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Volumn 23, Issue 3-4, 2004, Pages 347-363

Translational control in T lymphocytes

Author keywords

Initiation factors; MRNA; PKR; SLE; T cells; Translation

Indexed keywords

CYTOKINE; GENE PRODUCT; GROWTH FACTOR; PROTEIN;

EID: 3042571215     PISSN: 08830185     EISSN: None     Source Type: Journal    
DOI: 10.1080/08830180490452549     Document Type: Review
Times cited : (7)

References (103)
  • 1
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • V.M. Pain, Initiation of protein synthesis in eukaryotic cells, Eur. J. Biochem., 236: 747-771, 1996.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 2
    • 0000831271 scopus 로고    scopus 로고
    • RNA 5′-cap-binding protein elF4E and control of cell growth
    • (N. Sonenberg, J.W.B. Hershey, M.B. Mathews eds.) Cold Spring Harbor Laboratory Press
    • N. Sonenberg, RNA 5′-cap-binding protein elF4E and control of cell growth. Translational Control, (N. Sonenberg, J.W.B. Hershey, M.B. Mathews eds.) Cold Spring Harbor Laboratory Press, pp. 245-269, 1996.
    • (1996) Translational Control , pp. 245-269
    • Sonenberg, N.1
  • 3
    • 0028794785 scopus 로고
    • Growth control of translation in mammalian cells
    • D.R. Morris, Growth control of translation in mammalian cells, Prog. Nucleic Acids Res. Mol. Biol., 51: 339-363, 1995.
    • (1995) Prog. Nucleic Acids Res. Mol. Biol. , vol.51 , pp. 339-363
    • Morris, D.R.1
  • 4
    • 0029827631 scopus 로고    scopus 로고
    • Translational control of programmed cell death: Eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc
    • V.A. Polunovsky, I.B. Rosenwald, A.T. Tan, J. White, L. Chiang, N. Sonenberg, and P.B. Bitterman, Translational control of programmed cell death: Eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc, Mol. Cell. Biol., 16: 6573-6581, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6573-6581
    • Polunovsky, V.A.1    Rosenwald, I.B.2    Tan, A.T.3    White, J.4    Chiang, L.5    Sonenberg, N.6    Bitterman, P.B.7
  • 5
    • 0031755021 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells
    • W.E. Marissen and R.E. Lloyd, Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells, Mol. Cell. Biol., 18: 7565-7574, 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7565-7574
    • Marissen, W.E.1    Lloyd, R.E.2
  • 6
    • 0031469938 scopus 로고    scopus 로고
    • Excess putrescine accumulation inhibits the formation of modified eukaryotic initiation factor 5A (elF-5A) and induces apoptosis
    • M.E. Tome, S.M. Fiser, C.M Payne, and E.W. Gerner, Excess putrescine accumulation inhibits the formation of modified eukaryotic initiation factor 5A (elF-5A) and induces apoptosis, Biochem. J., 328: 847-854, 1997.
    • (1997) Biochem. J. , vol.328 , pp. 847-854
    • Tome, M.E.1    Fiser, S.M.2    Payne, C.M.3    Gerner, E.W.4
  • 7
    • 0344731406 scopus 로고    scopus 로고
    • Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB
    • J. Gil, J. Alcami, and M. Esteban, Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB, Mol. Cell. Biol., 19: 4653-4663, 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4653-4663
    • Gil, J.1    Alcami, J.2    Esteban, M.3
  • 8
    • 0027445185 scopus 로고
    • Translation factors as effectors of cell growth and tumorigenesis
    • N. Sonenberg, Translation factors as effectors of cell growth and tumorigenesis, Curr. Opin. Cell Biol., 5: 955-960, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 955-960
    • Sonenberg, N.1
  • 9
    • 0029964974 scopus 로고    scopus 로고
    • The role of elF4 in cell proliferation
    • A. Flynn, and C.G. Proud, The role of elF4 in cell proliferation, Cancer Surv., 27: 293-310, 1996.
    • (1996) Cancer Surv. , vol.27 , pp. 293-310
    • Flynn, A.1    Proud, C.G.2
  • 10
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: Intimations of translational control
    • M. Kozak, An analysis of vertebrate mRNA sequences: Intimations of translational control, J. Cell. Biol., 115: 887-903, 1991.
    • (1991) J. Cell. Biol. , vol.115 , pp. 887-903
    • Kozak, M.1
  • 11
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate meesenger RNAs
    • M. Kozak, An analysis of 5′-noncoding sequences from 699 vertebrate meesenger RNAs, Nucleic Acid. Res., 15: 8125-8148, 1987.
    • (1987) Nucleic Acid. Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 12
    • 0032967120 scopus 로고    scopus 로고
    • Translational control of growth factor and proto-oncogene expression
    • A.E. Willis, Translational control of growth factor and proto-oncogene expression, Int. J. Biochem. Cell. Biol., 31: 73-86, 1999.
