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Volumn 584, Issue 10, 2010, Pages 2070-2075

Effects of human T-cell leukemia virus type 1 (HTLV-1) p13 on mitochondrial K+ permeability: A new member of the viroporin family?

Author keywords

Apoptosis; Calcium homeostasis; HTLV 1; Leukemia; Mitochondria; Potassium channel; Viroporin

Indexed keywords

PROTEIN P13; UNCLASSIFIED DRUG; VIRAL CHANNEL PROTEIN; VIROPORIN; VIRUS PROTEIN;

EID: 77952673390     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.02.030     Document Type: Review
Times cited : (21)

References (53)
  • 2
    • 25444436726 scopus 로고    scopus 로고
    • Human T-cell leukemia/lymphoma virus type 1 nonstructural genes and their functions
    • Nicot C., Harrod R.L., Ciminale V., Franchini G. Human T-cell leukemia/lymphoma virus type 1 nonstructural genes and their functions. Oncogene 2005, 24:6026-6034.
    • (2005) Oncogene , vol.24 , pp. 6026-6034
    • Nicot, C.1    Harrod, R.L.2    Ciminale, V.3    Franchini, G.4
  • 4
    • 0028981316 scopus 로고
    • Intracellular trafficking of the human immunodeficiency virus type 1 Rev protein: involvement of continued rRNA synthesis in nuclear retention
    • D'Agostino D.M., Ciminale V., Pavlakis G.N., Chieco-Bianchi L. Intracellular trafficking of the human immunodeficiency virus type 1 Rev protein: involvement of continued rRNA synthesis in nuclear retention. AIDS Res. Hum. Retroviruses 1995, 11:1063-1071.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 1063-1071
    • D'Agostino, D.M.1    Ciminale, V.2    Pavlakis, G.N.3    Chieco-Bianchi, L.4
  • 6
    • 0037072932 scopus 로고    scopus 로고
    • Mitochondrial alterations induced by the p13II protein of human T-cell leukemia virus type 1. Critical role of arginine residues
    • D'Agostino D.M., et al. Mitochondrial alterations induced by the p13II protein of human T-cell leukemia virus type 1. Critical role of arginine residues. J. Biol. Chem. 2002, 277:34424-34433.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34424-34433
    • D'Agostino, D.M.1
  • 7
    • 0033526932 scopus 로고    scopus 로고
    • Mitochondrial targeting of the p13II protein coded by the x-II ORF of human T-cell leukemia/lymphotropic virus type I (HTLV-I)
    • Ciminale V., Zotti L., D'Agostino D.M., Ferro T., Casareto L., Franchini G., Bernardi P., Chieco-Bianchi L. Mitochondrial targeting of the p13II protein coded by the x-II ORF of human T-cell leukemia/lymphotropic virus type I (HTLV-I). Oncogene 1999, 18:4505-4514.
    • (1999) Oncogene , vol.18 , pp. 4505-4514
    • Ciminale, V.1    Zotti, L.2    D'Agostino, D.M.3    Ferro, T.4    Casareto, L.5    Franchini, G.6    Bernardi, P.7    Chieco-Bianchi, L.8
  • 8
    • 0035811031 scopus 로고    scopus 로고
    • A beta -hairpin structure in a 13-mer peptide that binds alpha -bungarotoxin with high affinity and neutralizes its toxicity
    • Scherf T., Kasher R., Balass M., Fridkin M., Fuchs S., Katchalski-Katzir E. A beta -hairpin structure in a 13-mer peptide that binds alpha -bungarotoxin with high affinity and neutralizes its toxicity. Proc. Natl. Acad. Sci. USA 2001, 98:6629-6634.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6629-6634
    • Scherf, T.1    Kasher, R.2    Balass, M.3    Fridkin, M.4    Fuchs, S.5    Katchalski-Katzir, E.6
  • 9
    • 0027340275 scopus 로고
    • The p12I, p13II, and p30II proteins encoded by human T-cell leukemia/lymphotropic virus type I open reading frames I and II are localized in three different cellular compartments
    • Koralnik I.J., Fullen J., Franchini G. The p12I, p13II, and p30II proteins encoded by human T-cell leukemia/lymphotropic virus type I open reading frames I and II are localized in three different cellular compartments. J. Virol. 1993, 67:2360-2366.
