Harper, N.1    Hughes, M.2    MacFarlane, M.3    Cohen, G.M.4
  • 16
    • 62349098335 scopus 로고    scopus 로고
    • Caspases: evolutionary aspects of their functions in vertebrates
    • Sakamaki K., Satou Y. Caspases: evolutionary aspects of their functions in vertebrates. J. Fish. Biol. 2009, 74(4):727-753.
    • (2009) J. Fish. Biol. , vol.74 , Issue.4 , pp. 727-753
    • Sakamaki, K.1    Satou, Y.2
  • 17
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: a comprehensive update of caspase substrates
    • Fischer U., Janicke R.U., Schulze-Osthoff K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 2003, 10:76-100.
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 19
    • 30344459150 scopus 로고    scopus 로고
    • In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
    • Tu S., McStay G.P., Boucher L.M., Mak T., Beere H.M., Green D.R. In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat. Cell Biol. 2006, 8:72-77.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 72-77
    • Tu, S.1    McStay, G.P.2    Boucher, L.M.3    Mak, T.4    Beere, H.M.5    Green, D.R.6
  • 20
    • 0034616336 scopus 로고    scopus 로고
    • Structure, expression, and function of the Xenopus laevis caspase family
    • Nakajima K., Takahashi A., Yaoita Y. Structure, expression, and function of the Xenopus laevis caspase family. J. Biol. Chem. 2000, 275:10484-10491.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10484-10491
    • Nakajima, K.1    Takahashi, A.2    Yaoita, Y.3
  • 21
    • 30044435192 scopus 로고    scopus 로고
    • Unique and overlapping substrate specificities of caspase-8 and caspase-10
    • Fischer U., Stroh C., Schulze-Osthoff K. Unique and overlapping substrate specificities of caspase-8 and caspase-10. Oncogene 2006, 25:152-159.
    • (2006) Oncogene , vol.25 , pp. 152-159
    • Fischer, U.1    Stroh, C.2    Schulze-Osthoff, K.3
  • 22
    • 34249282047 scopus 로고    scopus 로고
    • Conserved function of caspase-8 in apoptosis during bony fish evolution
    • Sakata S., Yan Y., Satou Y., et al. Conserved function of caspase-8 in apoptosis during bony fish evolution. Gene 2007, 396(1):134-148. 10.1016/j.gene.2007.03.010.
    • (2007) Gene , vol.396 , Issue.1 , pp. 134-148
    • Sakata, S.1    Yan, Y.2    Satou, Y.3
  • 23
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 26
    • 0141736945 scopus 로고    scopus 로고
    • Observations on the histological alterations in various tissues of EUS affected fish, Channa striatus (Bloch)
    • Mastan S.A., Qureshi T.A. Observations on the histological alterations in various tissues of EUS affected fish, Channa striatus (Bloch). J. Environ. Biol. 2003, 24(4):405-410.
    • (2003) J. Environ. Biol. , vol.24 , Issue.4 , pp. 405-410
    • Mastan, S.A.1    Qureshi, T.A.2
  • 28
    • 84928214231 scopus 로고    scopus 로고
    • Comparative analysis of CsCu/ZnSOD defense role by molecular characterization: gene expression-enzyme activity-protein level
    • Kumaresan V., Gnanam A.J., Pasupuleti M., Arasu M.V., Al-Dhabi N.A., Harikrishnan R., Arockiaraj J. Comparative analysis of CsCu/ZnSOD defense role by molecular characterization: gene expression-enzyme activity-protein level. Gene 2015, 564(1):53-62. 10.1016/j.gene.2015.03.042.
    • (2015) Gene , vol.564 , Issue.1 , pp. 53-62
    • Kumaresan, V.1    Gnanam, A.J.2    Pasupuleti, M.3    Arasu, M.V.4    Al-Dhabi, N.A.5    Harikrishnan, R.6    Arockiaraj, J.7
  • 29
    • 84912143362 scopus 로고    scopus 로고
    • An anti-apoptotic B-cell lymphoma-2 (BCL-2) from Channa striatus: Sequence analysis and delayed and advanced gene expression in response to fungal, bacterial and poly I: C induction
    • Arockiaraj J., Palanisamy R., Arasu A., Sathyamoorthi A., Kumaresan V., Bhatt P., Chaurasia M.K., Pasupuleti M., Gnanam A.J. An anti-apoptotic B-cell lymphoma-2 (BCL-2) from Channa striatus: Sequence analysis and delayed and advanced gene expression in response to fungal, bacterial and poly I: C induction. Mol. Immunol. 2015, 63(2):586-594. 10.1016/j.molimm.2014.07.018.
