메뉴 건너뛰기




Volumn 403, Issue 1-2, 2015, Pages 187-197

The BM2 protein of influenza B virus interacts with p53 and inhibits its transcriptional and apoptotic activities

Author keywords

Apoptosis; BM2; p53; Protein protein interaction

Indexed keywords

BM2 POLYPEPTIDE, INFLUENZA B VIRUS; CYCLIN DEPENDENT KINASE INHIBITOR 1A; LUCIFERASE; PROTEIN BINDING; PROTEIN P53; VIRUS PROTEIN;

EID: 84939941413     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-015-2349-7     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 0036007087 scopus 로고    scopus 로고
    • Influenza A virus M2 ion channel activity is essential for efficient replication in tissue culture
    • COI: 1:CAS:528:DC%2BD38XnvFCqsg%3D%3D, PID: 11773413
    • Takeda M, Pekosz A, Shuck K, Pinto LH, Lamb RA (2002) Influenza A virus M2 ion channel activity is essential for efficient replication in tissue culture. J Virol 76:1391–1399. doi:10.1128/jvi.76.3.1391-1399.2002
    • (2002) J Virol , vol.76 , pp. 1391-1399
    • Takeda, M.1    Pekosz, A.2    Shuck, K.3    Pinto, L.H.4    Lamb, R.A.5
  • 2
    • 0036828039 scopus 로고    scopus 로고
    • A reverse genetics approach for recovery of recombinant influenza B viruses entirely from cDNA
    • COI: 1:CAS:528:DC%2BD38XoslKjtLo%3D, PID: 12388735
    • Jackson D, Cadman A, Zurcher T, Barclay WS (2002) A reverse genetics approach for recovery of recombinant influenza B viruses entirely from cDNA. J Virol 76:11744–11747. doi:10.1128/jvi.76.22.11744-11747.2002
    • (2002) J Virol , vol.76 , pp. 11744-11747
    • Jackson, D.1    Cadman, A.2    Zurcher, T.3    Barclay, W.S.4
  • 3
    • 0020073663 scopus 로고
    • Sequence of RNA segment 7 of the influenza B virus genome: partial amino acid homology between the membrane proteins (M1) of influenza A and B viruses and conservation of a second open reading frame
    • COI: 1:CAS:528:DyaL38XhtFKltb4%3D, PID: 6278729
    • Briedis DJ, Lamb RA, Choppin PW (1982) Sequence of RNA segment 7 of the influenza B virus genome: partial amino acid homology between the membrane proteins (M1) of influenza A and B viruses and conservation of a second open reading frame. Virology 116:581–588. doi:10.1016/0042-6822(82)90150-7
    • (1982) Virology , vol.116 , pp. 581-588
    • Briedis, D.J.1    Lamb, R.A.2    Choppin, P.W.3
  • 4
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza A and B viruses
    • COI: 1:CAS:528:DC%2BD28XjtVSktrg%3D, PID: 16407184
    • Pinto LH, Lamb RA (2006) The M2 proton channels of influenza A and B viruses. J Biol Chem 281:8997–9000. doi:10.1074/jbc.R500020200
    • (2006) J Biol Chem , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 5
    • 0032837367 scopus 로고    scopus 로고
    • The BM2 protein of influenza B virus is synthesized in the late phase of infection and incorporated into virions as a subviral component
    • COI: 1:CAS:528:DyaK1MXmsVygsb4%3D, PID: 10573149
    • Odagiri T, Hong J, Ohara Y (1999) The BM2 protein of influenza B virus is synthesized in the late phase of infection and incorporated into virions as a subviral component. J Gen Virol 80:2573–2581
    • (1999) J Gen Virol , vol.80 , pp. 2573-2581
    • Odagiri, T.1    Hong, J.2    Ohara, Y.3
  • 6