    • (1993) J. Virol. , vol.67 , pp. 2360-2366
    • Koralnik, I.J.1    Fullen, J.2    Franchini, G.3
  • 10
    • 33846004438 scopus 로고    scopus 로고
    • Human T-cell leukemia virus type I p30 nuclear/nucleolar retention is mediated through interactions with RNA and a constituent of the 60 S ribosomal subunit
    • Ghorbel S., Sinha-Datta U., Dundr M., Brown M., Franchini G., Nicot C. Human T-cell leukemia virus type I p30 nuclear/nucleolar retention is mediated through interactions with RNA and a constituent of the 60 S ribosomal subunit. J. Biol. Chem. 2006, 281:37150-37158.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37150-37158
    • Ghorbel, S.1    Sinha-Datta, U.2    Dundr, M.3    Brown, M.4    Franchini, G.5    Nicot, C.6
  • 11
    • 67649274379 scopus 로고    scopus 로고
    • Modulation of mitochondrial K(+) permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1
    • Silic-Benussi M., et al. Modulation of mitochondrial K(+) permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1. Biochim. Biophys. Acta 2009, 1787:947-954.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 947-954
    • Silic-Benussi, M.1
  • 12
    • 0032524667 scopus 로고    scopus 로고
    • Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation By electron flow through the respiratory chain complex i
    • Fontaine E., Eriksson O., Ichas F., Bernardi P. Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation By electron flow through the respiratory chain complex i. J. Biol. Chem. 1998, 273:12662-12668.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12662-12668
    • Fontaine, E.1    Eriksson, O.2    Ichas, F.3    Bernardi, P.4
  • 14
    • 0034634318 scopus 로고    scopus 로고
    • The human T-cell leukemia virus type I (HTLV-I) X region encoded protein p13(II) interacts with cellular proteins
    • Hou X., Foley S., Cueto M., Robinson M.A. The human T-cell leukemia virus type I (HTLV-I) X region encoded protein p13(II) interacts with cellular proteins. Virology 2000, 277:127-135.
    • (2000) Virology , vol.277 , pp. 127-135
    • Hou, X.1    Foley, S.2    Cueto, M.3    Robinson, M.A.4
  • 17
    • 22544437317 scopus 로고    scopus 로고
    • Human T-lymphotropic virus type 1 mitochondrion-localizing protein p13II sensitizes Jurkat T cells to Ras-mediated apoptosis
    • Hiraragi H., Michael B., Nair A., Silic-Benussi M., Ciminale V., Lairmore M. Human T-lymphotropic virus type 1 mitochondrion-localizing protein p13II sensitizes Jurkat T cells to Ras-mediated apoptosis. J. Virol. 2005, 79:9449-9457.
    • (2005) J. Virol. , vol.79 , pp. 9449-9457
    • Hiraragi, H.1    Michael, B.2    Nair, A.3    Silic-Benussi, M.4    Ciminale, V.5    Lairmore, M.6
  • 18
    • 2342462205 scopus 로고    scopus 로고
    • Suppression of tumor growth and cell proliferation by p13II, a mitochondrial protein of human T cell leukemia virus type 1
    • Silic-Benussi M., et al. Suppression of tumor growth and cell proliferation by p13II, a mitochondrial protein of human T cell leukemia virus type 1. Proc. Natl. Acad. Sci. USA 2004, 101:6629-6634.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6629-6634
    • Silic-Benussi, M.1
  • 19
    • 34250725402 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ as a key regulator of cell life and death
    • Giacomello M., Drago I., Pizzo P., Pozzan T. Mitochondrial Ca2+ as a key regulator of cell life and death. Cell Death Differ. 2007, 14:1267-1274.
    • (2007) Cell Death Differ. , vol.14 , pp. 1267-1274
    • Giacomello, M.1    Drago, I.2    Pizzo, P.3    Pozzan, T.4
  • 20
    • 20644434910 scopus 로고    scopus 로고
    • Mitochondrial K(ATP) channels in cell survival and death
    • Ardehali H., O'Rourke B. Mitochondrial K(ATP) channels in cell survival and death. J. Mol. Cell. Cardiol. 2005, 39:7-16.
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 7-16
    • Ardehali, H.1    O'Rourke, B.2
  • 21
    • 0037423675 scopus 로고    scopus 로고
    • Differential actions of cardioprotective agents on the mitochondrial death pathway
    • Akao M., O'Rourke B., Kusuoka H., Teshima Y., Jones S.P., Marban E. Differential actions of cardioprotective agents on the mitochondrial death pathway. Circ. Res. 2003, 92:195-202.
