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Volumn 74, Issue 6, 2011, Pages 774-795

Diversity of human skeletal muscle in health and disease: Contribution of proteomics

Author keywords

DIGE; Mass spectrometry; Muscle; Proteomics

Indexed keywords

AGRIN; DYSTROPHIN; FUKUTIN; INTEGRIN; LAMININ ALPHA2; NEUREXIN; NITRIC OXIDE SYNTHASE; PROTEOME; SELENOPROTEIN;

EID: 79955477252     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.02.028     Document Type: Review
Times cited : (55)

References (147)
  • 1
    • 72849173018 scopus 로고
    • Interactions between motoneurones and muscles in respect of the characteristic speeds of their responses
    • Buller A.J., Eccles J.C., Eccles R.M. Interactions between motoneurones and muscles in respect of the characteristic speeds of their responses. J Physiol 1960, 150:417-439.
    • (1960) J Physiol , vol.150 , pp. 417-439
    • Buller, A.J.1    Eccles, J.C.2    Eccles, R.M.3
  • 2
    • 0019309793 scopus 로고
    • Do enzyme activities vary along muscle fibres?
    • Pette D., Wimmer M., Nemeth P. Do enzyme activities vary along muscle fibres?. Histochemistry 1980, 67:225-231.
    • (1980) Histochemistry , vol.67 , pp. 225-231
    • Pette, D.1    Wimmer, M.2    Nemeth, P.3
  • 3
    • 0035116376 scopus 로고    scopus 로고
    • Historical perspectives: plasticity of mammalian skeletal muscle
    • Pette D. Historical perspectives: plasticity of mammalian skeletal muscle. J Appl Physiol 2001, 90:1119-1124.
    • (2001) J Appl Physiol , vol.90 , pp. 1119-1124
    • Pette, D.1
  • 4
    • 33744908017 scopus 로고    scopus 로고
    • Regulation of antisense RNA expression during cardiac MHC gene switching in response to pressure overload
    • Haddad F., Qin A.X., Bodell P.W., Zhang L.Y., Guo H., Giger J.M., et al. Regulation of antisense RNA expression during cardiac MHC gene switching in response to pressure overload. Am J Physiol Heart Circ Physiol 2006, 290:H2351-H2361.
    • (2006) Am J Physiol Heart Circ Physiol , vol.290
    • Haddad, F.1    Qin, A.X.2    Bodell, P.W.3    Zhang, L.Y.4    Guo, H.5    Giger, J.M.6
  • 5
    • 0033516510 scopus 로고    scopus 로고
    • Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity
    • Weiss A., Schiaffino S., Leinwand L.A. Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity. J Mol Biol 1999, 290:61-75.
    • (1999) J Mol Biol , vol.290 , pp. 61-75
    • Weiss, A.1    Schiaffino, S.2    Leinwand, L.A.3
  • 6
    • 0023216267 scopus 로고
    • The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle
    • Staron R.S., Pette D. The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle. Biochem J 1987, 243:687-693.
    • (1987) Biochem J , vol.243 , pp. 687-693
    • Staron, R.S.1    Pette, D.2
  • 7
    • 0031023872 scopus 로고    scopus 로고
    • Mammalian skeletal muscle fiber type transitions
    • Pette D., Staron R.S. Mammalian skeletal muscle fiber type transitions. Int Rev Cytol 1997, 170:143-223.
    • (1997) Int Rev Cytol , vol.170 , pp. 143-223
    • Pette, D.1    Staron, R.S.2
  • 8
    • 0034665188 scopus 로고    scopus 로고
    • Myosin isoforms, muscle fiber types, and transitions
    • Pette D., Staron R.S. Myosin isoforms, muscle fiber types, and transitions. Microsc Res Tech 2000, 50:500-509.
    • (2000) Microsc Res Tech , vol.50 , pp. 500-509
    • Pette, D.1    Staron, R.S.2
  • 9
    • 0034910559 scopus 로고    scopus 로고
    • Hybrid skeletal muscle fibres: a rare or common phenomenon?
    • Stephenson G.M. Hybrid skeletal muscle fibres: a rare or common phenomenon?. Clin Exp Pharmacol Physiol 2001, 28:692-702.
