메뉴 건너뛰기




Volumn 1-3, Issue , 2003, Pages 305-309

Translational Control and Insulin Signaling

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0038160611     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012124546-7/50677-X     Document Type: Chapter
Times cited : (1)

References (66)
  • 1
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • J.W.B. Hershey (1991) Translational control in mammalian cells. Annu. Rev. Biochem. 60 717-755.
    • (1991) Annu. Rev. Biochem , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 2
    • 0032999830 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): Balancing the opposing forces of protein synthesis and degradation
    • P.B. Dennis, S. Fumagalli and G. Thomas (1999) Target of rapamycin (TOR): Balancing the opposing forces of protein synthesis and degradation. Curr. Opin. Genet. Dev. 9 49-54.
    • (1999) Curr. Opin. Genet. Dev , vol.9 , pp. 49-54
    • Dennis, P.B.1    Fumagalli, S.2    Thomas, G.3
  • 3
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • A.C. Gingras, B. Raught and N. Sonenberg (2001) Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15(7), 807-826.
    • (2001) Genes Dev , vol.15 , Issue.7 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 4
    • 0030666262 scopus 로고    scopus 로고
    • Molecular mechanisms for the control of translation by insulin
    • C.G. Proud and R.M. Denton (1997) Molecular mechanisms for the control of translation by insulin. Biochem. J. 328(Pt 2), 329-341.
    • (1997) Biochem. J , vol.328 , pp. 329-341
    • Proud, C.G.1    Denton, R.M.2
  • 5
    • 0033772338 scopus 로고    scopus 로고
    • An “encore” for ribosome biogenesis in cell proliferation
    • G. Thomas (2000) An “encore” for ribosome biogenesis in cell proliferation. Nat. Cell Biol. 2 E71-E72.
    • (2000) Nat. Cell Biol , vol.2 , pp. E71-E72
    • Thomas, G.1
  • 6
    • 0004041025 scopus 로고    scopus 로고
    • Translational control of ribosomal protein mRNAs in eukaryotes
    • J.W.B. Hershey, M.B. Mathews, N. Sonenberg,(Eds), Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • O. Meyuhas, D. Avni and S. Shama (1996) Translational control of ribosomal protein mRNAs in eukaryotes. J.W.B. Hershey, M.B. Mathews, N. Sonenberg,(Eds) Translational Control Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press 363-388.
    • (1996) Translational Control , pp. 363-388
    • Meyuhas, O.1    Avni, D.2    Shama, S.3
  • 7
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • O. Meyuhas (2000) Synthesis of the translational apparatus is regulated at the translational level. Eur. J. Biochem. 267(21), 6321-6330.
    • (2000) Eur. J. Biochem , vol.267 , Issue.21 , pp. 6321-6330
    • Meyuhas, O.1
  • 8
    • 0032568269 scopus 로고    scopus 로고
    • Translation control: connecting mitogens and the ribosome
    • R.T. Peterson and S.L. Schreiber (1998) Translation control: connecting mitogens and the ribosome. Curr. Biol. 8 R248-R250.
    • (1998) Curr. Biol , vol.8 , pp. R248-R250
    • Peterson, R.T.1    Schreiber, S.L.2
  • 9
    • 0027519385 scopus 로고
    • Regulation of rDNA transcription by insulin in primary cultures of rat hepatocytes
    • D.A. Antonetti, et al. (1993) Regulation of rDNA transcription by insulin in primary cultures of rat hepatocytes. J. Biol. Chem. 268(34), 25277-25284.
    • (1993) J. Biol. Chem , vol.268 , Issue.34 , pp. 25277-25284
    • Antonetti, D.A.1
  • 10
    • 0034009229 scopus 로고    scopus 로고
    • Signalling through the insulin receptor
    • J.P. Whitehead (2000) Signalling through the insulin receptor. Curr. Opin Cell Biol. 12(2), 222-228.
