메뉴 건너뛰기




Volumn 288, Issue 20, 2013, Pages 14554-14568

Expression of concern: Phosphorylation drives an apoptotic protein to activate antiapoptotic genes: paradigm of influenza a matrix 1 protein function (Journal of Biological Chemistry (2013) 288 (14554–14568) DOI: 10.1074/jbc.M112.447086);Phosphorylation drives an apoptotic protein to activate antiapoptotic genes: Paradigm of influenza a matrix 1 protein function

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; ALKYLATION; CELL DEATH; ENZYMES; PHOSPHORYLATION; VIRUSES;

EID: 84877899599     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.EC119.011071     Document Type: Erratum
Times cited : (13)

References (64)
  • 1
    • 0036852215 scopus 로고    scopus 로고
    • To kill or be killed: Viral evasion of apoptosis
    • DOI 10.1038/ni1102-1013
    • Benedict, C. A., Norris, P. S., and Ware, C. F. (2002) To kill or be killed: viral evasion of apoptosis. Nat. Immunol. 3, 1013-1018 (Pubitemid 35363651)
    • (2002) Nature Immunology , vol.3 , Issue.11 , pp. 1013-1018
    • Benedict, C.A.1    Norris, P.S.2    Ware, C.F.3
  • 2
    • 77958184901 scopus 로고    scopus 로고
    • Manipulation of host cell death pathways during microbial infections
    • Lamkanfi, M., and Dixit, V. M. (2010) Manipulation of host cell death pathways during microbial infections. Cell Host Microbe 8, 44-54
    • (2010) Cell Host Microbe , vol.8 , pp. 44-54
    • Lamkanfi, M.1    Dixit, V.M.2
  • 3
    • 54249096028 scopus 로고    scopus 로고
    • Caspases in apoptosis and beyond
    • Li, J., and Yuan, J. (2008) Caspases in apoptosis and beyond. Oncogene 27, 6194-6206
    • (2008) Oncogene , vol.27 , pp. 6194-6206
    • Li, J.1    Yuan, J.2
  • 4
    • 69449095860 scopus 로고    scopus 로고
    • Caspases and kinases in a death grip
    • Kurokawa, M., and Kornbluth, S. (2009) Caspases and kinases in a death grip. Cell 138, 838-854
    • (2009) Cell , vol.138 , pp. 838-854
    • Kurokawa, M.1    Kornbluth, S.2
  • 5
    • 0028113218 scopus 로고
    • Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
    • DOI 10.1016/0092-8674(94)90202-X
    • Boyd, J. M., Malstrom, S., Subramanian, T., Venkatesh, L. K., Schaeper, U., Elangovan, B., D'Sa-Eipper, C., and Chinnadurai, G. (1994) Adenovirus E1B 19 kDa and bcl-2 proteins interact with a common set of cellular proteins. Cell 79, 341-351 (Pubitemid 24324923)
    • (1994) Cell , vol.79 , Issue.2 , pp. 341-351
    • Boyd, J.M.1    Malstrom, S.2    Subramanian, T.3    Venkatesh, L.K.4    Schaeper, U.5    Elangovan, B.6    D'Sa-Eipper, C.7    Chinnadurai, G.8
  • 6
    • 0033634781 scopus 로고    scopus 로고
    • TNF-α signals apoptosis through a Bid-dependent conformational change in Bax that is inhibited by E1B 19K
    • Perez, D., and White, E. (2000) TNF-α signals apoptosis through a Bid-dependent conformational change in Bax that is inhibited by E1B 19K. Mol. Cell 6, 53-63
    • (2000) Mol. Cell , vol.6 , pp. 53-63
    • Perez, D.1    White, E.2
  • 8
    • 0031054439 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes a functional Bcl-2 homologue
    • DOI 10.1038/nm0397-293
    • Sarid, R., Sato, T., Bohenzky, R. A., Russo, J. J., and Chang, Y. (1997) Kaposi's sarcoma-associated herpesvirus encodes a functional bcl-2 homologue. Nat. Med. 3, 293-298 (Pubitemid 27112926)
    • (1997) Nature Medicine , vol.3 , Issue.3 , pp. 293-298
    • Sarid, R.1    Sato, T.2    Bohenzky, R.A.3    Russo, J.J.4    Chang, Y.5
  • 11
    • 0027292729 scopus 로고
    • SV40 T antigen abrogates p53-mediated transcriptional activity