    • (1999) Int. J. Biochem. Cell. Biol. , vol.31 , pp. 73-86
    • Willis, A.E.1
  • 13
    • 0032491579 scopus 로고    scopus 로고
    • Cyclin D expression is controlled post-transcriptionally via a phosphatidy linositol 3-kinase/Akt-dependent pathway
    • R.C. Muise-Helmericks, H.L. Grimes, A. Bellacosa, S.E. Malstrom, P.N. Tsichlis, and N. Rosen, Cyclin D expression is controlled post-transcriptionally via a phosphatidy linositol 3-kinase/Akt-dependent pathway, J. Biol. Chem., 273: 29864-29872, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29864-29872
    • Muise-Helmericks, R.C.1    Grimes, H.L.2    Bellacosa, A.3    Malstrom, S.E.4    Tsichlis, P.N.5    Rosen, N.6
  • 14
    • 0032413881 scopus 로고    scopus 로고
    • Translational control elements in the major human transforming growth factor-beta 1 mRNA
    • R.S. Allison, M.L. Mumy, and L.M. Wakefield, Translational control elements in the major human transforming growth factor-beta 1 mRNA, Growth Factors, 16: 89-100, 1998.
    • (1998) Growth Factors , vol.16 , pp. 89-100
    • Allison, R.S.1    Mumy, M.L.2    Wakefield, L.M.3
  • 15
    • 0024432688 scopus 로고
    • Translational blockade imposed by cytokine-derived UA-rich sequences
    • V. Kruys, O. Marinx, G. Shaw, J. Deschamps, and G. Huez, Translational blockade imposed by cytokine-derived UA-rich sequences, Science, 245: 852-855, 1989.
    • (1989) Science , vol.245 , pp. 852-855
    • Kruys, V.1    Marinx, O.2    Shaw, G.3    Deschamps, J.4    Huez, G.5
  • 16
    • 0030037685 scopus 로고    scopus 로고
    • Translational control of interleukin-2 messenger RNA as a molecular mechanism of T cell energy
    • J.A. Garcia-Sanz and D. Lenig, Translational control of interleukin-2 messenger RNA as a molecular mechanism of T cell energy, J. Exp. Med., 184: 159-164, 1996.
    • (1996) J. Exp. Med. , vol.184 , pp. 159-164
    • Garcia-Sanz, J.A.1    Lenig, D.2
  • 17
    • 0029801756 scopus 로고    scopus 로고
    • Transcriptional and translational control of TNF-alpha gene expression in human monocytes by major histocompatibility complex class II ligands
    • E. Espel, J.A. Garcia-Sanz, V. Aubert, V. Menoud, P. Sperisen, N. Fernandez, and F. Spertini, Transcriptional and translational control of TNF-alpha gene expression in human monocytes by major histocompatibility complex class II ligands, Eur. J. Immunol., 26: 2417-2424, 1996.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2417-2424
    • Espel, E.1    Garcia-Sanz, J.A.2    Aubert, V.3    Menoud, V.4    Sperisen, P.5    Fernandez, N.6    Spertini, F.7
  • 18
    • 0031964902 scopus 로고    scopus 로고
    • Relative contibution of transcription and translation to the induction of tumor necrosis factor-alpha by lipopolyscharide
    • T. Raabe, M. Bukrinsky, and R.A. Currie, Relative contibution of transcription and translation to the induction of tumor necrosis factor-alpha by lipopolyscharide, J. Biol. Chem., 273: 974-980, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 974-980
    • Raabe, T.1    Bukrinsky, M.2    Currie, R.A.3
  • 19
    • 0033593448 scopus 로고    scopus 로고
    • Identification of TIAR as a protein binding to the translational regulatory AU-rich element of tumor necrosis factor alpha mRNA
    • C. Gueydan, L. Droogmams, P. Chalon, G. Huez, D. Caput, and V. Kruys, Identification of TIAR as a protein binding to the translational regulatory AU-rich element of tumor necrosis factor alpha mRNA, J. Biol. Chem., 274: 2322-2326, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2322-2326
    • Gueydan, C.1    Droogmams, L.2    Chalon, P.3    Huez, G.4    Caput, D.5    Kruys, V.6
  • 20
    • 0032529209 scopus 로고    scopus 로고
    • Translational contol of MHC class II I-A molecules by IFN-gamma
    • E. Gonalons, M. Barrachina, J.A. Garcia-Sanz, and A. Celada, Translational contol of MHC class II I-A molecules by IFN-gamma, J. Immunol., 161: 1837-1843, 1998.
    • (1998) J. Immunol. , vol.161 , pp. 1837-1843
    • Gonalons, E.1    Barrachina, M.2    Garcia-Sanz, J.A.3    Celada, A.4
  • 21
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • J.W.B. Hershey, M.B. Mathews, and N. Sonenberg (Eds.), Cold Spring Harbor: CSHL Press
    • W.C. Merrick and J.W.B Hershey, The pathway and mechanism of eukaryotic protein synthesis, In J.W.B. Hershey, M.B. Mathews, and N. Sonenberg (Eds.), Translational Control, Cold Spring Harbor: CSHL Press, pp. 31-69, 1996.
    • (1996) Translational Control , pp. 31-69
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 22
    • 0021921587 scopus 로고
    • mRNA cap binding proteins: Essential factors for initiation translation
    • A.J. Shatkin, mRNA cap binding proteins: Essential factors for initiation translation, Cell, 40: 223-224, 1985.
    • (1985) Cell , vol.40 , pp. 223-224
    • Shatkin, A.J.1
  • 23
    • 0018143765 scopus 로고
    • A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA
    • N. Sonenberg, M.A. Morgan, W.C. Merrick, and A.J. Shatkin, A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA, Proc. Natl. Acad. Sci., 75: 4843-4847, 1978.