    • (2001) Clin Exp Pharmacol Physiol , vol.28 , pp. 692-702
    • Stephenson, G.M.1
  • 12
    • 0142212169 scopus 로고    scopus 로고
    • The effect of ageing and immobilization on structure and function of human skeletal muscle fibres
    • D'Antona G., Pellegrino M.A., Adami R., Rossi R., Carlizzi C.N., Canepari M., et al. The effect of ageing and immobilization on structure and function of human skeletal muscle fibres. J Physiol 2003, 552:499-511.
    • (2003) J Physiol , vol.552 , pp. 499-511
    • D'Antona, G.1    Pellegrino, M.A.2    Adami, R.3    Rossi, R.4    Carlizzi, C.N.5    Canepari, M.6
  • 13
    • 4344595487 scopus 로고    scopus 로고
    • Hybrid fibres under slow-to-fast transformations: expression is of myosin heavy and light chains in rat soleus muscle
    • Stevens L., Bastide B., Bozzo C., Mounier Y. Hybrid fibres under slow-to-fast transformations: expression is of myosin heavy and light chains in rat soleus muscle. Pflugers Arch 2004, 448:507-514.
    • (2004) Pflugers Arch , vol.448 , pp. 507-514
    • Stevens, L.1    Bastide, B.2    Bozzo, C.3    Mounier, Y.4
  • 14
    • 0027763495 scopus 로고
    • Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles
    • Larsson L., Moss R.L. Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. J Physiol 1993, 472:595-614.
    • (1993) J Physiol , vol.472 , pp. 595-614
    • Larsson, L.1    Moss, R.L.2
  • 15
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: gene regulation and functional significance
    • Schiaffino S., Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev 1996, 76:371-423.
    • (1996) Physiol Rev , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 17
    • 0033883216 scopus 로고    scopus 로고
    • Physiology of a microgravity environment invited review: microgravity and skeletal muscle
    • Fitts R.H., Riley D.R., Widrick J.J. Physiology of a microgravity environment invited review: microgravity and skeletal muscle. J Appl Physiol 2000, 89:823-839.
    • (2000) J Appl Physiol , vol.89 , pp. 823-839
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 18
    • 4644282234 scopus 로고    scopus 로고
    • Myogenic protein expression before and after resistance loading in 26- and 64-yr-old men and women
    • Bamman M.M., Ragan R.C., Kim J.S., Cross J.M., Hill V.J., Tuggle S.C., et al. Myogenic protein expression before and after resistance loading in 26- and 64-yr-old men and women. J Appl Physiol 2004, 97:1329-1337.
    • (2004) J Appl Physiol , vol.97 , pp. 1329-1337
    • Bamman, M.M.1    Ragan, R.C.2    Kim, J.S.3    Cross, J.M.4    Hill, V.J.5    Tuggle, S.C.6
  • 19
    • 0025653451 scopus 로고
    • Cellular and molecular diversities of mammalian skeletal muscle fibers
    • Pette D., Staron R.S. Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol 1990, 116:1-76.
    • (1990) Rev Physiol Biochem Pharmacol , vol.116 , pp. 1-76
    • Pette, D.1    Staron, R.S.2
  • 20
    • 79955477878 scopus 로고    scopus 로고
    • Signaling pathway controlling muscle fiber size and type in response to nerve activity. In: Springer, editor. Skeletal Muscle Plasticity in Health and Diseases: From Genes to Whole Muscle
    • Schiaffino S, Sandri M, Murgia M. Signaling pathway controlling muscle fiber size and type in response to nerve activity. In: Springer, editor. Skeletal Muscle Plasticity in Health and Diseases: From Genes to Whole Muscle 2006. p. 91-119.
    • (2006) , pp. 91-119
    • Schiaffino, S.1    Sandri, M.2    Murgia, M.3
  • 21
    • 43949109275 scopus 로고    scopus 로고
    • Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle
    • Mammucari C., Schiaffino S., Sandri M. Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle. Autophagy 2008, 4:524-526.
    • (2008) Autophagy , vol.4 , pp. 524-526
    • Mammucari, C.1    Schiaffino, S.2    Sandri, M.3
  • 22
    • 0018612076 scopus 로고
    • Muscle protein analysis. I. High-resolution two-dimensional electrophoresis of skeletal muscle proteins for analysis of small biopsy samples
    • Giometti C.S., Anderson N.G., Anderson N.L. Muscle protein analysis. I. High-resolution two-dimensional electrophoresis of skeletal muscle proteins for analysis of small biopsy samples. Clin Chem 1979, 25:1877-1884.
