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Volumn 5, Issue APR, 2015, Pages

The eEF1A proteins: At the crossroads of oncogenesis, apoptosis, and viral infections

Author keywords

Apoptosis; Cancer; eEF1A; HIV; Virus

Indexed keywords

ACTIN; CHAPERONE; INITIATION FACTOR 1A; PHOSPHOLIPID; PROTEIN KINASE B; RESVERATROL;

EID: 84934277859     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2015.00075     Document Type: Review
Times cited : (161)

References (112)
  • 1
    • 0141594606 scopus 로고    scopus 로고
    • Not just for housekeeping: protein initiation and elongation factors in cell growth and tumorigenesis
    • Thornton S, Anand N, Purcell D, Lee J. Not just for housekeeping: protein initiation and elongation factors in cell growth and tumorigenesis. J Mol Med (Berl) (2003) 81(9):536-48. doi:10.1007/s00109-003-0461-8
    • (2003) J Mol Med (Berl) , vol.81 , Issue.9 , pp. 536-548
    • Thornton, S.1    Anand, N.2    Purcell, D.3    Lee, J.4
  • 2
    • 79960630264 scopus 로고    scopus 로고
    • Central dogma at the single-molecule level in living cells
    • Li GW, Xie XS. Central dogma at the single-molecule level in living cells. Nature (2011) 475(7356):308-15. doi:10.1038/nature10315
    • (2011) Nature , vol.475 , Issue.7356 , pp. 308-315
    • Li, G.W.1    Xie, X.S.2
  • 3
    • 78650957050 scopus 로고    scopus 로고
    • Protein-protein interactions and cancer: targeting the central dogma
    • Garner AL, Janda KD. Protein-protein interactions and cancer: targeting the central dogma. Curr Top Med Chem (2011) 11(3):258-80. doi:10.2174/156802611794072614
    • (2011) Curr Top Med Chem , vol.11 , Issue.3 , pp. 258-280
    • Garner, A.L.1    Janda, K.D.2
  • 4
    • 0001618425 scopus 로고    scopus 로고
    • Modulation of molecular mechanisms involved in protein synthesis machinery as a new tool for the control of cell proliferation
    • Caraglia M, Budillon A, Vitale G, Lupoli G, Tagliaferri P, Abbruzzese A. Modulation of molecular mechanisms involved in protein synthesis machinery as a new tool for the control of cell proliferation. Eur J Biochem (2000) 267(13):3919-36. doi:10.1046/j.1432-1327.2000.01465.x
    • (2000) Eur J Biochem , vol.267 , Issue.13 , pp. 3919-3936
    • Caraglia, M.1    Budillon, A.2    Vitale, G.3    Lupoli, G.4    Tagliaferri, P.5    Abbruzzese, A.6
  • 5
    • 2342641580 scopus 로고    scopus 로고
    • Targets and mechanisms for the regulation of translation in malignant transformation
    • Clemens MJ. Targets and mechanisms for the regulation of translation in malignant transformation. Oncogene (2004) 23(18):3180-8. doi:10.1038/sj.onc.1207544
    • (2004) Oncogene , vol.23 , Issue.18 , pp. 3180-3188
    • Clemens, M.J.1
  • 6
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne GJ, Proud CG. Regulation of peptide-chain elongation in mammalian cells. Eur J Biochem (2002) 269(22):5360-8. doi:10.1046/j.1432-1033.2002.03290.x
    • (2002) Eur J Biochem , vol.269 , Issue.22 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 7
    • 68149126140 scopus 로고    scopus 로고
    • Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation
    • Soares DC, Barlow PN, Newbery HJ, Porteous DJ, Abbott CM. Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation. PLoS One (2009) 4(7):e6315. doi:10.1371/journal.pone.0006315
    • (2009) PLoS One , vol.4 , Issue.7
    • Soares, D.C.1    Barlow, P.N.2    Newbery, H.J.3    Porteous, D.J.4    Abbott, C.M.5
  • 8
    • 84929119370 scopus 로고    scopus 로고
    • Molecular docking uncovers TSPY binds more efficiently with eEF1A2 compared to eEF1A1
    • Panwar D, Rawal L, Ali S. Molecular docking uncovers TSPY binds more efficiently with eEF1A2 compared to eEF1A1. J Biomol Struct Dyn (2014) 9:1-12. doi:10.1080/07391102.2014.952664
    • (2014) J Biomol Struct Dyn , vol.9 , pp. 1-12
    • Panwar, D.1    Rawal, L.2    Ali, S.3
  • 10
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res (2003) 31(13):3381-5. doi:10.1093/nar/gkg520
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 11
    • 0027292202 scopus 로고
    • Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha
    • Knudsen SM, Frydenberg J, Clark BF, Leffers H. Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha. Eur J Biochem (1993) 215(3):549-54. doi:10.1111/j.1432-1033.1993.tb18064.x
    • (1993) Eur J Biochem , vol.215 , Issue.3 , pp. 549-554
    • Knudsen, S.M.1    Frydenberg, J.2    Clark, B.F.3    Leffers, H.4
  • 12
    • 84864439415 scopus 로고    scopus 로고
    • The many roles of the eukaryotic elongation factor 1 complex
    • Sasikumar AN, Perez WB, Kinzy TG. The many roles of the eukaryotic elongation factor 1 complex. Wiley Interdiscip Rev RNA. (2012) 3(4):543-55. doi:10.1002/wrna.1118
    • (2012) Wiley Interdiscip Rev RNA , vol.3 , Issue.4 , pp. 543-555
    • Sasikumar, A.N.1    Perez, W.B.2    Kinzy, T.G.3
  • 13
    • 84889656023 scopus 로고    scopus 로고
    • In vivo characterization of the role of tissue-specific translation elongation factor 1A2 in protein synthesis reveals insights into muscle atrophy
    • Doig J, Griffiths LA, Peberdy D, Dharmasaroja P, Vera M, Davies FJ, et al. In vivo characterization of the role of tissue-specific translation elongation factor 1A2 in protein synthesis reveals insights into muscle atrophy. FEBS J (2013) 280(24):6528-40. doi:10.1111/febs.12554
    • (2013) FEBS J , vol.280 , Issue.24 , pp. 6528-6540
    • Doig, J.1    Griffiths, L.A.2    Peberdy, D.3    Dharmasaroja, P.4    Vera, M.5    Davies, F.J.6
  • 14
    • 0032522219 scopus 로고    scopus 로고
    • The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein
    • Kahns S, Lund A, Kristensen P, Knudsen CR, Clark BF, Cavallius J, et al. The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein. Nucleic Acids Res (1998) 26(8):1884-90. doi:10.1093/nar/26.8.1884
    • (1998) Nucleic Acids Res , vol.26 , Issue.8 , pp. 1884-1890
    • Kahns, S.1    Lund, A.2    Kristensen, P.3    Knudsen, C.R.4    Clark, B.F.5    Cavallius, J.6
  • 15
    • 0030249704 scopus 로고    scopus 로고
    • Assignment of human elongation factor 1alpha genes: eEF1A maps to chromosome 6q14 and eEF1A2 to 20q13 3
    • Lund A, Knudsen SM, Vissing H, Clark B, Tommerup N. Assignment of human elongation factor 1alpha genes: eEF1A maps to chromosome 6q14 and eEF1A2 to 20q13.3. Genomics (1996) 36(2):359-61. doi:10.1006/geno.1996.0475
    • (1996) Genomics , vol.36 , Issue.2 , pp. 359-361
    • Lund, A.1    Knudsen, S.M.2    Vissing, H.3    Clark, B.4    Tommerup, N.5
  • 16
    • 84887387519 scopus 로고    scopus 로고
    • Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translational modification with significant enrichment around localised sites of sequence variation
    • Soares DC, Abbott CM. Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translational modification with significant enrichment around localised sites of sequence variation. Biol Direct (2013) 8:29. doi:10.1186/1745-6150-8-29
    • (2013) Biol Direct , vol.8 , pp. 29
    • Soares, D.C.1    Abbott, C.M.2
  • 17
    • 84859361244 scopus 로고    scopus 로고
