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Volumn 6, Issue 11, 2011, Pages

A plant virus movement protein regulates the Gcn2p kinase in budding yeast

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; GCN2P KINASE; INITIATION FACTOR 2ALPHA; PLANT VIRUS MOVEMENT PROTEIN; PROTEIN KINASE; RAPAMYCIN; TORP1 KINASE; UNCLASSIFIED DRUG; GCN2 PROTEIN, S CEREVISIAE; PROTEIN SERINE THREONINE KINASE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 80555154378     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027409     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch, AG, (2005) Translational regulation of GCN4 and the general amino acid control of yeast. Ann Rev of Microbiology 59: 407-450.
    • (2005) Ann Rev of Microbiology , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 2
    • 0027171069 scopus 로고
    • Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: Implications for activation of the protein kinase GCN2
    • Rolfes RJ, Hinnebusch AG, (1993) Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: Implications for activation of the protein kinase GCN2. Mol Cell Biol 13: 5099-111.
    • (1993) Mol Cell Biol , vol.13 , pp. 5099-5111
    • Rolfes, R.J.1    Hinnebusch, A.G.2
  • 3
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • Natarajan K, Meyer MR, Jackson BM, Slade D, Roberts C, et al. (2001) Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast. Mol Cell Biol 21: 4347-68.
    • (2001) Mol Cell Biol , vol.21 , pp. 4347-4368
    • Natarajan, K.1    Meyer, M.R.2    Jackson, B.M.3    Slade, D.4    Roberts, C.5
  • 4
    • 0042352484 scopus 로고    scopus 로고
    • Molecular cloning of an Arabidopsis homologue of GCN2, a protein kinase involved in co-ordinated response to amino acid starvation
    • Zhang Y, Dickinson JR, Paul MJ, Halford NG, (2003) Molecular cloning of an Arabidopsis homologue of GCN2, a protein kinase involved in co-ordinated response to amino acid starvation. Planta 217: 668-675.
    • (2003) Planta , vol.217 , pp. 668-675
    • Zhang, Y.1    Dickinson, J.R.2    Paul, M.J.3    Halford, N.G.4
  • 5
    • 84984837273 scopus 로고    scopus 로고
    • Regulation of carbon and amino acid metabolism, roles of sucrose nonfermenting-1-related protein kinase-1 and general control nonderepressible-2-related protein kinase
    • Halford, NG, (2006) Regulation of carbon and amino acid metabolism, roles of sucrose nonfermenting-1-related protein kinase-1 and general control nonderepressible-2-related protein kinase. Ad Bot Res 43: 93-142.
    • (2006) Ad Bot Res , vol.43 , pp. 93-142
    • Halford, N.G.1
  • 6
    • 17144403770 scopus 로고    scopus 로고
    • Adenoviral proteins mimic nutrient/growth signals to activate the mTOR pathway for viral replication
    • O'Shea CK, Klupsch S, Choi B, Bagus C, Soria J, et al. (2005) Adenoviral proteins mimic nutrient/growth signals to activate the mTOR pathway for viral replication. EMBO J 24: 1211-1221.
    • (2005) EMBO J , vol.24 , pp. 1211-1221
    • O'Shea, C.K.1    Klupsch, S.2    Choi, B.3    Bagus, C.4    Soria, J.5
  • 7
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud CG, (2005) eIF2 and the control of cell physiology. Semin Cell Dev Biol 16: 3-12.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 8
    • 0031017382 scopus 로고    scopus 로고
    • The c 1 34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1a to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA activated protein kinase
    • He B, Gross M, Roizman B, (1997) The c 1 34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1a to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA activated protein kinase. Proc Natl Acad Sci U S A 94: 843-848.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 9
    • 15844362424 scopus 로고    scopus 로고
    • Expression of Vaccinia Virus K3L Protein in Yeast Inhibits Eukaryotic Initiation Factor-2 Kinase GCN2 and the General Amino Acid Control Pathway
    • Qian W, Zhu S, Sobolev AY, Wek RC, (1996) Expression of Vaccinia Virus K3L Protein in Yeast Inhibits Eukaryotic Initiation Factor-2 Kinase GCN2 and the General Amino Acid Control Pathway. J Biol Chem 271: 13202-13207.
