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Volumn 300, Issue 3, 2011, Pages

Simvastatin represses protein synthesis in the muscle-derived C 2C12 cell line with a concomitant reduction in eukaryotic initiation factor 2B expression

Author keywords

3 hydroxy 3 methylglutaryl coenzyme A reductase; Messenger RNA translation; Myoblasts; Myotubes

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MESSENGER RNA; MEVALONIC ACID; PROTEASOME; SIMVASTATIN;

EID: 79952157824     PISSN: 01931849     EISSN: 15221555     Source Type: Journal    
DOI: 10.1152/ajpendo.00383.2010     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 38349074872 scopus 로고    scopus 로고
    • Hydrophobic statins induce autophagy in cultured human rhabdomyosarcoma cells
    • Araki M, Motojima K. Hydrophobic statins induce autophagy in cultured human rhabdomyosarcoma cells. Biochem Biophys Res Commun 367: 462-467, 2008.
    • (2008) Biochem Biophys Res Commun , vol.367 , pp. 462-467
    • Araki, M.1    Motojima, K.2
  • 3
    • 1642553650 scopus 로고    scopus 로고
    • Defective translational control facilitates vesicular stomatitis virus oncolysis
    • DOI 10.1016/S1535-6108(03)00330-1
    • Balachandran S, Barber GN. Defective translational control facilitates vesicular stomatitis virus oncolysis. Cancer Cell 5: 51-65, 2004. (Pubitemid 38121596)
    • (2004) Cancer Cell , vol.5 , Issue.1 , pp. 51-65
    • Balachandran, S.1    Barber, G.N.2
  • 4
    • 70349323604 scopus 로고    scopus 로고
    • Statin-induced muscle damage and atrogin-1 induction is the result of a geranylgeranylation defect
    • Cao P, Hanai J, Tanksale P, Imamura S, Sukhatme VP, Lecker SH. Statin-induced muscle damage and atrogin-1 induction is the result of a geranylgeranylation defect. FASEB J 23: 2844-2854, 2009.
    • (2009) FASEB J , vol.23 , pp. 2844-2854
    • Cao, P.1    Hanai, J.2    Tanksale, P.3    Imamura, S.4    Sukhatme, V.P.5    Lecker, S.H.6
  • 6
    • 4544333872 scopus 로고    scopus 로고
    • The proteasome inhibitor, MG132, promotes the reprogramming of translation in C2C12 myoblasts and facilitates the association of hsp25 with the eIF4F complex
    • DOI 10.1111/j.0014-2956.2004.04306.x
    • Cowan JL, Morley SJ. The proteasome inhibitor, MG132, promotes the reprogramming of translation in C2C12 myoblasts and facilitates the association of hsp25 with the eIF4F complex. Eur J Biochem 271: 3596-3611, 2004. (Pubitemid 39215350)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.17 , pp. 3596-3611
    • Cowan, J.L.1    Morley, S.J.2
  • 7
    • 35448961560 scopus 로고    scopus 로고
    • Selective inhibition of growth of Tuberous Sclerosis complex 2-null cells by atorvastatin is associated with impaired Rheb and Rho GTPase function and reduced mTOR/S6 kinase activity
