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Volumn 5, Issue 2, 2003, Pages 87-90

Signalling pathways that mediate skeletal muscle hypertrophy and atrophy

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; CALCINEURIN; CALCINEURIN INHIBITOR; CALMODULIN; CLENBUTEROL; CYCLOSPORIN A; DEXAMETHASONE; FK 506 BINDING PROTEIN; GLUCOCORTICOID; GLUCOSE; GLYCOGEN SYNTHASE KINASE 3; INSULIN RECEPTOR SUBSTRATE 1; LIPID; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEASOME INHIBITOR; PROTEIN KINASE B; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; RAPAMYCIN; RAS PROTEIN; S6 KINASE; SOMATOMEDIN C; TRANSCRIPTION FACTOR NFAT; UBIQUITIN PROTEIN LIGASE; UNINDEXED DRUG;

EID: 0037318822     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb0203-87     Document Type: Review
Times cited : (570)

References (52)
  • 1
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe, R.T. & Goldberg, A.L. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr. Opin. Clin. Nutr. Care 4, 183-190 (2001).
    • (2001) Curr. Opin. Clin. Nutr. Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 2
    • 0032760013 scopus 로고    scopus 로고
    • Lower recover of muscle protein lost during starvation in old rats despite a stimulation of protein synthesis
    • Mosoni, L. et al. Lower recover of muscle protein lost during starvation in old rats despite a stimulation of protein synthesis. Am. J. Physiol. Endocrinol. Metab. 277, E608-616 (1999).
    • (1999) Am. J. Physiol. Endocrinol. Metab. , vol.277
    • Mosoni, L.1
  • 3
    • 0035136062 scopus 로고    scopus 로고
    • Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
    • Musaro, A. et al. Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nature Genet. 27, 195-200 (2001).
    • (2001) Nature Genet. , vol.27 , pp. 195-200
    • Musaro, A.1
  • 4
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting - The role of the ubiquitin-proteasome pathway
    • Mitch, W.E. & Golberg, A.L. Mechanisms of muscle wasting - the role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 335, 1897-1905 (1996).
    • (1996) N. Engl. J. Med. , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Golberg, A.L.2
  • 5
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa, N.E. Jr, Odessey, R & Golberg, A.L. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J. Clin. Invest. 100, 197-203 (1997).
    • (1997) J. Clin. Invest. , vol.100 , pp. 197-203
    • Tawa N.E., Jr.1    Odessey, R.2    Golberg, A.L.3
  • 6
    • 0020660874 scopus 로고
    • Protein turnover measure in vivo and in nitro in muscles undergoing compensatory growth and subsequent denervation atrophy
    • Goldspink, D.F., Garlick, P.J. & McNurlan, M.A. Protein turnover measure in vivo and in nitro in muscles undergoing compensatory growth and subsequent denervation atrophy. Biochem. J. 210, 89-98 (1983).
    • (1983) Biochem. J. , vol.210 , pp. 89-98
    • Goldspink, D.F.1    Garlick, P.J.2    McNurlan, M.A.3
  • 7
    • 0025362896 scopus 로고
    • Activation of insulin-like growth factor gene expression during work-induced skeletal muscle growth
    • DeVol, D.L., Rotwein, P., Sadow, J.L., Novakofski, & Bechtel P.J. Activation of insulin-like growth factor gene expression during work-induced skeletal muscle growth. Am. J. Physiol. 259, E89-E95 (1990).
    • (1990) Am. J. Physiol. , vol.259
    • DeVol, D.L.1    Rotwein, P.2    Sadow, J.L.3    Novakofski, A.4    Bechtel, P.J.5
  • 8
    • 0029040848 scopus 로고
    • Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofibre hypertrophy in transgenic mice
    • Coleman, M.E. et al. Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofibre hypertrophy in transgenic mice. J. Biol. Chem. 270, 12109-12116 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12109-12116
    • Coleman, M.E.1
  • 9
    • 0033526991 scopus 로고    scopus 로고
    • IGH-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1
    • Musaro, A., McCullagh, K. J., Naya, F. J., Olson, E.N. & Rosenthal, N. IGH-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1 Nature 400, 581-585 (1999).