    • (1996) J Biol Chem , vol.271 , pp. 13202-13207
    • Qian, W.1    Zhu, S.2    Sobolev, A.Y.3    Wek, R.C.4
  • 10
    • 38349138566 scopus 로고    scopus 로고
    • Rotavirus Infection Induces the Phosphorylation of eIF2a but Prevents the Formation of Stress Granules
    • Montero H, Rojas M, Arias CA, Lopez S, (2008) Rotavirus Infection Induces the Phosphorylation of eIF2a but Prevents the Formation of Stress Granules. J Virol 82: 1496-1504.
    • (2008) J Virol , vol.82 , pp. 1496-1504
    • Montero, H.1    Rojas, M.2    Arias, C.A.3    Lopez, S.4
  • 11
    • 77957200555 scopus 로고    scopus 로고
    • Protein Kinase R Is Responsible for the Phosphorylation of eIF2α in Rotavirus Infection
    • Rojas M, Arias CF, López S, (2010) Protein Kinase R Is Responsible for the Phosphorylation of eIF2α in Rotavirus Infection. J Virol 84: 10457-10466.
    • (2010) J Virol , vol.84 , pp. 10457-10466
    • Rojas, M.1    Arias, C.F.2    López, S.3
  • 12
    • 60349119497 scopus 로고    scopus 로고
    • Arabidopsis eIF2α kinase GCN2 is essential for growth in stress conditions and is activated by wounding
    • Lageix S, Lanet E, Pouch-Pélissier MN, Espagnol MC, Robaglia C, et al. (2008) Arabidopsis eIF2α kinase GCN2 is essential for growth in stress conditions and is activated by wounding. BMC Pant Biol 8: 134.
    • (2008) BMC Pant Biol , vol.8 , pp. 134
    • Lageix, S.1    Lanet, E.2    Pouch-Pélissier, M.N.3    Espagnol, M.C.4    Robaglia, C.5
  • 13
    • 49449103129 scopus 로고    scopus 로고
    • GCN2-dependent phosphorylation of eukaryotic translation initiation factor-2α in Arabidopsis
    • Zhang Y, Wang Y, Kanyuka K, Parry MAJ, Powers J S, et al. (2008) GCN2-dependent phosphorylation of eukaryotic translation initiation factor-2α in Arabidopsis. J Exp Botany 59: 3131-3141.
    • (2008) J Exp Botany , vol.59 , pp. 3131-3141
    • Zhang, Y.1    Wang, Y.2    Kanyuka, K.3    Parry, M.A.J.4    Powers, J.S.5
  • 14
    • 0038668784 scopus 로고    scopus 로고
    • P58IPK, a plant ortholog of double-stranded RNA-dependent protein kinase PKR inhibitor, functions in viral pathogenesis
    • Bilgin DD, Liu Y, Schiff M, Dinesh-Kumar SP, (2003) P58IPK, a plant ortholog of double-stranded RNA-dependent protein kinase PKR inhibitor, functions in viral pathogenesis. Dev Cell 4: 651-661.
    • (2003) Dev Cell , vol.4 , pp. 651-661
    • Bilgin, D.D.1    Liu, Y.2    Schiff, M.3    Dinesh-Kumar, S.P.4
  • 15
    • 78751649327 scopus 로고    scopus 로고
    • Plasmodesmata as Active Conduits for Virus Cell-to-Cell Movement
    • In: Caranta C, Aranda MA, Tepfer M, Lopez-Moya JJ, editors, Caister Academic Press. ISBN: 978-1-904455-75-2
    • Fernandez-Calvino L, Faulkner C, Maule A, (2011) Plasmodesmata as Active Conduits for Virus Cell-to-Cell Movement. In: Caranta C, Aranda MA, Tepfer M, Lopez-Moya JJ, editors. Recent Advances in Plant Virology Caister Academic Press. ISBN: 978-1-904455-75-2.
    • (2011) Recent Advances in Plant Virology
    • Fernandez-Calvino, L.1    Faulkner, C.2    Maule, A.3
  • 16
    • 80555142297 scopus 로고    scopus 로고
    • Systemic movement of viruses via the plant phloem
    • In: Caranta C, Aranda MA, Tepfer M, Lopez-Moya JJ, editors, Caister Academic Press. ISBN: 978-1-904455-75-2
    • Pallás V, Genoves A, Sánchez-Pina MA, Navarro JA, (2011) Systemic movement of viruses via the plant phloem. In: Caranta C, Aranda MA, Tepfer M, Lopez-Moya JJ, editors. Recent Advances in Plant Virology Caister Academic Press. ISBN: 978-1-904455-75-2.
