메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages

Expression of measles virus nucleoprotein induces apoptosis and modulates diverse functional proteins in cultured mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 3; REACTIVE OXYGEN METABOLITE; VIRUS NUCLEOPROTEIN; NUCLEOPROTEIN; VIRUS PROTEIN;

EID: 79954990019     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018765     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0001010466 scopus 로고    scopus 로고
    • Measles virus
    • In: Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE, editors, Philadelphia, Lippincott Williams & Wilkins 4th ed
    • Griffin DE, (2001) Measles virus. In: Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE, editors. Fields Virology Philadelphia Lippincott Williams & Wilkins 4th ed pp. 1401-1441.
    • (2001) Fields Virology , pp. 1401-1441
    • Griffin, D.E.1
  • 2
    • 0024549988 scopus 로고
    • The Sendai virus nucleocapsid exists in at least four different helical states
    • Egelman EH, Wu SS, Amrein M, Portner A, Murti G, (1989) The Sendai virus nucleocapsid exists in at least four different helical states. J Virol 63: 2233-2243.
    • (1989) J Virol , vol.63 , pp. 2233-2243
    • Egelman, E.H.1    Wu, S.S.2    Amrein, M.3    Portner, A.4    Murti, G.5
  • 3
    • 0014711995 scopus 로고
    • Observations on the structure of the nucleocapsids of some paramyxoviruses
    • Finch JT, Gibbs AJ, (1970) Observations on the structure of the nucleocapsids of some paramyxoviruses. J Gen Virol 6: 141-150.
    • (1970) J Gen Virol , vol.6 , pp. 141-150
    • Finch, J.T.1    Gibbs, A.J.2
  • 4
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • In: Fields BN, Knipe DM, Howley PM, editors, Philadelphia, Lippincott Williams & Wilkins 4th ed
    • Lamb RA, Kolakofsky D, (2001) Paramyxoviridae: The viruses and their replication. In: Fields BN, Knipe DM, Howley PM, editors. Fields Virology Philadelphia Lippincott Williams & Wilkins 4th ed pp. 1305-1340.
    • (2001) Fields Virology , pp. 1305-1340
    • Lamb, R.A.1    Kolakofsky, D.2
  • 5
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, et al. (2001) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J Biol Chem 278: 18638-18648.
    • (2001) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5
  • 6
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis JM, Johansson K, Receveur-Brechot V, Oldfield CJ, Dunker KA, et al. (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res 99: 157-167.
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5
  • 7
    • 23644449725 scopus 로고    scopus 로고
    • The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded
    • Bourhis JM, Receveur-Brechot V, Oglesbee M, Zhang X, Buccellato M, et al. (2005) The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. Protein Sci 14: 1975-1992.
    • (2005) Protein Sci , vol.14 , pp. 1975-1992
    • Bourhis, J.M.1    Receveur-Brechot, V.2    Oglesbee, M.3    Zhang, X.4    Buccellato, M.5
  • 8
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, et al. (2003) Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J Biol Chem 278: 44567-44573.
    • (2003) J Biol Chem , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5
  • 9
    • 0036337962 scopus 로고    scopus 로고
    • Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein
    • Zhang X, Glendening C, Linke H, Parks CL, Brooks C, et al. (2002) Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein. J Virol 76: 8737-8746.
    • (2002) J Virol , vol.76 , pp. 8737-8746
    • Zhang, X.1    Glendening, C.2    Linke, H.3    Parks, C.L.4    Brooks, C.5
  • 10
    • 19444370973 scopus 로고    scopus 로고
    • Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
    • Zhang X, Bourhis JM, Longhi S, Carsillo T, Buccellato M, et al. (2005) Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus. Virology 337: 162-174.
    • (2005) Virology , vol.337 , pp. 162-174
    • Zhang, X.1    Bourhis, J.M.2    Longhi, S.3    Carsillo, T.4    Buccellato, M.5
  • 11
    • 0036199090 scopus 로고    scopus 로고
    • Recognition of the measles virus nucleocapsid as a mechanism of IRF-3 activation
    • tenOever BR, Servant MJ, Grandvaux N, Lin R, Hiscott J, (2002) Recognition of the measles virus nucleocapsid as a mechanism of IRF-3 activation. J Virol 76: 3659-3669.