    • (1978) Proc. Natl. Acad. Sci. , vol.75 , pp. 4843-4847
    • Sonenberg, N.1    Morgan, M.A.2    Merrick, W.C.3    Shatkin, A.J.4
  • 24
    • 0025314596 scopus 로고
    • Malignant transformation by a eukarotic initiation factor subunits that binds to mRNA 5′ cap
    • A. Lazaris-Karatzas, K.S. Montine, and N. Sonenberg, Malignant transformation by a eukarotic initiation factor subunits that binds to mRNA 5′ cap, Nature, 345: 44-547, 1990.
    • (1990) Nature , vol.345 , pp. 44-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 25
    • 0029827631 scopus 로고    scopus 로고
    • Translational control of programmed cell death: Eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated, Myc
    • V.A. Polunovsky, I.B. Rosenwald, A.T. Tan, J. White, L. Chiang, N. Sonenberg, and P.B. Bitterman, Translational control of programmed cell death: Eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated, Myc, Mol. Cell. Biol., 16: 6573-6581, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6573-6581
    • Polunovsky, V.A.1    Rosenwald, I.B.2    Tan, A.T.3    White, J.4    Chiang, L.5    Sonenberg, N.6    Bitterman, P.B.7
  • 26
    • 0034624746 scopus 로고    scopus 로고
    • Inhibition of Myc-dependent apoptosis by eukaryotic translation initiation factor 4E requires cyclin D1
    • A. Tan, P. Bitterman, N. Sonenberg, M. Peterson, and V. Polunovsky, Inhibition of Myc-dependent apoptosis by eukaryotic translation initiation factor 4E requires cyclin D1, Oncogene, 19: 1437-1447, 2000.
    • (2000) Oncogene , vol.19 , pp. 1437-1447
    • Tan, A.1    Bitterman, P.2    Sonenberg, N.3    Peterson, M.4    Polunovsky, V.5
  • 27
    • 0029772318 scopus 로고    scopus 로고
    • An essential E box in the promoter of the gene encoding the mRNA cap-binding protein (eukaryotic initiation factor 4E) is a target for activation by c-myc
    • R.M. Jones, J. Branda, K.A. Johnston, M. Polymenis, M. Gadd, A. Rustgi, L. Callanan, and E.V. Schmidt, An essential E box in the promoter of the gene encoding the mRNA cap-binding protein (eukaryotic initiation factor 4E) is a target for activation by c-myc, Mol. Cell. Biol., 16: 4754-4764, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4754-4764
    • Jones, R.M.1    Branda, J.2    Johnston, K.A.3    Polymenis, M.4    Gadd, M.5    Rustgi, A.6    Callanan, L.7    Schmidt, E.V.8
  • 28
    • 0025327221 scopus 로고
    • Alteration of the major phosphorylation site of eukaryotic protein synthesis initiation factor 4E prevents its association with the 48 S initiation complex
    • S. Joshi-Barve, W. Rychlik, and R.E. Rhoads, Alteration of the major phosphorylation site of eukaryotic protein synthesis initiation factor 4E prevents its association with the 48 S initiation complex, J. Biol. Chem., 265: 2979-2983, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2979-2983
    • Joshi-Barve, S.1    Rychlik, W.2    Rhoads, R.E.3
  • 29
    • 0025906412 scopus 로고
    • Phosphorylation of elF4F by protein kinase C or multipotential S6 kinase stimulates protein synthesis at initiation
    • S.J. Morley, T.E. Dever, D. Etchison, and J.A. Traugh, Phosphorylation of elF4F by protein kinase C or multipotential S6 kinase stimulates protein synthesis at initiation, J. Biol. Chem., 266: 4669-4672, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4669-4672
    • Morley, S.J.1    Dever, T.E.2    Etchison, D.3    Traugh, J.A.4
  • 30
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnkl and Mnk2
    • A.J. Waskiewicz, A. Flynn, C.G. Proud, J.A. Proud, and J.A. Cooper, Mitogen-activated protein kinases activate the serine/threonine kinases Mnkl and Mnk2, EMBO J., 16: 1909-1920, 1997.
    • (1997) EMBO J. , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Proud, J.A.4    Cooper, J.A.5
  • 31
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP-kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrate
    • R. Fukunaga and T. Hunter, MNK1, a new MAP-kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrate, EMBO J., 16: 1921-1933, 1997.
    • (1997) EMBO J. , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 33
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • A. Pause, G.J. Belsham, A.C. Gingras, O. Donze, T.A. Lin, J.C. Lawrence Jr., and N. Sonenberg, Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function, Nature, 371: 762-767, 1994.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 34
    • 0028786952 scopus 로고
    • Represson of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E
    • A. Haghighat, S. Mader, A. Pause, and N. Sonenberg, Represson of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E, EMBO J., 14: 5701-5709, 1995.
    • (1995) EMBO J. , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 36
    • 0030443685 scopus 로고    scopus 로고
    • The elF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • D. Rousseau, A. C. Gingras, A. Pause, and N. Sonenberg, The elF4E-binding proteins 1 and 2 are negative regulators of cell growth, Oncogene, 13: 2415-2420, 1996.