    • 0038347950 scopus 로고    scopus 로고
    • Influenza B virus BM2 protein has ion channel activity that conducts protons across membranes
    • COI: 1:CAS:528:DC%2BD3sXmt1Smsb0%3D, PID: 12852861
    • Mould JA, Paterson RG, Takeda M, Ohigashi Y, Venkataraman P, Lamb RA, Pinto LH (2003) Influenza B virus BM2 protein has ion channel activity that conducts protons across membranes. Dev Cell 5:175–184. doi:10.1016/s1534-5807(03)00190-4
    • (2003) Dev Cell , vol.5 , pp. 175-184
    • Mould, J.A.1    Paterson, R.G.2    Takeda, M.3    Ohigashi, Y.4    Venkataraman, P.5    Lamb, R.A.6    Pinto, L.H.7
  • 7
    • 0026520296 scopus 로고
    • Regulation of pH by the M2 protein of influenza A viruses
    • COI: 1:CAS:528:DyaK38Xkt1eju7Y%3D, PID: 1626420
    • Ciampor F, Thompson CA, Grambas S, Hay AJ (1992) Regulation of pH by the M2 protein of influenza A viruses. Virus Res 22:247–258. doi:10.1016/0168-1702(92)90056-f
    • (1992) Virus Res , vol.22 , pp. 247-258
    • Ciampor, F.1    Thompson, C.A.2    Grambas, S.3    Hay, A.J.4
  • 8
    • 2442655309 scopus 로고    scopus 로고
    • Influenza B virus requires BM2 protein for replication
    • COI: 1:CAS:528:DC%2BD2cXksFCgs7w%3D, PID: 15140954
    • Hatta M, Goto H, Kawaoka Y (2004) Influenza B virus requires BM2 protein for replication. J Virol 78:5576–5583. doi:10.1128/jvi.78.11.5576-5583.2004
    • (2004) J Virol , vol.78 , pp. 5576-5583
    • Hatta, M.1    Goto, H.2    Kawaoka, Y.3
  • 9
    • 4644316069 scopus 로고    scopus 로고
    • Influenza B virus BM2 protein is a crucial component for incorporation of viral ribonucleoprotein complex into virions during virus assembly
    • COI: 1:CAS:528:DC%2BD2cXotlKju70%3D, PID: 15452221
    • Imai M, Watanabe S, Ninomiya A, Obuchi M, Odagiri T (2004) Influenza B virus BM2 protein is a crucial component for incorporation of viral ribonucleoprotein complex into virions during virus assembly. J Virol 78:11007–11015. doi:10.1128/jvi.78.20.11007-11015.2004
    • (2004) J Virol , vol.78 , pp. 11007-11015
    • Imai, M.1    Watanabe, S.2    Ninomiya, A.3    Obuchi, M.4    Odagiri, T.5
  • 10
    • 37849040448 scopus 로고    scopus 로고
    • Cytoplasmic domain of influenza B virus BM2 protein plays critical roles in production of infectious virus
    • COI: 1:CAS:528:DC%2BD1cXmtFCmtw%3D%3D, PID: 17989175
    • Imai M, Kawasaki K, Odagiri T (2008) Cytoplasmic domain of influenza B virus BM2 protein plays critical roles in production of infectious virus. J Virol 82:728–739. doi:10.1128/jvi.01752-07
    • (2008) J Virol , vol.82 , pp. 728-739
    • Imai, M.1    Kawasaki, K.2    Odagiri, T.3
  • 11
    • 60549112774 scopus 로고    scopus 로고
    • Inflammasome recognition of influenza virus is essential for adaptive immune responses
    • COI: 1:CAS:528:DC%2BD1MXhtVOhtbY%3D, PID: 19139171
    • Ichinohe T, Lee HK, Ogura Y, Flavell R, Iwasaki A (2009) Inflammasome recognition of influenza virus is essential for adaptive immune responses. J Exp Med 206:79–87. doi:10.1084/jem.20081667
    • (2009) J Exp Med , vol.206 , pp. 79-87
    • Ichinohe, T.1    Lee, H.K.2    Ogura, Y.3    Flavell, R.4    Iwasaki, A.5
  • 12
    • 77951295418 scopus 로고    scopus 로고