    • (2000) Curr. Opin Cell Biol , vol.12 , Issue.2 , pp. 222-228
    • Whitehead, J.P.1
  • 11
    • 0040175067 scopus 로고    scopus 로고
    • Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction
    • M. Frodin and S. Gammeltoft (1999) Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction. Mol. Cell Endocrinol. 151(1–2), 65-77.
    • (1999) Mol. Cell Endocrinol , vol.151 , Issue.1-2 , pp. 65-77
    • Frodin, M.1    Gammeltoft, S.2
  • 12
    • 0032929762 scopus 로고    scopus 로고
    • Signalling through phosphoinositide 3-kinases: The lipids take centre stage
    • S.J. Leevers, B. Vanhaesebroeck and M.D. Waterfield (1999) Signalling through phosphoinositide 3-kinases: The lipids take centre stage. Curr. Opin Cell Biol. 11(2), 219-225.
    • (1999) Curr. Opin Cell Biol , vol.11 , Issue.2 , pp. 219-225
    • Leevers, S.J.1    Vanhaesebroeck, B.2    Waterfield, M.D.3
  • 13
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: a hard Akt to follow
    • D.P. Brazil and B.A. Hemmings (2001) Ten years of protein kinase B signalling: a hard Akt to follow. Trends Biochem. Sci. 26(11), 657-664.
    • (2001) Trends Biochem. Sci , vol.26 , Issue.11 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 14
    • 0032904432 scopus 로고    scopus 로고
    • PTEN: A tumour suppressor that functions as a phospholipid phosphatase
    • T. Maehama and J.E. Dixon (1999) PTEN: A tumour suppressor that functions as a phospholipid phosphatase. Trends Cell Biol. 9(4), 125-128.
    • (1999) Trends Cell Biol , vol.9 , Issue.4 , pp. 125-128
    • Maehama, T.1    Dixon, J.E.2
  • 15
    • 0030740005 scopus 로고    scopus 로고
    • s6k
    • N. Pullen and G. Thomas (1997) The modular phosphorylation and activation of p70s6k. FEBS Lett. 410 78-82.
    • (1997) FEBS Lett , vol.410 , pp. 78-82
    • Pullen, N.1    Thomas, G.2
  • 16
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • V.M. Pain (1996) Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236(3), 747-771.
    • (1996) Eur. J. Biochem , vol.236 , Issue.3 , pp. 747-771
    • Pain, V.M.1
  • 17
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • G.I. Welsh and C.G. Proud (1993) Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. 294 625-629.
    • (1993) Biochem. J , vol.294 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 18
    • 0029049719 scopus 로고
    • Phosphorylation of sites 3a and 3b (Ser640 and Ser644) in the control of rabbit muscle glycogen synthase
    • A.V. Skurat and P.J. Roach (1995) Phosphorylation of sites 3a and 3b (Ser640 and Ser644) in the control of rabbit muscle glycogen synthase. J. Biol. Chem. 270(21), 12491-12497.
    • (1995) J. Biol. Chem , vol.270 , Issue.21 , pp. 12491-12497
    • Skurat, A.V.1    Roach, P.J.2
  • 19
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • D.A. Cross, et al. (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1
  • 20
    • 0021246806 scopus 로고
    • Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2
    • C.A. Towle, et al. (1984) Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2. Biochem. Biophys. Res. Commun. 121 134-140.
    • (1984) Biochem. Biophys. Res. Commun , vol.121 , pp. 134-140
    • Towle, C.A.1
  • 21
    • 0035912725 scopus 로고    scopus 로고
    • Molecular mechanisms of translation initiation in eukaryotes
    • T.V. Pestova, et al. (2001) Molecular mechanisms of translation initiation in eukaryotes. Proc. Natl. Acad. Sci. USA 98(13), 7029-7036.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.13 , pp. 7029-7036
    • Pestova, T.V.1
  • 22
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • F. Rozen, et al. (1990) Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell Biol. 10(3), 1134-1144.
    • (1990) Mol. Cell Biol , vol.10 , Issue.3 , pp. 1134-1144
    • Rozen, F.1
  • 23
    • 0023124676 scopus 로고
    • Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control: Heat shock effects eIF-4F
    • R. Duncan, S.C. Milburn and J.W.B. Hershey (1987) Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control: Heat shock effects eIF-4F. J. Biol. Chem. 262 380-388.
