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Volumn 37, Issue 10 SPEC. ISS., 2005, Pages 1997-2011

Signal-transduction networks and the regulation of muscle protein degradation

Author keywords

Atrophy; Proteolysis; Turnover; Wasting

Indexed keywords

FIBROBLAST GROWTH FACTOR; INSULIN; PROTEIN; PROTEIN PROTEOLYSIS INDUCING FACTOR; SOMATOMEDIN; UNCLASSIFIED DRUG;

EID: 23944501319     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2005.02.020     Document Type: Review
Times cited : (30)

References (109)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • T.N. Akopian, A.F. Kisselev, and A.L. Goldberg Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum J Biol Chem 272 3 1997 1791 1798
    • (1997) J Biol Chem , vol.272 , Issue.3 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 2
    • 0022460012 scopus 로고
    • Binding properties and biological potencies of insulin-like growth factors in L6 myoblasts
    • F.J. Ballard, L.C. Read, G.L. Francis, C.J. Bagley, and J.C. Wallace Binding properties and biological potencies of insulin-like growth factors in L6 myoblasts Biochem J 233 1 1986 223 230
    • (1986) Biochem J , vol.233 , Issue.1 , pp. 223-230
    • Ballard, F.J.1    Read, L.C.2    Francis, G.L.3    Bagley, C.J.4    Wallace, J.C.5
  • 3
    • 0037169028 scopus 로고    scopus 로고
    • Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    • J.M. Barral, A.H. Hutagalung, A. Brinker, F.U. Hartl, and H.F. Epstein Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin Science 295 5555 2002 669 671
    • (2002) Science , vol.295 , Issue.5555 , pp. 669-671
    • Barral, J.M.1    Hutagalung, A.H.2    Brinker, A.3    Hartl, F.U.4    Epstein, H.F.5
  • 4
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • S.C. Bodine, E. Latres, S. Baumhueter, V.K. Lai, L. Nunez, and B.A. Clarke Identification of ubiquitin ligases required for skeletal muscle atrophy Science 294 5547 2001 1704 1708
    • (2001) Science , vol.294 , Issue.5547 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.4    Nunez, L.5    Clarke, B.A.6
  • 5
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • S.C. Bodine, T.N. Stitt, M. Gonzalez, W.O. Kline, G.L. Stover, and R. Bauerlein Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo Nat Cell Biol 3 11 2001 1014 1019
    • (2001) Nat Cell Biol , vol.3 , Issue.11 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3    Kline, W.O.4    Stover, G.L.5    Bauerlein, R.6
  • 6
    • 0023522453 scopus 로고
    • Nerve growth factor supports growth of rat skeletal myotubes in culture
    • C. Brodie, and S.R. Sampson Nerve growth factor supports growth of rat skeletal myotubes in culture Brain Res 435 1-2 1987 393 397
    • (1987) Brain Res , vol.435 , Issue.1-2 , pp. 393-397
    • Brodie, C.1    Sampson, S.R.2
  • 7
    • 0032510947 scopus 로고    scopus 로고
    • Insulin, but not contraction, activates Akt/PKB in isolated rat skeletal muscle
    • J.T. Brozinick Jr., and M.J. Birnbaum Insulin, but not contraction, activates Akt/PKB in isolated rat skeletal muscle J Biol Chem 273 24 1998 14679 14682
    • (1998) J Biol Chem , vol.273 , Issue.24 , pp. 14679-14682
    • Brozinick Jr., J.T.1    Birnbaum, M.J.2
  • 8
    • 2342612634 scopus 로고    scopus 로고
    • Differential functions of the C. elegans FGF receptor in axon outgrowth and maintenance of axon position
    • H.E. Bulow, T. Boulin, and O. Hobert Differential functions of the C. elegans FGF receptor in axon outgrowth and maintenance of axon position Neuron 42 3 2004 367 374
    • (2004) Neuron , vol.42 , Issue.3 , pp. 367-374
    • Bulow, H.E.1    Boulin, T.2    Hobert, O.3
  • 9
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • D. Cai, J.D. Frantz, N.E. Tawa Jr., P.A. Melendez, B.C. Oh, and H.G. Lidov IKKbeta/NF-kappaB activation causes severe muscle wasting in mice Cell 119 2 2004 285 298
    • (2004) Cell , vol.119 , Issue.2 , pp. 285-298
    • Cai, D.1    Frantz, J.D.2    Tawa Jr., N.E.3    Melendez, P.A.4    Oh, B.C.5    Lidov, H.G.6
  • 10
    • 0034651690 scopus 로고    scopus 로고
    • Muscular dystrophy in adult and aged anti-NGF transgenic mice resembles an inclusion body myopathy
    • S. Capsoni, F. Ruberti, E. Di Daniel, and A. Cattaneo Muscular dystrophy in adult and aged anti-NGF transgenic mice resembles an inclusion body myopathy J Neurosci Res 59 4 2000 553 560
    • (2000) J Neurosci Res , vol.59 , Issue.4 , pp. 553-560
    • Capsoni, S.1    Ruberti, F.2    Di Daniel, E.3    Cattaneo, A.4
  • 11
    • 0024504504 scopus 로고
    • Effect of recombinant human tumour necrosis factor alpha on protein synthesis in liver, skeletal muscle and skin of rats
    • Y. Charters, and R.F. Grimble Effect of recombinant human tumour necrosis factor alpha on protein synthesis in liver, skeletal muscle and skin of rats Biochem J 258 2 1989 493 497
    • (1989) Biochem J , vol.258 , Issue.2 , pp. 493-497
    • Charters, Y.1    Grimble, R.F.2
  • 12
    • 0015537695 scopus 로고
    • Conformational adaptability in enzymes