    • (2002) J Virol , vol.76 , pp. 3659-3669
    • tenOever, B.R.1    Servant, M.J.2    Grandvaux, N.3    Lin, R.4    Hiscott, J.5
  • 12
    • 35448995749 scopus 로고    scopus 로고
    • Measles Virus N Protein Inhibits Host Translation by Binding to eIF3-p40
    • Sato H, Masuda M, Kanai M, Tsukiyama-Kohara K, Yoneda M, et al. (2007) Measles Virus N Protein Inhibits Host Translation by Binding to eIF3-p40. J Virol 81: 11569-11576.
    • (2007) J Virol , vol.81 , pp. 11569-11576
    • Sato, H.1    Masuda, M.2    Kanai, M.3    Tsukiyama-Kohara, K.4    Yoneda, M.5
  • 13
    • 0035983614 scopus 로고    scopus 로고
    • Significant differences in nucleocapsid morphology within the Paramyxoviridae
    • Bhella D, Ralph A, Murphy LB, Yeo RP, (2002) Significant differences in nucleocapsid morphology within the Paramyxoviridae. J Gen Virol 83: 1831-1839.
    • (2002) J Gen Virol , vol.83 , pp. 1831-1839
    • Bhella, D.1    Ralph, A.2    Murphy, L.B.3    Yeo, R.P.4
  • 14
    • 0027166165 scopus 로고
    • Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures
    • Fooks AR, Stephenson JR, Warnes A, Dowsett AB, Rima BK, et al. (1993) Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures. J Gen Virol 74: 1439-1444.
    • (1993) J Gen Virol , vol.74 , pp. 1439-1444
    • Fooks, A.R.1    Stephenson, J.R.2    Warnes, A.3    Dowsett, A.B.4    Rima, B.K.5
  • 15
    • 0036441105 scopus 로고    scopus 로고
    • Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association
    • Karlin D, Longhi S, Canard B, (2002) Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association. Virology 302: 420-432.
    • (2002) Virology , vol.302 , pp. 420-432
    • Karlin, D.1    Longhi, S.2    Canard, B.3
  • 16
    • 0025983571 scopus 로고
    • Assembly of Nucleocapsid like structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein
    • Spehner D, Kirn A, Drillien R, (1991) Assembly of Nucleocapsid like structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein. J Virol 65: 6296-6300.
    • (1991) J Virol , vol.65 , pp. 6296-6300
    • Spehner, D.1    Kirn, A.2    Drillien, R.3
  • 17
    • 0029143791 scopus 로고
    • Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures
    • Warnes A, Fooks AR, Dowsett AB, Wilkinson GW, Stephenson JR, (1995) Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures. Gene 160: 173-178.
    • (1995) Gene , vol.160 , pp. 173-178
    • Warnes, A.1    Fooks, A.R.2    Dowsett, A.B.3    Wilkinson, G.W.4    Stephenson, J.R.5
  • 18
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC, Grignani F, Riccardi C, (1991) A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J Immunol Meth 139: 271-279.
    • (1991) J Immunol Meth , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 19
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry NA, Lazebnik Y, (1998) Caspases: enemies within. Science 281: 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 20
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR, (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26: 239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 21
    • 0013803932 scopus 로고
    • A histochemical study of hypertrophy and ischaemic injury of rat liver with special reference to changes in lysosomes
    • Kerr JF, (1965) A histochemical study of hypertrophy and ischaemic injury of rat liver with special reference to changes in lysosomes. J Pathol Bacterio l90: 419-35.