    • Raf kinases mediate the phosphorylation of eukaryotic translation elongation factor 1A and regulate its stability in eukaryotic cells
    • Sanges C, Scheuermann C, Zahedi RP, Sickmann A, Lamberti A, Migliaccio N, et al. Raf kinases mediate the phosphorylation of eukaryotic translation elongation factor 1A and regulate its stability in eukaryotic cells. Cell Death Dis (2012) 3:e276. doi:10.1038/cddis.2012.16
    • (2012) Cell Death Dis , vol.3
    • Sanges, C.1    Scheuermann, C.2    Zahedi, R.P.3    Sickmann, A.4    Lamberti, A.5    Migliaccio, N.6
  • 18
    • 59449087670 scopus 로고    scopus 로고
    • eEF1A is a novel component of the mammalian nuclear protein export machinery
    • Khacho M, Mekhail K, Pilon-Larose K, Pause A, Cote J, Lee S. eEF1A is a novel component of the mammalian nuclear protein export machinery. Mol Biol Cell (2008) 19(12):5296-308. doi:10.1091/mbc.E08-06-0562
    • (2008) Mol Biol Cell , vol.19 , Issue.12 , pp. 5296-5308
    • Khacho, M.1    Mekhail, K.2    Pilon-Larose, K.3    Pause, A.4    Cote, J.5    Lee, S.6
  • 19
    • 0034662783 scopus 로고    scopus 로고
    • The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity
    • Bischoff C, Kahns S, Lund A, Jorgensen HF, Praestegaard M, Clark BF, et al. The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity. Genomics (2000) 68(1):63-70. doi:10.1006/geno.2000.6271
    • (2000) Genomics , vol.68 , Issue.1 , pp. 63-70
    • Bischoff, C.1    Kahns, S.2    Lund, A.3    Jorgensen, H.F.4    Praestegaard, M.5    Clark, B.F.6
  • 20
    • 4143091385 scopus 로고    scopus 로고
    • The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: review article
    • Lamberti A, Caraglia M, Longo O, Marra M, Abbruzzese A, Arcari P. The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: review article. Amino Acids (2004) 26(4):443-8. doi:10.1007/s00726-004-0088-2
    • (2004) Amino Acids , vol.26 , Issue.4 , pp. 443-448
    • Lamberti, A.1    Caraglia, M.2    Longo, O.3    Marra, M.4    Abbruzzese, A.5    Arcari, P.6
  • 21
    • 84880667395 scopus 로고    scopus 로고
    • Degradation of newly synthesized polypeptides by ribosome-associated RACK1/c-Jun N-terminal kinase/eukaryotic elongation factor 1A2 complex
    • Gandin V, Gutierrez GJ, Brill LM, Varsano T, Feng Y, Aza-Blanc P, et al. Degradation of newly synthesized polypeptides by ribosome-associated RACK1/c-Jun N-terminal kinase/eukaryotic elongation factor 1A2 complex. Mol Cell Biol (2013) 33(13):2510-26. doi:10.1128/MCB.01362-12
    • (2013) Mol Cell Biol , vol.33 , Issue.13 , pp. 2510-2526
    • Gandin, V.1    Gutierrez, G.J.2    Brill, L.M.3    Varsano, T.4    Feng, Y.5    Aza-Blanc, P.6
  • 22
    • 84879800606 scopus 로고    scopus 로고
    • Exome sequencing reveals new causal mutations in children with epileptic encephalopathies
    • Veeramah KR, Johnstone L, Karafet TM, Wolf D, Sprissler R, Salogiannis J, et al. Exome sequencing reveals new causal mutations in children with epileptic encephalopathies. Epilepsia (2013) 54(7):1270-81. doi:10.1111/epi.12201
    • (2013) Epilepsia , vol.54 , Issue.7 , pp. 1270-1281
    • Veeramah, K.R.1    Johnstone, L.2    Karafet, T.M.3    Wolf, D.4    Sprissler, R.5    Salogiannis, J.6
  • 23
    • 77952494292 scopus 로고    scopus 로고
    • The utrophin A 5'-UTR drives cap-independent translation exclusively in skeletal muscles of transgenic mice and interacts with eEF1A2
    • Miura P, Coriati A, Belanger G, De RY, Lee J, Kothary R, et al. The utrophin A 5'-UTR drives cap-independent translation exclusively in skeletal muscles of transgenic mice and interacts with eEF1A2. Hum Mol Genet (2010) 19(7):1211-20. doi:10.1093/hmg/ddp591
    • (2010) Hum Mol Genet , vol.19 , Issue.7 , pp. 1211-1220
    • Miura, P.1    Coriati, A.2    Belanger, G.3    De, R.Y.4    Lee, J.5    Kothary, R.6
  • 24
    • 33947576553 scopus 로고    scopus 로고
    • Shaping the future of biomarker research in breast cancer to ensure clinical relevance
    • Hinestrosa MC, Dickersin K, Klein P, Mayer M, Noss K, Slamon D, et al. Shaping the future of biomarker research in breast cancer to ensure clinical relevance. Nat Rev Cancer (2007) 7(4):309-15. doi:10.1038/nrc2144
    • (2007) Nat Rev Cancer , vol.7 , Issue.4 , pp. 309-315
    • Hinestrosa, M.C.1    Dickersin, K.2    Klein, P.3    Mayer, M.4    Noss, K.5    Slamon, D.6
  • 25
    • 26844440904 scopus 로고    scopus 로고
    • Translation elongation factor eEF1A2 is a potential oncoprotein that is overexpressed in two-thirds of breast tumours
    • Tomlinson VA, Newbery HJ, Wray NR, Jackson J, Larionov A, Miller WR, et al. Translation elongation factor eEF1A2 is a potential oncoprotein that is overexpressed in two-thirds of breast tumours. BMC Cancer (2005) 5:113. doi:10.1186/1471-2407-5-113
    • (2005) BMC Cancer , vol.5 , pp. 113
    • Tomlinson, V.A.1    Newbery, H.J.2    Wray, N.R.3    Jackson, J.4    Larionov, A.5    Miller, W.R.6
  • 26
    • 79960182468 scopus 로고    scopus 로고
    • Novel flavonoids with antiproliferative activities against breast cancer cells
    • Yao N, Chen CY, Wu CY, Motonishi K, Kung HJ, Lam KS. Novel flavonoids with antiproliferative activities against breast cancer cells. J Med Chem (2011) 54(13):4339-49. doi:10.1021/jm101440r
    • (2011) J Med Chem , vol.54 , Issue.13 , pp. 4339-4349
    • Yao, N.1    Chen, C.Y.2    Wu, C.Y.3    Motonishi, K.4    Kung, H.J.5    Lam, K.S.6
  • 27
    • 34248340402 scopus 로고    scopus 로고
    • eEF1A2 activates Akt and stimulates Akt-dependent actin remodeling, invasion and migration
    • Amiri A, Noei F, Jeganathan S, Kulkarni G, Pinke DE, Lee JM. eEF1A2 activates Akt and stimulates Akt-dependent actin remodeling, invasion and migration. Oncogene (2007) 26(21):3027-40. doi:10.1038/sj.onc.1210101
    • (2007) Oncogene , vol.26 , Issue.21 , pp. 3027-3040
    • Amiri, A.1    Noei, F.2    Jeganathan, S.3    Kulkarni, G.4    Pinke, D.E.5    Lee, J.M.6
  • 28
    • 68949217138 scopus 로고    scopus 로고
    • Elongation factor 1 alpha interacts with phospho-Akt in breast cancer cells and regulates their proliferation, survival and motility
    • Pecorari L, Marin O, Silvestri C, Candini O, Rossi E, Guerzoni C, et al. Elongation factor 1 alpha interacts with phospho-Akt in breast cancer cells and regulates their proliferation, survival and motility. Mol Cancer (2009) 8:58. doi:10.1186/1476-4598-8-58
    • (2009) Mol Cancer , vol.8 , pp. 58
    • Pecorari, L.1    Marin, O.2    Silvestri, C.3    Candini, O.4    Rossi, E.5    Guerzoni, C.6
  • 29
    • 77956292558 scopus 로고    scopus 로고
    • eEF1A2 promotes cell growth, inhibits apoptosis and activates JAK/STAT and AKT signaling in mouse plasmacytomas
    • Li Z, Qi CF, Shin DM, Zingone A, Newbery HJ, Kovalchuk AL, et al. eEF1A2 promotes cell growth, inhibits apoptosis and activates JAK/STAT and AKT signaling in mouse plasmacytomas. PLoS One (2010) 5(5):e10755. doi:10.1371/journal.pone.0010755
    • (2010) PLoS One , vol.5 , Issue.5
    • Li, Z.1    Qi, C.F.2    Shin, D.M.3    Zingone, A.4    Newbery, H.J.5    Kovalchuk, A.L.6
  • 31
    • 77951568703 scopus 로고    scopus 로고