    • N. Citri Conformational adaptability in enzymes Adv Enzymol 37 397-648 1973
    • (1973) Adv Enzymol , vol.37 , Issue.397-648
    • Citri, N.1
  • 13
    • 0029779604 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and p70 s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I
    • D. Dardevet, C. Sornet, T. Vary, and J. Grizard Phosphatidylinositol 3-kinase and p70 s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I Endocrinology 137 10 1996 4087 4094
    • (1996) Endocrinology , vol.137 , Issue.10 , pp. 4087-4094
    • Dardevet, D.1    Sornet, C.2    Vary, T.3    Grizard, J.4
  • 14
    • 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 2 1998 262 267
    • (1998) Curr Opin Cell Biol , vol.10 , Issue.2 , pp. 262-267
    • Downward, J.1
  • 15
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • W.C. Earnshaw, L.M. Martins, and S.H. Kaufmann Mammalian caspases: structure, activation, substrates, and functions during apoptosis Annu Rev Biochem 68 1999 383 424
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 16
    • 0035911967 scopus 로고    scopus 로고
    • Oncogenic Ras-induced proliferation requires autocrine fibroblast growth factor 2 signaling in skeletal muscle cells
    • Y.V. Fedorov, R.S. Rosenthal, and B.B. Olwin Oncogenic Ras-induced proliferation requires autocrine fibroblast growth factor 2 signaling in skeletal muscle cells J Cell Biol 152 6 2001 1301 1305
    • (2001) J Cell Biol , vol.152 , Issue.6 , pp. 1301-1305
    • Fedorov, Y.V.1    Rosenthal, R.S.2    Olwin, B.B.3
  • 18
    • 0019036336 scopus 로고
    • Effects of diabetes on protein synthesis in fast- and slow-twitch rat skeletal muscle
    • K.E. Flaim, M.E. Copenhaver, and L.S. Jefferson Effects of diabetes on protein synthesis in fast- and slow-twitch rat skeletal muscle Am J Physiol 239 1 1980 88 95
    • (1980) Am J Physiol , vol.239 , Issue.1 , pp. 88-95
    • Flaim, K.E.1    Copenhaver, M.E.2    Jefferson, L.S.3
  • 19
    • 0141852285 scopus 로고    scopus 로고
    • Degradation of transgene-coded and endogenous proteins in the muscles of Caenorhabditis elegans
    • J.L. Fostel, L.B. Coste, and L.A. Jacobson Degradation of transgene-coded and endogenous proteins in the muscles of Caenorhabditis elegans Biochem Biophys Res Commun 312 2003 173 177
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 173-177
    • Fostel, J.L.1    Coste, L.B.2    Jacobson, L.A.3
  • 20
    • 0028128530 scopus 로고
    • Insulin-like growth factor I exerts growth hormone- and insulin-like actions on human muscle protein metabolism.
    • D.A. Fryburg Insulin-like growth factor I exerts growth hormone- and insulin-like actions on human muscle protein metabolism. Am J Physiol 267 2 Pt 1 1994 331 336
    • (1994) Am J Physiol , vol.267 , Issue.2 PART 1 , pp. 331-336
    • Fryburg, D.A.1
  • 22
    • 5444264831 scopus 로고    scopus 로고
    • Molecular networks in model systems
    • T. Galitski Molecular networks in model systems Annu Rev Genomics Hum Genet 5 2004 177 187
    • (2004) Annu Rev Genomics Hum Genet , vol.5 , pp. 177-187
    • Galitski, T.1
  • 23
    • 0028009670 scopus 로고
    • Interleukin-6 does not activate protein breakdown in rat skeletal muscle
    • C. Garcia-Martinez, F.J. Lopez-Soriano, and J.M. Argiles Interleukin-6 does not activate protein breakdown in rat skeletal muscle Cancer Lett 76 1 1994 1 4
    • (1994) Cancer Lett , vol.76 , Issue.1 , pp. 1-4
    • Garcia-Martinez, C.1    Lopez-Soriano, F.J.2    Argiles, J.M.3
  • 24
    • 0036584593 scopus 로고    scopus 로고
    • Genetic analysis of insulin signaling in Drosophila
    • R.S. Garofalo Genetic analysis of insulin signaling in Drosophila Trends Endocrinol Metab 13 4 2002 156 162
    • (2002) Trends Endocrinol Metab , vol.13 , Issue.4 , pp. 156-162
    • Garofalo, R.S.1
  • 26
    • 1542344328 scopus 로고    scopus 로고
    • Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation
    • A. Glading, R.J. Bodnar, I.J. Reynolds, H. Shiraha, L. Satish, and D.A. Potter Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation Mol Cell Biol 24 6 2004 2499 2512
    • (2004) Mol Cell Biol , vol.24 , Issue.6 , pp. 2499-2512
    • Glading, A.1    Bodnar, R.J.2    Reynolds, I.J.3    Shiraha, H.4    Satish, L.5    Potter, D.A.6
  • 27
    • 0041424822 scopus 로고    scopus 로고
    • Molecular mechanisms modulating muscle mass
    • D.J. Glass Molecular mechanisms modulating muscle mass Trends Mol Med 9 8 2003 344 350
    • (2003) Trends Mol Med , vol.9 , Issue.8 , pp. 344-350
    • Glass, D.J.1
  • 28
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • D.J. Glass Signalling pathways that mediate skeletal muscle hypertrophy and atrophy Nat Cell Biol 5 2 2003 87 90
    • (2003) Nat Cell Biol , vol.5 , Issue.2 , pp. 87-90
    • Glass, D.J.1
  • 29
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • in press.
    • Glass, D.J., (2005). Skeletal muscle hypertrophy and atrophy signaling pathways. Int J Biochem Cell Biol, in press.