    • DOI 10.1158/0008-5472.CAN-07-1394
    • Finlay GA, Malhowski AJ, Liu Y, Fanburg BL, Kwiatkowski DJ, Toksoz D. Selective inhibition of growth of tuberous sclerosis complex 2 null cells by atorvastatin is associated with impaired Rheb and Rho GTPase function and reduced mTOR/S6 kinase activity. Cancer Res 67: 9878-9886, 2007. (Pubitemid 47621236)
    • (2007) Cancer Research , vol.67 , Issue.20 , pp. 9878-9886
    • Finlay, G.A.1    Malhowski, A.J.2    Liu, Y.3    Fanburg, B.L.4    Kwiatkowski, D.J.5    Toksoz, D.6
  • 8
    • 0031194174 scopus 로고    scopus 로고
    • Inhibition of cholesterol synthesis by squalene synthase inhibitors does not induce myotoxicity in vitro
    • DOI 10.1006/taap.1997.8131
    • Flint OP, Masters BA, Gregg RE, Durham SK. Inhibition of cholesterol synthesis by squalene synthase inhibitors does not induce myotoxicity in vitro. Toxicol Appl Pharmacol 145: 91-98, 1997. (Pubitemid 27294774)
    • (1997) Toxicology and Applied Pharmacology , vol.145 , Issue.1 , pp. 91-98
    • Flint, O.P.1    Masters, B.A.2    Gregg, R.E.3    Durham, S.K.4
  • 9
    • 55349092971 scopus 로고    scopus 로고
    • Reduced eukaryotic initiation factor 2Bepsilon-subunit expression suppresses the transformed phenotype of cells overexpressing the protein
    • Gallagher JW, Kubica N, Kimball SR, Jefferson LS. Reduced eukaryotic initiation factor 2Bepsilon-subunit expression suppresses the transformed phenotype of cells overexpressing the protein. Cancer Res 68: 8752-8760, 2008.
    • (2008) Cancer Res , vol.68 , pp. 8752-8760
    • Gallagher, J.W.1    Kubica, N.2    Kimball, S.R.3    Jefferson, L.S.4
  • 10
    • 67749108145 scopus 로고    scopus 로고
    • History of the cholesterol hypothesis in Britain
    • Grimes DS. History of the cholesterol hypothesis in Britain. QJM 102: 436-438, 2009.
    • (2009) QJM , vol.102 , pp. 436-438
    • Grimes, D.S.1
  • 12
    • 1842863232 scopus 로고    scopus 로고
    • Phosphorylation of Eukaryotic Translation Initiation Factor 2Bepsilon by Glycogen Synthase Kinase-3beta Regulates beta-Adrenergic Cardiac Myocyte Hypertrophy
    • DOI 10.1161/01.RES.0000124977.59827.80
    • Hardt SE, Tomita H, Katus HA, Sadoshima J. Phosphorylation of eukaryotic translation initiation factor 2Bepsilon by glycogen synthase kinase-3beta regulates beta-adrenergic cardiac myocyte hypertrophy. Circ Res 94: 926-935, 2004. (Pubitemid 38490070)
    • (2004) Circulation Research , vol.94 , Issue.7 , pp. 926-935
    • Hardt, S.E.1    Tomita, H.2    Katus, H.A.3    Sadoshima, J.4
  • 13
    • 66149120589 scopus 로고    scopus 로고
    • Age-related deficit in load-induced skeletal muscle growth
    • Hwee DT, Bodine SC. Age-related deficit in load-induced skeletal muscle growth. J Gerontol A Biol Sci Med Sci 64: 618-628, 2009.
