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Volumn 21, Issue 3, 2015, Pages 479-492

Translational tolerance of mitochondrial genes to metabolic energy stress involves TISU and eIF1-eIF4GI cooperation in start codon selection

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 1; INITIATION FACTOR 1A; INITIATION FACTOR 2ALPHA; INITIATION FACTOR 3; INITIATION FACTOR 4E; INITIATION FACTOR 4F; INITIATION FACTOR 4G; INITIATION FACTOR 4GI; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; EIF1 PROTEIN, HUMAN; EIF4G1 PROTEIN, HUMAN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; INITIATION FACTOR; MESSENGER RNA; MITOCHONDRIAL MESSENGER RNA; NERVE PROTEIN; PRKAG1 PROTEIN, HUMAN; PRKAG2 PROTEIN, HUMAN; START CODON; TUMOR PROTEIN;

EID: 84924371001     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2015.02.010     Document Type: Article
Times cited : (73)

References (53)
  • 1
    • 0034307347 scopus 로고    scopus 로고
    • A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo
    • K. Asano, J. Clayton, A. Shalev, and A.G. Hinnebusch A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo Genes Dev. 14 2000 2534 2546
    • (2000) Genes Dev. , vol.14 , pp. 2534-2546
    • Asano, K.1    Clayton, J.2    Shalev, A.3    Hinnebusch, A.G.4
  • 3
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • D.R. Bolster, S.J. Crozier, S.R. Kimball, and L.S. Jefferson AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling J. Biol. Chem. 277 2002 23977 23980
    • (2002) J. Biol. Chem. , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 4
    • 66149118241 scopus 로고    scopus 로고
    • Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans
    • S.E. Calvo, D.J. Pagliarini, and V.K. Mootha Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans Proc. Natl. Acad. Sci. USA 106 2009 7507 7512
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7507-7512
    • Calvo, S.E.1    Pagliarini, D.J.2    Mootha, V.K.3
  • 8
    • 0037134910 scopus 로고    scopus 로고
    • Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase
    • P.F. Dubbelhuis, and A.J. Meijer Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase FEBS Lett. 521 2002 39 42
    • (2002) FEBS Lett. , vol.521 , pp. 39-42
    • Dubbelhuis, P.F.1    Meijer, A.J.2
  • 9
    • 52449118496 scopus 로고    scopus 로고
    • A translation initiation element specific to mRNAs with very short 5'UTR that also regulates transcription
    • R. Elfakess, and R. Dikstein A translation initiation element specific to mRNAs with very short 5'UTR that also regulates transcription PLoS ONE 3 2008 e3094
    • (2008) PLoS ONE , vol.3 , pp. e3094
    • Elfakess, R.1    Dikstein, R.2
  • 11
    • 0041589832 scopus 로고    scopus 로고
    • The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection
    • H. He, T. von der Haar, C.R. Singh, M. Ii, B. Li, A.G. Hinnebusch, J.E. McCarthy, and K. Asano The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection Mol. Cell. Biol. 23 2003 5431 5445
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5431-5445
    • He, H.1    Von Der Haar, T.2    Singh, C.R.3    Ii, M.4    Li, B.5    Hinnebusch, A.G.6    McCarthy, J.E.7    Asano, K.8
  • 12
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • A.G. Hinnebusch Molecular mechanism of scanning and start codon selection in eukaryotes Microbiol. Mol. Biol. Rev. 75 2011 434 467
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 13
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • H. Imataka, and N. Sonenberg Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A Mol. Cell. Biol. 17 1997 6940 6947
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 14
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • H. Imataka, A. Gradi, and N. Sonenberg A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation EMBO J. 17 1998 7480 7489
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 15
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • K. Inoki, T. Zhu, and K.L. Guan TSC2 mediates cellular energy response to control cell growth and survival Cell 115 2003 577 590