    • (2005) Int J Biochem Cell Biol
    • Glass, D.J.1
  • 30
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • M.D. Gomes, S.H. Lecker, R.T. Jagoe, A. Navon, and A.L. Goldberg Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy Proc Natl Acad Sci USA 98 25 2001 14440 14445
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.25 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 31
    • 0022969739 scopus 로고
    • Effect of testosterone on muscle protein synthesis in myotonic dystrophy
    • R.C. Griggs, D. Halliday, W. Kingston, and R.T. Moxley III Effect of testosterone on muscle protein synthesis in myotonic dystrophy Ann Neurol 20 5 1986 590 596
    • (1986) Ann Neurol , vol.20 , Issue.5 , pp. 590-596
    • Griggs, R.C.1    Halliday, D.2    Kingston, W.3    Moxley III, R.T.4
  • 32
    • 0029868517 scopus 로고    scopus 로고
    • Differentially expressed fibroblast growth factors regulate skeletal muscle development through autocrine and paracrine mechanisms
    • K. Hannon, A.J. Kudla, M.J. McAvoy, K.L. Clase, and B.B. Olwin Differentially expressed fibroblast growth factors regulate skeletal muscle development through autocrine and paracrine mechanisms J Cell Biol 132 6 1996 1151 1159
    • (1996) J Cell Biol , vol.132 , Issue.6 , pp. 1151-1159
    • Hannon, K.1    Kudla, A.J.2    McAvoy, M.J.3    Clase, K.L.4    Olwin, B.B.5
  • 33
    • 0021216583 scopus 로고
    • Protein metabolism in skeletal muscle tissue from hyperthyroid patients after preoperative treatment with antithyroid drug or selective beta-blocking agent. Results from a prospective, randomized study
    • P.O. Hasselgren, A. Adlerberth, U. Angeras, and G. Stenstrom Protein metabolism in skeletal muscle tissue from hyperthyroid patients after preoperative treatment with antithyroid drug or selective beta-blocking agent. Results from a prospective, randomized study J Clin Endocrinol Metab 59 5 1984 835 839
    • (1984) J Clin Endocrinol Metab , vol.59 , Issue.5 , pp. 835-839
    • Hasselgren, P.O.1    Adlerberth, A.2    Angeras, U.3    Stenstrom, G.4
  • 34
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • T. Hoppe, G. Cassata, J.M. Barral, W. Springer, A.H. Hutagalung, and H.F. Epstein Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans Cell 118 3 2004 337 349
    • (2004) Cell , vol.118 , Issue.3 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6
  • 35
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • C.Y. Huang, and J.E. Ferrell Jr. Ultrasensitivity in the mitogen-activated protein kinase cascade Proc Natl Acad Sci USA 93 19 1996 10078 10083
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.19 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 36
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • S.J. Hubbard The structural aspects of limited proteolysis of native proteins Biochim Biophys Acta 1382 2 1998 191 206
    • (1998) Biochim Biophys Acta , vol.1382 , Issue.2 , pp. 191-206
    • Hubbard, S.J.1
  • 37
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • T. Hunter Signaling-2000 and beyond Cell 100 1 2000 113 127
    • (2000) Cell , vol.100 , Issue.1 , pp. 113-127
    • Hunter, T.1
  • 38
    • 4544235672 scopus 로고    scopus 로고
    • The molecular basis of skeletal muscle atrophy
    • R.W. Jackman, and S.C. Kandarian The molecular basis of skeletal muscle atrophy Am J Physiol Cell Physiol 287 4 2004 834 843
    • (2004) Am J Physiol Cell Physiol , vol.287 , Issue.4 , pp. 834-843
    • Jackman, R.W.1    Kandarian, S.C.2
  • 39
    • 0023261107 scopus 로고
    • Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis
    • A.G. Kayali, V.R. Young, and M.N. Goodman Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis Am J Physiol 252 5 Pt 1 1987 621 626
    • (1987) Am J Physiol , vol.252 , Issue.5 PART 1 , pp. 621-626
    • Kayali, A.G.1    Young, V.R.2    Goodman, M.N.3
  • 40
    • 0027391814 scopus 로고
    • Interferon-gamma promotes proliferation of rat skeletal muscle cells in vitro and alters their AChR distribution
    • S. Kelic, T. Olsson, and K. Kristensson Interferon-gamma promotes proliferation of rat skeletal muscle cells in vitro and alters their AChR distribution J Neurol Sci 114 1 1993 62 67
    • (1993) J Neurol Sci , vol.114 , Issue.1 , pp. 62-67
    • Kelic, S.1    Olsson, T.2    Kristensson, K.3
  • 41
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • J.M. Kowalski, R.N. Parekh, J. Mao, and K.D. Wittrup Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control J Biol Chem 273 31 1998 19453 19458
    • (1998) J Biol Chem , vol.273 , Issue.31 , pp. 19453-19458
    • Kowalski, J.M.1    Parekh, R.N.2    Mao, J.3    Wittrup, K.D.4
  • 43
    • 0022552076 scopus 로고
    • Specific proteolytic modification of creatine kinase isoenzymes, Implication of C-terminal involvement in enzymic activity but not in subunit-subunit recognition
    • H.G. Lebherz, T. Burke, J.E. Shackelford, J.E. Strickler, and K.J. Wilson Specific proteolytic modification of creatine kinase isoenzymes, Implication of C-terminal involvement in enzymic activity but not in subunit-subunit recognition Biochem J 233 1 1986 51 56
    • (1986) Biochem J , vol.233 , Issue.1 , pp. 51-56
    • Lebherz, H.G.1    Burke, T.2    Shackelford, J.E.3    Strickler, J.E.4    Wilson, K.J.5
  • 44
    • 0347285363 scopus 로고    scopus 로고
    • Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    • S.H. Lecker, R.T. Jagoe, A. Gilbert, M. Gomes, V. Baracos, and J. Bailey Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression Faseb J 18 1 2004 39 51