    • Jiang, D., Srinivasan, A., Lozano, G., and Robbins, P. D. (1993) SV40 T antigen abrogates p53-mediated transcriptional activity. Oncogene 8, 2805-2812 (Pubitemid 23279109)
    • (1993) Oncogene , vol.8 , Issue.10 , pp. 2805-2812
    • Jiang, D.1    Srinivasan, A.2    Lozano, G.3    Robbins, P.D.4
  • 12
    • 33748250439 scopus 로고    scopus 로고
    • Crystal structure of SV40 large T-antigen bound to p53: Interplay between a viral oncoprotein and a cellular tumor suppressor
    • DOI 10.1101/gad.1456306
    • Lilyestrom, W., Klein, M. G., Zhang, R., Joachimiak, A., and Chen, X. S. (2006) Crystal structure of SV40 large T-antigen bound to p53: interplay between a viral oncoprotein and a cellular tumor suppressor. Genes Dev. 20, 2373-2382 (Pubitemid 44320386)
    • (2006) Genes and Development , vol.20 , Issue.17 , pp. 2373-2382
    • Lilyestrom, W.1    Klein, M.G.2    Zhang, R.3    Joachimiak, A.4    Chen, X.S.5
  • 14
    • 0028847870 scopus 로고
    • HPV-18 E6 mediated inhibition of p53 DNA binding activity is independent of E6 induced degradation
    • Thomas, M., Massimi, P., Jenkins, J., and Banks, L. (1995) HPV-18 E6 mediated inhibition of p53 DNA binding activity is independent of E6 induced degradation. Oncogene 10, 261-268
    • (1995) Oncogene , vol.10 , pp. 261-268
    • Thomas, M.1    Massimi, P.2    Jenkins, J.3    Banks, L.4
  • 16
    • 12244288291 scopus 로고    scopus 로고
    • The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects againts apoptosis
    • DOI 10.1038/sj.cdd.4401135
    • Jabbour, A. M., Ekert, P. G., Coulson, E. J., Knight, M. J., Ashley, D. M., and Hawkins, C. J. (2002) The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects against apoptosis. Cell Death Differ. 9, 1311-1320 (Pubitemid 36097701)
    • (2002) Cell Death and Differentiation , vol.9 , Issue.12 , pp. 1311-1320
    • Jabbour, A.M.1    Ekert, P.G.2    Coulson, E.J.3    Knight, M.J.4    Ashley, D.M.5    Hawkins, C.J.6
  • 17
    • 85047278700 scopus 로고    scopus 로고
    • Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo
    • Zoog, S. J., Schiller, J. J., Wetter, J. A., Chejanovsky, N., and Friesen, P. D. (2002) Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo. EMBO J. 21, 5130-5140
    • (2002) EMBO J. , vol.21 , pp. 5130-5140
    • Zoog, S.J.1    Schiller, J.J.2    Wetter, J.A.3    Chejanovsky, N.4    Friesen, P.D.5
  • 19
    • 0029114963 scopus 로고
    • Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway
    • Miura, M., Friedlander, R. M., and Yuan, J. (1995) Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway. Proc. Natl. Acad. Sci. U.S.A. 92, 8318-8322
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8318-8322
    • Miura, M.1    Friedlander, R.M.2    Yuan, J.3
  • 20
    • 0842281645 scopus 로고    scopus 로고
    • Cell Death: Critical Control Points
    • DOI 10.1016/S0092-8674(04)00046-7
    • Danial, N. N., and Korsmeyer, S. J. (2004) Cell death: critical control points. Cell 116, 205-219 (Pubitemid 38167313)
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 21
    • 77954930632 scopus 로고    scopus 로고
    • IAPs: From caspase inhibitors to modulators of NF-κB, inflammation and cancer
    • Gyrd-Hansen, M., and Meier, P. (2010) IAPs: From caspase inhibitors to modulators of NF-κB, inflammation and cancer. Nat. Rev. Cancer 10, 561-574
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 561-574
    • Gyrd-Hansen, M.1    Meier, P.2
  • 22
    • 43049091895 scopus 로고    scopus 로고
    • IAPs: What's in a Name?