    • (1987) J. Biol. Chem , vol.262 , pp. 380-388
    • Duncan, R.1    Milburn, S.C.2    Hershey, J.W.B.3
  • 24
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • A.J. Waskiewicz, et al. (1999) Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell Biol. 19(3), 1871-1880.
    • (1999) Mol. Cell Biol , vol.19 , Issue.3 , pp. 1871-1880
    • Waskiewicz, A.J.1
  • 25
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E
    • S. Pyronnet, et al. (1999) Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J. 18(1), 270-279.
    • (1999) EMBO J , vol.18 , Issue.1 , pp. 270-279
    • Pyronnet, S.1
  • 26
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • W.B. Minich, et al. (1994) Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. USA 91 7668-7672.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1
  • 27
    • 0034928792 scopus 로고    scopus 로고
    • Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2
    • U. Knauf, C. Tschopp and H. Gram (2001) Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol. Cell Biol. 21(16), 5500-5511.
    • (2001) Mol. Cell Biol , vol.21 , Issue.16 , pp. 5500-5511
    • Knauf, U.1    Tschopp, C.2    Gram, H.3
  • 28
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • A. Pause, et al. (1994) Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371 762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1
  • 29
    • 0029095931 scopus 로고
    • Control of PHAS-I by insulin in 3T3-L1 adipocytes
    • T.A. Lin, et al. (1995) Control of PHAS-I by insulin in 3T3-L1 adipocytes. J. Biol. Chem. 270 18531-18538.
    • (1995) J. Biol. Chem , vol.270 , pp. 18531-18538
    • Lin, T.A.1
  • 30
    • 0035498939 scopus 로고    scopus 로고
    • Hierarchical phosphorylation of the translation inhibitor 4E-BP1
    • A.C. Gingras, et al. (2001) Hierarchical phosphorylation of the translation inhibitor 4E-BP1. Genes Dev. 15(21), 2852-2864.
    • (2001) Genes Dev , vol.15 , Issue.21 , pp. 2852-2864
    • Gingras, A.C.1
  • 31
    • 0035881470 scopus 로고    scopus 로고
    • Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase
    • X. Wang, et al. (2001) Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J. 20(16), 4370-4379.
    • (2001) EMBO J , vol.20 , Issue.16 , pp. 4370-4379
    • Wang, X.1
  • 32
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • B. Raught, et al. (2000) Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19(3), 434-444.
    • (2000) EMBO J , vol.19 , Issue.3 , pp. 434-444
    • Raught, B.1
  • 33
    • 19044364287 scopus 로고    scopus 로고
    • Quick guide: Target of rapamycin
    • P.B. Dennis and G. Thomas (2002) Quick guide: Target of rapamycin. Curr. Biol. 12(8), R269.
    • (2002) Curr. Biol , vol.12 , Issue.8 , pp. R269
    • Dennis, P.B.1    Thomas, G.2
  • 34
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • A. Sekulic, et al. (2000) A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res. 60(13), 3504-3513.
    • (2000) Cancer Res , vol.60 , Issue.13 , pp. 3504-3513
    • Sekulic, A.1
  • 35
    • 0035798097 scopus 로고    scopus 로고
    • Mammalian TOR: A homeostatic ATP sensor
    • P.B. Dennis, et al. (2001) Mammalian TOR: A homeostatic ATP sensor. Science 294(5544), 1102-1105.
    • (2001) Science , vol.294 , Issue.5544 , pp. 1102-1105
    • Dennis, P.B.1
  • 36
    • 0034312279 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of dTOR, the Drosophila homolog of the target of rapamycin
    • S. Oldham, et al. (2000) Genetic and biochemical characterization of dTOR, the Drosophila homolog of the target of rapamycin. Genes Dev. 14(21), 2689-2694.