    • Phosphoinositide signalling in cancer: beyond PI3K and PTEN
    • Bunney TD, Katan M. Phosphoinositide signalling in cancer: beyond PI3K and PTEN. Nat Rev Cancer (2010) 10(5):342-52. doi:10.1038/nrc2842
    • (2010) Nat Rev Cancer , vol.10 , Issue.5 , pp. 342-352
    • Bunney, T.D.1    Katan, M.2
  • 32
    • 33745933535 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinases: old enzymes with emerging functions
    • Balla A, Balla T. Phosphatidylinositol 4-kinases: old enzymes with emerging functions. Trends Cell Biol (2006) 16(7):351-61. doi:10.1016/j.tcb.2006.05.003
    • (2006) Trends Cell Biol , vol.16 , Issue.7 , pp. 351-361
    • Balla, A.1    Balla, T.2
  • 33
    • 0029986938 scopus 로고    scopus 로고
    • Phosphoinositide kinases
    • Carpenter CL, Cantley LC. Phosphoinositide kinases. Curr Opin Cell Biol (1996) 8(2):153-8. doi:10.1016/S0955-0674(96)80060-3
    • (1996) Curr Opin Cell Biol , vol.8 , Issue.2 , pp. 153-158
    • Carpenter, C.L.1    Cantley, L.C.2
  • 34
    • 33847003355 scopus 로고    scopus 로고
    • Binding of elongation factor eEF1A2 to phosphatidylinositol 4-kinase beta stimulates lipid kinase activity and phosphatidylinositol 4-phosphate generation
    • Jeganathan S, Lee JM. Binding of elongation factor eEF1A2 to phosphatidylinositol 4-kinase beta stimulates lipid kinase activity and phosphatidylinositol 4-phosphate generation. J Biol Chem (2007) 282(1):372-80. doi:10.1074/jbc.M602955200
    • (2007) J Biol Chem , vol.282 , Issue.1 , pp. 372-380
    • Jeganathan, S.1    Lee, J.M.2
  • 35
    • 80052632423 scopus 로고    scopus 로고
    • The lipid kinase PI4KIIIbeta and the eEF1A2 oncogene co-operate to disrupt three-dimensional in vitro acinar morphogenesis
    • Pinke DE, Lee JM. The lipid kinase PI4KIIIbeta and the eEF1A2 oncogene co-operate to disrupt three-dimensional in vitro acinar morphogenesis. Exp Cell Res (2011) 317(17):2503-11. doi:10.1016/j.yexcr.2011.08.002
    • (2011) Exp Cell Res , vol.317 , Issue.17 , pp. 2503-2511
    • Pinke, D.E.1    Lee, J.M.2
  • 36
    • 47049120759 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 1A2 cooperates with phosphatidylinositol-4 kinase III beta to stimulate production of filopodia through increased phosphatidylinositol-4 5 bisphosphate generation
    • Jeganathan S, Morrow A, Amiri A, Lee JM. Eukaryotic elongation factor 1A2 cooperates with phosphatidylinositol-4 kinase III beta to stimulate production of filopodia through increased phosphatidylinositol-4,5 bisphosphate generation. Mol Cell Biol (2008) 28(14):4549-61. doi:10.1128/MCB.00150-08
    • (2008) Mol Cell Biol , vol.28 , Issue.14 , pp. 4549-4561
    • Jeganathan, S.1    Morrow, A.2    Amiri, A.3    Lee, J.M.4
  • 37
    • 84936411450 scopus 로고    scopus 로고
    • Proto-oncogenic isoform A2 of eukaryotic translation elongation factor eEF1 is a target of miR-663 and miR-744
    • Vislovukh A, Kratassiouk G, Porto E, Gralievska N, Beldiman C, Pinna G, et al. Proto-oncogenic isoform A2 of eukaryotic translation elongation factor eEF1 is a target of miR-663 and miR-744. Br J Cancer (2013) 108(11):2304-11. doi:10.1038/bjc.2013.243
    • (2013) Br J Cancer , vol.108 , Issue.11 , pp. 2304-2311
    • Vislovukh, A.1    Kratassiouk, G.2    Porto, E.3    Gralievska, N.4    Beldiman, C.5    Pinna, G.6
  • 38
    • 84877972047 scopus 로고    scopus 로고
    • Tumor suppressor p16(INK4a) inhibits cancer cell growth by downregulating eEF1A2 through a direct interaction
    • Lee MH, Choi BY, Cho YY, Lee SY, Huang Z, Kundu JK, et al. Tumor suppressor p16(INK4a) inhibits cancer cell growth by downregulating eEF1A2 through a direct interaction. J Cell Sci (2013) 126(Pt 8):1744-52. doi:10.1242/jcs.113613
    • (2013) J Cell Sci , vol.126 , pp. 1744-1752
    • Lee, M.H.1    Choi, B.Y.2    Cho, Y.Y.3    Lee, S.Y.4    Huang, Z.5    Kundu, J.K.6
  • 39
  • 40
    • 0036635310 scopus 로고    scopus 로고
    • Protein elongation factor eEF1A2 is a putative oncogene in ovarian cancer
    • Anand N, Murthy S, Amann G, Wernick M, Porter LA, Cukier IH, et al. Protein elongation factor eEF1A2 is a putative oncogene in ovarian cancer. Nat Genet (2002) 31(3):301-5. doi:10.1038/ng904
    • (2002) Nat Genet , vol.31 , Issue.3 , pp. 301-305
    • Anand, N.1    Murthy, S.2    Amann, G.3    Wernick, M.4    Porter, L.A.5    Cukier, I.H.6
  • 41
    • 33845651679 scopus 로고    scopus 로고
    • High resolution analysis of genomic aberrations by metaphase and array comparative genomic hybridization identifies candidate tumour genes in lung cancer cell lines
    • Zhu H, Lam DC, Han KC, Tin VP, Suen WS, Wang E, et al. High resolution analysis of genomic aberrations by metaphase and array comparative genomic hybridization identifies candidate tumour genes in lung cancer cell lines. Cancer Lett (2007) 245(1-2):303-14. doi:10.1016/j.canlet.2006.01.020
    • (2007) Cancer Lett , vol.245 , Issue.1-2 , pp. 303-314
    • Zhu, H.1    Lam, D.C.2    Han, K.C.3    Tin, V.P.4    Suen, W.S.5    Wang, E.6
  • 42
    • 33646368154 scopus 로고    scopus 로고
    • Identification of putative oncogenes in lung adenocarcinoma by a comprehensive functional genomic approach
    • Li R, Wang H, Bekele BN, Yin Z, Caraway NP, Katz RL, et al. Identification of putative oncogenes in lung adenocarcinoma by a comprehensive functional genomic approach. Oncogene (2006) 25(18):2628-35. doi:10.1038/sj.onc.1209289
    • (2006) Oncogene , vol.25 , Issue.18 , pp. 2628-2635
    • Li, R.1    Wang, H.2    Bekele, B.N.3    Yin, Z.4    Caraway, N.P.5    Katz, R.L.6
  • 43
    • 36248947214 scopus 로고    scopus 로고
    • The expression levels of the translational factors eEF1A 1/2 correlate with cell growth but not apoptosis in hepatocellular carcinoma cell lines with different differentiation grade
    • Grassi G, Scaggiante B, Farra R, Dapas B, Agostini F, Baiz D, et al. The expression levels of the translational factors eEF1A 1/2 correlate with cell growth but not apoptosis in hepatocellular carcinoma cell lines with different differentiation grade. Biochimie (2007) 89(12):1544-52. doi:10.1016/j.biochi.2007.07.007
    • (2007) Biochimie , vol.89 , Issue.12 , pp. 1544-1552
    • Grassi, G.1    Scaggiante, B.2    Farra, R.3    Dapas, B.4    Agostini, F.5    Baiz, D.6
  • 44
    • 39549099942 scopus 로고    scopus 로고
    • Etiology-dependent molecular mechanisms in human hepatocarcinogenesis
    • Schlaeger C, Longerich T, Schiller C, Bewerunge P, Mehrabi A, Toedt G, et al. Etiology-dependent molecular mechanisms in human hepatocarcinogenesis. Hepatology (2008) 47(2):511-20. doi:10.1002/hep.22033
    • (2008) Hepatology , vol.47 , Issue.2 , pp. 511-520
    • Schlaeger, C.1    Longerich, T.2    Schiller, C.3    Bewerunge, P.4    Mehrabi, A.5    Toedt, G.6
  • 45
    • 0029563611 scopus 로고
    • Amplification of chromosomal region 20q13 in invasive breast cancer: prognostic implications
    • Tanner MM, Tirkkonen M, Kallioniemi A, Holli K, Collins C, Kowbel D, et al. Amplification of chromosomal region 20q13 in invasive breast cancer: prognostic implications. Clin Cancer Res (1995) 1(12):1455-61.