    • (2004) Faseb J , vol.18 , Issue.1 , pp. 39-51
    • Lecker, S.H.1    Jagoe, R.T.2    Gilbert, A.3    Gomes, M.4    Baracos, V.5    Bailey, J.6
  • 45
    • 2542496898 scopus 로고    scopus 로고
    • Regulation of muscle protein degradation: Coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase
    • S.W. Lee, G. Dai, Z. Hu, X. Wang, J. Du, and W.E. Mitch Regulation of muscle protein degradation: coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase J Am Soc Nephrol 15 6 2004 1537 1545
    • (2004) J Am Soc Nephrol , vol.15 , Issue.6 , pp. 1537-1545
    • Lee, S.W.1    Dai, G.2    Hu, Z.3    Wang, X.4    Du, J.5    Mitch, W.E.6
  • 46
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties [In Process Citation]
    • A. Levchenko, J. Bruck, and P.W. Sternberg Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties [In Process Citation] Proc Natl Acad Sci USA 97 11 2000 5818 5823
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.11 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 47
    • 0037380570 scopus 로고    scopus 로고
    • Daf-28 encodes a C. elegans insulin superfamily member that is regulated by environmental cues and acts in the DAF-2 signaling pathway
    • W. Li, S.G. Kennedy, and G. Ruvkun daf-28 encodes a C. elegans insulin superfamily member that is regulated by environmental cues and acts in the DAF-2 signaling pathway Genes Dev 17 7 2003 844 858
    • (2003) Genes Dev , vol.17 , Issue.7 , pp. 844-858
    • Li, W.1    Kennedy, S.G.2    Ruvkun, G.3
  • 48
    • 0034810913 scopus 로고    scopus 로고
    • C-peptide attenuates protein tyrosine phosphatase activity and enhances glycogen synthesis in L6 myoblasts
    • Z.G. Li, X. Qiang, A.A. Sima, and G. Grunberger C-peptide attenuates protein tyrosine phosphatase activity and enhances glycogen synthesis in L6 myoblasts Biochem Biophys Res Commun 280 3 2001 615 619
    • (2001) Biochem Biophys Res Commun , vol.280 , Issue.3 , pp. 615-619
    • Li, Z.G.1    Qiang, X.2    Sima, A.A.3    Grunberger, G.4
  • 49
  • 50
    • 0030880483 scopus 로고    scopus 로고
    • Induction of muscle protein degradation by a tumour factor
    • M.J. Lorite, P. Cariuk, and M.J. Tisdale Induction of muscle protein degradation by a tumour factor Br J Cancer 76 8 1997 1035 1040
    • (1997) Br J Cancer , vol.76 , Issue.8 , pp. 1035-1040
    • Lorite, M.J.1    Cariuk, P.2    Tisdale, M.J.3
  • 51
    • 0034934948 scopus 로고    scopus 로고
    • Activation of ATP-ubiquitin-dependent proteolysis in skeletal muscle in vivo and murine myoblasts in vitro by a proteolysis-inducing factor (PIF)
    • M.J. Lorite, H.J. Smith, J.A. Arnold, A. Morris, M.G. Thompson, and M.J. Tisdale Activation of ATP-ubiquitin-dependent proteolysis in skeletal muscle in vivo and murine myoblasts in vitro by a proteolysis-inducing factor (PIF) Br J Cancer 85 2 2001 297 302
    • (2001) Br J Cancer , vol.85 , Issue.2 , pp. 297-302
    • Lorite, M.J.1    Smith, H.J.2    Arnold, J.A.3    Morris, A.4    Thompson, M.G.5    Tisdale, M.J.6
  • 52
    • 0031656804 scopus 로고    scopus 로고
    • Mechanism of muscle protein degradation induced by a cancer cachectic factor
    • M.J. Lorite, M.G. Thompson, J.L. Drake, G. Carling, and M.J. Tisdale Mechanism of muscle protein degradation induced by a cancer cachectic factor Br J Cancer 78 7 1998 850 856
    • (1998) Br J Cancer , vol.78 , Issue.7 , pp. 850-856
    • Lorite, M.J.1    Thompson, M.G.2    Drake, J.L.3    Carling, G.4    Tisdale, M.J.5
  • 53
    • 0036830127 scopus 로고    scopus 로고
    • Interferon gamma modulates trauma-induced muscle wasting and immune dysfunction
    • S.V. Madihally, M. Toner, M.L. Yarmush, and R.N. Mitchell Interferon gamma modulates trauma-induced muscle wasting and immune dysfunction Ann Surg 236 5 2002 649 657
    • (2002) Ann Surg , vol.236 , Issue.5 , pp. 649-657
    • Madihally, S.V.1    Toner, M.2    Yarmush, M.L.3    Mitchell, R.N.4
  • 54
    • 1842591231 scopus 로고    scopus 로고
    • Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases
    • M.D. Marmor, and Y. Yarden Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases Oncogene 23 11 2004 2057 2070
    • (2004) Oncogene , vol.23 , Issue.11 , pp. 2057-2070
    • Marmor, M.D.1    Yarden, Y.2
  • 55
    • 0026442992 scopus 로고
    • Metabolic acidosis accelerates whole body protein degradation and leucine oxidation by a glucocorticoid-dependent mechanism
    • R.C. May, T. Masud, B. Logue, J. Bailey, and B.K. England Metabolic acidosis accelerates whole body protein degradation and leucine oxidation by a glucocorticoid-dependent mechanism Miner Electrolyte Metab 18 2-5 1992 245 249
    • (1992) Miner Electrolyte Metab , vol.18 , Issue.2-5 , pp. 245-249
    • May, R.C.1    Masud, T.2    Logue, B.3    Bailey, J.4    England, B.K.5
  • 56
    • 0032456208 scopus 로고    scopus 로고
    • The role of insulin and other hormones in the regulation of amino acid and protein metabolism in humans
    • W.R. Miers, and E.J. Barrett The role of insulin and other hormones in the regulation of amino acid and protein metabolism in humans J Basic Clin Physiol Pharmacol 9 2-4 1998 235 253
    • (1998) J Basic Clin Physiol Pharmacol , vol.9 , Issue.2-4 , pp. 235-253
    • Miers, W.R.1    Barrett, E.J.2
  • 57
    • 0021472509 scopus 로고
    • Effects of epinephrine infusion on leucine and alanine kinetics in humans.