    • Influenza virus activates inflammasomes via its intracellular M2 ion channel
    • COI: 1:CAS:528:DC%2BC3cXksFaks7Y%3D, PID: 20383149
    • Ichinohe T, Pang IK, Iwasaki A (2010) Influenza virus activates inflammasomes via its intracellular M2 ion channel. Nat Immunol 11:404–461. doi:10.1038/ni.1861
    • (2010) Nat Immunol , vol.11 , pp. 404-461
    • Ichinohe, T.1    Pang, I.K.2    Iwasaki, A.3
  • 13
    • 4544343313 scopus 로고    scopus 로고
    • Human tumor suppressor p53 and DNA viruses
    • COI: 1:CAS:528:DC%2BD2cXos1Cntbw%3D, PID: 15334538
    • Collot-Teixeira S, Bass J, Denis F, Ranger-Rogez S (2004) Human tumor suppressor p53 and DNA viruses. Rev Med Virol 14:301–319. doi:10.1002/rmv.431
    • (2004) Rev Med Virol , vol.14 , pp. 301-319
    • Collot-Teixeira, S.1    Bass, J.2    Denis, F.3    Ranger-Rogez, S.4
  • 14
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: the growing complexity of p53
    • COI: 1:CAS:528:DC%2BD1MXlvFams74%3D, PID: 19410540
    • Vousden KH, Prives C (2009) Blinded by the light: the growing complexity of p53. Cell 137:413–431. doi:10.1016/j.cell.2009.04.037
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 15
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • COI: 1:CAS:528:DC%2BD3cXosVemtrY%3D, PID: 11099028
    • Vogelstein B, Lane D, Levine AJ (2000) Surfing the p53 network. Nature 408:307–310. doi:10.1038/35042675
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 16
    • 80053005260 scopus 로고    scopus 로고
    • Introduction: the changing directions of p53 research
    • PID: 21785490
    • Levine AJ (2011) Introduction: the changing directions of p53 research. Genes Cancer 2:382–384. doi:10.1177/1947601911413463
    • (2011) Genes Cancer , vol.2 , pp. 382-384
    • Levine, A.J.1
  • 17
    • 84871955225 scopus 로고    scopus 로고
    • Interactions between the tumor suppressor p53 and immune responses
    • COI: 1:CAS:528:DC%2BC38XhvVSisrrN, PID: 23150340
    • Menendez D, Shatz M, Resnick MA (2013) Interactions between the tumor suppressor p53 and immune responses. Curr Opin Oncol 25:85–92. doi:10.1097/CCO.0b013e32835b6386
    • (2013) Curr Opin Oncol , vol.25 , pp. 85-92
    • Menendez, D.1    Shatz, M.2    Resnick, M.A.3
  • 18
    • 80051709190 scopus 로고    scopus 로고
    • Inflammation and p53: a tale of two stresses
    • COI: 1:CAS:528:DC%2BC3MXhtVKju7%2FF, PID: 21779518
    • Gudkov AV, Gurova KV, Komarova EA (2011) Inflammation and p53: a tale of two stresses. Genes Cancer 2:503–516. doi:10.1177/1947601911409747
    • (2011) Genes Cancer , vol.2 , pp. 503-516
    • Gudkov, A.V.1    Gurova, K.V.2    Komarova, E.A.3
  • 20
    • 0242363230 scopus 로고    scopus 로고
    • Borna disease virus phosphoprotein represses p53-mediated transcriptional activity by interference with HMGB1
    • COI: 1:CAS:528:DC%2BD3sXovVant7c%3D, PID: 14581561
    • Zhang GQ, Kobayashi T, Kamitani W, Komoto S, Yamashita M, Baba S, Yanai H, Ikuta K, Tomonaga K (2003) Borna disease virus phosphoprotein represses p53-mediated transcriptional activity by interference with HMGB1. J Virol 77:12243–12251. doi:10.1128/jvi.77.22.12243-12251.2003
    • (2003) J Virol , vol.77 , pp. 12243-12251