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 38
    • 0026723117 scopus 로고
    • mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor elF-4E
    • A.E. Koromilas, A. Lazaris-Karatzas, and N. Sonenberg, mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor elF-4E, EMBO J., 11: 4153-4158, 1992.
    • (1992) EMBO J. , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 39
    • 0027365517 scopus 로고
    • Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E
    • I.B. Rosenwald, A. Lazaris-Karatzas, N. Sonenberg, and E.V. Schmidt, Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E, Mol. Cell. Biol., 13: 7358-7363, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7358-7363
    • Rosenwald, I.B.1    Lazaris-Karatzas, A.2    Sonenberg, N.3    Schmidt, E.V.4
  • 41
    • 0030041884 scopus 로고    scopus 로고
    • Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E
    • D. Rousseau, R. Kaspar, I. Rosenwald, L. Gehrke, and N. Sonenberg, Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E, Proc. Natl. Acad. Sci. USA, 93: 1065-1070, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1065-1070
    • Rousseau, D.1    Kaspar, R.2    Rosenwald, I.3    Gehrke, L.4    Sonenberg, N.5
  • 42
    • 0030011284 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor elF-4E
    • L.M. Shantz, R.H. Hu, and A.E. Pegg, Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor elF-4E, Cancer Res., 56: 3265-3269, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 3265-3269
    • Shantz, L.M.1    Hu, R.H.2    Pegg, A.E.3
  • 43
    • 0031558804 scopus 로고    scopus 로고
    • Translation of ODC mRNA and polyamine transport are suppressed in ras-transformed CREF cells by depleting translation initiation factor 4E
    • J.R. Graff, A. De Benedetti, J.W. Olson, P. Tamez, R.A. Casero Jr., and S.G. Zimmer, Translation of ODC mRNA and polyamine transport are suppressed in ras-transformed CREF cells by depleting translation initiation factor 4E, Biochem. Biophys. Res. Commun., 240: 15-20, 1997.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 15-20
    • Graff, J.R.1    De Benedetti, A.2    Olson, J.W.3    Tamez, P.4    Casero Jr., R.A.5    Zimmer, S.G.6
  • 44
    • 0033005366 scopus 로고    scopus 로고
    • Eukaryotic initiation factor elF2
    • S.R. Kimball, Eukaryotic initiation factor elF2, Int. J. Biochem. Cell Biol., 31: 25-29, 1999.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 25-29
    • Kimball, S.R.1
  • 45
    • 0030267336 scopus 로고    scopus 로고
    • The elF-2alpha kinases and the control of protein synthesis
    • C. De Haro, R. Mendez, and J. Santoyo, The elF-2alpha kinases and the control of protein synthesis, FASEB J., 10: 1378-1387, 1996.
    • (1996) FASEB J. , vol.10 , pp. 1378-1387
    • De Haro, C.1    Mendez, R.2    Santoyo, J.3
  • 46
    • 0000108932 scopus 로고
    • dsRNA-activated protein kinase (PKR): Antiproliferative antiviral and antitumoral functions
    • A.G. Hovanessian, dsRNA-activated protein kinase (PKR): Antiproliferative antiviral and antitumoral functions, Semin. Virol., 4: 237-245, 1993.
    • (1993) Semin. Virol. , vol.4 , pp. 237-245
    • Hovanessian, A.G.1
  • 47
    • 0030725442 scopus 로고    scopus 로고
    • The double stranded RNA-dependent protein kinase PKR: Structure and function
    • M.J. Clemens and A. Elia, The double stranded RNA-dependent protein kinase PKR: Structure and function, J. Interferon Cytokine Res., 17: 503-524, 1997.
    • (1997) J. Interferon Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 49
    • 0342681053 scopus 로고    scopus 로고
    • PKR: A general transducer of the cellular stress response leading to apoptosis
    • Sonenberg, N., Hershey, J.W.B., Mathews, M.B., eds. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • R. Kaufman and S.P. Srivasyava, PKR: A general transducer of the cellular stress response leading to apoptosis, in Translational Control, Sonenberg, N., Hershey, J.W.B., Mathews, M.B., eds. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1996.
    • (1996) Translational Control
    • Kaufman, R.1    Srivasyava, S.P.2
  • 50
    • 0026701570 scopus 로고
    • Malignant transormation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • A.E. Koromilas, S. Roy, G.N. Barber, M. Katze, and N. Sonenberg, Malignant transormation by a mutant of the IFN-inducible dsRNA-dependent protein kinase, Science, 257: 5041-5044, 1992.
    • (1992) Science , vol.257 , pp. 5041-5044
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.4    Sonenberg, N.5
  • 52
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • S.B. Lee and M. Esteban, The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis, Virology, 199: 491-496, 1994.