    • (2003) Circ. Res. , vol.92 , pp. 195-202
    • Akao, M.1    O'Rourke, B.2    Kusuoka, H.3    Teshima, Y.4    Jones, S.P.5    Marban, E.6
  • 22
    • 0031871102 scopus 로고    scopus 로고
    • Viruses and apoptosis
    • O'Brien V. Viruses and apoptosis. J. Gen. Virol. 1998, 79(Pt 8):1833-1845.
    • (1998) J. Gen. Virol. , vol.79 , Issue.PART 8 , pp. 1833-1845
    • O'Brien, V.1
  • 23
    • 0032567325 scopus 로고    scopus 로고
    • Two types of death of poliovirus-infected cells: caspase involvement in the apoptosis but not cytopathic effect
    • Agol V.I., et al. Two types of death of poliovirus-infected cells: caspase involvement in the apoptosis but not cytopathic effect. Virology 1998, 252:343-353.
    • (1998) Virology , vol.252 , pp. 343-353
    • Agol, V.I.1
  • 24
    • 0031820706 scopus 로고    scopus 로고
    • Caspase activation and specific cleavage of substrates after coxsackievirus B3-induced cytopathic effect in HeLa cells
    • Carthy C.M., Granville D.J., Watson K.A., Anderson D.R., Wilson J.E., Yang D., Hunt D.W., McManus B.M. Caspase activation and specific cleavage of substrates after coxsackievirus B3-induced cytopathic effect in HeLa cells. J. Virol. 1998, 72:7669-7675.
    • (1998) J. Virol. , vol.72 , pp. 7669-7675
    • Carthy, C.M.1    Granville, D.J.2    Watson, K.A.3    Anderson, D.R.4    Wilson, J.E.5    Yang, D.6    Hunt, D.W.7    McManus, B.M.8
  • 25
    • 0032473496 scopus 로고    scopus 로고
    • Alphaviruses induce apoptosis in Bcl-2-overexpressing cells: evidence for a caspase-mediated, proteolytic inactivation of Bcl-2
    • Grandgirard D., Studer E., Monney L., Belser T., Fellay I., Borner C., Michel M.R. Alphaviruses induce apoptosis in Bcl-2-overexpressing cells: evidence for a caspase-mediated, proteolytic inactivation of Bcl-2. EMBO J. 1998, 17:1268-1278.
    • (1998) EMBO J. , vol.17 , pp. 1268-1278
    • Grandgirard, D.1    Studer, E.2    Monney, L.3    Belser, T.4    Fellay, I.5    Borner, C.6    Michel, M.R.7
  • 26
    • 0032816080 scopus 로고    scopus 로고
    • Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer
    • An S., Chen C.J., Yu X., Leibowitz J.L., Makino S. Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer. J. Virol. 1999, 73:7853-7859.
    • (1999) J. Virol. , vol.73 , pp. 7853-7859
    • An, S.1    Chen, C.J.2    Yu, X.3    Leibowitz, J.L.4    Makino, S.5
  • 27
    • 0035970309 scopus 로고    scopus 로고
    • Hepatitis C virus protein expression induces apoptosis in HepG2 cells
    • Kalkeri G., Khalap N., Garry R.F., Fermin C.D., Dash S. Hepatitis C virus protein expression induces apoptosis in HepG2 cells. Virology 2001, 282:26-37.
    • (2001) Virology , vol.282 , pp. 26-37
    • Kalkeri, G.1    Khalap, N.2    Garry, R.F.3    Fermin, C.D.4    Dash, S.5
  • 29
    • 0035658084 scopus 로고    scopus 로고
    • A novel influenza A virus mitochondrial protein that induces cell death
    • Chen W., et al. A novel influenza A virus mitochondrial protein that induces cell death. Nat. Med. 2001, 7:1306-1312.
    • (2001) Nat. Med. , vol.7 , pp. 1306-1312
    • Chen, W.1
  • 30
    • 0141893997 scopus 로고    scopus 로고
    • Influenza virus induction of apoptosis by intrinsic and extrinsic mechanisms
    • Lowy R.J. Influenza virus induction of apoptosis by intrinsic and extrinsic mechanisms. Int. Rev. Immunol. 2003, 22:425-449.
    • (2003) Int. Rev. Immunol. , vol.22 , pp. 425-449
    • Lowy, R.J.1
  • 31
    • 77951059450 scopus 로고    scopus 로고
    • Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1
    • Zamarin D., Garcia-Sastre A., Xiao X., Wang R., Palese P. Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog. 2005, 1:e4.