    • (1995) Clin Cancer Res , vol.1 , Issue.12 , pp. 1455-1461
    • Tanner, M.M.1    Tirkkonen, M.2    Kallioniemi, A.3    Holli, K.4    Collins, C.5    Kowbel, D.6
  • 46
    • 0029911314 scopus 로고    scopus 로고
    • Elongation factor-1 alpha is an overexpressed actin binding protein in metastatic rat mammary adenocarcinoma
    • Edmonds BT, Wyckoff J, Yeung YG, Wang Y, Stanley ER, Jones J, et al. Elongation factor-1 alpha is an overexpressed actin binding protein in metastatic rat mammary adenocarcinoma. J Cell Sci (1996) 109(Pt 11):2705-14.
    • (1996) J Cell Sci , vol.109 , pp. 2705-2714
    • Edmonds, B.T.1    Wyckoff, J.2    Yeung, Y.G.3    Wang, Y.4    Stanley, E.R.5    Jones, J.6
  • 47
    • 3142670417 scopus 로고    scopus 로고
    • Expression profile of eukaryotic translation factors in human cancer tissues and cell lines
    • Joseph P, O'Kernick CM, Othumpangat S, Lei YX, Yuan BZ, Ong TM. Expression profile of eukaryotic translation factors in human cancer tissues and cell lines. Mol Carcinog (2004) 40(3):171-9. doi:10.1002/mc.20033
    • (2004) Mol Carcinog , vol.40 , Issue.3 , pp. 171-179
    • Joseph, P.1    O'Kernick, C.M.2    Othumpangat, S.3    Lei, Y.X.4    Yuan, B.Z.5    Ong, T.M.6
  • 48
    • 84904689591 scopus 로고    scopus 로고
    • Up-regulation of eEF1A2 promotes proliferation and inhibits apoptosis in prostate cancer
    • Sun Y, Du C, Wang B, Zhang Y, Liu X, Ren G. Up-regulation of eEF1A2 promotes proliferation and inhibits apoptosis in prostate cancer. Biochem Biophys Res Commun (2014) 450(1):1-6. doi:10.1016/j.bbrc.2014.05.045
    • (2014) Biochem Biophys Res Commun , vol.450 , Issue.1 , pp. 1-6
    • Sun, Y.1    Du, C.2    Wang, B.3    Zhang, Y.4    Liu, X.5    Ren, G.6
  • 49
    • 84857068469 scopus 로고    scopus 로고
    • iTRAQ identification of candidate serum biomarkers associated with metastatic progression of human prostate cancer
    • Rehman I, Evans CA, Glen A, Cross SS, Eaton CL, Down J, et al. iTRAQ identification of candidate serum biomarkers associated with metastatic progression of human prostate cancer. PLoS One (2012) 7(2):e30885. doi:10.1371/journal.pone.0030885
    • (2012) PLoS One , vol.7 , Issue.2
    • Rehman, I.1    Evans, C.A.2    Glen, A.3    Cross, S.S.4    Eaton, C.L.5    Down, J.6
  • 50
    • 0026700016 scopus 로고
    • Elongation factor-1 alpha gene determines susceptibility to transformation
    • Tatsuka M, Mitsui H, Wada M, Nagata A, Nojima H, Okayama H. Elongation factor-1 alpha gene determines susceptibility to transformation. Nature (1992) 359(6393):333-6. doi:10.1038/359333a0
    • (1992) Nature , vol.359 , Issue.6393 , pp. 333-336
    • Tatsuka, M.1    Mitsui, H.2    Wada, M.3    Nagata, A.4    Nojima, H.5    Okayama, H.6
  • 51
    • 0043240182 scopus 로고    scopus 로고
    • Ovarian cancer: strategies for overcoming resistance to chemotherapy
    • Agarwal R, Kaye SB. Ovarian cancer: strategies for overcoming resistance to chemotherapy. Nat Rev Cancer (2003) 3(7):502-16. doi:10.1038/nrc1123
    • (2003) Nat Rev Cancer , vol.3 , Issue.7 , pp. 502-516
    • Agarwal, R.1    Kaye, S.B.2
  • 52
    • 18344380440 scopus 로고    scopus 로고
    • Ovarian cancer metastasis: integrating insights from disparate model organisms
    • Naora H, Montell DJ. Ovarian cancer metastasis: integrating insights from disparate model organisms. Nat Rev Cancer (2005) 5(5):355-66. doi:10.1038/nrc1611
    • (2005) Nat Rev Cancer , vol.5 , Issue.5 , pp. 355-366
    • Naora, H.1    Montell, D.J.2
  • 53
    • 70349847555 scopus 로고    scopus 로고
    • Ovarian cancer
    • Hennessy BT, Coleman RL, Markman M. Ovarian cancer. Lancet (2009) 374(9698):1371-82. doi:10.1016/S0140-6736(09)61338-6
    • (2009) Lancet , vol.374 , Issue.9698 , pp. 1371-1382
    • Hennessy, B.T.1    Coleman, R.L.2    Markman, M.3
  • 54
    • 84856802424 scopus 로고    scopus 로고
    • Therapeutic strategies in epithelial ovarian cancer
    • Kim A, Ueda Y, Naka T, Enomoto T. Therapeutic strategies in epithelial ovarian cancer. J Exp Clin Cancer Res (2012) 31:14. doi:10.1186/1756-9966-31-14
    • (2012) J Exp Clin Cancer Res , vol.31 , pp. 14
    • Kim, A.1    Ueda, Y.2    Naka, T.3    Enomoto, T.4
  • 55
    • 34248570992 scopus 로고    scopus 로고
    • Expression of eEF1A2 is associated with clear cell histology in ovarian carcinomas: overexpression of the gene is not dependent on modifications at the eEF1A2 locus
    • Tomlinson VA, Newbery HJ, Bergmann JH, Boyd J, Scott D, Wray NR, et al. Expression of eEF1A2 is associated with clear cell histology in ovarian carcinomas: overexpression of the gene is not dependent on modifications at the eEF1A2 locus. Br J Cancer (2007) 96(10):1613-20. doi:10.1038/sj.bjc.6603748
    • (2007) Br J Cancer , vol.96 , Issue.10 , pp. 1613-1620
    • Tomlinson, V.A.1    Newbery, H.J.2    Bergmann, J.H.3    Boyd, J.4    Scott, D.5    Wray, N.R.6
  • 56
    • 39249084058 scopus 로고    scopus 로고
    • The prognostic significance of elongation factor eEF1A2 in ovarian cancer
    • Pinke DE, Kalloger SE, Francetic T, Huntsman DG, Lee JM. The prognostic significance of elongation factor eEF1A2 in ovarian cancer. Gynecol Oncol (2008) 108(3):561-8. doi:10.1016/j.ygyno.2007.11.019
    • (2008) Gynecol Oncol , vol.108 , Issue.3 , pp. 561-568
    • Pinke, D.E.1    Kalloger, S.E.2    Francetic, T.3    Huntsman, D.G.4    Lee, J.M.5
  • 57
    • 69149088653 scopus 로고    scopus 로고
    • eEF1A2 as a putative oncogene
    • Lee MH, Surh YJ. eEF1A2 as a putative oncogene. Ann N Y Acad Sci (2009) 1171:87-93. doi:10.1111/j.1749-6632.2009.04909.x
    • (2009) Ann N Y Acad Sci , vol.1171 , pp. 87-93
    • Lee, M.H.1    Surh, Y.J.2
  • 58
    • 51949093672 scopus 로고    scopus 로고
    • The eukaryotic translation elongation factor eEF1A2 induces neoplastic properties and mediates tumorigenic effects of ZNF217 in precursor cells of human ovarian carcinomas
    • Sun Y, Wong N, Guan Y, Salamanca CM, Cheng JC, Lee JM, et al. The eukaryotic translation elongation factor eEF1A2 induces neoplastic properties and mediates tumorigenic effects of ZNF217 in precursor cells of human ovarian carcinomas. Int J Cancer (2008) 123(8):1761-9. doi:10.1002/ijc.23708
    • (2008) Int J Cancer , vol.123 , Issue.8 , pp. 1761-1769
    • Sun, Y.1    Wong, N.2    Guan, Y.3    Salamanca, C.M.4    Cheng, J.C.5    Lee, J.M.6
  • 59
    • 51349132313 scopus 로고    scopus 로고
    • Cancer chemopreventive and therapeutic potential of resveratrol: mechanistic perspectives