    • J.M. Miles, S.L. Nissen, J.E. Gerich, and M.W. Haymond Effects of epinephrine infusion on leucine and alanine kinetics in humans. Am J Physiol 247 2 Pt 1 1984 166 172
    • (1984) Am J Physiol , vol.247 , Issue.2 PART 1 , pp. 166-172
    • Miles, J.M.1    Nissen, S.L.2    Gerich, J.E.3    Haymond, M.W.4
  • 58
    • 1342321743 scopus 로고    scopus 로고
    • Two ubiquitin-like conjugation systems essential for autophagy
    • Y. Ohsumi, and N. Mizushima Two ubiquitin-like conjugation systems essential for autophagy Semin Cell Dev Biol 15 2 2004 231 236
    • (2004) Semin Cell Dev Biol , vol.15 , Issue.2 , pp. 231-236
    • Ohsumi, Y.1    Mizushima, N.2
  • 59
    • 0023747394 scopus 로고
    • Cell surface fibroblast growth factor and epidermal growth factor receptors are permanently lost during skeletal muscle terminal differentiation in culture
    • B.B. Olwin, and S.D. Hauschka Cell surface fibroblast growth factor and epidermal growth factor receptors are permanently lost during skeletal muscle terminal differentiation in culture J Cell Biol 107 2 1988 761 769
    • (1988) J Cell Biol , vol.107 , Issue.2 , pp. 761-769
    • Olwin, B.B.1    Hauschka, S.D.2
  • 60
    • 0032529189 scopus 로고    scopus 로고
    • Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor
    • S. Paradis, and G. Ruvkun Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor Genes Dev 12 16 1998 2488 2498
    • (1998) Genes Dev , vol.12 , Issue.16 , pp. 2488-2498
    • Paradis, S.1    Ruvkun, G.2
  • 61
    • 1842833926 scopus 로고    scopus 로고
    • Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions
    • M.G. Price, M.L. Landsverk, J.M. Barral, and H.F. Epstein Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions J Cell Sci 115 Pt 21 2002 4013 4023
    • (2002) J Cell Sci , vol.115 , Issue.21 PART , pp. 4013-4023
    • Price, M.G.1    Landsverk, M.L.2    Barral, J.M.3    Epstein, H.F.4
  • 62
    • 0029861468 scopus 로고    scopus 로고
    • Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription
    • S.R. Price, J.L. Bailey, X. Wang, C. Jurkovitz, B.K. England, and X. Ding Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription J Clin Invest 98 8 1996 1703 1708
    • (1996) J Clin Invest , vol.98 , Issue.8 , pp. 1703-1708
    • Price, S.R.1    Bailey, J.L.2    Wang, X.3    Jurkovitz, C.4    England, B.K.5    Ding, X.6
  • 63
    • 0035156842 scopus 로고    scopus 로고
    • Molecular mechanisms regulating protein turnover in muscle
    • S.R. Price, J.D. Du, J.L. Bailey, and W.E. Mitch Molecular mechanisms regulating protein turnover in muscle Am J Kidney Dis 37 1 Suppl 2 2001 S112 S114
    • (2001) Am J Kidney Dis , vol.37 , Issue.1 SUPPL. 2
    • Price, S.R.1    Du, J.D.2    Bailey, J.L.3    Mitch, W.E.4
  • 64
    • 0035812696 scopus 로고    scopus 로고
    • Rapid activation of ERK1/2 mitogen-activated protein kinase by corticosterone in PC12 cells
    • J. Qiu, P. Wang, Q. Jing, W. Zhang, X. Li, and Y. Zhong Rapid activation of ERK1/2 mitogen-activated protein kinase by corticosterone in PC12 cells Biochem Biophys Res Commun 287 4 2001 1017 1024
    • (2001) Biochem Biophys Res Commun , vol.287 , Issue.4 , pp. 1017-1024
    • Qiu, J.1    Wang, P.2    Jing, Q.3    Zhang, W.4    Li, X.5    Zhong, Y.6
  • 65
    • 0022476631 scopus 로고
    • The use of NMR spectroscopy for the understanding of disease
    • G.K. Radda The use of NMR spectroscopy for the understanding of disease Science 233 4764 1986 640 645
    • (1986) Science , vol.233 , Issue.4764 , pp. 640-645
    • Radda, G.K.1
  • 66
    • 0018004269 scopus 로고
    • Glucocorticoid effects on peptide-chain initiation in skeletal muscle and heart
    • S.R. Rannels, D.E. Rannels, A.E. Pegg, and L.S. Jefferson Glucocorticoid effects on peptide-chain initiation in skeletal muscle and heart Am J Physiol 235 2 1978 134 139
    • (1978) Am J Physiol , vol.235 , Issue.2 , pp. 134-139
    • Rannels, S.R.1    Rannels, D.E.2    Pegg, A.E.3    Jefferson, L.S.4
  • 67
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: Proteasomal protein processing
    • M. Rape, and S. Jentsch Taking a bite: proteasomal protein processing Nat Cell Biol 4 5 2002 113 116
    • (2002) Nat Cell Biol , vol.4 , Issue.5 , pp. 113-116
    • Rape, M.1    Jentsch, S.2
  • 68
    • 0026792869 scopus 로고
    • Ammonium chloride-induced acidosis increases protein breakdown and amino acid oxidation in humans
    • D. Reaich, S.M. Channon, C.M. Scrimgeour, and T.H. Goodship Ammonium chloride-induced acidosis increases protein breakdown and amino acid oxidation in humans Am J Physiol 263 4 Pt 1 1992 735 739
    • (1992) Am J Physiol , vol.263 , Issue.4 PART 1 , pp. 735-739
    • Reaich, D.1    Channon, S.M.2    Scrimgeour, C.M.3    Goodship, T.H.4
  • 69
    • 0033607784 scopus 로고    scopus 로고
    • Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt
    • C. Rommel, B.A. Clarke, S. Zimmermann, L. Nunez, R. Rossman, and K. Reid Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt Science 286 5445 1999 1738 1741
    • (1999) Science , vol.286 , Issue.5445 , pp. 1738-1741
    • Rommel, C.1    Clarke, B.A.2    Zimmermann, S.3    Nunez, L.4    Rossman, R.5    Reid, K.6
  • 70
    • 0030802370 scopus 로고    scopus 로고
    • Hormonal regulation of human muscle protein metabolism
    • O.E. Rooyackers, and K.S. Nair Hormonal regulation of human muscle protein metabolism Annu Rev Nutr 17 1997 457 485
    • (1997) Annu Rev Nutr , vol.17 , pp. 457-485
    • Rooyackers, O.E.1    Nair, K.S.2