    • (2011) Recent Advances in Plant Virology
    • Pallás, V.1    Genoves, A.2    Sánchez-Pina, M.A.3    Navarro, J.A.4
  • 17
    • 3042581415 scopus 로고    scopus 로고
    • The ins and outs ofnondestructive cell-to-cell and systemic movement of plant viruses
    • Waigmann E, Ueki S, Trutnyeva K, Citovsky V, (2004) The ins and outs ofnondestructive cell-to-cell and systemic movement of plant viruses. Crit Rev Plant Sci 23: 195-250.
    • (2004) Crit Rev Plant Sci , vol.23 , pp. 195-250
    • Waigmann, E.1    Ueki, S.2    Trutnyeva, K.3    Citovsky, V.4
  • 18
    • 0033971647 scopus 로고    scopus 로고
    • The "30K" superfamily of viral movement proteins
    • Melcher U, (2000) The "30K" superfamily of viral movement proteins. J Gen Virol 81: 257-266.
    • (2000) J Gen Virol , vol.81 , pp. 257-266
    • Melcher, U.1
  • 19
    • 3042761274 scopus 로고    scopus 로고
    • Roles for host factors in plant viral pathogenicity
    • Whitham SA, Wang YZ, (2004) Roles for host factors in plant viral pathogenicity. Current Opinion Plant Biol 7: 365-371.
    • (2004) Current Opinion Plant Biol , vol.7 , pp. 365-371
    • Whitham, S.A.1    Wang, Y.Z.2
  • 20
    • 33644691831 scopus 로고    scopus 로고
    • Virus-host interactions during movement processes
    • Boevink P, Oparka KJ, (2005) Virus-host interactions during movement processes. Plant Physiol 138: 1815-1821.
    • (2005) Plant Physiol , vol.138 , pp. 1815-1821
    • Boevink, P.1    Oparka, K.J.2
  • 21
    • 29244440855 scopus 로고    scopus 로고
    • Plant viral movement proteins: Agents for cell-to-cell trafficking of viral genomes
    • Lucas WJ, (2006) Plant viral movement proteins: Agents for cell-to-cell trafficking of viral genomes. Virology 344: 169-184.
    • (2006) Virology , vol.344 , pp. 169-184
    • Lucas, W.J.1
  • 22
    • 34247256783 scopus 로고    scopus 로고
    • MPB2C, a microtubule-associated plant factor, is required for microtubular accumulation of tobacco mosaic virus movement protein in plants
    • Curin M, Ojangu EL, Trutnyeva K, Llau B, Truve E, et al. (2007) MPB2C, a microtubule-associated plant factor, is required for microtubular accumulation of tobacco mosaic virus movement protein in plants. Plant Physiol 143: 801-811.
    • (2007) Plant Physiol , vol.143 , pp. 801-811
    • Curin, M.1    Ojangu, E.L.2    Trutnyeva, K.3    Llau, B.4    Truve, E.5
  • 23
    • 34250659699 scopus 로고    scopus 로고
    • Downregulation of the NbNACa1 gene encoding a movement-protein-interacting protein reduces cell-to-cell movement of brome mosaic virus in Nicotiana benthamiana
    • Kaido M, Inoue Y, Takeda Y, Takeda A, Mori M, et al. (2007) Downregulation of the NbNACa1 gene encoding a movement-protein-interacting protein reduces cell-to-cell movement of brome mosaic virus in Nicotiana benthamiana. Mol Plant-Microbe Interact 20: 671-681.
    • (2007) Mol Plant-Microbe Interact , vol.20 , pp. 671-681
    • Kaido, M.1    Inoue, Y.2    Takeda, Y.3    Takeda, A.4    Mori, M.5
  • 24
    • 60349088866 scopus 로고    scopus 로고
    • Over-expression of putative transcriptional coactivator KELP interferes with Tomato mosaic virus cell-to-cell movement
    • Sasaki N, Ogata T, Deguchi M, Nagai S, Tamai A, et al. (2009) Over-expression of putative transcriptional coactivator KELP interferes with Tomato mosaic virus cell-to-cell movement. Mol Plant Pathol 10: 161-173.
    • (2009) Mol Plant Pathol , vol.10 , pp. 161-173
    • Sasaki, N.1    Ogata, T.2    Deguchi, M.3    Nagai, S.4    Tamai, A.5
  • 25
    • 67349191497 scopus 로고    scopus 로고
    • Identification of a novel tobacco DnaJ-like protein that interacts with the movement protein of tobacco mosaic virus
    • Shimizu T, Yoshii A, Sakurai K, Hamada K, Yamaji Y, et al. (2009) Identification of a novel tobacco DnaJ-like protein that interacts with the movement protein of tobacco mosaic virus. Arch Virol 154: 959-967.