    • Kundu JK, Surh YJ. Cancer chemopreventive and therapeutic potential of resveratrol: mechanistic perspectives. Cancer Lett (2008) 269(2):243-61. doi:10.1016/j.canlet.2008.03.057
    • (2008) Cancer Lett , vol.269 , Issue.2 , pp. 243-261
    • Kundu, J.K.1    Surh, Y.J.2
  • 60
    • 84893806758 scopus 로고    scopus 로고
    • Resveratrol, a sirtuin 1 activator, increases IL-6 production by peripheral blood mononuclear cells of patients with knee osteoarthritis
    • Wendling D, Abbas W, Godfrin-Valnet M, Guillot X, Khan KA, Cedoz JP, et al. Resveratrol, a sirtuin 1 activator, increases IL-6 production by peripheral blood mononuclear cells of patients with knee osteoarthritis. Clin Epigenetics (2013) 5(1):10. doi:10.1186/1868-7083-5-10
    • (2013) Clin Epigenetics , vol.5 , Issue.1 , pp. 10
    • Wendling, D.1    Abbas, W.2    Godfrin-Valnet, M.3    Guillot, X.4    Khan, K.A.5    Cedoz, J.P.6
  • 61
    • 70349736107 scopus 로고    scopus 로고
    • Resveratrol suppresses growth of human ovarian cancer cells in culture and in a murine xenograft model: eukaryotic elongation factor 1A2 as a potential target
    • Lee MH, Choi BY, Kundu JK, Shin YK, Na HK, Surh YJ. Resveratrol suppresses growth of human ovarian cancer cells in culture and in a murine xenograft model: eukaryotic elongation factor 1A2 as a potential target. Cancer Res (2009) 69(18):7449-58. doi:10.1158/0008-5472.CAN-09-1266
    • (2009) Cancer Res , vol.69 , Issue.18 , pp. 7449-7458
    • Lee, M.H.1    Choi, B.Y.2    Kundu, J.K.3    Shin, Y.K.4    Na, H.K.5    Surh, Y.J.6
  • 62
    • 77955635233 scopus 로고    scopus 로고
    • Cancer statistics 2010
    • Jemal A, Siegel R, Xu J, Ward E. Cancer statistics, 2010. CA Cancer J Clin (2010) 60(5):277-300. doi:10.3322/caac.20073
    • (2010) CA Cancer J Clin , vol.60 , Issue.5 , pp. 277-300
    • Jemal, A.1    Siegel, R.2    Xu, J.3    Ward, E.4
  • 63
    • 70349910584 scopus 로고    scopus 로고
    • Comparison of time trends in lung cancer mortality (1990-2006) in the world, from the WHO mortality database
    • Marugame T, Hirabayashi Y. Comparison of time trends in lung cancer mortality (1990-2006) in the world, from the WHO mortality database. Jpn J Clin Oncol (2009) 39(10):696-7. doi:10.1093/jjco/hyp138
    • (2009) Jpn J Clin Oncol , vol.39 , Issue.10 , pp. 696-697
    • Marugame, T.1    Hirabayashi, Y.2
  • 64
    • 34247850957 scopus 로고    scopus 로고
    • Establishment and expression profiling of new lung cancer cell lines from Chinese smokers and lifetime never-smokers
    • Lam DC, Girard L, Suen WS, Chung LP, Tin VP, Lam WK, et al. Establishment and expression profiling of new lung cancer cell lines from Chinese smokers and lifetime never-smokers. J Thorac Oncol (2006) 1(9):932-42. doi:10.1097/01243894-200611000-00003
    • (2006) J Thorac Oncol , vol.1 , Issue.9 , pp. 932-942
    • Lam, D.C.1    Girard, L.2    Suen, W.S.3    Chung, L.P.4    Tin, V.P.5    Lam, W.K.6
  • 65
    • 77950620399 scopus 로고    scopus 로고
    • Molecular pathology in early hepatocarcinogenesis
    • Effendi K, Sakamoto M. Molecular pathology in early hepatocarcinogenesis. Oncology (2010) 78(2):157-60. doi:10.1159/000312658
    • (2010) Oncology , vol.78 , Issue.2 , pp. 157-160
    • Effendi, K.1    Sakamoto, M.2
  • 66
    • 77951212202 scopus 로고    scopus 로고
    • CT and MRI of hepatocellular carcinoma: an update
    • Ayyappan AP, Jhaveri KS. CT and MRI of hepatocellular carcinoma: an update. Expert Rev Anticancer Ther (2010) 10(4):507-19. doi:10.1586/era.10.24
    • (2010) Expert Rev Anticancer Ther , vol.10 , Issue.4 , pp. 507-519
    • Ayyappan, A.P.1    Jhaveri, K.S.2
  • 67
    • 84899485564 scopus 로고    scopus 로고
    • eEF1A2 inactivates p53 by way of PI3K/AKT/mTOR-dependent stabilization of MDM4 in hepatocellular carcinoma
    • Pellegrino R, Calvisi DF, Neumann O, Kolluru V, Wesely J, Chen X, et al. eEF1A2 inactivates p53 by way of PI3K/AKT/mTOR-dependent stabilization of MDM4 in hepatocellular carcinoma. Hepatology (2014) 59(5):1886-99. doi:10.1002/hep.26954
    • (2014) Hepatology , vol.59 , Issue.5 , pp. 1886-1899
    • Pellegrino, R.1    Calvisi, D.F.2    Neumann, O.3    Kolluru, V.4    Wesely, J.5    Chen, X.6
  • 68
    • 33747830764 scopus 로고    scopus 로고
    • Hepatocellular carcinoma pathogenesis: from genes to environment
    • Farazi PA, DePinho RA. Hepatocellular carcinoma pathogenesis: from genes to environment. Nat Rev Cancer (2006) 6(9):674-87. doi:10.1038/nrc1934
    • (2006) Nat Rev Cancer , vol.6 , Issue.9 , pp. 674-687
    • Farazi, P.A.1    DePinho, R.A.2
  • 69
    • 1642588228 scopus 로고    scopus 로고
    • Pancreatic cancer
    • Li D, Xie K, Wolff R, Abbruzzese JL. Pancreatic cancer. Lancet (2004) 363(9414):1049-57. doi:10.1016/S0140-6736(04)15841-8
    • (2004) Lancet , vol.363 , Issue.9414 , pp. 1049-1057
    • Li, D.1    Xie, K.2    Wolff, R.3    Abbruzzese, J.L.4
  • 70
    • 33745117233 scopus 로고    scopus 로고
    • The epidemiology of pancreatic cancer in the United States: changes below the surface
    • Shaib YH, Davila JA, El-Serag HB. The epidemiology of pancreatic cancer in the United States: changes below the surface. Aliment Pharmacol Ther (2006) 24(1):87-94. doi:10.1111/j.1365-2036.2006.02961.x
    • (2006) Aliment Pharmacol Ther , vol.24 , Issue.1 , pp. 87-94
    • Shaib, Y.H.1    Davila, J.A.2    El-Serag, H.B.3
  • 71
    • 59649092180 scopus 로고    scopus 로고
    • Regulation and functional role of eEF1A2 in pancreatic carcinoma
    • Cao H, Zhu Q, Huang J, Li B, Zhang S, Yao W, et al. Regulation and functional role of eEF1A2 in pancreatic carcinoma. Biochem Biophys Res Commun (2009) 380(1):11-6. doi:10.1016/j.bbrc.2008.12.171
    • (2009) Biochem Biophys Res Commun , vol.380 , Issue.1 , pp. 11-16
    • Cao, H.1    Zhu, Q.2    Huang, J.3    Li, B.4    Zhang, S.5    Yao, W.6
  • 72
    • 84890434612 scopus 로고    scopus 로고
    • eEF1A2 promotes cell migration, invasion and metastasis in pancreatic cancer by upregulating MMP-9 expression through Akt activation
    • Xu C, Hu DM, Zhu Q. eEF1A2 promotes cell migration, invasion and metastasis in pancreatic cancer by upregulating MMP-9 expression through Akt activation. Clin Exp Metastasis (2013) 30(7):933-44. doi:10.1007/s10585-013-9593-6
    • (2013) Clin Exp Metastasis , vol.30 , Issue.7 , pp. 933-944
    • Xu, C.1    Hu, D.M.2    Zhu, Q.3
  • 73
    • 84879574111 scopus 로고    scopus 로고
    • eEF1A2 protein expression correlates with lymph node metastasis and decreased survival in pancreatic ductal adenocarcinoma