  • 72
    • 0033977188 scopus 로고    scopus 로고
    • Effect of contraction on mitogen-activated protein kinase signal-transduction in skeletal muscle. Involvement of the mitogen- and stress-activated protein kinase 1
    • J.W. Ryder, R. Fahlman, H. Wallberg Henriksson, D.R. Alessi, A. Krook, and J.R. Zierath Effect of contraction on mitogen-activated protein kinase signal-transduction in skeletal muscle. Involvement Of the mitogen- and stress-activated protein kinase 1 J Biol Chem 275 2 2000 1457 1462
    • (2000) J Biol Chem , vol.275 , Issue.2 , pp. 1457-1462
    • Ryder, J.W.1    Fahlman, R.2    Wallberg Henriksson, H.3    Alessi, D.R.4    Krook, A.5    Zierath, J.R.6
  • 73
    • 4544293878 scopus 로고    scopus 로고
    • IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
    • J.M. Sacheck, A. Ohtsuka, S.C. McLary, and A.L. Goldberg IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1 Am J Physiol Endocrinol Metab 287 4 2004 591 601
    • (2004) Am J Physiol Endocrinol Metab , vol.287 , Issue.4 , pp. 591-601
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 74
    • 0034069726 scopus 로고    scopus 로고
    • An overexpression of fibroblast growth factor (FGF) and FGF receptor 4 in a severe clinical phenotype of facioscapulohumeral muscular dystrophy
    • A. Saito, I. Higuchi, M. Nakagawa, M. Saito, Y. Uchida, and M. Inose An overexpression of fibroblast growth factor (FGF) and FGF receptor 4 in a severe clinical phenotype of facioscapulohumeral muscular dystrophy Muscle Nerve 23 4 2000 490 497
    • (2000) Muscle Nerve , vol.23 , Issue.4 , pp. 490-497
    • Saito, A.1    Higuchi, I.2    Nakagawa, M.3    Saito, M.4    Uchida, Y.5    Inose, M.6
  • 75
    • 0035986085 scopus 로고    scopus 로고
    • Invited review: Intracellular signaling in contracting skeletal muscle
    • K. Sakamoto, and L.J. Goodyear Invited review: intracellular signaling in contracting skeletal muscle J Appl Physiol 93 1 2002 369 383
    • (2002) J Appl Physiol , vol.93 , Issue.1 , pp. 369-383
    • Sakamoto, K.1    Goodyear, L.J.2
  • 76
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • M. Sandri, C. Sandri, A. Gilbert, C. Skurk, E. Calabria, and A. Picard Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy Cell 117 3 2004 399 412
    • (2004) Cell , vol.117 , Issue.3 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6
  • 77
    • 0035489468 scopus 로고    scopus 로고
    • PKB/AKT: Functional insights from genetic models
    • M.P. Scheid, and J.R. Woodgett PKB/AKT: functional insights from genetic models Nat Rev Mol Cell Biol 2 10 2001 760 768
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.10 , pp. 760-768
    • Scheid, M.P.1    Woodgett, J.R.2
  • 78
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • U. Schubert, L.C. Anton, J. Gibbs, C.C. Norbury, J.W. Yewdell, and J.R. Bennink Rapid degradation of a large fraction of newly synthesized proteins by proteasomes Nature 404 6779 2000 770 774
    • (2000) Nature , vol.404 , Issue.6779 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 79
    • 0033229932 scopus 로고    scopus 로고
    • Effect of a cancer cachectic factor on protein synthesis/degradation in murine C2C12 myoblasts: Modulation by eicosapentaenoic acid
    • H.J. Smith, M.J. Lorite, and M.J. Tisdale Effect of a cancer cachectic factor on protein synthesis/degradation in murine C2C12 myoblasts: modulation by eicosapentaenoic acid Cancer Res 59 21 1999 5507 5513
    • (1999) Cancer Res , vol.59 , Issue.21 , pp. 5507-5513
    • Smith, H.J.1    Lorite, M.J.2    Tisdale, M.J.3
  • 80
    • 0345303943 scopus 로고    scopus 로고
    • Signal transduction pathways involved in proteolysis-inducing factor induced proteasome expression in murine myotubes
    • H.J. Smith, and M.J. Tisdale Signal transduction pathways involved in proteolysis-inducing factor induced proteasome expression in murine myotubes Br J Cancer 89 9 2003 1783 1788
    • (2003) Br J Cancer , vol.89 , Issue.9 , pp. 1783-1788
    • Smith, H.J.1    Tisdale, M.J.2
  • 81
    • 2642526999 scopus 로고    scopus 로고
    • Role of protein kinase C and NF-kappaB in proteolysis-inducing factor-induced proteasome expression in C(2)C(12) myotubes
    • H.J. Smith, S.M. Wyke, and M.J. Tisdale Role of protein kinase C and NF-kappaB in proteolysis-inducing factor-induced proteasome expression in C(2)C(12) myotubes Br J Cancer 90 9 2004 1850 1857
    • (2004) Br J Cancer , vol.90 , Issue.9 , pp. 1850-1857
    • Smith, H.J.1    Wyke, S.M.2    Tisdale, M.J.3
  • 82
    • 0031947371 scopus 로고    scopus 로고
    • Developmentally regulated expression and localization of fibroblast growth factor receptors in the human muscle
    • V. Sogos, L. Balaci, M.G. Ennas, P. Dell'era, M. Presta, and F. Gremo Developmentally regulated expression and localization of fibroblast growth factor receptors in the human muscle Dev Dyn 211 4 1998 362 373
    • (1998) Dev Dyn , vol.211 , Issue.4 , pp. 362-373
    • Sogos, V.1    Balaci, L.2    Ennas, M.G.3    Dell'Era, P.4    Presta, M.5    Gremo, F.6
  • 83
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • V. Solomon, and A.L. Goldberg Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts J Biol Chem 271 43 1996 26690 26697
    • (1996) J Biol Chem , vol.271 , Issue.43 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 84
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • V. Solomon, S.H. Lecker, and A.L. Goldberg The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle J Biol Chem 273 39 1998 25216 25222