    • (2000) Genes Dev , vol.14 , Issue.21 , pp. 2689-2694
    • Oldham, S.1
  • 37
    • 0036501277 scopus 로고    scopus 로고
    • A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells
    • D.J. Kwiatkowski, et al. (2002) A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells. Hum Mol. Genet. 11(5), 525-534.
    • (2002) Hum Mol. Genet , vol.11 , Issue.5 , pp. 525-534
    • Kwiatkowski, D.J.1
  • 38
    • 0037191045 scopus 로고    scopus 로고
    • Tuberous sclerosis complex tumor suppressor-mediated S6 kinase inhibition by phosphatidylinositide-3-OH kinase is mTOR independent
    • A. Jaeschke, et al. (2002) Tuberous sclerosis complex tumor suppressor-mediated S6 kinase inhibition by phosphatidylinositide-3-OH kinase is mTOR independent. J. Cell Biol. 159(2), 217-224.
    • (2002) J. Cell Biol , vol.159 , Issue.2 , pp. 217-224
    • Jaeschke, A.1
  • 39
    • 0037108682 scopus 로고    scopus 로고
    • Activated mammalian target of rapamycin pathway in the pathogenesis of tuberous sclerosis complex renal tumors
    • H.L. Kenerson, et al. (2002) Activated mammalian target of rapamycin pathway in the pathogenesis of tuberous sclerosis complex renal tumors. Cancer Res. 62(20), 5645-5650.
    • (2002) Cancer Res , vol.62 , Issue.20 , pp. 5645-5650
    • Kenerson, H.L.1
  • 40
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • K. Inoki, et al. (2002) TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4(9), 648-657.
    • (2002) Nat. Cell Biol , vol.4 , Issue.9 , pp. 648-657
    • Inoki, K.1
  • 41
    • 0036712905 scopus 로고    scopus 로고
    • Tsc tumour suppressor proteins antagonize amino-acid-TOR signalling
    • X. Gao, et al. (2002) Tsc tumour suppressor proteins antagonize amino-acid-TOR signalling. Nat. Cell Biol. 4(9), 699-704.
    • (2002) Nat. Cell Biol , vol.4 , Issue.9 , pp. 699-704
    • Gao, X.1
  • 42
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • B.D. Manning, et al. (2002) Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10(1), 151-162.
    • (2002) Mol. Cell , vol.10 , Issue.1 , pp. 151-162
    • Manning, B.D.1
  • 43
    • 0028356914 scopus 로고
    • Vertebrate mRNAs with a 5′-terminal pyrimidine tract are candidates for translation repression in quiescent cells. Characterization of the translational cis-regulatory element (TLRE)
    • D. Avni, et al. (1994) Vertebrate mRNAs with a 5′-terminal pyrimidine tract are candidates for translation repression in quiescent cells. Characterization of the translational cis-regulatory element (TLRE). Mol. Cell. Biol. 14 3822-3833.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 3822-3833
    • Avni, D.1
  • 44
    • 0028207001 scopus 로고
    • Rapamycin selectively represses translation of the “polypyrimidine tract” mRNA family
    • H.B.J. Jefferies, et al. (1994) Rapamycin selectively represses translation of the “polypyrimidine tract” mRNA family. Proc. Natl. Acad. Sci. USA 91 4441-4445.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4441-4445
    • Jefferies, H.B.J.1
  • 45
    • 0030915898 scopus 로고    scopus 로고
    • s6k
    • H.B.J. Jefferies, et al. (1997) Rapamycin suppresses 5′TOP mRNA translation through inhibition of p70s6k. EMBO J. 12 3693-3704.
    • (1997) EMBO J , vol.12 , pp. 3693-3704
    • Jefferies, H.B.J.1
  • 46
    • 0001798492 scopus 로고    scopus 로고
    • S6 phosphorylation and signal transduction
    • N. Sonenberg, J.W.B. Hershey, M.B. Mathews,(Eds), Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • S. Fumagalli and G. Thomas (2000) S6 phosphorylation and signal transduction. N. Sonenberg, J.W.B. Hershey, M.B. Mathews,(Eds) Translational Control of Gene Expression Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • (2000) Translational Control of Gene Expression
    • Fumagalli, S.1    Thomas, G.2
  • 47
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • E.F. Blommaart, et al. (1995) Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J. Biol. Chem. 270(5), 2320-2326.