    • (2005) PLoS Pathog. , vol.1
    • Zamarin, D.1    Garcia-Sastre, A.2    Xiao, X.3    Wang, R.4    Palese, P.5
  • 32
    • 33846553599 scopus 로고    scopus 로고
    • The PB1-F2 protein of Influenza A virus: increasing pathogenicity by disrupting alveolar macrophages
    • Coleman J.R. The PB1-F2 protein of Influenza A virus: increasing pathogenicity by disrupting alveolar macrophages. Virol. J. 2007, 4:9.
    • (2007) Virol. J. , vol.4 , pp. 9
    • Coleman, J.R.1
  • 33
    • 33746858906 scopus 로고    scopus 로고
    • Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice
    • Zamarin D., Ortigoza M.B., Palese P. Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice. J. Virol. 2006, 80:7976-7983.
    • (2006) J. Virol. , vol.80 , pp. 7976-7983
    • Zamarin, D.1    Ortigoza, M.B.2    Palese, P.3
  • 34
    • 34848897191 scopus 로고    scopus 로고
    • Influenza A virus PB1-F2: a small protein with a big punch
    • Conenello G.M., Palese P. Influenza A virus PB1-F2: a small protein with a big punch. Cell Host Microbe 2007, 2:207-209.
    • (2007) Cell Host Microbe , vol.2 , pp. 207-209
    • Conenello, G.M.1    Palese, P.2
  • 35
    • 36049034216 scopus 로고    scopus 로고
    • A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence
    • Conenello G.M., Zamarin D., Perrone L.A., Tumpey T., Palese P. A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence. PLoS Pathog. 2007, 3:1414-1421.
    • (2007) PLoS Pathog. , vol.3 , pp. 1414-1421
    • Conenello, G.M.1    Zamarin, D.2    Perrone, L.A.3    Tumpey, T.4    Palese, P.5
  • 37
    • 70350736558 scopus 로고    scopus 로고
    • Phosphorylation of the influenza A virus protein PB1-F2 by PKC is crucial for apoptosis promoting functions in monocytes
    • Mitzner D., et al. Phosphorylation of the influenza A virus protein PB1-F2 by PKC is crucial for apoptosis promoting functions in monocytes. Cell. Microbiol. 2009, 11:1502-1516.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1502-1516
    • Mitzner, D.1
  • 38
    • 0042335650 scopus 로고    scopus 로고
    • Mechanisms of membrane permeabilization by picornavirus 2B viroporin
    • Nieva J.L., Agirre A., Nir S., Carrasco L. Mechanisms of membrane permeabilization by picornavirus 2B viroporin. FEBS Lett. 2003, 552:68-73.
    • (2003) FEBS Lett. , vol.552 , pp. 68-73
    • Nieva, J.L.1    Agirre, A.2    Nir, S.3    Carrasco, L.4
  • 39
    • 0029821259 scopus 로고    scopus 로고
    • Mutagenesis of the coxsackie B3 virus 2B/2C cleavage site: determinants of processing efficiency and effects on viral replication
    • van Kuppeveld F.J., van den Hurk P.J., Zoll J., Galama J.M., Melchers W.J. Mutagenesis of the coxsackie B3 virus 2B/2C cleavage site: determinants of processing efficiency and effects on viral replication. J. Virol. 1996, 70:7632-7640.
    • (1996) J. Virol. , vol.70 , pp. 7632-7640
    • van Kuppeveld, F.J.1    van den Hurk, P.J.2    Zoll, J.3    Galama, J.M.4    Melchers, W.J.5
  • 40
    • 71749091651 scopus 로고    scopus 로고
    • A peptide based on the pore-forming domain of pro-apoptotic poliovirus 2B viroporin targets mitochondria
    • Madan V., Sanchez-Martinez S., Carrasco L., Nieva J.L. A peptide based on the pore-forming domain of pro-apoptotic poliovirus 2B viroporin targets mitochondria. Biochim. Biophys. Acta 2010, 1798:52-58.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 52-58
    • Madan, V.1    Sanchez-Martinez, S.2    Carrasco, L.3    Nieva, J.L.4
  • 43
    • 0034598337 scopus 로고    scopus 로고
    • The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore
    • Jacotot E., et al. The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore. J. Exp. Med. 2000, 191:33-46.
    • (2000) J. Exp. Med. , vol.191 , pp. 33-46
    • Jacotot, E.1
  • 44
    • 0035265946 scopus 로고    scopus 로고
    • Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
    • Jain C., Belasco J.G. Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants. Mol. Cell 2001, 7:603-614.