    • DOI 10.1016/j.molcel.2008.03.008, PII S1097276508002086
    • Srinivasula, S. M., and Ashwell, J. D. (2008) IAPs: what's in a name? Mol. Cell 30, 123-135 (Pubitemid 351626688)
    • (2008) Molecular Cell , vol.30 , Issue.2 , pp. 123-135
    • Srinivasula, S.M.1    Ashwell, J.D.2
  • 23
  • 24
    • 7644244878 scopus 로고    scopus 로고
    • FLIP overexpression inhibits death receptor-induced apoptosis in malignant mesothelial cells
    • DOI 10.1038/sj.onc.1208051
    • Rippo, M. R., Moretti, S., Vescovi, S., Tomasetti, M., Orecchia, S., Amici, G., Catalano, A., and Procopio, A. (2004) FLIP overexpression inhibits death receptor-induced apoptosis in malignant mesothelial cells. Oncogene 23, 7753-7760 (Pubitemid 39457025)
    • (2004) Oncogene , vol.23 , Issue.47 , pp. 7753-7760
    • Rippo, M.R.1    Moretti, S.2    Vescovi, S.3    Tomasetti, M.4    Orecchia, S.5    Amici, G.6    Catalano, A.7    Procopio, A.8
  • 25
    • 0142105387 scopus 로고    scopus 로고
    • Genetic analysis of NF-κB/Rel transcription factors defines functional specificities
    • DOI 10.1093/emboj/cdg534
    • Hoffmann, A., Leung, T. H., and Baltimore, D. (2003) Genetic analysis of NF-κB/Rel transcription factors defines functional specificities. EMBO J. 22, 5530-5539 (Pubitemid 37279962)
    • (2003) EMBO Journal , vol.22 , Issue.20 , pp. 5530-5539
    • Hoffmann, A.1    Leung, T.H.2    Baltimore, D.3
  • 27
    • 0028817585 scopus 로고
    • Multiorgan inflammation and hematopoietic abnormalities in mice with a targeted disruption of RelB, a member of the NF-κB/Rel family
    • Weih, F., Carrasco, D., Durham, S. K., Barton, D. S., Rizzo, C. A., Ryseck, R. P., Lira, S. A., and Bravo, R. (1995) Multiorgan inflammation and hematopoietic abnormalities in mice with a targeted disruption of RelB, a member of the NF-κB/Rel family. Cell 80, 331-340
    • (1995) Cell , vol.80 , pp. 331-340
    • Weih, F.1    Carrasco, D.2    Durham, S.K.3    Barton, D.S.4    Rizzo, C.A.5    Ryseck, R.P.6    Lira, S.A.7    Bravo, R.8
  • 28
  • 30
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor κB signaling
    • Hoffmann, A., and Baltimore, D. (2006) Circuitry of nuclear factor κB signaling. Immunol. Rev. 210, 171-186
    • (2006) Immunol. Rev. , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 31
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3
    • Drané, P., Ouararhni, K., Depaux, A., Shuaib, M., and Hamiche, A. (2010) The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 24, 1253-1265
    • (2010) Genes Dev. , vol.24 , pp. 1253-1265
    • Drané, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 32
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • Lewis, P. W., Elsaesser, S. J., Noh, K. M., Stadler, S. C., and Allis, C. D. (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U.S.A. 107, 14075-14080
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 33
    • 84869886446 scopus 로고    scopus 로고
    • DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition
    • Elsässer, S. J., Huang, H., Lewis, P. W., Chin, J. W., Allis, C. D., and Patel, D. J. (2012) DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature 491, 560-565
    • (2012) Nature , vol.491 , pp. 560-565
    • Elsässer, S.J.1    Huang, H.2    Lewis, P.W.3    Chin, J.W.4    Allis, C.D.5    Patel, D.J.6
  • 34
    • 0037305847 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity
    • DOI 10.1128/MCB.23.3.950-960.2003
    • Ecsedy, J. A., Michaelson, J. S., and Leder, P. (2003) Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity. Mol. Cell. Biol. 23, 950-960 (Pubitemid 36133513)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.3 , pp. 950-960
    • Ecsedy, J.A.1    Michaelson, J.S.2    Leder, P.3
  • 37
    • 32644487258 scopus 로고    scopus 로고
    • Daxx: Death or survival protein?