    • (1995) J. Biol. Chem , vol.270 , Issue.5 , pp. 2320-2326
    • Blommaart, E.F.1
  • 48
    • 0026584008 scopus 로고
    • Autophagy and other vacuolar protein degradation mechanisms
    • P.O. Seglen and P. Bohley (1992) Autophagy and other vacuolar protein degradation mechanisms. Experientia 48(2), 158-172.
    • (1992) Experientia , vol.48 , Issue.2 , pp. 158-172
    • Seglen, P.O.1    Bohley, P.2
  • 49
    • 0030957959 scopus 로고    scopus 로고
    • Autophagic proteolysis: control and specificity
    • E.F. Blommaart, J.J. Luiken and A.J. Meijer (1997) Autophagic proteolysis: control and specificity. Histochem J. 29(5), 365-385.
    • (1997) Histochem J , vol.29 , Issue.5 , pp. 365-385
    • Blommaart, E.F.1    Luiken, J.J.2    Meijer, A.J.3
  • 50
    • 0025868969 scopus 로고
    • Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes
    • N.T. Price, et al. (1991) Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes. FEBS Lett. 282(2), 253-258.
    • (1991) FEBS Lett , vol.282 , Issue.2 , pp. 253-258
    • Price, N.T.1
  • 51
    • 0029966106 scopus 로고    scopus 로고
    • Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway
    • N.T. Redpath, E.J. Foulstone and C.G. Proud (1996) Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway. EMBO J. 15 2291-2297.
    • (1996) EMBO J , vol.15 , pp. 2291-2297
    • Redpath, N.T.1    Foulstone, E.J.2    Proud, C.G.3
  • 52
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • A.R. Saltiel and C.R. Kahn (2001) Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414(6865), 799-806.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 53
    • 0033049422 scopus 로고    scopus 로고
    • Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts
    • Q. Wang, et al. (1999) Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts. Mol. Cell Biol. 19(6), 4008-4018.
    • (1999) Mol. Cell Biol , vol.19 , Issue.6 , pp. 4008-4018
    • Wang, Q.1
  • 54
    • 0031724590 scopus 로고    scopus 로고
    • Requirement of atypical protein kinase clambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes
    • K. Kotani, et al. (1998) Requirement of atypical protein kinase clambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes. Mol. Cell Biol. 18(12), 6971-6982.
    • (1998) Mol. Cell Biol , vol.18 , Issue.12 , pp. 6971-6982
    • Kotani, K.1
  • 55
    • 0034830519 scopus 로고    scopus 로고
    • GLUT-4 translocation in skeletal muscle studied with a cell-free assay: involvement of phospholipase D
    • S. Kristiansen, et al. (2001) GLUT-4 translocation in skeletal muscle studied with a cell-free assay: involvement of phospholipase D. Am. J. Physiol. Endocrinol. Metab. 281(3), E608-E618.
    • (2001) Am. J. Physiol. Endocrinol. Metab , vol.281 , Issue.3 , pp. E608-E618
    • Kristiansen, S.1
  • 56
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • K. Gottlob, et al. (2001) Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev. 15(11), 1406-1418.
    • (2001) Genes Dev , vol.15 , Issue.11 , pp. 1406-1418
    • Gottlob, K.1
  • 57
    • 0034177152 scopus 로고    scopus 로고
    • Partial purification and characterization of a wortmannin-sensitive and insulin-stimulated protein kinase that activates heart 6-phosphofructo-2-kinase
    • J. Deprez, et al. (2000) Partial purification and characterization of a wortmannin-sensitive and insulin-stimulated protein kinase that activates heart 6-phosphofructo-2-kinase. Biochem. J. 347(Pt 1), 305-312.