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 53
    • 0029981093 scopus 로고    scopus 로고
    • An essential role for the interferon-inducible, dsRNA-activated protein kinase, PKR, in the tumor necrosis factor-induced apoptosis in U937 cells
    • M.C. Yeung, J. Liu, and A.S. Lau, An essential role for the interferon-inducible, dsRNA-activated protein kinase, PKR, in the tumor necrosis factor-induced apoptosis in U937 cells, Proc. Natl. Acad. Sci., 93: 12451-12455, 1996.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 12451-12455
    • Yeung, M.C.1    Liu, J.2    Lau, A.S.3
  • 54
    • 0030992545 scopus 로고    scopus 로고
    • A dsRNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • S.D. Der, Y.L. Yang, C. Weissman, and B.R. Williams, A dsRNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis, Proc. Natl. Acad. Sci., 94: 3279-3283, 1997.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.L.2    Weissman, C.3    Williams, B.R.4
  • 55
    • 0343812093 scopus 로고    scopus 로고
    • The apoptosis pathway triggered by the interferon-induced protein kinase, PKR requires the third basic domain, initiates upstream of Bcl-2, and involves ICE-like proteases
    • S.B. Lee, D. Rodriguez, J.R. Rodriguez, and M. Esteban, The apoptosis pathway triggered by the interferon-induced protein kinase, PKR requires the third basic domain, initiates upstream of Bcl-2, and involves ICE-like proteases, Virology, 231: 81-88, 1997.
    • (1997) Virology , vol.231 , pp. 81-88
    • Lee, S.B.1    Rodriguez, D.2    Rodriguez, J.R.3    Esteban, M.4
  • 56
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of elF2 mediates apoptosis in response to activation of PKR
    • S.P. Srivastava, K.U. Kumar, and R.J. Kaufman, Phosphorylation of elF2 mediates apoptosis in response to activation of PKR, J. Biol. Chem., 273: 2416-2423, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 57
    • 0033541366 scopus 로고    scopus 로고
    • Regulatable expression of the interferon-induced double-stranded RNA dependent protein kinase PKR induces apoptosis and Fas receptor expression
    • O. Donze, J. Dostie, and N. Sonenberg, Regulatable expression of the interferon-induced double-stranded RNA dependent protein kinase PKR induces apoptosis and Fas receptor expression, Virology, 256: 322-329, 1999.
    • (1999) Virology , vol.256 , pp. 322-329
    • Donze, O.1    Dostie, J.2    Sonenberg, N.3
  • 58
    • 0032404120 scopus 로고    scopus 로고
    • Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling
    • S. Balachandran, N. Kim, W.-C. Yeh, T.W. Mak, K. Bhalla, and G.N. Barber, Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling, EMBO J., 17: 6888-6902, 1998.
    • (1998) EMBO J. , vol.17 , pp. 6888-6902
    • Balachandran, S.1    Kim, N.2    Yeh, W.-C.3    Mak, T.W.4    Bhalla, K.5    Barber, G.N.6
  • 59
    • 0025997530 scopus 로고
    • Mechanism of activation of protein synthesis initiation in mitogen-stimulated T lymphocytes
    • P. Jedlicka and R. Panniers, Mechanism of activation of protein synthesis initiation in mitogen-stimulated T lymphocytes, J. Biol. Chem., 266: 15663-15669, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15663-15669
    • Jedlicka, P.1    Panniers, R.2
  • 60
    • 0025132887 scopus 로고
    • Increased elF-2 alpha expression in mitogen-activated primary T lymphocytes
    • R.B. Cohen, T.R. Boal, and B. Safer, Increased elF-2 alpha expression in mitogen-activated primary T lymphocytes, EMBO J., 9: 3831-3837, 1990.
    • (1990) EMBO J. , vol.9 , pp. 3831-3837
    • Cohen, R.B.1    Boal, T.R.2    Safer, B.3
  • 63
    • 0031884519 scopus 로고    scopus 로고
    • Translational control: A general mechanism for gene regulation during T cell activation
    • J.A. Garcia-Sanz, W. Mikulits, A. Livingstone, I. Lefkovits, and E.W. Mullner, Translational control: A general mechanism for gene regulation during T cell activation, FASEB J., 12: 299-306, 1998.
    • (1998) FASEB J. , vol.12 , pp. 299-306
    • Garcia-Sanz, J.A.1    Mikulits, W.2    Livingstone, A.3    Lefkovits, I.4    Mullner, E.W.5
  • 64
    • 0030656997 scopus 로고    scopus 로고
    • Signalling through either the p38 or ERK mitogen-activated protein (MAP) kinase pathway is obligatory for phorbol ester and T cell receptor complex (TCR-CD3)-stimulated phosphorylation of initiation factor (elF) 4E in jurkat T cells
    • S.J. Morley, Signalling through either the p38 or ERK mitogen-activated protein (MAP) kinase pathway is obligatory for phorbol ester and T cell receptor complex (TCR-CD3)-stimulated phosphorylation of initiation factor (elF) 4E in jurkat T cells, FEBS Lett., 418: 327-332, 1997.
    • (1997) FEBS Lett. , vol.418 , pp. 327-332
    • Morley, S.J.1
  • 65
    • 0032481114 scopus 로고    scopus 로고
    • Degradation of eukaryotic polypeptide chain initiation factor (elF) 4G in response to induction of apoptosis in human lymphoma cell lines
    • M.J. Clemens, M. Bushell, and S.J. Morley, Degradation of eukaryotic polypeptide chain initiation factor (elF) 4G in response to induction of apoptosis in human lymphoma cell lines, Oncogene, 17: 2921-2931, 1998.
    • (1998) Oncogene , vol.17 , pp. 2921-2931
    • Clemens, M.J.1    Bushell, M.2    Morley, S.J.3
  • 66
    • 0032582744 scopus 로고    scopus 로고
    • Cleavage of translation initiation factor 4G (elF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase
    • S.J. Morley, L. McKendrick, and M. Bushell, Cleavage of translation initiation factor 4G (elF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase, FEBS Lett., 438: 41-48, 1998.