    • (2015) Mol. Immunol. , vol.63 , Issue.2 , pp. 586-594
    • Arockiaraj, J.1    Palanisamy, R.2    Arasu, A.3    Sathyamoorthi, A.4    Kumaresan, V.5    Bhatt, P.6    Chaurasia, M.K.7    Pasupuleti, M.8    Gnanam, A.J.9
  • 30
    • 84879498569 scopus 로고    scopus 로고
    • Apoptotic responses of zebrafish (Danio rerio) after exposure with microcystin-LR under different ambient temperatures
    • Ji W., Liang H., Zhou W., Zhang X. Apoptotic responses of zebrafish (Danio rerio) after exposure with microcystin-LR under different ambient temperatures. J. Appl. Toxicol. 2013 Aug, 33(8):799-806. 10.1002/jat.2735.
    • (2013) J. Appl. Toxicol. , vol.33 , Issue.8 , pp. 799-806
    • Ji, W.1    Liang, H.2    Zhou, W.3    Zhang, X.4
  • 31
    • 33748785440 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene
    • Reis M.I., Nascimento D.S., do Vale A., Silva M.T., dos Santos N.M. Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene. Mol. Immunol. 2007 Feb, 44(5):774-783.
    • (2007) Mol. Immunol. , vol.44 , Issue.5 , pp. 774-783
    • Reis, M.I.1    Nascimento, D.S.2    do Vale, A.3    Silva, M.T.4    dos Santos, N.M.5
  • 32
    • 84866629314 scopus 로고    scopus 로고
    • Development of a caspase-3 antibody as a tool for detecting apoptosis in cells from rainbow trout (Oncorhynchus mykiss)
    • Rojas V., Guzmán F., Valenzuela C., Marshall S., Mercado L. Development of a caspase-3 antibody as a tool for detecting apoptosis in cells from rainbow trout (Oncorhynchus mykiss). Electron. J. Biotechnol. 2012, 15:1-11.
    • (2012) Electron. J. Biotechnol. , vol.15 , pp. 1-11
    • Rojas, V.1    Guzmán, F.2    Valenzuela, C.3    Marshall, S.4    Mercado, L.5
  • 33
    • 35649028361 scopus 로고    scopus 로고
    • Molecular cloning, expression, and functional analysis of caspase-10 from Japanese flounder Paralichthys olivaceus
    • Kurobe T., Hirono I., Kondo H., Yamashita M., Aoki T. Molecular cloning, expression, and functional analysis of caspase-10 from Japanese flounder Paralichthys olivaceus. Fish. Shellfish Immunol. 2007 Dec, 23(6):1266-1274.
    • (2007) Fish. Shellfish Immunol. , vol.23 , Issue.6 , pp. 1266-1274
    • Kurobe, T.1    Hirono, I.2    Kondo, H.3    Yamashita, M.4    Aoki, T.5
  • 35
    • 84904088877 scopus 로고    scopus 로고
    • Three representative subtypes of caspase in miiuy croaker: genomic organization, evolution and immune responses to bacterial challenge
    • Ren L., Wang R., Xu T. Three representative subtypes of caspase in miiuy croaker: genomic organization, evolution and immune responses to bacterial challenge. Fish. Shellfish Immunol. 2014 Sep, 40(1):61-68.
    • (2014) Fish. Shellfish Immunol. , vol.40 , Issue.1 , pp. 61-68
    • Ren, L.1    Wang, R.2    Xu, T.3
  • 36
    • 34548209240 scopus 로고    scopus 로고
    • Molecular and functional characterization of gilthead seabream Sparus aurata caspase-1: the first identification of an inflammatory caspase in fish
    • López-Castejón G., Sepulcre M.P., Mulero I., Pelegrín P., Meseguer J., Mulero V. Molecular and functional characterization of gilthead seabream Sparus aurata caspase-1: the first identification of an inflammatory caspase in fish. Mol. Immunol. 2008 Jan, 45(1):49-57.