    • (1979) Clin Chem , vol.25 , pp. 1877-1884
    • Giometti, C.S.1    Anderson, N.G.2    Anderson, N.L.3
  • 23
    • 0018836434 scopus 로고
    • Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skeletal muscle
    • Giometti C.S., Barany M., Danon M.J., Anderson N.G. Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skeletal muscle. Clin Chem 1980, 26:1152-1155.
    • (1980) Clin Chem , vol.26 , pp. 1152-1155
    • Giometti, C.S.1    Barany, M.2    Danon, M.J.3    Anderson, N.G.4
  • 24
    • 0019820410 scopus 로고
    • Muscle protein analysis. III. Analysis of solubilized frozen-tissue sections by two-dimensional electrophoresis
    • Giometti C.S., Anderson N.G. Muscle protein analysis. III. Analysis of solubilized frozen-tissue sections by two-dimensional electrophoresis. Clin Chem 1981, 27:1918-1921.
    • (1981) Clin Chem , vol.27 , pp. 1918-1921
    • Giometti, C.S.1    Anderson, N.G.2
  • 26
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan J.X., Wait R., Berkelman T., Harry R.A., Westbrook J.A., Wheeler C.H., et al. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 2000, 21:3666-3672.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6
  • 27
    • 34548129610 scopus 로고    scopus 로고
    • Advances in hyphenated analytical techniques for shotgun proteome and peptidome analysis-a review
    • Hu L., Ye M., Jiang X., Feng S., Zou H. Advances in hyphenated analytical techniques for shotgun proteome and peptidome analysis-a review. Anal Chim Acta 2007, 598:193-204.
    • (2007) Anal Chim Acta , vol.598 , pp. 193-204
    • Hu, L.1    Ye, M.2    Jiang, X.3    Feng, S.4    Zou, H.5
  • 28
    • 23944456877 scopus 로고    scopus 로고
    • Comparison of alternative analytical techniques for the characterisation of the human serum proteome in HUPO Plasma Proteome Project
    • Li X., Gong Y., Wang Y., Wu S., Cai Y., He P., et al. Comparison of alternative analytical techniques for the characterisation of the human serum proteome in HUPO Plasma Proteome Project. Proteomics 2005, 5:3423-3441.
    • (2005) Proteomics , vol.5 , pp. 3423-3441
    • Li, X.1    Gong, Y.2    Wang, Y.3    Wu, S.4    Cai, Y.5    He, P.6
  • 29
    • 39749097121 scopus 로고    scopus 로고
    • Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS
    • Hojlund K., Yi Z., Hwang H., Bowen B., Lefort N., Flynn C.R., et al. Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. Mol Cell Proteomics 2008, 7:257-267.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 257-267
    • Hojlund, K.1    Yi, Z.2    Hwang, H.3    Bowen, B.4    Lefort, N.5    Flynn, C.R.6
  • 30
    • 53049093175 scopus 로고    scopus 로고
    • Global relationship between the proteome and transcriptome of human skeletal muscle
    • Yi Z., Bowen B.P., Hwang H., Jenkinson C.P., Coletta D.K., Lefort N., et al. Global relationship between the proteome and transcriptome of human skeletal muscle. J Proteome Res 2008, 7:3230-3241.
    • (2008) J Proteome Res , vol.7 , pp. 3230-3241
    • Yi, Z.1    Bowen, B.P.2    Hwang, H.3    Jenkinson, C.P.4    Coletta, D.K.5    Lefort, N.6
  • 31
    • 33749605124 scopus 로고    scopus 로고
    • Parallel protein and transcript profiles of FSHD patient muscles correlate to the D4Z4 arrangement and reveal a common impairment of slow to fast fibre differentiation and a general deregulation of MyoD-dependent genes
    • Celegato B., Capitanio D., Pescatori M., Romualdi C., Pacchioni B., Cagnin S., et al. Parallel protein and transcript profiles of FSHD patient muscles correlate to the D4Z4 arrangement and reveal a common impairment of slow to fast fibre differentiation and a general deregulation of MyoD-dependent genes. Proteomics 2006, 6:5303-5321.