    • (1998) FEBS Lett. , vol.438 , pp. 41-48
    • Morley, S.J.1    McKendrick, L.2    Bushell, M.3
  • 68
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • D.M. Sabatini, H. Erdjument-Bromage, M. Lui, P. Tempst, and S.H. Snyder, RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs, Cell, 78: 35-43, 1994.
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 71
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation
    • L. Beretta, A.C. Gingras, Y. Svitkin, M.N. Hall, and N. Sonenberg, Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation EMBO J., 15: 658-664, 1996.
    • (1996) EMBO J. , vol.15 , pp. 658-664
    • Beretta, L.1    Gingras, A.C.2    Svitkin, Y.3    Hall, M.N.4    Sonenberg, N.5
  • 72
    • 0009489905 scopus 로고    scopus 로고
    • Rapamycin selectively inhibits a growth-dependent activation of the initiation step of translation
    • L. Beretta and A. Grolleau, Rapamycin selectively inhibits a growth-dependent activation of the initiation step of translation, Med. Sci., 5: 600-602, 1998.
    • (1998) Med. Sci. , vol.5 , pp. 600-602
    • Beretta, L.1    Grolleau, A.2
  • 73
    • 0030598885 scopus 로고    scopus 로고
    • A signaling pathway to translational control
    • E.J. Brown and S.L. Schreiber, A signaling pathway to translational control, Cell, 86: 517-520, 1996.
    • (1996) Cell , vol.86 , pp. 517-520
    • Brown, E.J.1    Schreiber, S.L.2
  • 74
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AKTion blocks apoptosis
    • T.F. Franke, D.R. Kaplan, and L.C. Cantley, PI3K: Downstream AKTion blocks apoptosis, Cell, 88: 435-437, 1997.
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 75
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • J. Downward, Mechanisms and consequences of activation of protein kinase B/Akt, Curr. Opin. Cell. Biol., 10: 262-267, 1998.
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 262-267
    • Downward, J.1
  • 77
    • 0024566240 scopus 로고
    • Molecular and cellular events of T cell development
    • B.J. Fowlkes and D.M. Pardoll, Molecular and cellular events of T cell development, Adv. Immunol., 44: 207-264, 1989.
    • (1989) Adv. Immunol. , vol.44 , pp. 207-264
    • Fowlkes, B.J.1    Pardoll, D.M.2
  • 78
    • 0023770725 scopus 로고
    • Thymocyte subpopulations during early fetal development in the BALB/c mouse
    • L.A. Husman, R.P. Shimonkevitz, I.N. Crispe, and M.J. Bevan, Thymocyte subpopulations during early fetal development in the BALB/c mouse, J. Immunol., 141: 736-740, 1988.
    • (1988) J. Immunol. , vol.141 , pp. 736-740
    • Husman, L.A.1    Shimonkevitz, R.P.2    Crispe, I.N.3    Bevan, M.J.4
  • 79
    • 0040226744 scopus 로고
    • Discrete stages of human intrathymic differentiation: Analysis of normal thymocytes and leukemic lymphoblasts of T-cell lineage
    • E.L. Reinherz, P.C. Kung, G. Goldstein, R.H. Levey, and S.F. Schlossman, Discrete stages of human intrathymic differentiation: Analysis of normal thymocytes and leukemic lymphoblasts of T-cell lineage, Proc. Natl. Acad. Sci. USA, 77: 1588-1592, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1588-1592
    • Reinherz, E.L.1    Kung, P.C.2    Goldstein, G.3    Levey, R.H.4    Schlossman, S.F.5
  • 81
    • 0026067468 scopus 로고
    • Towards an integrated view of thymopoiesis
    • R.L. Boyd and P. Hugo, Towards an integrated view of thymopoiesis, Immunol. Today, 12: 71-79, 1991.
    • (1991) Immunol. Today , vol.12 , pp. 71-79
    • Boyd, R.L.1    Hugo, P.2
  • 82
    • 0028332026 scopus 로고
    • The dsRNA-dependent protein kinase, PKR, activates transcription factor NF-kB by phosphorylating lkB
    • A. Kumar, J. Haque, J. Lacoste, J. Hiscott, and B.R. Williams, The dsRNA-dependent protein kinase, PKR, activates transcription factor NF-kB by phosphorylating lkB, Proc. Natl. Acad. Sci. USA, 91: 6288-6292, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6288-6292
    • Kumar, A.1    Haque, J.2    Lacoste, J.3    Hiscott, J.4    Williams, B.R.5
  • 83
    • 17444449609 scopus 로고    scopus 로고
    • Deficient cytolkine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: Role of IRF-1 and NFkappaB
    • A. Kumar, Y.L. Yang, V. Flati, S. Der, S. Kadereit, A. Deb, J. Haque, L. Reis, C. Weissmann, and B.R. Williams, Deficient cytolkine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: Role of IRF-1 and NFkappaB, EMBO J., 16: 406-416, 1997.