    • (2009) J Gerontol A Biol Sci Med Sci , vol.64 , pp. 618-628
    • Hwee, D.T.1    Bodine, S.C.2
  • 14
    • 0032967514 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle
    • DOI 10.1016/S1357-2725(98)00141-1, PII S1357272598001411
    • Jefferson LS, Fabian JR, Kimball SR. Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle. Int J Biochem Cell Biol 31: 191-200, 1999. (Pubitemid 29094799)
    • (1999) International Journal of Biochemistry and Cell Biology , vol.31 , Issue.1 , pp. 191-200
    • Jefferson, L.S.1    Fabian, J.R.2    Kimball, S.R.3
  • 15
    • 17144389838 scopus 로고    scopus 로고
    • Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
    • DOI 10.1074/jbc.M413660200
    • Jiang HY, Wek RC. Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition. J Biol Chem 280: 14189-14202, 2005. (Pubitemid 40517321)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14189-14202
    • Jiang, H.-Y.1    Wek, R.C.2
  • 16
    • 0032553411 scopus 로고    scopus 로고
    • Implication of eIF2B rather than eIF4E in the regulation of global protein synthesis by amino acids in L6 myoblasts
    • DOI 10.1074/jbc.273.47.30945
    • Kimball SR, Horetsky RL, Jefferson LS. Implication of eIF2B rather than eIF4E in the regulation of global protein synthesis by amino acids in L6 myoblasts. J Biol Chem 273: 30945-30953, 1998. (Pubitemid 28533098)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 30945-30953
    • Kimball, S.R.1    Horetsky, R.L.2    Jefferson, L.S.3
  • 17
    • 0030876593 scopus 로고    scopus 로고
    • A novel interaction between adrenergic receptors and the alpha-subunit of Eukaryotic initiation factor 2B
    • DOI 10.1074/jbc.272.31.19099
    • Klein U, Ramirez MT, Kobilka BK, von Zastrow M. A novel interaction between adrenergic receptors and the alpha-subunit of eukaryotic initiation factor 2B. J Biol Chem 272: 19099-19102, 1997. (Pubitemid 27337693)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19099-19102
    • Klein, U.1    Ramirez, M.T.2    Kobilka, B.K.3    Von, Z.M.4
  • 18
    • 48349096394 scopus 로고    scopus 로고
    • Activation of the mammalian target of rapamycin complex 1 is both necessary and sufficient to stimulate eukaryotic initiation factor 2Bvarepsilon mRNA translation and protein synthesis
    • Kubica N, Crispino JL, Gallagher JW, Kimball SR, Jefferson LS. Activation of the mammalian target of rapamycin complex 1 is both necessary and sufficient to stimulate eukaryotic initiation factor 2Bvarepsilon mRNA translation and protein synthesis. Int J Biochem Cell Biol 40: 2522-2533, 2008.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 2522-2533
    • Kubica, N.1    Crispino, J.L.2    Gallagher, J.W.3    Kimball, S.R.4    Jefferson, L.S.5
  • 20
    • 41549164284 scopus 로고    scopus 로고
    • Atorvastatin slows the progression of cardiac remodeling in mice with pressure overload and inhibits epidermal growth factor receptor activation
    • DOI 10.1291/hypres.31.335
    • Liao Y, Zhao H, Ogai A, Kato H, Asakura M, Kim J, Asanuma H, Minamino T, Takashima S, Kitakaze M. Atorvastatin slows the progression of cardiac remodeling in mice with pressure overload and inhibits epidermal growth factor receptor activation. Hypertens Res 31: 335-344, 2008. (Pubitemid 351461114)
    • (2008) Hypertension Research , vol.31 , Issue.2 , pp. 335-344
    • Liao, Y.1    Zhao, H.2    Ogai, A.3    Kato, H.4    Asakura, M.5    KIm, J.6    Asanuma, H.7    Minamino, T.8    Takashima, S.9    Kitakaze, M.10
  • 21
    • 58149307451 scopus 로고    scopus 로고
    • Blunted Akt/FOXO signalling and activation of genes controlling atrophy and fuel use in statin myopathy
    • Mallinson JE, Constantin-Teodosiu D, Sidaway J, Westwood FR, Greenhaff PL. Blunted Akt/FOXO signalling and activation of genes controlling atrophy and fuel use in statin myopathy. J Physiol 587: 219-230, 2009.
    • (2009) J Physiol , vol.587 , pp. 219-230
    • Mallinson, J.E.1    Constantin-Teodosiu, D.2    Sidaway, J.3    Westwood, F.R.4    Greenhaff, P.L.5
  • 22
    • 0028962803 scopus 로고
    • In vitro myotoxicity of the 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors, pravastatin, lovastatin, and simvastatin, using neonatal rat skeletal myocytes
    • Masters BA, Palmoski MJ, Flint OP, Gregg RE, Wang-Iverson D, Durham SK. In vitro myotoxicity of the 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors, pravastatin, lovastatin, and simvastatin, using neonatal rat skeletal myocytes. Toxicol Appl Pharmacol 131: 163-174, 1995.