    • (2006) Proteomics , vol.6 , pp. 5303-5321
    • Celegato, B.1    Capitanio, D.2    Pescatori, M.3    Romualdi, C.4    Pacchioni, B.5    Cagnin, S.6
  • 33
    • 34548264161 scopus 로고    scopus 로고
    • Activity-dependent signaling pathways controlling muscle diversity and plasticity
    • Schiaffino S., Sandri M., Murgia M. Activity-dependent signaling pathways controlling muscle diversity and plasticity. Physiology (Bethesda) 2007, 22:269-278.
    • (2007) Physiology (Bethesda) , vol.22 , pp. 269-278
    • Schiaffino, S.1    Sandri, M.2    Murgia, M.3
  • 34
    • 9244247879 scopus 로고    scopus 로고
    • Signaling pathways weigh in on decisions to make or break skeletal muscle
    • Guttridge D.C. Signaling pathways weigh in on decisions to make or break skeletal muscle. Curr Opin Clin Nutr Metab Care 2004, 7:443-450.
    • (2004) Curr Opin Clin Nutr Metab Care , vol.7 , pp. 443-450
    • Guttridge, D.C.1
  • 35
    • 33744494538 scopus 로고    scopus 로고
    • The sarcomeric Z-disc: a nodal point in signalling and disease
    • Frank D., Kuhn C., Katus H.A., Frey N. The sarcomeric Z-disc: a nodal point in signalling and disease. J Mol Med 2006, 84:446-468.
    • (2006) J Mol Med , vol.84 , pp. 446-468
    • Frank, D.1    Kuhn, C.2    Katus, H.A.3    Frey, N.4
  • 36
    • 70449436408 scopus 로고    scopus 로고
    • In vivo phosphoproteome of human skeletal muscle revealed by phosphopeptide enrichment and HPLC-ESI-MS/MS
    • Hojlund K., Bowen B.P., Hwang H., Flynn C.R., Madireddy L., Geetha T., et al. In vivo phosphoproteome of human skeletal muscle revealed by phosphopeptide enrichment and HPLC-ESI-MS/MS. J Proteome Res 2009, 8:4954-4965.
    • (2009) J Proteome Res , vol.8 , pp. 4954-4965
    • Hojlund, K.1    Bowen, B.P.2    Hwang, H.3    Flynn, C.R.4    Madireddy, L.5    Geetha, T.6
  • 37
    • 67651151024 scopus 로고    scopus 로고
    • Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS
    • Lefort N., Yi Z., Bowen B., Glancy B., De Filippis E.A., Mapes R., et al. Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. J Proteomics 2009, 72:1046-1060.
    • (2009) J Proteomics , vol.72 , pp. 1046-1060
    • Lefort, N.1    Yi, Z.2    Bowen, B.3    Glancy, B.4    De Filippis, E.A.5    Mapes, R.6
  • 38
    • 78651069971 scopus 로고    scopus 로고
    • Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes
    • (Electronic publication ahead of print)
    • Zhao X., Leon I.R., Bak S., Mogensen M., Wrzesinski K., Hojlund K., et al. Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol Cell Proteomics 2010, (Electronic publication ahead of print).
    • (2010) Mol Cell Proteomics
    • Zhao, X.1    Leon, I.R.2    Bak, S.3    Mogensen, M.4    Wrzesinski, K.5    Hojlund, K.6
  • 39
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: a single gel method for detecting changes in protein extracts
    • Unlu M., Morgan M.E., Minden J.S. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 40
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge R., Shaw J., Middleton B., Rowlinson R., Rayner S., Young J., et al. Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1:377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3    Rowlinson, R.4    Rayner, S.5    Young, J.6
  • 41
    • 22044437550 scopus 로고    scopus 로고
    • Comparison of protein expression in human deltoideus and vastus lateralis muscles using two-dimensional gel electrophoresis
    • Capitanio D., Vigano A., Ricci E., Cerretelli P., Wait R., Gelfi C. Comparison of protein expression in human deltoideus and vastus lateralis muscles using two-dimensional gel electrophoresis. Proteomics 2005, 5:2577-2586.