    • (1999) Nature , vol.400 , pp. 581-585
    • Musaro, A.1    McCullagh, K.J.2    Naya, F.J.3    Olson, E.N.4    Rosenthal, N.5
  • 10
    • 0033527021 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy is mediated by a calcium-dependent calcineurin signalling pathway
    • Semsarian, C. et al. Skeletal muscle hypertrophy is mediated by a calcium-dependent calcineurin signalling pathway. Nature 400, 576-581 (1999).
    • (1999) Nature , vol.400 , pp. 576-581
    • Semsarian, C.1
  • 11
    • 0033618462 scopus 로고    scopus 로고
    • Calcineurin is required for skeletal muscle hypertrophy
    • Dunn, S. E., Burns, J. L. & Michel, R. N. Calcineurin is required for skeletal muscle hypertrophy. J. Biol. Chem. 274, 21908-21912 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21908-21912
    • Dunn, S.E.1    Burns, J.L.2    Michel, R.N.3
  • 12
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine, S. C. et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nature Cell Biol. 3, 1014-1019 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 1014-1019
    • Bodine, S.C.1
  • 13
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel, C. et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nature Cell Biol. 3, 1009-1013 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 1009-1013
    • Rommel, C.1
  • 14
    • 0037018145 scopus 로고    scopus 로고
    • Nfat: Ubiquitous regulator of cell differentiation and adaptation
    • Horsley, V. & Pavlath, G. K. Nfat: ubiquitous regulator of cell differentiation and adaptation. J. Cell Biol. 156, 771-774 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 771-774
    • Horsley, V.1    Pavlath, G.K.2
  • 15
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • Molkentin, J.D. et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell 93, 215-228 (1998).
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1
  • 16
    • 0035818491 scopus 로고    scopus 로고
    • Calcineurin controls nerve activity-dependent specification of slow skeletal muscle fibres but not muscle growth
    • Serrano, A.L. et al. Calcineurin controls nerve activity-dependent specification of slow skeletal muscle fibres but not muscle growth. Proc. Natl Acad. Sci. USA 98, 13108-13113 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13108-13113
    • Serrano, A.L.1
  • 18
    • 0034681315 scopus 로고    scopus 로고
    • Stimulation of slow skeletal muscle fibre gene expression by calcineurin in vivo
    • Naya, F. J. et al. Stimulation of slow skeletal muscle fibre gene expression by calcineurin in vivo. J. Biol. Chem. 275, 4545-4548 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4545-4548
    • Naya, F.J.1
  • 19
    • 0034735544 scopus 로고    scopus 로고
    • Matching of calcineurin activity to upstream effectors is critical for skeletal muscle fibre growth
    • Dunn, S. E., Chin, E. R. & Michel, R. N. Matching of calcineurin activity to upstream effectors is critical for skeletal muscle fibre growth. J. Cell Biol. 151, 663-672 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 663-672
    • Dunn, S.E.1    Chin, E.R.2    Michel, R.N.3
  • 20
    • 0033780040 scopus 로고    scopus 로고
    • Ras is involved in nerve-activity-dependent regulation of muscle genes
    • Murgia, M. et al. Ras is involved in nerve-activity-dependent regulation of muscle genes. Nature Cell Biol. 2, 142-147 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 142-147
    • Murgia, M.1
  • 21
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco, I. & Sawyers, C. L. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nature Rev. Cancer 2, 489-501 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 22
    • 0036269886 scopus 로고    scopus 로고
    • Myogenic Akt signalling regulates blood vessel recruitment during myofibre growth
    • Takahashi, A. et al. Myogenic Akt signalling regulates blood vessel recruitment during myofibre growth. Mol. Cell Biol. 22, 4803-4814 (2002).
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4803-4814
    • Takahashi, A.1
  • 23
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fibre type specification
    • Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M. & Schiaffino, S. A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fibre type specification. Proc. Natl Acad. Sci. USA 99, 9213-9218 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 24
    • 0035448879 scopus 로고    scopus 로고
    • Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene
    • Chen, W.S. et al. Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene. Genes Dev. 15, 2203-2208 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2203-2208
    • Chen, W.S.1
  • 25
    • 0035368548 scopus 로고    scopus 로고
    • Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB β)
    • Cho, H. et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB β). Science 292, 1728-1731 (2001).