    • (2009) Arch Virol , vol.154 , pp. 959-967
    • Shimizu, T.1    Yoshii, A.2    Sakurai, K.3    Hamada, K.4    Yamaji, Y.5
  • 26
    • 35148834683 scopus 로고    scopus 로고
    • Virus-induced disease: altering host physiology one interaction at a time
    • Culver JN, Padmanabhan MS, (2007) Virus-induced disease: altering host physiology one interaction at a time. Annu Rev Phytopathol 45: 221-243.
    • (2007) Annu Rev Phytopathol , vol.45 , pp. 221-243
    • Culver, J.N.1    Padmanabhan, M.S.2
  • 27
    • 0000365514 scopus 로고
    • Ilarvirus Vectors
    • Mink GI, (1992) Ilarvirus Vectors. Ad. Dis Vector Res 9: 261-281.
    • (1992) Ad. Dis Vector Res , vol.9 , pp. 261-281
    • Mink, G.I.1
  • 28
    • 0030938801 scopus 로고    scopus 로고
    • Evolutionary relationships in the ilarviruses: Nucleotide sequence of prunus necrotic ringspot virus RNA 3
    • Sánchez-Navarro JA, Pallás V, (1997) Evolutionary relationships in the ilarviruses: Nucleotide sequence of prunus necrotic ringspot virus RNA 3. Arch Virol 142: 749-763.
    • (1997) Arch Virol , vol.142 , pp. 749-763
    • Sánchez-Navarro, J.A.1    Pallás, V.2
  • 29
    • 0042389435 scopus 로고    scopus 로고
    • The coat protein of prunus necrotic ringspot virus specifically binds to and regulates the conformation of its genomic RNA
    • Aparicio F, Vilar M, Perez-Paya E, Pallás V, (2003) The coat protein of prunus necrotic ringspot virus specifically binds to and regulates the conformation of its genomic RNA. Virology 313: 213-223.
    • (2003) Virology , vol.313 , pp. 213-223
    • Aparicio, F.1    Vilar, M.2    Perez-Paya, E.3    Pallás, V.4
  • 30
    • 0036345842 scopus 로고    scopus 로고
    • Molecular variability analysis of the RNA 3 of fifteen isolates of Prunus necrotic ringspot virus sheds light on the minimal requirements for the synthesis of the subgenomic RNA
    • Aparicio F, Pallás V, (2002) Molecular variability analysis of the RNA 3 of fifteen isolates of Prunus necrotic ringspot virus sheds light on the minimal requirements for the synthesis of the subgenomic RNA. Virus Genes 25: 75-84.
    • (2002) Virus Genes , vol.25 , pp. 75-84
    • Aparicio, F.1    Pallás, V.2
  • 31
    • 1642344605 scopus 로고    scopus 로고
    • RNA-binding properties and mapping of RNA-binding domain from the movement protein of Prunus necrotic ringspot virus
    • Herranz MC, Pallas V, (2004) RNA-binding properties and mapping of RNA-binding domain from the movement protein of Prunus necrotic ringspot virus. J Gen Virol 85: 761-768.
    • (2004) J Gen Virol , vol.85 , pp. 761-768
    • Herranz, M.C.1    Pallas, V.2
  • 32
    • 42449118804 scopus 로고    scopus 로고
    • Genetic diversity of the movement and coat protein genes of South American isolates of Prunus necrotic ringspot virus
    • Fiore N, Fajardo TVM, Prodan S, Herranz MC, Aparicio F, et al. (2008) Genetic diversity of the movement and coat protein genes of South American isolates of Prunus necrotic ringspot virus. Arch Virol 153: 909-919.
    • (2008) Arch Virol , vol.153 , pp. 909-919
    • Fiore, N.1    Fajardo, T.V.M.2    Prodan, S.3    Herranz, M.C.4    Aparicio, F.5
  • 33
    • 23244439546 scopus 로고    scopus 로고
    • Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement
    • Herranz MC, Sanchez-Navarro JA, Sauri A, Mingarro I, Pallas V, (2005) Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement. Virology 339: 31-41.
    • (2005) Virology , vol.339 , pp. 31-41
    • Herranz, M.C.1    Sanchez-Navarro, J.A.2    Sauri, A.3    Mingarro, I.4    Pallas, V.5
  • 34
    • 66149100998 scopus 로고    scopus 로고
    • Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein
    • Martínez-Gil L, Sánchez-Navarro JA, Cruz A, Pallás V, Pérez-Gil J, et al. (2009) Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein. J Virol 83: 5535-5543.