    • (1965) J Pathol Bacterio , vol.l90 , pp. 419-435
    • Kerr, J.F.1
  • 22
    • 0003060920 scopus 로고    scopus 로고
    • Microgel electrophoresis of DNA from individual cells: principles and methodology
    • In: Pfeifer J, editors, Plenum Press, NY
    • Singh NP, (1996) Microgel electrophoresis of DNA from individual cells: principles and methodology. In: Pfeifer J, editors. Technology for Detection of DNA Damage and Mutation pp. 3-24 Plenum Press, NY.
    • (1996) Technology for Detection of DNA Damage and Mutation , pp. 3-24
    • Singh, N.P.1
  • 23
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • Chua BT, Volbracht C, Tan KO, Li R, Yu VC, et al. (2003) Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat Cell Biol 5: 1083-1089.
    • (2003) Nat Cell Biol , vol.5 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4    Yu, V.C.5
  • 24
    • 70349651926 scopus 로고    scopus 로고
    • Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
    • Klamt F, Zdanov S, Levine RL, Pariser A, Zhang Y, et al. (2009) Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat Cell Biol 11: 1241-1246.
    • (2009) Nat Cell Biol , vol.11 , pp. 1241-1246
    • Klamt, F.1    Zdanov, S.2    Levine, R.L.3    Pariser, A.4    Zhang, Y.5
  • 25
    • 33745034465 scopus 로고    scopus 로고
    • Measles virus contact with T cells impedes cytoskeletal remodeling associated with spreading, polarization, and CD3 clustering
    • Müller N, Avota E, Schneider-Schaulies J, Harms H, Krohne G, et al. (2006) Measles virus contact with T cells impedes cytoskeletal remodeling associated with spreading, polarization, and CD3 clustering. Traffic 7: 849-858.
    • (2006) Traffic , vol.7 , pp. 849-858
    • Müller, N.1    Avota, E.2    Schneider-Schaulies, J.3    Harms, H.4    Krohne, G.5
  • 26
    • 10344232013 scopus 로고    scopus 로고
    • A novel eIF5A complex functions as a regulator of p53 and p53-dependent apoptosis
    • Li AL, Li HY, Jin BF, Ye QN, Zhou T, et al. (2004) A novel eIF5A complex functions as a regulator of p53 and p53-dependent apoptosis. J Biol Chem 279: 49251-49258.
    • (2004) J Biol Chem , vol.279 , pp. 49251-49258
    • Li, A.L.1    Li, H.Y.2    Jin, B.F.3    Ye, Q.N.4    Zhou, T.5
  • 27
    • 33846608688 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5A induces apoptosis in colon cancer cells and associates with the nucleus in response to tumour necrosis factor alpha signalling
    • Taylor CA, Sun Z, Cliche DO, Ming H, Eshaque B, et al. (2007) Eukaryotic translation initiation factor 5A induces apoptosis in colon cancer cells and associates with the nucleus in response to tumour necrosis factor alpha signalling. Exp Cell Res 313: 437-449.
    • (2007) Exp Cell Res , vol.313 , pp. 437-449
    • Taylor, C.A.1    Sun, Z.2    Cliche, D.O.3    Ming, H.4    Eshaque, B.5
  • 28
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L, Roeder RG, Luo Y, (2003) S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114: 255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 29
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, et al. (2005) S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 7: 665-674.
    • (2005) Nat Cell Biol , vol.7 , pp. 665-674
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3    Cascio, M.B.4    Fujimuro, M.5
  • 31
    • 37549072681 scopus 로고    scopus 로고
    • Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress
    • Ralser M, Wamelink MM, Kowald A, Gerisch B, Heeren G, et al. (2007) Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress. J Biol 6: 10.
    • (2007) J Biol , vol.6 , pp. 10
    • Ralser, M.1    Wamelink, M.M.2    Kowald, A.3    Gerisch, B.4    Heeren, G.5
  • 32
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: survival proteins in cancer
    • Jaattela M, (1999) Escaping cell death: survival proteins in cancer. Exp Cell Res 248: 30-43.