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 16
    • 78149277351 scopus 로고    scopus 로고
    • Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1)
    • I.P. Ivanov, G. Loughran, M.S. Sachs, and J.F. Atkins Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1) Proc. Natl. Acad. Sci. USA 107 2010 18056 18060
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18056-18060
    • Ivanov, I.P.1    Loughran, G.2    Sachs, M.S.3    Atkins, J.F.4
  • 17
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • R.J. Jackson, C.U. Hellen, and T.V. Pestova The mechanism of eukaryotic translation initiation and principles of its regulation Nat. Rev. Mol. Cell Biol. 11 2010 113 127
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 18
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha
    • S. Jäger, C. Handschin, J. St-Pierre, and B.M. Spiegelman AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha Proc. Natl. Acad. Sci. USA 104 2007 12017 12022
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12017-12022
    • Jäger, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 20
    • 0034731347 scopus 로고    scopus 로고
    • Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1
    • N.L. Korneeva, B.J. Lamphear, F.L. Hennigan, and R.E. Rhoads Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1 J. Biol. Chem. 275 2000 41369 41376
    • (2000) J. Biol. Chem. , vol.275 , pp. 41369-41376
    • Korneeva, N.L.1    Lamphear, B.J.2    Hennigan, F.L.3    Rhoads, R.E.4
  • 21
    • 0021760394 scopus 로고
    • Selection of initiation sites by eucaryotic ribosomes: Effect of inserting AUG triplets upstream from the coding sequence for preproinsulin
    • M. Kozak Selection of initiation sites by eucaryotic ribosomes: effect of inserting AUG triplets upstream from the coding sequence for preproinsulin Nucleic Acids Res. 12 1984 3873 3893
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3873-3893
    • Kozak, M.1
  • 22
    • 0005218668 scopus 로고
    • Influences of mRNA secondary structure on initiation by eukaryotic ribosomes
    • M. Kozak Influences of mRNA secondary structure on initiation by eukaryotic ribosomes Proc. Natl. Acad. Sci. USA 83 1986 2850 2854
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2850-2854
    • Kozak, M.1
  • 23
    • 0026151096 scopus 로고
    • Effects of long 5′ leader sequences on initiation by eukaryotic ribosomes in vitro
    • M. Kozak Effects of long 5′ leader sequences on initiation by eukaryotic ribosomes in vitro Gene Expr. 1 1991 117 125
    • (1991) Gene Expr. , vol.1 , pp. 117-125
    • Kozak, M.1
  • 24
    • 0026151349 scopus 로고
    • A short leader sequence impairs the fidelity of initiation by eukaryotic ribosomes
    • M. Kozak A short leader sequence impairs the fidelity of initiation by eukaryotic ribosomes Gene Expr. 1 1991 111 115
    • (1991) Gene Expr. , vol.1 , pp. 111-115
    • Kozak, M.1
  • 25
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • M. Kozak Structural features in eukaryotic mRNAs that modulate the initiation of translation J. Biol. Chem. 266 1991 19867 19870
    • (1991) J. Biol. Chem. , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 26
    • 0032212132 scopus 로고    scopus 로고
    • Primer extension analysis of eukaryotic ribosome-mRNA complexes
    • M. Kozak Primer extension analysis of eukaryotic ribosome-mRNA complexes Nucleic Acids Res. 26 1998 4853 4859
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4853-4859
    • Kozak, M.1
  • 27
    • 0036364274 scopus 로고    scopus 로고
    • Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes
    • U. Krause, L. Bertrand, and L. Hue Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes Eur. J. Biochem. 269 2002 3751 3759
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3751-3759
    • Krause, U.1    Bertrand, L.2    Hue, L.3
  • 28
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • M. Laplante, and D.M. Sabatini mTOR signaling in growth control and disease Cell 149 2012 274 293
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 30