    • (1995) Toxicol Appl Pharmacol , vol.131 , pp. 163-174
    • Masters, B.A.1    Palmoski, M.J.2    Flint, O.P.3    Gregg, R.E.4    Wang-Iverson, D.5    Durham, S.K.6
  • 23
    • 70350488075 scopus 로고    scopus 로고
    • Immunomodulatory and anti-inflammatory activities of statins
    • Mira E, Manes S. Immunomodulatory and anti-inflammatory activities of statins. Endocr Metab Immune Disord Drug Targets 9: 237-247, 2009.
    • (2009) Endocr Metab Immune Disord Drug Targets , vol.9 , pp. 237-247
    • Mira, E.1    Manes, S.2
  • 24
    • 33747033675 scopus 로고    scopus 로고
    • HMG-CoA reductase inhibitor fluvastatin prevents angiotensin II-induced cardiac hypertrophy via Rho kinase and inhibition of cyclin D1
    • DOI 10.1016/j.lfs.2006.04.005, PII S0024320506003304
    • Morikawa-Futamatsu K, Adachi S, Maejima Y, Tamamori-Adachi M, Suzuki J, Kitajima S, Ito H, Isobe M. HMG-CoA reductase inhibitor fluvastatin prevents angiotensin II-induced cardiac hypertrophy via Rho kinase and inhibition of cyclin D1. Life Sci 79: 1380-1390, 2006. (Pubitemid 44215930)
    • (2006) Life Sciences , vol.79 , Issue.14 , pp. 1380-1390
    • Morikawa-Futamatsu, K.1    Adachi, S.2    Maejima, Y.3    Tamamori-Adachi, M.4    Suzuki, J.-I.5    Kitajima, S.6    Ito, H.7    Isobe, M.8
  • 25
    • 0029758869 scopus 로고    scopus 로고
    • Itraconazole drastically increases plasma concentrations of lovastatin and lovastatin acid
    • Neuvonen PJ, Jalava KM. Itraconazole drastically increases plasma concentrations of lovastatin and lovastatin acid. Clin Pharmacol Ther 60: 54-61, 1996. (Pubitemid 26279221)
    • (1996) Clinical Pharmacology and Therapeutics , vol.60 , Issue.1 , pp. 54-61
    • Neuvonen, P.J.1    Jalava, K.-M.2
  • 26
    • 72049130254 scopus 로고    scopus 로고
    • Meta-analysis of comparative efficacy of increasing dose of Atorvastatin versus Rosuvastatin versus Simvastatin on lowering levels of atherogenic lipids (from VOYAGER)
    • Nicholls SJ, Brandrup-Wognsen G, Palmer M, Barter PJ. Meta-analysis of comparative efficacy of increasing dose of Atorvastatin versus Rosuvastatin versus Simvastatin on lowering levels of atherogenic lipids (from VOYAGER). Am J Cardiol 105: 69-76, 2010.