    • Zhang, G.Q.1    Kobayashi, T.2    Kamitani, W.3    Komoto, S.4    Yamashita, M.5    Baba, S.6    Yanai, H.7    Ikuta, K.8    Tomonaga, K.9
  • 21
    • 5344223369 scopus 로고    scopus 로고
    • The vaccinia virus B1R kinase induces p53 downregulation by an Mdm2-dependent mechanism
    • COI: 1:CAS:528:DC%2BD2cXotF2nu7w%3D, PID: 15464845
    • Santos CR, Vega FM, Blanco S, Barcia R, Lazo PA (2004) The vaccinia virus B1R kinase induces p53 downregulation by an Mdm2-dependent mechanism. Virology 328:254–265. doi:10.1016/j.virol.2004.08.013
    • (2004) Virology , vol.328 , pp. 254-265
    • Santos, C.R.1    Vega, F.M.2    Blanco, S.3    Barcia, R.4    Lazo, P.A.5
  • 22
    • 21644454525 scopus 로고    scopus 로고
    • Influenza virus infection increases p53 activity: role of p53 in cell death and viral replication
    • COI: 1:CAS:528:DC%2BD2MXmtFOjs78%3D, PID: 15994774
    • Turpin E, Luke M, Jones J, Tumpey T, Konan K, Schultz-Cherry S (2005) Influenza virus infection increases p53 activity: role of p53 in cell death and viral replication. J Virol 79:8802–8811. doi:10.1128/jvi.79.14.8802-8811.2005
    • (2005) J Virol , vol.79 , pp. 8802-8811
    • Turpin, E.1    Luke, M.2    Jones, J.3    Tumpey, T.4    Konan, K.5    Schultz-Cherry, S.6
  • 23
    • 83755195791 scopus 로고    scopus 로고
    • p53 Serves as a host antiviral factor that enhances innate and adaptive immune responses to influenza A virus
    • COI: 1:CAS:528:DC%2BC3MXhsFOgt7rK, PID: 22105999
    • Munoz-Fontela C, Pazos M, Delgado I, Murk W, Mungamuri SK, Lee SW, Garcia-Sastre A, Moran TM, Aaronson SA (2011) p53 Serves as a host antiviral factor that enhances innate and adaptive immune responses to influenza A virus. J Immunol 187:6428–6436. doi:10.4049/jimmunol.1101459
    • (2011) J Immunol , vol.187 , pp. 6428-6436
    • Munoz-Fontela, C.1    Pazos, M.2    Delgado, I.3    Murk, W.4    Mungamuri, S.K.5    Lee, S.W.6    Garcia-Sastre, A.7    Moran, T.M.8    Aaronson, S.A.9
  • 24
    • 77951929071 scopus 로고    scopus 로고
    • The non-structural (NS1) protein of influenza A virus associates with p53 and inhibits p53-mediated transcriptional activity and apoptosis
    • COI: 1:CAS:528:DC%2BC3cXlt1ahtLg%3D, PID: 20361939
    • Wang XD, Shen Y, Qiu YF, Shi ZX, Shao DH, Chen PJ, Tong GZ, Ma ZY (2010) The non-structural (NS1) protein of influenza A virus associates with p53 and inhibits p53-mediated transcriptional activity and apoptosis. Biochem Biophys Res Commun 395:141–145. doi:10.1016/j.bbrc.2010.03.160
    • (2010) Biochem Biophys Res Commun , vol.395 , pp. 141-145
    • Wang, X.D.1    Shen, Y.2    Qiu, Y.F.3    Shi, Z.X.4    Shao, D.H.5    Chen, P.J.6    Tong, G.Z.7    Ma, Z.Y.8
  • 25
    • 84873499696 scopus 로고    scopus 로고
    • Identification of cellular proteins interacting with influenza A virus PB1-F2 protein
    • COI: 1:CAS:528:DC%2BC3sXovVemtQ%3D%3D, PID: 23043599
    • Guan ZH, Zhang ML, Hou PL, Duan M, Cui YM, Wang XR (2012) Identification of cellular proteins interacting with influenza A virus PB1-F2 protein. Acta Virol 56:199–207. doi:10.4149/av_2012_03_199
    • (2012) Acta Virol , vol.56 , pp. 199-207
    • Guan, Z.H.1    Zhang, M.L.2    Hou, P.L.3    Duan, M.4    Cui, Y.M.5    Wang, X.R.6
  • 26