    • Duanmin H, Chao X, Qi Z. eEF1A2 protein expression correlates with lymph node metastasis and decreased survival in pancreatic ductal adenocarcinoma. Hepatogastroenterology (2013) 60(124):870-5. doi:10.5754/hge12869
    • (2013) Hepatogastroenterology , vol.60 , Issue.124 , pp. 870-875
    • Duanmin, H.1    Chao, X.2    Qi, Z.3
  • 74
    • 52949102178 scopus 로고    scopus 로고
    • Apoptosis-induced compensatory proliferation The cell is dead
    • Fan Y, Bergmann A. Apoptosis-induced compensatory proliferation. The cell is dead. Long live the cell! Trends Cell Biol (2008) 18(10):467-73. doi:10.1016/j.tcb.2008.08.001
    • (2008) Long live the cell! Trends Cell Biol , vol.18 , Issue.10 , pp. 467-473
    • Fan, Y.1    Bergmann, A.2
  • 75
    • 34748924281 scopus 로고    scopus 로고
    • Bcl-2-regulated apoptosis: mechanism and therapeutic potential
    • Adams JM, Cory S. Bcl-2-regulated apoptosis: mechanism and therapeutic potential. Curr Opin Immunol (2007) 19(5):488-96. doi:10.1016/j.coi.2007.05.004
    • (2007) Curr Opin Immunol , vol.19 , Issue.5 , pp. 488-496
    • Adams, J.M.1    Cory, S.2
  • 76
    • 33846450656 scopus 로고    scopus 로고
    • Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress
    • Chang R, Wang E. Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress. J Cell Biochem (2007) 100(2):267-78. doi:10.1002/jcb.20969
    • (2007) J Cell Biochem , vol.100 , Issue.2 , pp. 267-278
    • Chang, R.1    Wang, E.2
  • 77
    • 84896779178 scopus 로고    scopus 로고
    • Blockade of BFA-mediated apoptosis in macrophages by the HIV-1 Nef protein
    • Abbas W, Khan KA, Kumar A, Tripathy MK, Dichamp I, Keita M, et al. Blockade of BFA-mediated apoptosis in macrophages by the HIV-1 Nef protein. Cell Death Dis (2014) 5:e1080. doi:10.1038/cddis.2014.16
    • (2014) Cell Death Dis , vol.5
    • Abbas, W.1    Khan, K.A.2    Kumar, A.3    Tripathy, M.K.4    Dichamp, I.5    Keita, M.6
  • 78
    • 0034714430 scopus 로고    scopus 로고
    • Rapid up-regulation of peptide elongation factor EF-1alpha protein levels is an immediate early event during oxidative stress-induced apoptosis
    • Chen E, Proestou G, Bourbeau D, Wang E. Rapid up-regulation of peptide elongation factor EF-1alpha protein levels is an immediate early event during oxidative stress-induced apoptosis. Exp Cell Res (2000) 259(1):140-8. doi:10.1006/excr.2000.4952
    • (2000) Exp Cell Res , vol.259 , Issue.1 , pp. 140-148
    • Chen, E.1    Proestou, G.2    Bourbeau, D.3    Wang, E.4
  • 79
    • 84862777700 scopus 로고    scopus 로고
    • Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival
    • Day AM, Brown JD, Taylor SR, Rand JD, Morgan BA, Veal EA. Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival. Mol Cell (2012) 45(3):398-408. doi:10.1016/j.molcel.2011.11.027
    • (2012) Mol Cell , vol.45 , Issue.3 , pp. 398-408
    • Day, A.M.1    Brown, J.D.2    Taylor, S.R.3    Rand, J.D.4    Morgan, B.A.5    Veal, E.A.6
  • 80
    • 0036024027 scopus 로고    scopus 로고
    • Elongation factor-1 alpha is a selective regulator of growth factor withdrawal and ER stress-induced apoptosis
    • Talapatra S, Wagner JD, Thompson CB. Elongation factor-1 alpha is a selective regulator of growth factor withdrawal and ER stress-induced apoptosis. Cell Death Differ (2002) 9(8):856-61. doi:10.1038/sj.cdd.4401078
    • (2002) Cell Death Differ , vol.9 , Issue.8 , pp. 856-861
    • Talapatra, S.1    Wagner, J.D.2    Thompson, C.B.3
  • 81
    • 35349028811 scopus 로고    scopus 로고
    • Translation elongation factor eEF1A2 is essential for post-weaning survival in mice
    • Newbery HJ, Loh DH, O'Donoghue JE, Tomlinson VA, Chau YY, Boyd JA, et al. Translation elongation factor eEF1A2 is essential for post-weaning survival in mice. J Biol Chem (2007) 282(39):28951-9. doi:10.1074/jbc.M703962200
    • (2007) J Biol Chem , vol.282 , Issue.39 , pp. 28951-28959
    • Newbery, H.J.1    Loh, D.H.2    O'Donoghue, J.E.3    Tomlinson, V.A.4    Chau, Y.Y.5    Boyd, J.A.6
  • 82
    • 0032515985 scopus 로고    scopus 로고
    • The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1alpha, encoded by the Eef1a2 gene
    • Chambers DM, Peters J, Abbott CM. The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1alpha, encoded by the Eef1a2 gene. Proc Natl Acad Sci U S A (1998) 95(8):4463-8. doi:10.1073/pnas.95.8.4463
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.8 , pp. 4463-4468
    • Chambers, D.M.1    Peters, J.2    Abbott, C.M.3
  • 83
    • 0345267269 scopus 로고    scopus 로고
    • The wst gene regulates multiple forms of thymocyte apoptosis
    • Potter M, Bernstein A, Lee JM. The wst gene regulates multiple forms of thymocyte apoptosis. Cell Immunol (1998) 188(2):111-7. doi:10.1006/cimm.1998.1346
    • (1998) Cell Immunol , vol.188 , Issue.2 , pp. 111-117
    • Potter, M.1    Bernstein, A.2    Lee, J.M.3
  • 84
    • 84925233693 scopus 로고    scopus 로고
    • De novo eEF1A2 mutations in patients with characteristic facial features, intellectual disability, autistic behaviors and epilepsy
    • Nakajima J, Okamoto N, Tohyama J, Kato M, Arai H, Funahashi O, et al. De novo eEF1A2 mutations in patients with characteristic facial features, intellectual disability, autistic behaviors and epilepsy. Clin Genet (2015) 87(4):356-61. doi:10.1111/cge.12394
    • (2015) Clin Genet , vol.87 , Issue.4 , pp. 356-361
    • Nakajima, J.1    Okamoto, N.2    Tohyama, J.3    Kato, M.4    Arai, H.5    Funahashi, O.6
  • 85
    • 0037085362 scopus 로고    scopus 로고
    • Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis
    • Ruest LB, Marcotte R, Wang E. Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis. J Biol Chem (2002) 277(7):5418-25. doi:10.1074/jbc.M110685200
    • (2002) J Biol Chem , vol.277 , Issue.7 , pp. 5418-5425
    • Ruest, L.B.1    Marcotte, R.2    Wang, E.3
  • 87
    • 84878246922 scopus 로고    scopus 로고
    • The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis
    • Li D, Wei T, Abbott CM, Harrich D. The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis. Microbiol Mol Biol Rev (2013) 77(2):253-66. doi:10.1128/MMBR.00059-12
    • (2013) Microbiol Mol Biol Rev , vol.77 , Issue.2 , pp. 253-266
    • Li, D.1    Wei, T.2    Abbott, C.M.3    Harrich, D.4
  • 88
    • 0032989103 scopus 로고    scopus 로고
    • Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein
    • Cimarelli A, Luban J. Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein. J Virol (1999) 73(7):5388-401.