    • DOI 10.1016/j.tcb.2005.12.002, PII S0962892405003107
    • Salomoni, P., and Khelifi, A. F. (2006) Daxx: death or survival protein? Trends Cell Biol. 16, 97-104 (Pubitemid 43247405)
    • (2006) Trends in Cell Biology , vol.16 , Issue.2 , pp. 97-104
    • Salomoni, P.1    Khelifi, A.F.2
  • 38
    • 33749459830 scopus 로고    scopus 로고
    • Daxx represses expression of a subset of antiapoptotic genes regulated by nuclear factor-κB
    • DOI 10.1158/0008-5472.CAN-06-1047
    • Croxton, R., Puto, L. A., de Belle, I., Thomas, M., Torii, S., Hanaii, F., Cuddy, M., and Reed, J. C. (2006) Daxx represses expression of a subset of antiapoptotic genes regulated by nuclear factor-κB. Cancer Res. 66, 9026-9035 (Pubitemid 44521121)
    • (2006) Cancer Research , vol.66 , Issue.18 , pp. 9026-9035
    • Croxton, R.1    Puto, L.A.2    De Belle, I.3    Thomas, M.4    Torii, S.5    Hanaii, F.6    Cuddy, M.7    Reed, J.C.8
  • 39
    • 42149185026 scopus 로고    scopus 로고
    • Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation
    • DOI 10.1101/gad.1632208
    • Puto, L. A., and Reed, J. C. (2008) Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation. Genes Dev. 22, 998-1010 (Pubitemid 351544239)
    • (2008) Genes and Development , vol.22 , Issue.8 , pp. 998-1010
    • Puto, L.A.1    Reed, J.C.2
  • 41
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • DOI 10.1038/nrm2277, PII NRM2277
    • Bernardi, R., and Pandolfi, P. P. (2007) Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 8, 1006-1016 (Pubitemid 350174636)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 42
    • 37349033209 scopus 로고    scopus 로고
    • Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection
    • DOI 10.1128/JVI.01685-07
    • Tavalai, N., Papior, P., Rechter, S., and Stamminger, T. (2008) Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. J. Virol. 82, 126-137 (Pubitemid 350309130)
    • (2008) Journal of Virology , vol.82 , Issue.1 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 43
    • 48449083440 scopus 로고    scopus 로고
    • A role for cytoplasmic PML in cellular resistance to viral infection
    • McNally, B. A., Trgovcich, J., Maul, G. G., Liu, Y., and Zheng, P. (2008) A role for cytoplasmic PML in cellular resistance to viral infection. PLoS One 3, e2277
    • (2008) PLoS One , vol.3
    • McNally, B.A.1    Trgovcich, J.2    Maul, G.G.3    Liu, Y.4    Zheng, P.5
  • 44
    • 33644768122 scopus 로고    scopus 로고
    • Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption
    • DOI 10.1128/JVI.80.6.3042-3049.2006
    • Hoppe, A., Beech, S. J., Dimmock, J., and Leppard, K. N. (2006) Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption. J. Virol. 80, 3042-3049 (Pubitemid 43346399)
    • (2006) Journal of Virology , vol.80 , Issue.6 , pp. 3042-3049
    • Hoppe, A.1    Beech, S.J.2    Dimmock, J.3    Leppard, K.N.4
  • 45
    • 2942711737 scopus 로고    scopus 로고
    • HPV E6 proteins interact with specific PML isoforms and allow distinctions to be made between different POD structures
    • DOI 10.1038/sj.onc.1207631
    • Guccione, E., Lethbridge, K. J., Killick, N., Leppard, K. N., and Banks, L. (2004) HPV E6 proteins interact with specific PML isoforms and allow distinctions to be made between different POD structures. Oncogene 23, 4662-4672 (Pubitemid 38859455)
    • (2004) Oncogene , vol.23 , Issue.27 , pp. 4662-4672
    • Guccione, E.1    Lethbridge, K.J.2    Killick, N.3    Leppard, K.N.4    Banks, L.5
  • 46
    • 12844263583 scopus 로고    scopus 로고
    • Human papillomavirus oncoprotein E7 targets the promyelocytic leukemia protein and circumvents cellular senescence via the Rb and p53 tumor suppressor pathways
    • DOI 10.1128/MCB.25.3.1013-1024.2005