    • 79953140465 scopus 로고    scopus 로고
    • Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway
    • COI: 1:CAS:528:DC%2BC3cXhtl2it7nF, PID: 21204021
    • Guan ZH, Liu D, Mi SF, Zhang J, Ye QN, Wang M, Gao GF, Yan JH (2010) Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway. Protein Cell 1:944–955. doi:10.1007/s13238-010-0115-x
    • (2010) Protein Cell , vol.1 , pp. 944-955
    • Guan, Z.H.1    Liu, D.2    Mi, S.F.3    Zhang, J.4    Ye, Q.N.5    Wang, M.6    Gao, G.F.7    Yan, J.H.8
  • 28
    • 74249089749 scopus 로고    scopus 로고
    • Stress-mediated nuclear stabilization of p53 is regulated by ubiquitination and importin-alpha3 binding
    • COI: 1:CAS:528:DC%2BC3cXjt12juw%3D%3D, PID: 19927155
    • Marchenko ND, Hanel W, Li D, Becker K, Reich N, Moll UM (2010) Stress-mediated nuclear stabilization of p53 is regulated by ubiquitination and importin-alpha3 binding. Cell Death Differ 17:255–267. doi:10.1038/cdd.2009.173
    • (2010) Cell Death Differ , vol.17 , pp. 255-267
    • Marchenko, N.D.1    Hanel, W.2    Li, D.3    Becker, K.4    Reich, N.5    Moll, U.M.6
  • 29
    • 33845202484 scopus 로고    scopus 로고
    • Regulation of p53 localization and activity by Ubc13
    • COI: 1:CAS:528:DC%2BD28Xht1yqsLbM, PID: 17000756
    • Laine A, Topisirovic I, Zhai D, Reed JC, Borden KL, Ronai Z (2006) Regulation of p53 localization and activity by Ubc13. Mol Cell Biol 26:8901–8913. doi:10.1128/MCB.01156-06
    • (2006) Mol Cell Biol , vol.26 , pp. 8901-8913
    • Laine, A.1    Topisirovic, I.2    Zhai, D.3    Reed, J.C.4    Borden, K.L.5    Ronai, Z.6
  • 30
    • 77953834412 scopus 로고    scopus 로고
    • MG132 as a proteasome inhibitor induces cell growth inhibition and cell death in A549 lung cancer cells via influencing reactive oxygen species and GSH level
    • Han YH, Park WH (2013) MG132 as a proteasome inhibitor induces cell growth inhibition and cell death in A549 lung cancer cells via influencing reactive oxygen species and GSH level. Hum Exp Toxicol 29:607–614. doi:10.1177/0960327109358733
    • (2013) Hum Exp Toxicol , vol.29 , pp. 607-614
    • Han, Y.H.1    Park, W.H.2
  • 31
    • 34248577475 scopus 로고    scopus 로고
    • p53 and p21 determine the sensitivity of noscapine-induced apoptosis in colon cancer cells
    • COI: 1:CAS:528:DC%2BD2sXkt1Kitbg%3D, PID: 17440101
    • Aneja R, Ghaleb AM, Zhou J, Yang VW, Joshi HC (2007) p53 and p21 determine the sensitivity of noscapine-induced apoptosis in colon cancer cells. Cancer Res 67:3862–3870. doi:10.1158/0008-5472.CAN-06-4282
    • (2007) Cancer Res , vol.67 , pp. 3862-3870
    • Aneja, R.1    Ghaleb, A.M.2    Zhou, J.3    Yang, V.W.4    Joshi, H.C.5
  • 32
    • 84878528369 scopus 로고    scopus 로고
    • Rotavirus-encoded nonstructural protein 1 modulates cellular apoptotic machinery by targeting tumor suppressor protein p53
    • COI: 1:CAS:528:DC%2BC3sXptlKkurg%3D, PID: 23576507
    • Bhowmick R, Halder UC, Chattopadhyay S, Nayak MK, Chawla-Sarkar M (2013) Rotavirus-encoded nonstructural protein 1 modulates cellular apoptotic machinery by targeting tumor suppressor protein p53. J Virol 87:6840–6850. doi:10.1128/JVI.00734-13
    • (2013) J Virol , vol.87 , pp. 6840-6850