    • (1997) EMBO J. , vol.16 , pp. 406-416
    • Kumar, A.1    Yang, Y.L.2    Flati, V.3    Der, S.4    Kadereit, S.5    Deb, A.6    Haque, J.7    Reis, L.8    Weissmann, C.9    Williams, B.R.10
  • 84
    • 0343852938 scopus 로고    scopus 로고
    • Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and douvle-stranded RNA signaling pathways
    • A.H.T. Wong, N.W.N. Tam, Y.L. Yang, A.R. Cuddihy, S. Li, S. Kirchhoff, H. Hauser, T. Decker, and A.E. Koromilas, Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and douvle-stranded RNA signaling pathways, EMBO J., 16: 1291-1304, 1997.
    • (1997) EMBO J. , vol.16 , pp. 1291-1304
    • Wong, A.H.T.1    Tam, N.W.N.2    Yang, Y.L.3    Cuddihy, A.R.4    Li, S.5    Kirchhoff, S.6    Hauser, H.7    Decker, T.8    Koromilas, A.E.9
  • 85
    • 0027966119 scopus 로고
    • Interleukin 3 stimulates protein synthesis by regulating double-stranded RNA-dependent protein kinase
    • T. Ito, R. Jagus, and W.S. May, Interleukin 3 stimulates protein synthesis by regulating double-stranded RNA-dependent protein kinase, Proc. Natl. Acad. Sci. USA, 91: 7455-7459, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7455-7459
    • Ito, T.1    Jagus, R.2    May, W.S.3
  • 87
    • 0034672105 scopus 로고    scopus 로고
    • Negative regulation of CD8 + T cell function by the IFN-induced and double-stranded RNA-activated kinase PKR
    • S. Kadereit, H. Xu, T.M. Engeman, Y.L. Yang, R.L. Fairchild, and B.R.G. Williams, Negative regulation of CD8 + T cell function by the IFN-induced and double-stranded RNA-activated kinase PKR, J. Immunol., 165: 6896-6901, 2001.
    • (2001) J. Immunol. , vol.165 , pp. 6896-6901
    • Kadereit, S.1    Xu, H.2    Engeman, T.M.3    Yang, Y.L.4    Fairchild, R.L.5    Williams, B.R.G.6
  • 88
  • 89
    • 0026602547 scopus 로고
    • Lymphocyte abnormalities in human lupus
    • G.C. Tsokos, Lymphocyte abnormalities in human lupus, Clin. Immunol. Immunopathol., 63: 7-9, 1992.
    • (1992) Clin. Immunol. Immunopathol. , vol.63 , pp. 7-9
    • Tsokos, G.C.1
  • 90
    • 0036560022 scopus 로고    scopus 로고
    • Abnormal T cell signal transduction in systemic lupus erythematosus
    • G.M. Kammer, A. Perl, B.C. Richardson, and G.C. Tsokos, Abnormal T cell signal transduction in systemic lupus erythematosus, Arthritis Rheum., 46: 1139-1154, 2002.
    • (2002) Arthritis Rheum. , vol.46 , pp. 1139-1154
    • Kammer, G.M.1    Perl, A.2    Richardson, B.C.3    Tsokos, G.C.4
  • 91
    • 0028278214 scopus 로고
    • Deficient type I protein kinase A isozyme activity in systemic lupus erythematosus T lymphocytes
    • G.M. Kammer, I. Khan, and C. Malemud, Deficient type I protein kinase A isozyme activity in systemic lupus erythematosus T lymphocytes, J. Clin. Invest., 94: 422-430, 1994.
    • (1994) J. Clin. Invest. , vol.94 , pp. 422-430
    • Kammer, G.M.1    Khan, I.2    Malemud, C.3
  • 92
    • 0035877052 scopus 로고    scopus 로고
    • Protein kinase A RIβ subunit deficiency in lupus T lymphocytes: Bypassing a block in RIβ translation reconstitutes protein kinase A activity and augments IL-2 production
    • I.U. Khan, D. Laxminarayana, and G.M. Kammer, Protein kinase A RIβ subunit deficiency in lupus T lymphocytes: Bypassing a block in RIβ translation reconstitutes protein kinase A activity and augments IL-2 production, J. Immunol., 166: 7600-7605, 2001.
    • (2001) J. Immunol. , vol.166 , pp. 7600-7605
    • Khan, I.U.1    Laxminarayana, D.2    Kammer, G.M.3
  • 93
    • 0029929607 scopus 로고    scopus 로고
    • Defective antigen-presenting cell function in patients with systemic lupus erythematosus: Role of the B7-1 (CD80) costimulatory molecule
    • G.C. Tsokos, B. Kovacs, P.P. Sfikakis, S. Theocharis, S.A. Vogelgesang, and C.S. Via, Defective antigen-presenting cell function in patients with systemic lupus erythematosus: Role of the B7-1 (CD80) costimulatory molecule, Arthritis Rheum., 39: 600-609, 1996.
    • (1996) Arthritis Rheum. , vol.39 , pp. 600-609
    • Tsokos, G.C.1    Kovacs, B.2    Sfikakis, P.P.3    Theocharis, S.4    Vogelgesang, S.A.5    Via, C.S.6
  • 94
    • 0029862164 scopus 로고    scopus 로고
    • Increased expression of CD40 ligand on systemic lupus erythematosus lymphocytes
    • M. Koshy, D. Berger, and M.K. Crow, Increased expression of CD40 ligand on systemic lupus erythematosus lymphocytes, J. Clin. Invest., 98: 826-837, 1996.