    • (2000) Biochem. J , vol.347 , pp. 305-312
    • Deprez, J.1
  • 58
    • 0032741437 scopus 로고    scopus 로고
    • Heart 6-phosphofructo-2-kinase activation by insulin results from Ser-466 and Ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase B
    • L. Bertrand, et al. (1999) Heart 6-phosphofructo-2-kinase activation by insulin results from Ser-466 and Ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase B. J. Biol. Chem. 274(43), 30927-30933.
    • (1999) J. Biol. Chem , vol.274 , Issue.43 , pp. 30927-30933
    • Bertrand, L.1
  • 59
    • 0032409588 scopus 로고    scopus 로고
    • Regulation of System A amino acid transport in L6 rat skeletal muscle cells by insulin, chemical and hyperthermic stress
    • H.E. McDowell, P.A. Eyers and H.S. Hundal (1998) Regulation of System A amino acid transport in L6 rat skeletal muscle cells by insulin, chemical and hyperthermic stress. FEBS lett. 441(1), 15-19.
    • (1998) FEBS lett , vol.441 , Issue.1 , pp. 15-19
    • McDowell, H.E.1    Eyers, P.A.2    Hundal, H.S.3
  • 60
    • 0029124249 scopus 로고
    • Insulin stimulates cationic amino acid transport activity in the isolated perfused rat pancreas
    • M. Munoz, J.H. Sweiry and G.E. Mann (1995) Insulin stimulates cationic amino acid transport activity in the isolated perfused rat pancreas. Exp. Physiol. 80(5), 745-753.
    • (1995) Exp. Physiol , vol.80 , Issue.5 , pp. 745-753
    • Munoz, M.1    Sweiry, J.H.2    Mann, G.E.3
  • 61
    • 0034847757 scopus 로고    scopus 로고
    • Amino acid regulation of gene expression
    • discussion 2486S–2487S
    • L.S. Jefferson and S.R. Kimball (2001) Amino acid regulation of gene expression. J. Nutr. 131(9 Suppl), 2460S-2466S. discussion 2486S–2487S
    • (2001) J. Nutr , vol.131 , Issue.9 , pp. 2460S-2466S
    • Jefferson, L.S.1    Kimball, S.R.2
  • 62
    • 0033597129 scopus 로고    scopus 로고
    • Leucine regulates translation of specific mRNAs in L6 myoblasts through mTOR-mediated changes in availability of eIF4E and phosphorylation of ribosomal protein S6
    • S.R. Kimball, et al. (1999) Leucine regulates translation of specific mRNAs in L6 myoblasts through mTOR-mediated changes in availability of eIF4E and phosphorylation of ribosomal protein S6. J. Biol. Chem. 274(17), 11647-11652.
    • (1999) J. Biol. Chem , vol.274 , Issue.17 , pp. 11647-11652
    • Kimball, S.R.1
  • 63
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • T. Schmelzle and M.N. Hall (2000) TOR, a central controller of cell growth. Cell 103(2), 193-200.
    • (2000) Cell , vol.103 , Issue.2 , pp. 193-200
    • Schmelzle, T.1    Hall, M.N.2
  • 64
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macro-autophagy in HT-29 cells
    • A. Petiot, et al. (2000) Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macro-autophagy in HT-29 cells. J. Biol. Chem. 275(2), 992-998.
    • (2000) J. Biol. Chem , vol.275 , Issue.2 , pp. 992-998
    • Petiot, A.1
  • 65
    • 0033534734 scopus 로고    scopus 로고
    • Regulation of translational effectors by amino acid and mammalian target of rapamycin signaling pathways. Possible involvement of autophagy in cultured hepatoma cells
    • K. Shigemitsu, et al. (1999) Regulation of translational effectors by amino acid and mammalian target of rapamycin signaling pathways. Possible involvement of autophagy in cultured hepatoma cells. J. Biol. Chem. 274(2), 1058-1065.
    • (1999) J. Biol. Chem , vol.274 , Issue.2 , pp. 1058-1065
    • Shigemitsu, K.1
  • 66
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • S. Arico, et al. (2001) The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway. J. Biol. Chem. 276(38), 35243-35246.
    • (2001) J. Biol. Chem , vol.276 , Issue.38 , pp. 35243-35246
    • Arico, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.