    • Bhowmick, R.1    Halder, U.C.2    Chattopadhyay, S.3    Nayak, M.K.4    Chawla-Sarkar, M.5
  • 33
    • 84869504554 scopus 로고    scopus 로고
    • Angiogenin functionally interacts with p53 and regulates p53-mediated apoptosis and cell survival
    • COI: 1:CAS:528:DC%2BC38Xhs1Ogt7%2FN, PID: 22266868
    • Sadagopan S, Veettil MV, Chakraborty S, Sharma-Walia N, Paudel N, Bottero V, Chandran B (2012) Angiogenin functionally interacts with p53 and regulates p53-mediated apoptosis and cell survival. Oncogene 31:4835–4847. doi:10.1038/onc.2011.648
    • (2012) Oncogene , vol.31 , pp. 4835-4847
    • Sadagopan, S.1    Veettil, M.V.2    Chakraborty, S.3    Sharma-Walia, N.4    Paudel, N.5    Bottero, V.6    Chandran, B.7
  • 34
    • 78650900240 scopus 로고    scopus 로고
    • RNF43 interacts with NEDL1 and regulates p53-mediated transcription
    • COI: 1:CAS:528:DC%2BC3MXksFOmtw%3D%3D, PID: 21108931
    • Shinada K, Tsukiyama T, Sho T, Okumura F, Asaka M, Hatakeyama S (2011) RNF43 interacts with NEDL1 and regulates p53-mediated transcription. Biochem Biophys Res Commun 404:143–147. doi:10.1016/j.bbrc.2010.11.082
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 143-147
    • Shinada, K.1    Tsukiyama, T.2    Sho, T.3    Okumura, F.4    Asaka, M.5    Hatakeyama, S.6
  • 35
    • 84863158307 scopus 로고    scopus 로고
    • Human annexin A6 Interacts with influenza A virus protein M2 and negatively modulates infection
    • COI: 1:CAS:528:DC%2BC38XhsV2nurY%3D, PID: 22114333
    • Ma HL, Kien F, Maniere M, Zhang Y, Lagarde N, Tse KS, Poon LLM, Nal B (2012) Human annexin A6 Interacts with influenza A virus protein M2 and negatively modulates infection. J Virol 86:1789–1801. doi:10.1128/jvi.06003-11
    • (2012) J Virol , vol.86 , pp. 1789-1801
    • Ma, H.L.1    Kien, F.2    Maniere, M.3    Zhang, Y.4    Lagarde, N.5    Tse, K.S.6    Poon, L.L.M.7    Nal, B.8
  • 39
    • 0026560315 scopus 로고
    • Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein
    • COI: 1:CAS:528:DyaK38XktVGhsL4%3D, PID: 1533443
    • Yew PR, Berk AJ (1992) Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein. Nature 357:82–85. doi:10.1038/357082a0
    • (1992) Nature , vol.357 , pp. 82-85
    • Yew, P.R.1    Berk, A.J.2
  • 41
    • 0032913880 scopus 로고    scopus 로고
    • New insights into the mechanism of inhibition of p53 by simian virus 40 large T antigen
    • COI: 1:CAS:528:DyaK1MXit1amtL0%3D, PID: 10082540
    • Sheppard HM, Corneillie SI, Espiritu C, Gatti A, Liu XA (1999) New insights into the mechanism of inhibition of p53 by simian virus 40 large T antigen. Mol Cell Biol 19:2746–2753
    • (1999) Mol Cell Biol , vol.19 , pp. 2746-2753
    • Sheppard, H.M.1    Corneillie, S.I.2    Espiritu, C.3    Gatti, A.4    Liu, X.A.5
  • 43
    • 34250828457 scopus 로고    scopus 로고
    • Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling
    • COI: 1:CAS:528:DC%2BD2sXmvVyqurs%3D, PID: 17468837
    • Zhirnov OP, Klenk HD (2007) Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling. Apoptosis 12:1419–1432. doi:10.1007/s10495-007-0071-y
    • (2007) Apoptosis , vol.12 , pp. 1419-1432
    • Zhirnov, O.P.1    Klenk, H.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.