    • Bischof, O., Nacerddine, K., and Dejean, A. (2005) Human papillomavirus oncoprotein E7 targets the promyelocytic leukemia protein and circumvents cellular senescence via the Rb and p53 tumor suppressor pathways. Mol. Cell. Biol. 25, 1013-1024 (Pubitemid 40165809)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.3 , pp. 1013-1024
    • Bischof, O.1    Nacerddine, K.2    Dejean, A.3
  • 47
    • 28244483929 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells
    • DOI 10.1158/0008-5472.CAN-05-0880
    • Herzer, K., Weyer, S., Krammer, P. H., Galle, P. R., and Hofmann, T. G. (2005) Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells. Cancer Res. 65, 10830-10837 (Pubitemid 41713350)
    • (2005) Cancer Research , vol.65 , Issue.23 , pp. 10830-10837
    • Herzer, K.1    Weyer, S.2    Krammer, P.H.3    Galle, P.R.4    Hofmann, T.G.5
  • 49
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • DOI 10.1038/sj.onc.1204854
    • Regad, T., and Chelbi-Alix, M. K. (2001) Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20, 7274-7286 (Pubitemid 33105016)
    • (2001) Oncogene , vol.20 , Issue.49 REV. IIS. 6 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 50
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett, R. D. (2001) DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20, 7266-7273
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 51
    • 0038205593 scopus 로고    scopus 로고
    • Localization of influenza virus proteins to nuclear dot 10 structures in influenza virus-infected cells
    • DOI 10.1016/S0042-6822(03)00104-1, PII S0042682203001041
    • Sato, Y., Yoshioka, K., Suzuki, C., Awashima, S., Hosaka, Y., Yewdell, J., and Kuroda, K. (2003) Localization of influenza virus proteins to nuclear dot 10 structures in influenza virus-infected cells. Virology 310, 29-40 (Pubitemid 38352579)
    • (2003) Virology , vol.310 , Issue.1 , pp. 29-40
    • Sato, Y.1    Yoshioka, K.2    Suzuki, C.3    Awashima, S.4    Hosaka, Y.5    Yewdell, J.6    Kuroda, K.7
  • 52
    • 55849083076 scopus 로고    scopus 로고
    • Influenza A replication and host nuclear compartments: Many changes and many questions
    • Josset, L., Frobert, E., and Rosa-Calatrava, M. (2008) Influenza A replication and host nuclear compartments: many changes and many questions. J. Clin. Virol. 43, 381-390
    • (2008) J. Clin. Virol. , vol.43 , pp. 381-390
    • Josset, L.1    Frobert, E.2    Rosa-Calatrava, M.3
  • 53
    • 0034702018 scopus 로고    scopus 로고
    • The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C
    • DOI 10.1016/S0378-1135(00)00169-3, PII S0378113500001693
    • Reinhardt, J., and Wolff, T. (2000) The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. Vet. Microbiol. 74, 87-100 (Pubitemid 30224647)
    • (2000) Veterinary Microbiology , vol.74 , Issue.1-2 , pp. 87-100
    • Reinhardt, J.1    Wolff, T.2
  • 54
    • 0028835724 scopus 로고
    • Nucleus-targeting domain of the matrix protein (M1) of influenza virus
    • Ye, Z., Robinson, D., and Wagner, R. R. (1995) Nucleus-targeting domain of the matrix protein (M1) of influenza virus. J. Virol. 69, 1964-1970
    • (1995) J. Virol. , vol.69 , pp. 1964-1970
    • Ye, Z.1    Robinson, D.2    Wagner, R.R.3
  • 55
    • 0028961386 scopus 로고
    • Hyperphosphorylation of mutant influenza virus matrix protein, M1, causes its retention in the nucleus
    • Whittaker, G., Kemler, I., and Helenius, A. (1995) Hyperphosphorylation of mutant influenza virus matrix protein, M1, causes its retention in the nucleus. J. Virol. 69, 439-445 (Pubitemid 24378822)
    • (1995) Journal of Virology , vol.69 , Issue.1 , pp. 439-445
    • Whittaker, G.1    Kemler, I.2    Helenius, A.3
  • 56
    • 80053400600 scopus 로고    scopus 로고