    • (2001) Science , vol.292 , pp. 1728-1731
    • Cho, H.1
  • 26
    • 0032475861 scopus 로고    scopus 로고
    • Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
    • Stambolic, V. et al. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell 95, 29-39 (1998).
    • (1998) Cell , vol.95 , pp. 29-39
    • Stambolic, V.1
  • 27
    • 0033572644 scopus 로고    scopus 로고
    • Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/P13-kinase signalling pathway
    • Goberdhan, D. C., Paricio, N., Goodman, E. C., Mlodzik, M. & Wilson , C. Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/P13-kinase signalling pathway. Genes Dev. 13, 3244-3258 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 3244-3258
    • Goberdhan, D.C.1    Paricio, N.2    Goodman, E.C.3    Mlodzik, M.4    Wilson, C.5
  • 28
    • 0033376684 scopus 로고    scopus 로고
    • PTEN affects cell size, cell proliferation and apoptosis dudring Drosophila eye development
    • Huang, H. et al. PTEN affects cell size, cell proliferation and apoptosis dudring Drosophila eye development. Development 126, 5365-5372 (1999).
    • (1999) Development , vol.126 , pp. 5365-5372
    • Huang, H.1
  • 29
    • 0035135318 scopus 로고    scopus 로고
    • Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3L1 adipocytes via its 5′-phosphatase catalytic activity
    • Wada, T. et al. Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3L1 adipocytes via its 5′-phosphatase catalytic activity. Mol. Cell. Biol. 21, 1633-1646 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1633-1646
    • Wada, T.1
  • 30
    • 0036094108 scopus 로고    scopus 로고
    • Essential role of Akt-1/Protein kinase Bα in PTEN-controlled tumorigenesis
    • Stiles, B. et al. Essential role of Akt-1/Protein kinase Bα in PTEN-controlled tumorigenesis. Mol. Cell. Biol. 22, 3842-3851 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3842-3851
    • Stiles, B.1
  • 31
    • 0035804251 scopus 로고    scopus 로고
    • The lipid phosphatase SHIP2 controls insulin sensitivity
    • Clement, S. et al. The lipid phosphatase SHIP2 controls insulin sensitivity. Nature 409, 92-97 (2001).
    • (2001) Nature , vol.409 , pp. 92-97
    • Clement, S.1
  • 32
    • 0029830237 scopus 로고    scopus 로고
    • The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth
    • Leevers, S. J., Weinkove, D., MacDougall, L. K., Hafen, E. & Waterfield, M. D. The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth. EMBO J. 15, 6584-6594 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6584-6594
    • Leevers, S.J.1    Weinkove, D.2    MacDougall, L.K.3    Hafen, E.4    Waterfield, M.D.5
  • 33
    • 0034312315 scopus 로고    scopus 로고
    • Regulation of cellular growth by the Drosophila target of rapamycin dTOR
    • Zhang, H., Stallock, J. P., Ng, J. C., Reinhard, C. & Neufeld, T. P. Regulation of cellular growth by the Drosophila target of rapamycin dTOR. Genes Dev. 14, 2712-2724 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2712-2724
    • Zhang, H.1    Stallock, J.P.2    Ng, J.C.3    Reinhard, C.4    Neufeld, T.P.5
  • 34
    • 0032843917 scopus 로고    scopus 로고
    • Drosophila S6 kinase: A regulator of cell size
    • Montagne, J. et al. Drosophila S6 kinase: a regulator of cell size. Science 285, 2126-2129 (1999).
    • (1999) Science , vol.285 , pp. 2126-2129
    • Montagne, J.1
  • 35
    • 0032578998 scopus 로고    scopus 로고
    • s6k by PDK1
    • s6k by PDK1. Science 279, 707-710 (1998).
    • (1998) Science , vol.279 , pp. 707-710
    • Pullen, N.1
  • 36
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave, B. T., Ouwens, M., Withers, D. J., Alessi, D. R. & Shepherd, P. R. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 344, 427-431 (1999).