    • (2010) Am J Cardiol , vol.105 , pp. 69-76
    • Nicholls, S.J.1    Brandrup-Wognsen, G.2    Palmer, M.3    Barter, P.J.4
  • 27
    • 33847412697 scopus 로고    scopus 로고
    • Simvastatin reduces insulin-like growth factor-1 signaling in differentiating C2C12 mouse myoblast cells in an HMG-CoA reductase inhibition-independent manner
    • DOI 10.2131/jts.32.57
    • Ogura T, Tanaka Y, Nakata T, Namikawa T, Kataoka H, Ohtsubo Y. Simvastatin reduces insulin-like growth factor-1 signaling in differentiating C2C12 mouse myoblast cells in an HMG-CoA reductase inhibition-independent manner. J Toxicol Sci 32: 57-67, 2007. (Pubitemid 46334070)
    • (2007) Journal of Toxicological Sciences , vol.32 , Issue.1 , pp. 57-67
    • Ogura, T.1    Tanaka, Y.2    Nakata, T.3    Namikawa, T.4    Kataoka, H.5    Ohtsubo, Y.6
  • 28
    • 34548318655 scopus 로고    scopus 로고
    • Reduction of protein synthesis and statin-induced cardiomyocyte cell death
    • DOI 10.1007/s12012-007-0003-7
    • Rabkin SW, Lodha P, Kong JY. Reduction of protein synthesis and statin-induced cardiomyocyte cell death. Cardiovasc Toxicol 7: 1-9, 2007. (Pubitemid 47338489)
    • (2007) Cardiovascular Toxicology , vol.7 , Issue.1 , pp. 1-9
    • Rabkin, S.W.1    Lodha, P.2    Kong, J.Y.3
  • 29
    • 1542344340 scopus 로고    scopus 로고
    • Mutations Causing Childhood Ataxia with Central Nervous System Hypomyelination Reduce Eukaryotic Initiation Factor 2B Complex Formation and Activity
    • DOI 10.1128/MCB.24.6.2352-2363.2004
    • Richardson JP, Mohammad SS, Pavitt GD. Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity. Mol Cell Biol 24: 2352-2363, 2004. (Pubitemid 38325992)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.6 , pp. 2352-2363
    • Richardson, J.P.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 30
    • 0023878562 scopus 로고
    • The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2
    • Rowlands AG, Panniers R, Henshaw EC. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J Biol Chem 263: 5526-5533, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 5526-5533
    • Rowlands, A.G.1    Panniers, R.2    Henshaw, E.C.3
  • 31
    • 48249135492 scopus 로고    scopus 로고
    • Lovastatin effect in rat neuroblasts of the CNS: Inhibition of cap-dependent translation
    • Santa-Catalina MO, Garcia-Marin LJ, Bragado MJ. Lovastatin effect in rat neuroblasts of the CNS: inhibition of cap-dependent translation. J Neurochem 106: 1078-1091, 2008.
    • (2008) J Neurochem , vol.106 , pp. 1078-1091
    • Santa-Catalina, M.O.1    Garcia-Marin, L.J.2    Bragado, M.J.3
  • 32
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis
    • Scorsone KA, Panniers R, Rowlands AG, Henshaw EC. Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis. J Biol Chem 262: 14538-14543, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 33
    • 41349113141 scopus 로고    scopus 로고
    • Statin induced myotoxicity: The lactone forms are more potent than the acid forms in human skeletal muscle cells in vitro
    • Skottheim IB, Gedde-Dahl A, Hejazifar S, Hoel K, Asberg A. Statin induced myotoxicity: the lactone forms are more potent than the acid forms in human skeletal muscle cells in vitro. Eur J Pharm Sci 33: 317-325, 2008.
    • (2008) Eur J Pharm Sci , vol.33 , pp. 317-325
    • Skottheim, I.B.1    Gedde-Dahl, A.2    Hejazifar, S.3    Hoel, K.4    Asberg, A.5
  • 35
    • 77954932534 scopus 로고    scopus 로고
    • Ectopic expression of eIF2Bε in rat skeletal muscle rescues the sepsis-induced reduction in guanine nucleotide exchange activity and protein synthesis
    • Tuckow AP, Vary TC, Kimball SR, Jefferson LS. Ectopic expression of eIF2Bε in rat skeletal muscle rescues the sepsis-induced reduction in guanine nucleotide exchange activity and protein synthesis. Am J Physiol Endocrinol Metab 299: E241-E248, 2010.