    • (2001) Mol. Cell , vol.7 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 45
    • 0030065395 scopus 로고    scopus 로고
    • Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import
    • Gallay P., Stitt V., Mundy C., Oettinger M., Trono D. Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. J. Virol. 1996, 70:1027-1032.
    • (1996) J. Virol. , vol.70 , pp. 1027-1032
    • Gallay, P.1    Stitt, V.2    Mundy, C.3    Oettinger, M.4    Trono, D.5
  • 46
    • 34248594865 scopus 로고    scopus 로고
    • The cell cycle independence of HIV infections is not determined by known karyophilic viral elements
    • Yamashita M., Emerman M. The cell cycle independence of HIV infections is not determined by known karyophilic viral elements. PLoS Pathog. 2005, 1:e18.
    • (2005) PLoS Pathog. , vol.1
    • Yamashita, M.1    Emerman, M.2
  • 47
    • 0029993519 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 cell cycle control: Vpr is cytostatic and mediates G2 accumulation by a mechanism which differs from DNA damage checkpoint control
    • Bartz S.R., Rogel M.E., Emerman M. Human immunodeficiency virus type 1 cell cycle control: Vpr is cytostatic and mediates G2 accumulation by a mechanism which differs from DNA damage checkpoint control. J. Virol. 1996, 70:2324-2331.
    • (1996) J. Virol. , vol.70 , pp. 2324-2331
    • Bartz, S.R.1    Rogel, M.E.2    Emerman, M.3
  • 48
    • 0003124066 scopus 로고    scopus 로고
    • HIV-1 Vpr increases viral expression by manipulation of the cell cycle: a mechanism for selection of Vpr in vivo
    • Goh W.C., Rogel M.E., Kinsey C.M., Michael S.F., Fultz P.N., Nowak M.A., Hahn B.H., Emerman M. HIV-1 Vpr increases viral expression by manipulation of the cell cycle: a mechanism for selection of Vpr in vivo. Nat. Med. 1998, 4:65-71.
    • (1998) Nat. Med. , vol.4 , pp. 65-71
    • Goh, W.C.1    Rogel, M.E.2    Kinsey, C.M.3    Michael, S.F.4    Fultz, P.N.5    Nowak, M.A.6    Hahn, B.H.7    Emerman, M.8
  • 49
    • 0028853961 scopus 로고
    • Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity
    • He J., Choe S., Walker R., Di Marzio P., Morgan D.O., Landau N.R. Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity. J. Virol. 1995, 69:6705-6711.
    • (1995) J. Virol. , vol.69 , pp. 6705-6711
    • He, J.1    Choe, S.2    Walker, R.3    Di Marzio, P.4    Morgan, D.O.5    Landau, N.R.6
  • 50
    • 0032504065 scopus 로고    scopus 로고
    • Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents
    • Poon B., Grovit-Ferbas K., Stewart S.A., Chen I.S. Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents. Science 1998, 281:266-269.
    • (1998) Science , vol.281 , pp. 266-269
    • Poon, B.1    Grovit-Ferbas, K.2    Stewart, S.A.3    Chen, I.S.4
  • 51
    • 0032717268 scopus 로고    scopus 로고
    • Lentiviral delivery of HIV-1 Vpr protein induces apoptosis in transformed cells
    • Stewart S.A., Poon B., Jowett J.B., Xie Y., Chen I.S. Lentiviral delivery of HIV-1 Vpr protein induces apoptosis in transformed cells. Proc. Natl. Acad. Sci. USA 1999, 96:12039-12043.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12039-12043
    • Stewart, S.A.1    Poon, B.2    Jowett, J.B.3    Xie, Y.4    Chen, I.S.5
  • 52
    • 0035181481 scopus 로고    scopus 로고
    • Anticancer effect of a lentiviral vector capable of expressing HIV-1 Vpr
    • Pang S., et al. Anticancer effect of a lentiviral vector capable of expressing HIV-1 Vpr. Clin. Cancer Res. 2001, 7:3567-3573.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 3567-3573
    • Pang, S.1
  • 53
    • 0141922982 scopus 로고    scopus 로고
    • Retrograde signaling is regulated by the dynamic interaction between Rtg2p and Mks1p
    • Liu Z., Sekito T., Spirek M., Thornton J., Butow R.A. Retrograde signaling is regulated by the dynamic interaction between Rtg2p and Mks1p. Mol. Cell 2003, 12:401-411.
    • (2003) Mol. Cell , vol.12 , pp. 401-411
    • Liu, Z.1    Sekito, T.2    Spirek, M.3    Thornton, J.4    Butow, R.A.5


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