메뉴 건너뛰기




Volumn 6, Issue 4, 2009, Pages 295-301

Expression, purification and characterization of C-FADD

Author keywords

C FADD; Expression; Monomer; Purification

Indexed keywords

CASEIN KINASE IALPHA; FAS ASSOCIATED DEATH DOMAIN PROTEIN; GLUTARALDEHYDE; POLYHISTIDINE TAG; FADD PROTEIN, MOUSE; PEPTIDE FRAGMENT; FAS ASSOCIATED DEATH DOMAIN PROTEIN[80-205]; NICKEL; UNCLASSIFIED DRUG;

EID: 69949148307     PISSN: 16727681     EISSN: None     Source Type: Journal    
DOI: 10.1038/cmi.2009.39     Document Type: Article
Times cited : (6)

References (31)
  • 1
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • DOI 10.1038/32681
    • Zhang JK, Cado D, Chen A, Kabra NH, Winoto A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature. 1998;392:296-300. (Pubitemid 28155104)
    • (1998) Nature , vol.392 , Issue.6673 , pp. 296-299
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 2
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh WC, de la Pompa JL, McCurrach ME, et al. FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science. 1998;279:954-1958.
    • (1998) Science , vol.279 , pp. 954-1958
    • Yeh, W.C.1    De La Pompa, J.L.2    McCurrach, M.E.3
  • 3
    • 0034142374 scopus 로고    scopus 로고
    • Phosphorylation of FADD/MORT1 at serine 194 and association with a 70- KDa cell cycle-regulated protein kinase
    • Scaffidi C, Volkland J, Blomberg I, Hoffmann I, Krammer PH, Peter ME. Phosphorylation of FADD/MORT1 at serine 194 and association with a 70-kDa cell cycle-regulated protein kinase. J Immunol. 2000;164:1236-1242. (Pubitemid 30067235)
    • (2000) Journal of Immunology , vol.164 , Issue.3 , pp. 1236-1242
    • Scaffidi, C.1    Volkland, J.2    Blomberg, I.3    Hoffmann, I.4    Krammer, P.H.5    Peter, M.E.6
  • 5
    • 0030001051 scopus 로고    scopus 로고
    • A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis
    • Zhang J, Winoto A. A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis. Mol Cell Biol. 1996;16:2756-2763. (Pubitemid 26163375)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.6 , pp. 2756-2763
    • Zhang, J.1    Winoto, A.2
  • 6
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin MP, Varfolomeev EE, Pancer Z, Mett IL, Camonis JH, Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem. 1995;270:7795-7798.
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 7
    • 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. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell. 1995;81:505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 8
    • 0037276437 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) DISC and beyond
    • Peter ME, Krammer PH. The CD95 (APO-1/Fas) DISC and beyond. Cell Death Differ. 2003;10:26-35.
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 9
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: Signaling and modulation. Science. 1998;281:1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 10
    • 0035192884 scopus 로고    scopus 로고
    • FLICE-inhibitory proteins: Regulators of death receptor-mediated apoptosis
    • DOI 10.1128/MCB.21.24.8247-8254.2001
    • Krueger A, Baumann S, Krammer PH, Kirchhoff S. FLICE-inhibitory proteins: Regulators of death receptor-mediated apoptosis. Mol Cell Biol. 2001;21:8247-8254. (Pubitemid 33108586)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.24 , pp. 8247-8254
    • Krueger, A.1    Baumann, S.2    Krammer, P.H.3    Kirchhoff, S.4
  • 11
    • 33751213356 scopus 로고    scopus 로고
    • Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation
    • Werner MH, Wu CW, Walsh CM. Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation. Cell Cycle. 2006;5:2332-2338.
    • (2006) Cell Cycle , vol.5 , pp. 2332-2338
    • Werner, M.H.1    Wu, C.W.2    Walsh, C.M.3
  • 14
    • 0142211350 scopus 로고    scopus 로고
    • Cell Cycle Effects by C-FADD Depend on its C-terminal Phosphorylation Site
    • DOI 10.1074/jbc.C300385200
    • Alappat EC, Volkland J, Peter ME. Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site. J Biol Chem. 2003;278:41585-41588. (Pubitemid 37310412)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 41585-41588
    • Alappat, E.C.1    Volkland, J.2    Peter, M.E.3
  • 15
  • 16
    • 0037397756 scopus 로고    scopus 로고
    • A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region
    • DOI 10.1016/S1074-7613(03)00083-9
    • Hua ZC, Sohn SJ, Kang C, Cado D, Winoto A. A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region. Immunity. 2003;18:513-521. (Pubitemid 36513633)