    • Cell death regulation during influenza A virus infection by matrix (M1) protein: A model of viral control over the cellular survival pathway
    • Halder, U. C., Bagchi, P., Chattopadhyay, S., Dutta, D., and Chawla-Sarkar, M. (2011) Cell death regulation during influenza A virus infection by matrix (M1) protein: a model of viral control over the cellular survival pathway. Cell Death Dis. 2, e197
    • (2011) Cell Death Dis. , vol.2
    • Halder, U.C.1    Bagchi, P.2    Chattopadhyay, S.3    Dutta, D.4    Chawla-Sarkar, M.5
  • 57
    • 0018830570 scopus 로고
    • A simplified plaque assay for influenza viruses in Madin-Darby kidney (MDCK) cells
    • DOI 10.1016/0166-0934(80)90020-8
    • Huprikar, J., and Rabinowitz, S. (1980) A simplified plaque assay for influenza viruses in Madin-Darby kidney (MDCK) cells. J. Virol. Methods. 1, 117-120 (Pubitemid 10109873)
    • (1980) Journal of Virological Methods , vol.1 , Issue.2 , pp. 117-120
    • Huprikar, J.1    Rabinowitz, S.2
  • 58
    • 0024284028 scopus 로고
    • A simple salting out procedure for extracting DNA from human nucleated cells
    • Miller, S. A., Dykes, D. D., and Polesky, H. F. (1988) A simple salting out procedure for extracting DNA from human nucleated cells. Nucleic Acids Res. 16, 1215
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1215
    • Miller, S.A.1    Dykes, D.D.2    Polesky, H.F.3
  • 59
    • 78649773554 scopus 로고    scopus 로고
    • Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C
    • Escobar-Cabrera, E., Lau, D. K., Giovinazzi, S., Ishov, A. M., and McIntosh, L. P. (2010) Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. Structure 18, 1642-1653
    • (2010) Structure , vol.18 , pp. 1642-1653
    • Escobar-Cabrera, E.1    Lau, D.K.2    Giovinazzi, S.3    Ishov, A.M.4    McIntosh, L.P.5
  • 60
    • 0037101953 scopus 로고    scopus 로고
    • Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek
    • Hollenbach, A. D., McPherson, C. J., Mientjes, E. J., Iyengar, R., and Grosveld, G. (2002) Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell Sci. 115, 3319-3330 (Pubitemid 34960184)
    • (2002) Journal of Cell Science , vol.115 , Issue.16 , pp. 3319-3330
    • Hollenbach, A.D.1    McPherson, C.J.2    Mientjes, E.J.3    Iyengar, R.4    Grosveld, G.5
  • 61
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function, and beyond
    • DOI 10.1146/annurev.biochem.75.103004.142615
    • Bialik, S., and Kimchi, A. (2006) The death-associated protein kinases: structure, function, and beyond. Annu. Rev. Biochem. 75, 189-210 (Pubitemid 44118031)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 62
    • 0034955802 scopus 로고    scopus 로고
    • Molecular pathogenesis of influenza A virus infection and virus-induced regulation of cytokine gene expression
    • DOI 10.1016/S1359-6101(00)00026-5, PII S1359610100000265
    • Julkunen, I., Sareneva, T., Pirhonen, J., Ronni, T., Melén, K., and Matikainen, S. (2001) Molecular pathogenesis of influenza A virus infection and virus-induced regulation of cytokine gene expression. Cytokine Growth Factor Rev. 12, 171-180 (Pubitemid 32588143)
    • (2001) Cytokine and Growth Factor Reviews , vol.12 , Issue.2-3 , pp. 171-180
    • Julkunen, I.1    Sareneva, T.2    Pirhonen, J.3    Ronni, T.4    Melen, K.5    Matikainen, S.6
  • 64
    • 21744452337 scopus 로고    scopus 로고
    • Daxx is required for stress-induced cell death and JNK activation
    • DOI 10.1038/sj.cdd.4401559
    • Khelifi, A. F., D'Alcontres, M. S., and Salomoni, P. (2005) Daxx is required for stress-induced cell death and JNK activation. Cell Death Differ. 12, 724-733 (Pubitemid 40945980)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.7 , pp. 724-733
    • Khelifi, A.F.1    D'Alcontres, M.S.2    Salomoni, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.