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • J. Lin, C. Handschin, and B.M. Spiegelman Metabolic control through the PGC-1 family of transcription coactivators Cell Metab. 1 2005 361 370
    • (2005) Cell Metab. , vol.1 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 31
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • D. Maag, C.A. Fekete, Z. Gryczynski, and J.R. Lorsch A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon Mol. Cell 17 2005 265 275
    • (2005) Mol. Cell , vol.17 , pp. 265-275
    • Maag, D.1    Fekete, C.A.2    Gryczynski, Z.3    Lorsch, J.R.4
  • 32
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • S. Mader, H. Lee, A. Pause, and N. Sonenberg The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins Mol. Cell. Biol. 15 1995 4990 4997
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 34
    • 83255187893 scopus 로고    scopus 로고
    • Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons
    • P. Martin-Marcos, Y.N. Cheung, and A.G. Hinnebusch Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons Mol. Cell. Biol. 31 2011 4814 4831
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4814-4831
    • Martin-Marcos, P.1    Cheung, Y.N.2    Hinnebusch, A.G.3
  • 35
    • 84884541284 scopus 로고    scopus 로고
    • β-Hairpin loop of eukaryotic initiation factor 1 (eIF1) mediates 40 S ribosome binding to regulate initiator tRNA(Met) recruitment and accuracy of AUG selection in vivo
    • P. Martin-Marcos, J. Nanda, R.E. Luna, G. Wagner, J.R. Lorsch, and A.G. Hinnebusch β-Hairpin loop of eukaryotic initiation factor 1 (eIF1) mediates 40 S ribosome binding to regulate initiator tRNA(Met) recruitment and accuracy of AUG selection in vivo J. Biol. Chem. 288 2013 27546 27562
    • (2013) J. Biol. Chem. , vol.288 , pp. 27546-27562
    • Martin-Marcos, P.1    Nanda, J.2    Luna, R.E.3    Wagner, G.4    Lorsch, J.R.5    Hinnebusch, A.G.6
  • 36
    • 84892748582 scopus 로고    scopus 로고
    • Enhanced eIF1 binding to the 40S ribosome impedes conformational rearrangements of the preinitiation complex and elevates initiation accuracy
    • P. Martin-Marcos, J.S. Nanda, R.E. Luna, F. Zhang, A.K. Saini, V.A. Cherkasova, G. Wagner, J.R. Lorsch, and A.G. Hinnebusch Enhanced eIF1 binding to the 40S ribosome impedes conformational rearrangements of the preinitiation complex and elevates initiation accuracy RNA 20 2014 150 167
    • (2014) RNA , vol.20 , pp. 150-167
    • Martin-Marcos, P.1    Nanda, J.S.2    Luna, R.E.3    Zhang, F.4    Saini, A.K.5    Cherkasova, V.A.6    Wagner, G.7    Lorsch, J.R.8    Hinnebusch, A.G.9
  • 37
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3
    • N. Méthot, M.S. Song, and N. Sonenberg A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3 Mol. Cell. Biol. 16 1996 5328 5334
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5328-5334
    • Méthot, N.1    Song, M.S.2    Sonenberg, N.3
  • 38
    • 55549118605 scopus 로고    scopus 로고
    • Should i stay or should i go? Eukaryotic translation initiation factors 1 and 1A control start codon recognition
    • S.F. Mitchell, and J.R. Lorsch Should I stay or should I go? Eukaryotic translation initiation factors 1 and 1A control start codon recognition J. Biol. Chem. 283 2008 27345 27349
    • (2008) J. Biol. Chem. , vol.283 , pp. 27345-27349
    • Mitchell, S.F.1    Lorsch, J.R.2
  • 41
    • 0021799353 scopus 로고
    • Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency
    • J. Pelletier, and N. Sonenberg Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency Cell 40 1985 515 526
    • (1985) Cell , vol.40 , pp. 515-526
    • Pelletier, J.1    Sonenberg, N.2
  • 42
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • T.V. Pestova, and V.G. Kolupaeva The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection Genes Dev. 16 2002 2906 2922
    • (2002) Genes Dev. , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 43
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • T.V. Pestova, S.I. Borukhov, and C.U. Hellen Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons Nature 394 1998 854 859