    • (2003) Immunity , vol.18 , Issue.4 , pp. 513-521
    • Hua, Z.C.1    Sohn, S.J.2    Kang, C.3    Cado, D.4    Winoto, A.5
  • 17
    • 0029965280 scopus 로고    scopus 로고
    • FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis
    • Chinnaiyan AM, Tepper CG, Seldin MF, et al. FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis. J Biol Chem. 1996;271:4961-4965.
    • (1996) J Biol Chem , vol.271 , pp. 4961-4965
    • Chinnaiyan, A.M.1    Tepper, C.G.2    Seldin, M.F.3
  • 19
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • DOI 10.1093/emboj/17.3.706
    • Newton K, Harris AW, Bath ML, Smith KG, Strasser A. A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes. EMBO J. 1998;17:706-718. (Pubitemid 28062050)
    • (1998) EMBO Journal , vol.17 , Issue.3 , pp. 706-718
    • Newton, K.1    Harris, A.W.2    Bath, M.L.3    Smith, K.G.C.4    Strasser, A.5
  • 20
    • 0040189996 scopus 로고    scopus 로고
    • A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts
    • DOI 10.1074/jbc.275.14.10453
    • Hueber AO, Zornig M, Bernard AM, Chautan M, Evan G.. A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts. J Biol Chem. 2000;275:10453-10462. (Pubitemid 30202106)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10453-10462
    • Hueber, A.-O.1    Zornig, M.2    Bernard, A.-M.3    Chautan, M.4    Evan, G.5
  • 24
    • 0033522889 scopus 로고    scopus 로고
    • The solution structure of FADD death domain: Structural basis of death domain interactions of Fas and FADD
    • Jeong EJ, Bang S, Lee TH, Park YI, Sim WS, Kim KS. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. J Biol Chem. 1999;274:16337-16342. (Pubitemid 129526385)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.23 , pp. 16337-16342
    • Jeong, E.-J.1    Bang, S.2    Lee, T.H.3    Park, Y.I.4    Sim, W.-S.5    Kim, K.-S.6
  • 25
    • 33846803879 scopus 로고    scopus 로고
    • Self-assembly and structural characterization of Echinococcus granulosus antigen B recombinant subunit oligomers
    • Monteiro KM, Scapin SMN, Navarro MVAS, et al. Self-assembly and structural characterization of Echinococcus granulosus antigen B recombinant subunit oligomers. Biochim Biophys Acta-Proteins and Proteomics. 2007;1774:278-285.
    • (2007) Biochim Biophys Acta-Proteins and Proteomics , vol.1774 , pp. 278-285
    • Monteiro, K.M.1    Scapin, S.M.N.2    Navarro, M.V.A.S.3
  • 26
    • 33748504779 scopus 로고    scopus 로고
    • Immobilized protein ZZ, an affinity tool for immunoglobulin isolation and immunological experimentation
    • DOI 10.1042/BA20060055
    • Chen C, Huang QL, Jiang SH, Pan X, Hua ZC. Immobilized protein ZZ, an affinity tool for immunoglobulin isolation and immunological experimentation. Biotechnol Appl Biochem. 2006;45:87-92. (Pubitemid 44358594)
    • (2006) Biotechnology and Applied Biochemistry , vol.45 , Issue.2 , pp. 87-92
    • Chen, C.1    Huang, Q.-L.2    Jiang, S.-H.3    Pan, X.4    Hua, Z.-C.5
  • 27
    • 33847211797 scopus 로고    scopus 로고
    • Polyethylenimine-complexed plasmid particles targeting focal adhesion kinase function as melanoma tumor therapeutics
    • DOI 10.1038/sj.mt.6300072, PII 6300072
    • Li SF, Dong W, Zong YW, et al. Polyethylenimine-complexed plasmid particles targeting focal adhesion kinase function as melanoma tumor therapeutics. Mol Ther. 2007;15:515-523. (Pubitemid 46306594)
    • (2007) Molecular Therapy , vol.15 , Issue.3 , pp. 515-523
    • Li, S.1    Dong, W.2    Zong, Y.3    Yin, W.4    Jin, G.5    Hu, Q.6    Huang, X.7    Jiang, W.8    Hua, Z.-C.9
  • 28
    • 0003022686 scopus 로고    scopus 로고
    • Determining the CD spectrum of a protein
    • John Wiley & Sons, Inc
    • Pain R. Determining the CD spectrum of a protein. In: Current Protocols in Protein Science. John Wiley & Sons, Inc; 1996;7:1-23.
    • (1996) Current Protocols in Protein Science , vol.7 , pp. 1-23
    • Pain, R.1
  • 30
    • 33744517489 scopus 로고    scopus 로고
    • Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis
    • DOI 10.1038/sj.cdd.4401855, PII 4401855
    • Muppidi JR, Lobito AA, Ramaswamy M, Yang JK, Wang L, Wu H, Siegel RM. Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis. Cell Death Differ. 2006;13:1641-1650. (Pubitemid 44390852)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.10 , pp. 1641-1650
    • Muppidi, J.R.1    Lobito, A.A.2    Ramaswamy, M.3    Yang, J.K.4    Wang, L.5    Wu, H.6    Siegel, R.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.