    • (2008) Mol. Immunol. , vol.45 , Issue.1 , pp. 49-57
    • López-Castejón, G.1    Sepulcre, M.P.2    Mulero, I.3    Pelegrín, P.4    Meseguer, J.5    Mulero, V.6
  • 37
    • 84884125631 scopus 로고    scopus 로고
    • Cadmium triggers kidney cell apoptosis of purse red common carp (Cyprinus carpio) without caspase-8 activation
    • Gao D., Xu Z., Zhang X., Zhu C., Wang Y., Min W. Cadmium triggers kidney cell apoptosis of purse red common carp (Cyprinus carpio) without caspase-8 activation. Dev. Comp. Immunol. 2013 Dec, 41(4):728-737.
    • (2013) Dev. Comp. Immunol. , vol.41 , Issue.4 , pp. 728-737
    • Gao, D.1    Xu, Z.2    Zhang, X.3    Zhu, C.4    Wang, Y.5    Min, W.6
  • 38
    • 84872600707 scopus 로고    scopus 로고
    • An upstream initiator caspase 10 of snakehead murrel Channa striatus, containing DED, p20 and p10 subunits: molecular cloning, gene expression and proteolytic activity
    • Arockiaraj J., Gnanam A.J., Muthukrishnan D., Pasupuleti M., Milton J., Singh A. An upstream initiator caspase 10 of snakehead murrel Channa striatus, containing DED, p20 and p10 subunits: molecular cloning, gene expression and proteolytic activity. Fish. Shellfish Immunol. 2013, 34(2):505-513.
    • (2013) Fish. Shellfish Immunol. , vol.34 , Issue.2 , pp. 505-513
    • Arockiaraj, J.1    Gnanam, A.J.2    Muthukrishnan, D.3    Pasupuleti, M.4    Milton, J.5    Singh, A.6
  • 39
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001 Dec, 25(4):402-408.
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 40
    • 77449146076 scopus 로고    scopus 로고
    • Protection of retinal ganglion cells by caspase substrate-binding peptide IQACRG from N-methyl-d-aspartate receptor-mediated excitotoxicity
    • Seki M., Soussou W., Manabe S., Lipton S.A. Protection of retinal ganglion cells by caspase substrate-binding peptide IQACRG from N-methyl-d-aspartate receptor-mediated excitotoxicity. Investig. Ophthalmol. Vis. Sci. 2010, 51(2):1198-1207. 10.1167/iovs.09-4102.
    • (2010) Investig. Ophthalmol. Vis. Sci. , vol.51 , Issue.2 , pp. 1198-1207
    • Seki, M.1    Soussou, W.2    Manabe, S.3    Lipton, S.A.4
  • 41
    • 84923233758 scopus 로고    scopus 로고
    • Comparative structural analysis of the caspase family with other clan CD cysteine peptidases
    • McLuskey K., Mottram J.C. Comparative structural analysis of the caspase family with other clan CD cysteine peptidases. Biochem. J. 2015, 466(Pt 2):219-232.
    • (2015) Biochem. J. , vol.466 , pp. 219-232
    • McLuskey, K.1    Mottram, J.C.2
  • 42
    • 41949117115 scopus 로고    scopus 로고
    • Dynamic regulation of neutrophil survival through tyrosine phosphorylation or dephosphorylation of caspase-8
    • Jia S.H., Parodo J., Kapus A., Rotstein O.D., Marshall J.C. Dynamic regulation of neutrophil survival through tyrosine phosphorylation or dephosphorylation of caspase-8. J. Biol. Chem. 2008, 283(9):5402-5413.
    • (2008) J. Biol. Chem. , vol.283 , Issue.9 , pp. 5402-5413
    • Jia, S.H.1    Parodo, J.2    Kapus, A.3    Rotstein, O.D.4    Marshall, J.C.5
  • 44
    • 84879033457 scopus 로고    scopus 로고
    • Transmembrane Protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis
    • Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B. Transmembrane Protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis. J. Biol. Chem. 2013 Jun 14, 288(24):17908-17917.