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.3
  • 44
    • 38449123748 scopus 로고    scopus 로고
    • Assembly and analysis of eukaryotic translation initiation complexes
    • A.V. Pisarev, A. Unbehaun, C.U. Hellen, and T.V. Pestova Assembly and analysis of eukaryotic translation initiation complexes Methods Enzymol. 430 2007 147 177
    • (2007) Methods Enzymol. , vol.430 , pp. 147-177
    • Pisarev, A.V.1    Unbehaun, A.2    Hellen, C.U.3    Pestova, T.V.4
  • 45
    • 17444415304 scopus 로고    scopus 로고
    • Repression of protein synthesis and mTOR signaling in rat liver mediated by the AMPK activator aminoimidazole carboxamide ribonucleoside
    • A.K. Reiter, D.R. Bolster, S.J. Crozier, S.R. Kimball, and L.S. Jefferson Repression of protein synthesis and mTOR signaling in rat liver mediated by the AMPK activator aminoimidazole carboxamide ribonucleoside Am. J. Physiol. Endocrinol. Metab. 288 2005 E980 E988
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.288 , pp. E980-E988
    • Reiter, A.K.1    Bolster, D.R.2    Crozier, S.J.3    Kimball, S.R.4    Jefferson, L.S.5
  • 46
    • 0025060769 scopus 로고
    • Translation initiation at a downstream AUG occurs with increased efficiency when the upstream AUG is located very close to the 5′ cap
    • S.A. Sedman, G.W. Gelembiuk, and J.E. Mertz Translation initiation at a downstream AUG occurs with increased efficiency when the upstream AUG is located very close to the 5′ cap J. Virol. 64 1990 453 457
    • (1990) J. Virol. , vol.64 , pp. 453-457
    • Sedman, S.A.1    Gelembiuk, G.W.2    Mertz, J.E.3
  • 47
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • N. Sonenberg, and A.G. Hinnebusch Regulation of translation initiation in eukaryotes: mechanisms and biological targets Cell 136 2009 731 745
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 48
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • L. Valásek, K.H. Nielsen, and A.G. Hinnebusch Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo EMBO J. 21 2002 5886 5898
    • (2002) EMBO J. , vol.21 , pp. 5886-5898
    • Valásek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 49
    • 84887853618 scopus 로고    scopus 로고
    • Human eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosome
    • N. Villa, A. Do, J.W. Hershey, and C.S. Fraser Human eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosome J. Biol. Chem. 288 2013 32932 32940
    • (2013) J. Biol. Chem. , vol.288 , pp. 32932-32940
    • Villa, N.1    Do, A.2    Hershey, J.W.3    Fraser, C.S.4
  • 50
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • W.W. Winder, B.F. Holmes, D.S. Rubink, E.B. Jensen, M. Chen, and J.O. Holloszy Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle J. Appl. Physiol. 88 2000 2219 2226
    • (2000) J. Appl. Physiol. , vol.88 , pp. 2219-2226
    • Winder, W.W.1    Holmes, B.F.2    Rubink, D.S.3    Jensen, E.B.4    Chen, M.5    Holloszy, J.O.6
  • 51
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • D. Yaffe, and O. Saxel Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle Nature 270 1977 725 727
    • (1977) Nature , vol.270 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2
  • 52
    • 62849126891 scopus 로고    scopus 로고
    • Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap
    • A. Yanagiya, Y.V. Svitkin, S. Shibata, S. Mikami, H. Imataka, and N. Sonenberg Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap Mol. Cell. Biol. 29 2009 1661 1669
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1661-1669
    • Yanagiya, A.1    Svitkin, Y.V.2    Shibata, S.3    Mikami, S.4    Imataka, H.5    Sonenberg, N.6
  • 53
    • 65349177200 scopus 로고    scopus 로고
    • AMPK: An emerging drug target for diabetes and the metabolic syndrome
    • B.B. Zhang, G. Zhou, and C. Li AMPK: an emerging drug target for diabetes and the metabolic syndrome Cell Metab. 9 2009 407 416
    • (2009) Cell Metab. , vol.9 , pp. 407-416
    • Zhang, B.B.1    Zhou, G.2    Li, C.3


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