    • (1996) J. Clin. Invest. , vol.98 , pp. 826-837
    • Koshy, M.1    Berger, D.2    Crow, M.K.3
  • 95
    • 0033179001 scopus 로고    scopus 로고
    • Abnormal NF-KappaB activity in T lymphocytes from patients with systemic lupus erythematosus is associated with decreased p65-RelA protein expression
    • H.K. Wong, G.M. Kammer, G. Dennis, and G.C. Tsokos, Abnormal NF-KappaB activity in T lymphocytes from patients with systemic lupus erythematosus is associated with decreased p65-RelA protein expression, J. Immunol., 163: 1682-1689, 1999.
    • (1999) J. Immunol. , vol.163 , pp. 1682-1689
    • Wong, H.K.1    Kammer, G.M.2    Dennis, G.3    Tsokos, G.C.4
  • 96
    • 0037111374 scopus 로고    scopus 로고
    • Defective production of functional 98-kDa form of Elf-1 is responsible for the decreased expression of TCR zeta-chain in patients with systemic lupus erythematosus
    • Y.T. Juang, K. Tenbrock, M.P. Nambiar, M.F. Gourley, and G.C. Tsokos, Defective production of functional 98-kDa form of Elf-1 is responsible for the decreased expression of TCR zeta-chain in patients with systemic lupus erythematosus, J. Immunol., 169: 6048-6055, 2002.
    • (2002) J. Immunol. , vol.169 , pp. 6048-6055
    • Juang, Y.T.1    Tenbrock, K.2    Nambiar, M.P.3    Gourley, M.F.4    Tsokos, G.C.5
  • 97
    • 0025666735 scopus 로고
    • Evidence for impaired T cell DNA methylation in systemic lupus erythematosus and rheumatoid arthritis
    • B. Richardson, L. Scheinbart, J. Strahler, L. Gross, S. Hanash, and M. Johnson, Evidence for impaired T cell DNA methylation in systemic lupus erythematosus and rheumatoid arthritis, Arthritis Rheum., 33: 1665-1673, 1990.
    • (1990) Arthritis Rheum. , vol.33 , pp. 1665-1673
    • Richardson, B.1    Scheinbart, L.2    Strahler, J.3    Gross, L.4    Hanash, S.5    Johnson, M.6
  • 98
    • 0035096761 scopus 로고    scopus 로고
    • Decreased Ras-mitogen-activated protein kinase signalling may cause DNA hypomethylation in T lymphocytes from lupus patients
    • C. Deng, M.J. Kaplan, J. Yang, D. Ray, Z. Zhang, W.J. McCune, S.M. Hanash, and B.C. Richardson, Decreased Ras-mitogen-activated protein kinase signalling may cause DNA hypomethylation in T lymphocytes from lupus patients. Arthritis Rheum., 44: 397-407, 2001.
    • (2001) Arthritis Rheum. , vol.44 , pp. 397-407
    • Deng, C.1    Kaplan, M.J.2    Yang, J.3    Ray, D.4    Zhang, Z.5    McCune, W.J.6    Hanash, S.M.7    Richardson, B.C.8
  • 99
    • 0034519709 scopus 로고    scopus 로고
    • Impaired translational response and increased protein kinase PKR expression in T cells from lupus patients
    • A. Grolleau, M.J. Kaplan, S.M. Hanash, L. Beretta, and B. Richardson, Impaired translational response and increased protein kinase PKR expression in T cells from lupus patients, J. Clin. Invest., 106: 1561-1568, 2000.
    • (2000) J. Clin. Invest. , vol.106 , pp. 1561-1568
    • Grolleau, A.1    Kaplan, M.J.2    Hanash, S.M.3    Beretta, L.4    Richardson, B.5
  • 100
    • 0024270622 scopus 로고
    • The inhibition of protein synthesis by IgG containing anti-ribosome P autoantibodies from systemice lupus erythematosus patients
    • D.W. Stacey, S. Shelly, T. Watson, K. Elkon, H. Weissbach, and N. Brot, The inhibition of protein synthesis by IgG containing anti-ribosome P autoantibodies from systemice lupus erythematosus patients, Arch. Biochem. Biophys., 267: 398-403, 1988.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 398-403
    • Stacey, D.W.1    Shelly, S.2    Watson, T.3    Elkon, K.4    Weissbach, H.5    Brot, N.6
  • 101
    • 0032845153 scopus 로고    scopus 로고
    • Messenger RNA translation state: The second dimension of high-throughout expression screening
    • Q.M. Zong, L. Schummer, L. Hood, and D.R. Morris, Messenger RNA translation state: The second dimension of high-throughout expression screening, Proc. Natl. Acad. Sci. USA, 96: 10362-10636, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10362-10636
    • Zong, Q.M.1    Schummer, L.2    Hood, L.3    Morris, D.R.4
  • 102
    • 0033539681 scopus 로고    scopus 로고
    • Identification of eukaryotic mRNAs that are translated at reduced cap binding complex elF4F concentrations using a cDNA microarray
    • G. Johannes, M.S. Carter, M.B. Eisen, P.O. Brown, and P. Sarrow, Identification of eukaryotic mRNAs that are translated at reduced cap binding complex elF4F concentrations using a cDNA microarray, Proc. Natl. Acad. Sci. USA, 96: 13118-13123, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13118-13123
    • Johannes, G.1    Carter, M.S.2    Eisen, M.B.3    Brown, P.O.4    Sarrow, P.5


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