    • (2013) J. Biol. Chem. , vol.288 , Issue.24 , pp. 17908-17917
    • Li, C.1    Wei, J.2    Li, Y.3    He, X.4    Zhou, Q.5    Yan, J.6    Zhang, J.7    Liu, Y.8    Liu, Y.9    Shu, H.B.10
  • 45
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome C maintains mitochondrial transmembrane potential and Atp generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • Waterhouse N.J., Goldstein J.C., von Ahsen O., Schuler M., Newmeyer D.D., Green D.R. Cytochrome C maintains mitochondrial transmembrane potential and Atp generation after outer mitochondrial membrane permeabilization during the apoptotic process. J. Cell Biol. 2001, 153(2):319-328.
    • (2001) J. Cell Biol. , vol.153 , Issue.2 , pp. 319-328
    • Waterhouse, N.J.1    Goldstein, J.C.2    von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 46
    • 0037184928 scopus 로고    scopus 로고
    • Activation of initiator caspases through a stable dimeric intermediate
    • Chen M., Orozco A., Spencer D.M., Wang J. Activation of initiator caspases through a stable dimeric intermediate. J. Biol. Chem. 2002, 277:50761-50767.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50761-50767
    • Chen, M.1    Orozco, A.2    Spencer, D.M.3    Wang, J.4
  • 47
    • 0037291890 scopus 로고    scopus 로고
    • Insights into the regulatory mechanism for caspase-8 activation
    • Donepudi M., Sweeney A.M., Briand C., Grutter M.G. Insights into the regulatory mechanism for caspase-8 activation. Mol. Cell. 2003, 11:543-549.
    • (2003) Mol. Cell. , vol.11 , pp. 543-549
    • Donepudi, M.1    Sweeney, A.M.2    Briand, C.3    Grutter, M.G.4
  • 48
    • 8844224859 scopus 로고    scopus 로고
    • The biochemical mechanism of caspase-2 activation
    • Baliga B.C., Read S.H., Kumar S. The biochemical mechanism of caspase-2 activation. Cell Death Differ. 2004, 11:1234-1241.
    • (2004) Cell Death Differ. , vol.11 , pp. 1234-1241
    • Baliga, B.C.1    Read, S.H.2    Kumar, S.3
  • 50
    • 70549089770 scopus 로고    scopus 로고
    • Cellular and nuclear degradation during apoptosis
    • He B., Lu N., Zhou Z. Cellular and nuclear degradation during apoptosis. Curr. Opin. Cell Biol. 2009, 21(6):900-912.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , Issue.6 , pp. 900-912
    • He, B.1    Lu, N.2    Zhou, Z.3
  • 52
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 β-converting enzyme
    • Kumar S., Kinoshita M., Noda M., Copeland N.G., Jenkins N.A. Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 β-converting enzyme. Genes Dev. 1994, 8:1613-1626.
    • (1994) Genes Dev. , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 53
    • 0033590598 scopus 로고    scopus 로고
    • Structure and chromosome localization of the human CASP8 gene
    • Grenet J., Teitz T., Wei T., Valentine V., Kidd V.J. Structure and chromosome localization of the human CASP8 gene. Gene 1999, 226(2):225-232.
    • (1999) Gene , vol.226 , Issue.2 , pp. 225-232
    • Grenet, J.1    Teitz, T.2    Wei, T.3    Valentine, V.4    Kidd, V.J.5
  • 55
    • 9644307904 scopus 로고    scopus 로고
    • Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids
    • Enoksson M., Robertson J.D., Gogvadze V., Bu P., Kropotov A., Zhivotovsky B., Orrenius S. Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids. J. Biol. Chem. 2004 Nov 26, 279(48):49575-49578.
    • (2004) J. Biol. Chem. , vol.279 , Issue.48 , pp. 49575-49578
    • Enoksson, M.1    Robertson, J.D.2    Gogvadze, V.3    Bu, P.4    Kropotov, A.5    Zhivotovsky, B.6    Orrenius, S.7
  • 58
    • 84904088877 scopus 로고    scopus 로고
    • Three representative subtypes of caspase in miiuy croaker: genomic organization, evolution and immune responses to bacterial challenge
    • Ren L., Wang R., Xu T. Three representative subtypes of caspase in miiuy croaker: genomic organization, evolution and immune responses to bacterial challenge. Fish. Shellfish Immunol. 2014 Sep, 40(1):61-68.