    • (1998) J Biol Chem , vol.273 , Issue.39 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 85
    • 0028880716 scopus 로고
    • LET-23-mediated signal transduction during Caenorhabditis elegans development
    • P.W. Sternberg, G. Lesa, J. Lee, W.S. Katz, C. Yoon, and T.R. Clandinin LET-23-mediated signal transduction during Caenorhabditis elegans development Mol Reprod Dev 42 4 1995 523 528
    • (1995) Mol Reprod Dev , vol.42 , Issue.4 , pp. 523-528
    • Sternberg, P.W.1    Lesa, G.2    Lee, J.3    Katz, W.S.4    Yoon, C.5    Clandinin, T.R.6
  • 86
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • T.N. Stitt, D. Drujan, B.A. Clarke, F. Panaro, Y. Timofeyva, and W.O. Kline The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors Mol Cell 14 3 2004 395 403
    • (2004) Mol Cell , vol.14 , Issue.3 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6
  • 87
  • 88
    • 0034045950 scopus 로고    scopus 로고
    • Genetic defects in acetylcholine signalling promote protein degradation in muscle cells of Caenorhabditis elegans
    • N.J. Szewczyk, J.J. Hartman, S.J. Barmada, and L.A. Jacobson Genetic defects in acetylcholine signalling promote protein degradation in muscle cells of Caenorhabditis elegans J Cell Sci 113 Pt 2000 2003 2010
    • (2000) J Cell Sci , vol.113 , Issue.PART , pp. 2003-2010
    • Szewczyk, N.J.1    Hartman, J.J.2    Barmada, S.J.3    Jacobson, L.A.4
  • 89
    • 0141865502 scopus 로고    scopus 로고
    • Activated EGL-15 FGF receptor promotes protein degradation in muscles of Caenorhabditis elegans
    • N.J. Szewczyk, and L.A. Jacobson Activated EGL-15 FGF receptor promotes protein degradation in muscles of Caenorhabditis elegans EMBO J 22 2003 5058 5067
    • (2003) EMBO J , vol.22 , pp. 5058-5067
    • Szewczyk, N.J.1    Jacobson, L.A.2
  • 90
    • 0036261726 scopus 로고    scopus 로고
    • Activation of Ras and the mitogen-activated protein kinase pathway promotes protein degradation in muscle cells of Caenorhabditis elegans
    • N.J. Szewczyk, B.K. Peterson, and L.A. Jacobson Activation of Ras and the mitogen-activated protein kinase pathway promotes protein degradation in muscle cells of Caenorhabditis elegans Mol Cell Biol 22 12 2002 4181 4188
    • (2002) Mol Cell Biol , vol.22 , Issue.12 , pp. 4181-4188
    • Szewczyk, N.J.1    Peterson, B.K.2    Jacobson, L.A.3
  • 91
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • N.E. Tawa Jr., R. Odessey, and A.L. Goldberg Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles J Clin Invest 100 1 1997 197 203
    • (1997) J Clin Invest , vol.100 , Issue.1 , pp. 197-203
    • Tawa Jr., N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 92
    • 0031962507 scopus 로고    scopus 로고
    • Signalling pathways regulating protein turnover in skeletal muscle
    • M.G. Thompson, and R.M. Palmer Signalling pathways regulating protein turnover in skeletal muscle Cell Signal 10 1998 1 11
    • (1998) Cell Signal , vol.10 , pp. 1-11
    • Thompson, M.G.1    Palmer, R.M.2
  • 93
    • 0035259388 scopus 로고    scopus 로고
    • Loss of skeletal muscle in cancer: Biochemical mechanisms
    • M.J. Tisdale Loss of skeletal muscle in cancer: biochemical mechanisms Front Biosci 6 2001 164 174
    • (2001) Front Biosci , vol.6 , pp. 164-174
    • Tisdale, M.J.1
  • 95
    • 13344261948 scopus 로고    scopus 로고
    • Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice
    • T. Tsujinaka, J. Fujita, C. Ebisui, M. Yano, E. Kominami, and K. Suzuki Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice J Clin Invest 97 1 1996 244 249
    • (1996) J Clin Invest , vol.97 , Issue.1 , pp. 244-249
    • Tsujinaka, T.1    Fujita, J.2    Ebisui, C.3    Yano, M.4    Kominami, E.5    Suzuki, K.6
  • 96
    • 0034528256 scopus 로고    scopus 로고
    • Protein kinase C-alpha is an upstream activator of the IkappaB kinase complex in the TPA signal transduction pathway to NF-kappaB in U2OS cells
    • A.C. Vertegaal, H.B. Kuiperij, S. Yamaoka, G. Courtois, A.J. van der Eb, and A. Zantema Protein kinase C-alpha is an upstream activator of the IkappaB kinase complex in the TPA signal transduction pathway to NF-kappaB in U2OS cells Cell Signal 12 11-12 2000 759 768
    • (2000) Cell Signal , vol.12 , Issue.11-12 , pp. 759-768
    • Vertegaal, A.C.1    Kuiperij, H.B.2    Yamaoka, S.3    Courtois, G.4    Van Der Eb, A.J.5    Zantema, A.6
  • 97
    • 0033987607 scopus 로고    scopus 로고
    • Effects of ciliary neurotrophic factor (CNTF) on protein turnover in cultured muscle cells
    • M.C. Wang, and N.E. Forsberg Effects of ciliary neurotrophic factor (CNTF) on protein turnover in cultured muscle cells Cytokine 12 1 2000 41 48
    • (2000) Cytokine , vol.12 , Issue.1 , pp. 41-48
    • Wang, M.C.1    Forsberg, N.E.2
  • 98
    • 0033517849 scopus 로고    scopus 로고
    • Lysozyme degradation by the bovine multicatalytic proteinase complex (proteasome): Evidence for a nonprocessive mode of degradation
    • R. Wang, B.T. Chait, I. Wolf, R.A. Kohanski, and C. Cardozo Lysozyme degradation by the bovine multicatalytic proteinase complex (proteasome): evidence for a nonprocessive mode of degradation Biochemistry 38 44 1999 14573 14581
    • (1999) Biochemistry , vol.38 , Issue.44 , pp. 14573-14581
    • Wang, R.1    Chait, B.T.2    Wolf, I.3    Kohanski, R.A.4    Cardozo, C.5
  • 99
    • 0000823299 scopus 로고
    • Muscle
    • W. Wood and the Community of C. elegans Researchers (Eds.), Cold Spring Harbor: Cold Spring Harbor Laboratory.