    • (1999) J Virol , vol.73 , Issue.7 , pp. 5388-5401
    • Cimarelli, A.1    Luban, J.2
  • 89
    • 0034606670 scopus 로고    scopus 로고
    • Actin-binding cellular proteins inside human immunodeficiency virus type 1
    • Ott DE, Coren LV, Johnson DG, Kane BP, Sowder RC, Kim YD, et al. Actin-binding cellular proteins inside human immunodeficiency virus type 1. Virology (2000) 266(1):42-51. doi:10.1006/viro.1999.0075
    • (2000) Virology , vol.266 , Issue.1 , pp. 42-51
    • Ott, D.E.1    Coren, L.V.2    Johnson, D.G.3    Kane, B.P.4    Sowder, R.C.5    Kim, Y.D.6
  • 90
    • 84862236625 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors
    • Warren K, Wei T, Li D, Qin F, Warrilow D, Lin MH, et al. Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors. Proc Natl Acad Sci U S A (2012) 109(24):9587-92. doi:10.1073/pnas.1204673109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.24 , pp. 9587-9592
    • Warren, K.1    Wei, T.2    Li, D.3    Qin, F.4    Warrilow, D.5    Lin, M.H.6
  • 91
    • 84855226549 scopus 로고    scopus 로고
    • Identification of cellular factors binding to acetylated HIV-1 integrase
    • Allouch A, Cereseto A. Identification of cellular factors binding to acetylated HIV-1 integrase. Amino Acids (2011) 41(5):1137-45. doi:10.1007/s00726-009-0444-3
    • (2011) Amino Acids , vol.41 , Issue.5 , pp. 1137-1145
    • Allouch, A.1    Cereseto, A.2
  • 92
    • 0035163810 scopus 로고    scopus 로고
    • Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60
    • Parissi V, Calmels C, De Soultrait VR, Caumont A, Fournier M, Chaignepain S, et al. Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60. J Virol (2001) 75(23):11344-53. doi:10.1128/JVI.75.23.11344-11353.2001
    • (2001) J Virol , vol.75 , Issue.23 , pp. 11344-11353
    • Parissi, V.1    Calmels, C.2    De Soultrait, V.R.3    Caumont, A.4    Fournier, M.5    Chaignepain, S.6
  • 93
    • 84870549921 scopus 로고    scopus 로고
    • Nef interaction with actin compromises human podocyte actin cytoskeletal integrity
    • Tan R, Patni H, Tandon P, Luan L, Sharma B, Salhan D, et al. Nef interaction with actin compromises human podocyte actin cytoskeletal integrity. Exp Mol Pathol (2013) 94(1):51-7. doi:10.1016/j.yexmp.2012.06.001
    • (2013) Exp Mol Pathol , vol.94 , Issue.1 , pp. 51-57
    • Tan, R.1    Patni, H.2    Tandon, P.3    Luan, L.4    Sharma, B.5    Salhan, D.6
  • 94
    • 0030068092 scopus 로고    scopus 로고
    • Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA
    • Wu-Baer F, Lane WS, Gaynor RB. Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA. J Biol Chem (1996) 271(8):4201-8. doi:10.1074/jbc.271.8.4201
    • (1996) J Biol Chem , vol.271 , Issue.8 , pp. 4201-4208
    • Wu-Baer, F.1    Lane, W.S.2    Gaynor, R.B.3
  • 95
    • 84861811714 scopus 로고    scopus 로고
    • The HIV-1 Nef protein interacts with two components of the 40S small ribosomal subunit, the RPS10 protein and the 18S rRNA
    • Abbas W, Dichamp I, Herbein G. The HIV-1 Nef protein interacts with two components of the 40S small ribosomal subunit, the RPS10 protein and the 18S rRNA. Virol J (2012) 9:103. doi:10.1186/1743-422X-9-103
    • (2012) Virol J , vol.9 , pp. 103
    • Abbas, W.1    Dichamp, I.2    Herbein, G.3
  • 96
    • 0032539731 scopus 로고    scopus 로고
    • Interaction of the second coding exon of Tat with human EF-1 delta delineates a mechanism for HIV-1-mediated shut-off of host mRNA translation
    • Xiao H, Neuveut C, Benkirane M, Jeang KT. Interaction of the second coding exon of Tat with human EF-1 delta delineates a mechanism for HIV-1-mediated shut-off of host mRNA translation. Biochem Biophys Res Commun (1998) 244(2):384-9. doi:10.1006/bbrc.1998.8274
    • (1998) Biochem Biophys Res Commun , vol.244 , Issue.2 , pp. 384-389
    • Xiao, H.1    Neuveut, C.2    Benkirane, M.3    Jeang, K.T.4
  • 97
    • 84859781039 scopus 로고    scopus 로고
    • Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongation factor 1 alpha 1
    • Lin WS, Jiao BY, Wu YL, Chen WN, Lin X. Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongation factor 1 alpha 1. J Med Virol (2012) 84(6):871-7. doi:10.1002/jmv.23283
    • (2012) J Med Virol , vol.84 , Issue.6 , pp. 871-877
    • Lin, W.S.1    Jiao, B.Y.2    Wu, Y.L.3    Chen, W.N.4    Lin, X.5
  • 98
    • 67649518050 scopus 로고    scopus 로고
    • The hepatitis delta virus RNA genome interacts with eEF1A1, p54(nrb), hnRNP-L
    • Sikora D, Greco-Stewart VS, Miron P, Pelchat M. The hepatitis delta virus RNA genome interacts with eEF1A1, p54(nrb), hnRNP-L, GAPDH and ASF/SF2. Virology (2009) 390(1):71-8. doi:10.1016/j.virol.2009.04.022
    • (2009) GAPDH and ASF/SF2. Virology. , vol.390 , Issue.1 , pp. 71-78
    • Sikora, D.1    Greco-Stewart, V.S.2    Miron, P.3    Pelchat, M.4
  • 99
    • 80052293913 scopus 로고    scopus 로고
    • Cutaneous human papillomavirus type 38 E7 regulates actin cytoskeleton structure for increasing cell proliferation through CK2 and the eukaryotic elongation factor 1A
    • Yue J, Shukla R, Accardi R, Zanella-Cleon I, Siouda M, Cros MP, et al. Cutaneous human papillomavirus type 38 E7 regulates actin cytoskeleton structure for increasing cell proliferation through CK2 and the eukaryotic elongation factor 1A. J Virol (2011) 85(17):8477-94. doi:10.1128/JVI.02561-10
    • (2011) J Virol , vol.85 , Issue.17 , pp. 8477-8494
    • Yue, J.1    Shukla, R.2    Accardi, R.3    Zanella-Cleon, I.4    Siouda, M.5    Cros, M.P.6
  • 100
    • 0030761459 scopus 로고    scopus 로고
    • Translation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNA
    • Blackwell JL, Brinton MA. Translation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNA. J Virol (1997) 71(9):6433-44.