    • (2009) J Virol , vol.83 , pp. 5535-5543
    • Martínez-Gil, L.1    Sánchez-Navarro, J.A.2    Cruz, A.3    Pallás, V.4    Pérez-Gil, J.5
  • 35
    • 33745379832 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae: A useful model host to study fundamental biology of viral replication
    • Alves-Rodrigues I, Galao RP, Meyerhans A, Díez J, (2006) Saccharomyces cerevisiae: A useful model host to study fundamental biology of viral replication. Virus Research 120: 49-56.
    • (2006) Virus Research , vol.120 , pp. 49-56
    • Alves-Rodrigues, I.1    Galao, R.P.2    Meyerhans, A.3    Díez, J.4
  • 36
    • 51849139963 scopus 로고    scopus 로고
    • Yeast as a Model Host to Explore Plant Virus-Host Interactions
    • Nagy PD, (2008) Yeast as a Model Host to Explore Plant Virus-Host Interactions. Annu Rev Phytopathol 46: 217-42.
    • (2008) Annu Rev Phytopathol , vol.46 , pp. 217-242
    • Nagy, P.D.1
  • 37
    • 32944474055 scopus 로고    scopus 로고
    • Heterologous expression of membrane and soluble proteins derepresses GCN4 mRNA translation in the yeast Saccharomyces cerevisiae
    • Steffensen L, Pedersen PA, (2006) Heterologous expression of membrane and soluble proteins derepresses GCN4 mRNA translation in the yeast Saccharomyces cerevisiae. Eukaryot Cell 5: 248-61.
    • (2006) Eukaryot Cell , vol.5 , pp. 248-261
    • Steffensen, L.1    Pedersen, P.A.2
  • 38
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signaling and the control of translation
    • Dufner A, Thomas, G, (1999) Ribosomal S6 kinase signaling and the control of translation. Exp Cell Res 253: 100-109.
    • (1999) Exp Cell Res , vol.253 , pp. 100-109
    • Dufner, A.1    Thomas, G.2
  • 40
    • 0035021735 scopus 로고    scopus 로고
    • The RNA 5 of Prunus necrotic ringspot virus is a biologically inactive copy of the 3′-UTR of the genomic RNA 3
    • Di Terlizzi B, Skrzeczkowski LJ, Mink GI, Scott SW, Zimmerman MT, (2001) The RNA 5 of Prunus necrotic ringspot virus is a biologically inactive copy of the 3′-UTR of the genomic RNA 3. Arch Virol 146: 825-833.
    • (2001) Arch Virol , vol.146 , pp. 825-833
    • Di Terlizzi, B.1    Skrzeczkowski, L.J.2    Mink, G.I.3    Scott, S.W.4    Zimmerman, M.T.5
  • 41
    • 79953791690 scopus 로고    scopus 로고
    • Viral factor TAV recruits TOR/S6K1 signalling to activate reinitiation after long ORF translation
    • Schepetilnikov M, Kobayashi K, Geldreich A, Caranta C, Robaglia C, et al. (2011) Viral factor TAV recruits TOR/S6K1 signalling to activate reinitiation after long ORF translation. EMBO J 30: 1343-56.
    • (2011) EMBO J , vol.30 , pp. 1343-1356
    • Schepetilnikov, M.1    Kobayashi, K.2    Geldreich, A.3    Caranta, C.4    Robaglia, C.5
  • 42
    • 77952755857 scopus 로고    scopus 로고
    • Integration of general amino acid control and target of rapamycin (TOR) regulatory pathways in nitrogen assimilation in yeast
    • Staschke KA, Dey S, Zaborske JM, Palam LR, McClintick JN, et al. (2010) Integration of general amino acid control and target of rapamycin (TOR) regulatory pathways in nitrogen assimilation in yeast. J Biol Chem 285: 16893-911.
    • (2010) J Biol Chem , vol.285 , pp. 16893-16911
    • Staschke, K.A.1    Dey, S.2    Zaborske, J.M.3    Palam, L.R.4    McClintick, J.N.5
  • 45
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman RJ, (1999) Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev 13: 1211-1233.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 46
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • Harding HP, Calfon M, Urano F, Novoa I, Ron D, (2002) Transcriptional and translational control in the Mammalian unfolded protein response. Annu Rev Cell Dev Biol 18: 575-599.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 47
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher VG, Tibshirani R, Chu G, (2001) Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci U S A 98: 5116-5121.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3


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