    • (1999) Exp Cell Res , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 33
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BB, Cain K, Mosser DD, Mahboubi A, et al. (2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2: 469-475.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3    Mosser, D.D.4    Mahboubi, A.5
  • 35
    • 20144389422 scopus 로고    scopus 로고
    • Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress
    • Kim RH, Smith PD, Aleyasin H, Hayley S, Mount MP, et al. (2005) Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc Natl Acad Sci U S A 02: 5215-5220.
    • (2005) Proc Natl Acad Sci U S A , vol.2 , pp. 5215-5220
    • Kim, R.H.1    Smith, P.D.2    Aleyasin, H.3    Hayley, S.4    Mount, M.P.5
  • 36
    • 0033542425 scopus 로고    scopus 로고
    • Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function
    • Wang S, Nath N, Adlam M, Chellappan S, (1999) Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function. Oncogene 18: 3501-3510.
    • (1999) Oncogene , vol.18 , pp. 3501-3510
    • Wang, S.1    Nath, N.2    Adlam, M.3    Chellappan, S.4
  • 37
    • 0032721090 scopus 로고    scopus 로고
    • Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals
    • Wang S, Nath N, Fusaro G, Chellappan S, (1999) Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals. Mol Cell Biol 19: 7447-7460.
    • (1999) Mol Cell Biol , vol.19 , pp. 7447-7460
    • Wang, S.1    Nath, N.2    Fusaro, G.3    Chellappan, S.4
  • 39
    • 0028960688 scopus 로고
    • Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe M, Hirano A, Stenglein S, Nelson J, Thomas G, et al. (1995) Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J Virol 69: 3206-3210.
    • (1995) J Virol , vol.69 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3    Nelson, J.4    Thomas, G.5
  • 40
    • 19344361801 scopus 로고    scopus 로고
    • Enhancement of gene delivery to cancer cells by a retargeted adenovirus
    • Oh KS, Engler JA, Joung I, (2005) Enhancement of gene delivery to cancer cells by a retargeted adenovirus. J Microbiol 43: 179-182.
    • (2005) J Microbiol , vol.43 , pp. 179-182
    • Oh, K.S.1    Engler, J.A.2    Joung, I.3
  • 41
    • 0033954001 scopus 로고    scopus 로고
    • Targeting adenovirus
    • Wickham TJ, (2000) Targeting adenovirus. Gene Ther 7: 110-114.
    • (2000) Gene Ther , vol.7 , pp. 110-114
    • Wickham, T.J.1
  • 42
    • 0033601275 scopus 로고    scopus 로고
    • Connective tissue growth factor induces apoptosis in human breast cancer cell line MCF-7
    • Hishikawa K, Oemar BS, Tanner FC, Nakaki T, Luscher TF, et al. (1999) Connective tissue growth factor induces apoptosis in human breast cancer cell line MCF-7. J Biol Chem 274: 37461-37466.
    • (1999) J Biol Chem , vol.274 , pp. 37461-37466
    • Hishikawa, K.1    Oemar, B.S.2    Tanner, F.C.3    Nakaki, T.4    Luscher, T.F.5
  • 43
    • 0034037611 scopus 로고    scopus 로고
    • Single cell gel/comet assay: guidelines for in vitro and in vivo genetic toxicology testing
    • Tice RR, Agurell E, Anderson D, Burlinson B, Hartmann A, et al. (2000) Single cell gel/comet assay: guidelines for in vitro and in vivo genetic toxicology testing. Environ Mol Mutagen 35: 206-221.
    • (2000) Environ Mol Mutagen , vol.35 , pp. 206-221
    • Tice, R.R.1    Agurell, E.2    Anderson, D.3    Burlinson, B.4    Hartmann, A.5
  • 44
    • 5444232086 scopus 로고    scopus 로고
    • Mass spectrometric analysis of protein markers for ovarian cancer
    • Wang Z, Yip C, Ying Y, Wang J, Meng XY, et al. (2003) Mass spectrometric analysis of protein markers for ovarian cancer. Clin Chem 50: 1939-1942.
    • (2003) Clin Chem , vol.50 , pp. 1939-1942
    • Wang, Z.1    Yip, C.2    Ying, Y.3    Wang, J.4    Meng, X.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.