    • (2014) Fish. Shellfish Immunol. , vol.40 , Issue.1 , pp. 61-68
    • Ren, L.1    Wang, R.2    Xu, T.3
  • 61
    • 0033647484 scopus 로고    scopus 로고
    • Caspase-8 in apoptosis: the beginning of "the end"?
    • Kruidering M., Evan G.I. Caspase-8 in apoptosis: the beginning of "the end"?. IUBMB Life 2000 Aug, 50(2):85-90.
    • (2000) IUBMB Life , vol.50 , Issue.2 , pp. 85-90
    • Kruidering, M.1    Evan, G.I.2
  • 62
    • 0037269681 scopus 로고    scopus 로고
    • Caspase-9 takes part in programmed cell death in developing mouse kidney
    • Araki T., Hayashi M., Nakanishi K., Morishima N., Saruta T. Caspase-9 takes part in programmed cell death in developing mouse kidney. Nephron Exp. Nephrol. 2003, 93(3):e117-e124.
    • (2003) Nephron Exp. Nephrol. , vol.93 , Issue.3 , pp. e117-e124
    • Araki, T.1    Hayashi, M.2    Nakanishi, K.3    Morishima, N.4    Saruta, T.5
  • 64
    • 84906535354 scopus 로고    scopus 로고
    • A long-awaited merger of the pathways mediating host defence and programmed cell death
    • Blander J.M. A long-awaited merger of the pathways mediating host defence and programmed cell death. Nat. Rev. Immunol. 2014 Sep, 14(9):601-618.
    • (2014) Nat. Rev. Immunol. , vol.14 , Issue.9 , pp. 601-618
    • Blander, J.M.1
  • 65
    • 84897923374 scopus 로고    scopus 로고
    • Inflammasome-mediated cell death in response to bacterial pathogens that access the host cell cytosol: lessons from legionella pneumophila
    • Casson C.N., Shin S. Inflammasome-mediated cell death in response to bacterial pathogens that access the host cell cytosol: lessons from legionella pneumophila. Front. Cell. Infect. Microbiol. 2013, 3:111.
    • (2013) Front. Cell. Infect. Microbiol. , vol.3 , pp. 111
    • Casson, C.N.1    Shin, S.2
  • 66
    • 1542375390 scopus 로고    scopus 로고
    • Caspase activation during virus infection: more than just the kiss of death?
    • Best S.M., Bloom M.E. Caspase activation during virus infection: more than just the kiss of death?. Virology 2004 Mar 15, 320(2):191-194.
    • (2004) Virology , vol.320 , Issue.2 , pp. 191-194
    • Best, S.M.1    Bloom, M.E.2
  • 67
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • Miao E.A., Leaf I.A., Treuting P.M., et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat. Immunol. 2010, 11(12):1136-1142.
    • (2010) Nat. Immunol. , vol.11 , Issue.12 , pp. 1136-1142
    • Miao, E.A.1    Leaf, I.A.2    Treuting, P.M.3
  • 68
    • 84864818802 scopus 로고    scopus 로고
    • Roles of inflammatory caspases during processing of zebrafish interleukin-1β in Francisella noatunensis infection
    • Bäumler AJ, ed
    • Vojtech L.N., Scharping N., Woodson J.C., Hansen J.D. Roles of inflammatory caspases during processing of zebrafish interleukin-1β in Francisella noatunensis infection. Infect. Immun. 2012, 80(8):2878-2885. Bäumler AJ, ed.
    • (2012) Infect. Immun. , vol.80 , Issue.8 , pp. 2878-2885
    • Vojtech, L.N.1    Scharping, N.2    Woodson, J.C.3    Hansen, J.D.4
  • 69
    • 84861209808 scopus 로고    scopus 로고
    • Fungal-induced cell cycle impairment, chromosome instability and apoptosis via differential activation of NF-κB
    • Ben-Abdallah M., Sturny-Leclère A., Avé P., Louise A., Moyrand F., Weih F., Janbon G., Mémet S. Fungal-induced cell cycle impairment, chromosome instability and apoptosis via differential activation of NF-κB. PLoS Pathog. 2012, 8(3):e1002555.
    • (2012) PLoS Pathog. , vol.8 , Issue.3 , pp. e1002555
    • Ben-Abdallah, M.1    Sturny-Leclère, A.2    Avé, P.3    Louise, A.4    Moyrand, F.5    Weih, F.6    Janbon, G.7    Mémet, S.8


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