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 37
    • 0032560521 scopus 로고    scopus 로고
    • Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signalling pathway
    • Scott, P. H., Brunn, G. J., Kohn, A. D., Roth, R. A. and Lawrence J. C. Jr Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signalling pathway. Proc. Natl Acad. Sci. USA 95, 77772-7777 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 77772-77777
    • Scott, P.H.1    Brunn, G.J.2    Kohn, A.D.3    Roth, R.A.4    Lawrence J.C., Jr.5
  • 38
    • 0037123438 scopus 로고    scopus 로고
    • Control of Ser 2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load
    • Reynolds, T. H. t., Bodine, S. C. & Lawrence, J. C. Jr. Control of Ser 2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load. J. Biol. Chem. 277, 17657-17662 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17657-17662
    • Reynolds, T.H.T.1    Bodine, S.C.2    Lawrence J.C., Jr.3
  • 39
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppression mTOR signalling
    • Inoki, K., Li, Y., Zhu, T., Wu, J. & Guan, K. L. TSC2 is phosphorylated and inhibited by Akt and suppression mTOR signalling. Nature Cell Biol. 4, 648-657 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 40
    • 0037108750 scopus 로고    scopus 로고
    • Tuberous sclerosis complex-1 and -2 gene products function together to inhibition mammalian target of rapamycin (mTOR)-mediated downstream signalling
    • Tee, A. R. et al. Tuberous sclerosis complex-1 and -2 gene products function together to inhibition mammalian target of rapamycin (mTOR)-mediated downstream signalling. Proc. Natl Acad. Sci. USA 99, 13571-13576 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13571-13576
    • Tee, A.R.1
  • 42
    • 0030716488 scopus 로고    scopus 로고
    • Regulation of eIF-4E BP1 phosphorylation by mTOR
    • Hara, K. et al. Regulation of eIF-4E BP1 phosphorylation by mTOR. J. Biol. Chem. 272, 26457-26463 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26457-26463
    • Hara, K.1
  • 43
    • 0034976004 scopus 로고    scopus 로고
    • The translation inhibitor 4E-BP is an effector pf PI(3)K/Akt signalling and cell growth in Drosophila
    • Miron, M. et al. The translation inhibitor 4E-BP is an effector pf PI(3)K/Akt signalling and cell growth in Drosophila Nature Cell Biol. 3, 596-601 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 596-601
    • Miron, M.1
  • 44
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediate by protein kinase B
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M. & Hemmings, B.A. Inhibition of glycogen synthase kinase-3 by insulin mediate by protein kinase B. Nature 378, 785-789 (1995).
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 45
    • 0036239191 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and anti-atrophy effects of clenbuterol are mediated by the β2-adrenergic receptor
    • Hinkle, R. T. et al. Skeletal muscle hypertrophy and anti-atrophy effects of clenbuterol are mediated by the β2-adrenergic receptor. Muscle Nerve 25, 729-734 (2002).
    • (2002) Muscle Nerve , vol.25 , pp. 729-734
    • Hinkle, R.T.1
  • 46
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits
    • Crespo, P., Xu, N., Simonds, W. F. & Gutkind, J. S. Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits. Nature 369, 418-420 (1994).
    • (1994) Nature , vol.369 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 47
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • Lecker, S. H. et al. Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J. Clin. Invest. 104, 1411-1420 (1999).
    • (1999) J. Clin. Invest. , vol.104 , pp. 1411-1420
    • Lecker, S.H.1
  • 49
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A. & Goldberg, A. L. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl Acad. Sci. USA 98, 14440-14445 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 50
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine, S. C. et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294, 1704-1708 (2001).
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1
  • 51
    • 0035793703 scopus 로고    scopus 로고
    • Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain
    • Centner, T. et al. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J. Mol. Biol. 306, 717-726 (2001).
    • (2001) J. Mol. Biol. , vol.306 , pp. 717-726
    • Centner, T.1
  • 52
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • McElhinny, A. S., Kakinuma, K., Sorimachi, H., Labeit, S. & Gregorio, C. C. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J. Cell Biol. 157, 125-136 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 125-136
    • McElhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5


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