    • Waterston, R. H. (1988). Muscle. In W. Wood and the Community of C. elegans Researchers (Eds.), The nematode Caenorhabditis elegans (pp. 281-335). Cold Spring Harbor: Cold Spring Harbor Laboratory.
    • (1988) The nematode Caenorhabditis elegans , pp. 281-335
    • Waterston, R.H.1
  • 100
    • 2642588897 scopus 로고    scopus 로고
    • Selective activators of thyroid hormone receptors
    • P. Webb Selective activators of thyroid hormone receptors Expert Opin Investig Drugs 13 5 2004 489 500
    • (2004) Expert Opin Investig Drugs , vol.13 , Issue.5 , pp. 489-500
    • Webb, P.1
  • 101
    • 0031033159 scopus 로고    scopus 로고
    • Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase
    • T. Webb, P.J. Jackson, and G.E. Morris Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase Biochem J 321 Pt 1 1997 83 88
    • (1997) Biochem J , vol.321 , Issue.1 PART , pp. 83-88
    • Webb, T.1    Jackson, P.J.2    Morris, G.E.3
  • 103
    • 0033515888 scopus 로고    scopus 로고
    • Complexity in biological signaling systems
    • G. Weng, U.S. Bhalla, and R. Iyengar Complexity in biological signaling systems Science 284 5411 1999 92 96
    • (1999) Science , vol.284 , Issue.5411 , pp. 92-96
    • Weng, G.1    Bhalla, U.S.2    Iyengar, R.3
  • 105
    • 0024450017 scopus 로고
    • Fibroblast growth factor is stored in fiber extracellular matrix and plays a role in regulating muscle hypertrophy
    • S. Yamada, N. Buffinger, J. DiMario, and R.C. Strohman Fibroblast growth factor is stored in fiber extracellular matrix and plays a role in regulating muscle hypertrophy Med Sci Sports Exerc 21 5 Suppl 1989 173 180
    • (1989) Med Sci Sports Exerc , vol.21 , Issue.5 SUPPL. , pp. 173-180
    • Yamada, S.1    Buffinger, N.2    Dimario, J.3    Strohman, R.C.4
  • 106
    • 0242361581 scopus 로고    scopus 로고
    • Transcriptional regulation by the MAP kinase signaling cascades
    • S.H. Yang, A.D. Sharrocks, and A.J. Whitmarsh Transcriptional regulation by the MAP kinase signaling cascades Gene 320 2003 3 21
    • (2003) Gene , vol.320 , pp. 3-21
    • Yang, S.H.1    Sharrocks, A.D.2    Whitmarsh, A.J.3
  • 107
    • 0030884259 scopus 로고    scopus 로고
    • Transgene-coded chimeric proteins as reporters of intracellular proteolysis: Starvation-induced catabolism of a lacZ fusion protein in muscle cells of Caenorhabditis elegans
    • L.A. Zdinak, I.B. Greenberg, N.J. Szewczyk, S.J. Barmada, M. Cardamone Rayner, and J.J. Hartman Transgene-coded chimeric proteins as reporters of intracellular proteolysis: starvation-induced catabolism of a lacZ fusion protein in muscle cells of Caenorhabditis elegans J Cell Biochem 67 1 1997 143 153
    • (1997) J Cell Biochem , vol.67 , Issue.1 , pp. 143-153
    • Zdinak, L.A.1    Greenberg, I.B.2    Szewczyk, N.J.3    Barmada, S.J.4    Cardamone Rayner, M.5    Hartman, J.J.6
  • 108
    • 0022402473 scopus 로고
    • Regulation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium
    • R.J. Zeman, T. Kameyama, K. Matsumoto, P. Bernstein, and J.D. Etlinger Regulation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium J Biol Chem 260 25 1985 13619 13624
    • (1985) J Biol Chem , vol.260 , Issue.25 , pp. 13619-13624
    • Zeman, R.J.1    Kameyama, T.2    Matsumoto, K.3    Bernstein, P.4    Etlinger, J.D.5
  • 109
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • S. Zimmermann, and K. Moelling Phosphorylation and regulation of Raf by Akt (protein kinase B) Science 286 5445 1999 1741 1744
    • (1999) Science , vol.286 , Issue.5445 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2


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