    • (1997) J Virol , vol.71 , Issue.9 , pp. 6433-6444
    • Blackwell, J.L.1    Brinton, M.A.2
  • 101
    • 35348822495 scopus 로고    scopus 로고
    • Interaction between the cellular protein eEF1A and the 3'-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis
    • Davis WG, Blackwell JL, Shi PY, Brinton MA. Interaction between the cellular protein eEF1A and the 3'-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis. J Virol (2007) 81(18):10172-87. doi:10.1128/JVI.00531-07
    • (2007) J Virol , vol.81 , Issue.18 , pp. 10172-10187
    • Davis, W.G.1    Blackwell, J.L.2    Shi, P.Y.3    Brinton, M.A.4
  • 102
    • 84885664703 scopus 로고    scopus 로고
    • Reduced sphingosine kinase 1 activity in dengue virus type-2 infected cells can be mediated by the 3' untranslated region of dengue virus type-2 RNA
    • Carr JM, Kua T, Clarke JN, Calvert JK, Zebol JR, Beard MR, et al. Reduced sphingosine kinase 1 activity in dengue virus type-2 infected cells can be mediated by the 3' untranslated region of dengue virus type-2 RNA. J Gen Virol (2013) 94(Pt 11):2437-48. doi:10.1099/vir.0.055616-0
    • (2013) J Gen Virol , vol.94 , pp. 2437-2448
    • Carr, J.M.1    Kua, T.2    Clarke, J.N.3    Calvert, J.K.4    Zebol, J.R.5    Beard, M.R.6
  • 103
    • 84904747440 scopus 로고    scopus 로고
    • EF1A interacting with nucleocapsid protein of transmissible gastroenteritis coronavirus and plays a role in virus replication
    • Zhang X, Shi H, Chen J, Shi D, Li C, Feng L. EF1A interacting with nucleocapsid protein of transmissible gastroenteritis coronavirus and plays a role in virus replication. Vet Microbiol (2014) 172(3-4):443-8. doi:10.1016/j.vetmic.2014.05.034
    • (2014) Vet Microbiol , vol.172 , Issue.3-4 , pp. 443-448
    • Zhang, X.1    Shi, H.2    Chen, J.3    Shi, D.4    Li, C.5    Feng, L.6
  • 104
    • 70449450114 scopus 로고    scopus 로고
    • Analysis of virion associated host proteins in vesicular stomatitis virus using a proteomics approach
    • Moerdyk-Schauwecker M, Hwang SI, Grdzelishvili VZ. Analysis of virion associated host proteins in vesicular stomatitis virus using a proteomics approach. Virol J (2009) 6:166. doi:10.1186/1743-422X-6-166
    • (2009) Virol J , vol.6 , pp. 166
    • Moerdyk-Schauwecker, M.1    Hwang, S.I.2    Grdzelishvili, V.Z.3
  • 105
    • 33144457296 scopus 로고    scopus 로고
    • Vaccinia virus proteome: identification of proteins in vaccinia virus intracellular mature virion particles
    • Chung CS, Chen CH, Ho MY, Huang CY, Liao CL, Chang W. Vaccinia virus proteome: identification of proteins in vaccinia virus intracellular mature virion particles. J Virol (2006) 80(5):2127-40. doi:10.1128/JVI.80.5.2127-2140.2006
    • (2006) J Virol , vol.80 , Issue.5 , pp. 2127-2140
    • Chung, C.S.1    Chen, C.H.2    Ho, M.Y.3    Huang, C.Y.4    Liao, C.L.5    Chang, W.6
  • 106
    • 33846014226 scopus 로고    scopus 로고
    • Protein composition of the vaccinia virus mature virion
    • Resch W, Hixson KK, Moore RJ, Lipton MS, Moss B. Protein composition of the vaccinia virus mature virion. Virology (2007) 358(1):233-47. doi:10.1016/j.virol.2006.08.025
    • (2007) Virology , vol.358 , Issue.1 , pp. 233-247
    • Resch, W.1    Hixson, K.K.2    Moore, R.J.3    Lipton, M.S.4    Moss, B.5
  • 107
    • 4644341105 scopus 로고    scopus 로고
    • Identification of proteins associated with murine cytomegalovirus virions
    • Kattenhorn LM, Mills R, Wagner M, Lomsadze A, Makeev V, Borodovsky M, et al. Identification of proteins associated with murine cytomegalovirus virions. J Virol (2004) 78(20):11187-97. doi:10.1128/JVI.78.20.11187-11197.2004
    • (2004) J Virol , vol.78 , Issue.20 , pp. 11187-11197
    • Kattenhorn, L.M.1    Mills, R.2    Wagner, M.3    Lomsadze, A.4    Makeev, V.5    Borodovsky, M.6
  • 108
    • 4644312884 scopus 로고    scopus 로고
    • Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome
    • Varnum SM, Streblow DN, Monroe ME, Smith P, Auberry KJ, Pasa-Tolic L, et al. Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome. J Virol (2004) 78(20):10960-6. doi:10.1128/JVI.78.23.13395.2004
    • (2004) J Virol , vol.78 , Issue.20 , pp. 10960-10966
    • Varnum, S.M.1    Streblow, D.N.2    Monroe, M.E.3    Smith, P.4    Auberry, K.J.5    Pasa-Tolic, L.6
  • 109
    • 43949136115 scopus 로고    scopus 로고
    • Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3
    • Neuman BW, Joseph JS, Saikatendu KS, Serrano P, Chatterjee A, Johnson MA, et al. Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3. J Virol (2008) 82(11):5279-94. doi:10.1128/JVI.02631-07
    • (2008) J Virol , vol.82 , Issue.11 , pp. 5279-5294
    • Neuman, B.W.1    Joseph, J.S.2    Saikatendu, K.S.3    Serrano, P.4    Chatterjee, A.5    Johnson, M.A.6
  • 110
    • 33748288087 scopus 로고    scopus 로고
    • Molecular functions and biological roles of hepatitis B virus x protein
    • Tang H, Oishi N, Kaneko S, Murakami S. Molecular functions and biological roles of hepatitis B virus x protein. Cancer Sci (2006) 97(10):977-83. doi:10.1111/j.1349-7006.2006.00299.x
    • (2006) Cancer Sci , vol.97 , Issue.10 , pp. 977-983
    • Tang, H.1    Oishi, N.2    Kaneko, S.3    Murakami, S.4
  • 111
    • 77149149956 scopus 로고    scopus 로고
    • The biological properties of E6 and E7 oncoproteins from human papillomaviruses
    • Ghittoni R, Accardi R, Hasan U, Gheit T, Sylla B, Tommasino M. The biological properties of E6 and E7 oncoproteins from human papillomaviruses. Virus Genes (2010) 40(1):1-13. doi:10.1007/s11262-009-0412-8
    • (2010) Virus Genes , vol.40 , Issue.1 , pp. 1-13
    • Ghittoni, R.1    Accardi, R.2    Hasan, U.3    Gheit, T.4    Sylla, B.5    Tommasino, M.6
  • 112
    • 33748479920 scopus 로고    scopus 로고
    • Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages
    • Chertova E, Chertov O, Coren LV, Roser JD, Trubey CM, Bess JW Jr, et al. Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages. J Virol (2006) 80(18):9039-52. doi:10.1128/JVI.01013-06
    • (2006) J Virol , vol.80 , Issue.18 , pp. 9039-9052
    • Chertova, E.1    Chertov, O.2    Coren, L.V.3    Roser, J.D.4    Trubey, C.M.5    Bess, J.W.6


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