    • (2010) Am J Physiol Endocrinol Metab , vol.299
    • Tuckow, A.P.1    Vary, T.C.2    Kimball, S.R.3    Jefferson, L.S.4
  • 36
    • 33644802663 scopus 로고    scopus 로고
    • Changes in ubiquitin proteasome pathway gene expression in skeletal muscle with exercise and statins
    • DOI 10.1161/01.ATV.0000190608.28704.71, PII 0004360520051200000019
    • Urso ML, Clarkson PM, Hittel D, Hoffman EP, Thompson PD. Changes in ubiquitin proteasome pathway gene expression in skeletal muscle with exercise and statins. Arterioscler Thromb Vasc Biol 25: 2560-2566, 2005. (Pubitemid 43732279)
    • (2005) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.25 , Issue.12 , pp. 2560-2566
    • Urso, M.L.1    Clarkson, P.M.2    Hittel, D.3    Hoffman, E.P.4    Thompson, P.D.5
  • 40
    • 40749151132 scopus 로고    scopus 로고
    • A novel mechanism for the control of translation initiation by amino acids, mediated by phosphorylation of eukaryotic initiation factor 2B
    • Wang X, Proud CG. A novel mechanism for the control of translation initiation by amino acids, mediated by phosphorylation of eukaryotic initiation factor 2B. Mol Cell Biol 28: 1429-1442, 2008.
    • (2008) Mol Cell Biol , vol.28 , pp. 1429-1442
    • Wang, X.1    Proud, C.G.2
  • 41
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • DOI 10.1016/S0014-5793(97)01548-2, PII S0014579397015482
    • Welsh GI, Miller CM, Loughlin AJ, Price NT, Proud CG. Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett 421: 125-130, 1998. (Pubitemid 28288076)
    • (1998) FEBS Letters , vol.421 , Issue.2 , pp. 125-130
    • Welsh, G.I.1    Miller, C.M.2    Loughlin, A.J.3    Price, N.T.4    Proud, C.G.5
  • 42
    • 0035830846 scopus 로고    scopus 로고
    • Characterization of the initiation factor eIF2B and its regulation in Drosophila melanogaster
    • Williams DD, Pavitt GD, Proud CG. Characterization of the initiation factor eIF2B and its regulation in Drosophila melanogaster. J Biol Chem 276: 3733-3742, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 3733-3742
    • Williams, D.D.1    Pavitt, G.D.2    Proud, C.G.3
  • 43
    • 33745894649 scopus 로고    scopus 로고
    • Simvastatin attenuates hypertrophic responses induced by cardiotrophin-1 via JAK-STAT pathway in cultured cardiomyocytes
    • DOI 10.1007/s11010-005-9014-5
    • Wu L, Zhao L, Zheng Q, Shang F, Wang X, Wang L, Lang B. Simvastatin attenuates hypertrophic responses induced by cardiotrophin-1 via JAK-STAT pathway in cultured cardiomyocytes. Mol Cell Biochem 284: 65-71, 2006. (Pubitemid 44404411)
    • (2006) Molecular and Cellular Biochemistry , vol.284 , Issue.1-2 , pp. 65-71
    • Wu, L.J.1    Zhao, L.Y.2    Zheng, Q.S.3    Shang, F.J.4    Wang, X.M.5    Wang, L.F.6    Lang, B.7
  • 44
    • 45349091778 scopus 로고    scopus 로고
    • Phosphorylation of eIF2alpha in response to 26S proteasome inhibition is mediated by the haem-regulated inhibitor (HRI) kinase
    • DOI 10.1042/BJ20080324
    • Yerlikaya A, Kimball SR, Stanley BA. Phosphorylation of eIF2alpha in response to 26S proteasome inhibition is mediated by the haem-regulated inhibitor (HRI) kinase. Biochem J 412: 579-588, 2008. (Pubitemid 351846423)
    • (2008) Biochemical Journal , vol.412 , Issue.3 , pp. 579-588
    • Yerlikaya, A.1    Kimball, S.R.2    Stanley, B.A.3


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