    • (2005) Proteomics , vol.5 , pp. 2577-2586
    • Capitanio, D.1    Vigano, A.2    Ricci, E.3    Cerretelli, P.4    Wait, R.5    Gelfi, C.6
  • 44
    • 17844391820 scopus 로고    scopus 로고
    • Proteome analysis of skeletal muscle from obese and morbidly obese women
    • Hittel D.S., Hathout Y., Hoffman E.P., Houmard J.A. Proteome analysis of skeletal muscle from obese and morbidly obese women. Diabetes 2005, 54:1283-1288.
    • (2005) Diabetes , vol.54 , pp. 1283-1288
    • Hittel, D.S.1    Hathout, Y.2    Hoffman, E.P.3    Houmard, J.A.4
  • 45
    • 0038576291 scopus 로고    scopus 로고
    • Proteome analysis reveals phosphorylation of ATP synthase beta-subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes
    • Hojlund K., Wrzesinski K., Larsen P.M., Fey S.J., Roepstorff P., Handberg A., et al. Proteome analysis reveals phosphorylation of ATP synthase beta-subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes. J Biol Chem 2003, 278:10436-10442.
    • (2003) J Biol Chem , vol.278 , pp. 10436-10442
    • Hojlund, K.1    Wrzesinski, K.2    Larsen, P.M.3    Fey, S.J.4    Roepstorff, P.5    Handberg, A.6
  • 46
    • 55849092859 scopus 로고    scopus 로고
    • Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia
    • Vigano A., Ripamonti M., De Palma S., Capitanio D., Vasso M., Wait R., et al. Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia. Proteomics 2008, 8:4668-4679.
    • (2008) Proteomics , vol.8 , pp. 4668-4679
    • Vigano, A.1    Ripamonti, M.2    De Palma, S.3    Capitanio, D.4    Vasso, M.5    Wait, R.6
  • 47
    • 34249292919 scopus 로고    scopus 로고
    • Metabolic modulation induced by chronic hypoxia in rats using a comparative proteomic analysis of skeletal muscle tissue
    • De Palma S., Ripamonti M., Vigano A., Moriggi M., Capitanio D., Samaja M., et al. Metabolic modulation induced by chronic hypoxia in rats using a comparative proteomic analysis of skeletal muscle tissue. J Proteome Res 2007, 6:1974-1984.
    • (2007) J Proteome Res , vol.6 , pp. 1974-1984
    • De Palma, S.1    Ripamonti, M.2    Vigano, A.3    Moriggi, M.4    Capitanio, D.5    Samaja, M.6
  • 48
    • 17044399794 scopus 로고    scopus 로고
    • Protein expression patterns in zebrafish skeletal muscle: initial characterization and the effects of hypoxic exposure
    • Bosworth CAt, Chou C.W., Cole R.B., Rees B.B. Protein expression patterns in zebrafish skeletal muscle: initial characterization and the effects of hypoxic exposure. Proteomics 2005, 5:1362-1371.
    • (2005) Proteomics , vol.5 , pp. 1362-1371
    • Bosworth, C.1    Chou, C.W.2    Cole, R.B.3    Rees, B.B.4
  • 49
    • 77951878397 scopus 로고    scopus 로고
    • Role of intermittent hypoxia in the treatment of bronchial asthma and chronic obstructive pulmonary disease
    • Vogtel M., Michels A. Role of intermittent hypoxia in the treatment of bronchial asthma and chronic obstructive pulmonary disease. Curr Opin Allergy Clin Immunol 2010, 10:206-213.
    • (2010) Curr Opin Allergy Clin Immunol , vol.10 , pp. 206-213
    • Vogtel, M.1    Michels, A.2
  • 50
    • 0015547811 scopus 로고
    • Data on the distribution of fibre types in thirty-six human muscles. An autopsy study
    • Johnson M.A., Polgar J., Weightman D., Appleton D. Data on the distribution of fibre types in thirty-six human muscles. An autopsy study. J Neurol Sci 1973, 18:111-129.
    • (1973) J Neurol Sci , vol.18 , pp. 111-129
    • Johnson, M.A.1    Polgar, J.2    Weightman, D.3    Appleton, D.4
  • 52
    • 0030055292 scopus 로고    scopus 로고
    • Microgravity-induced transformations of myosin isoforms and contractile properties of skeletal muscle
    • Caiozzo V.J., Haddad F., Baker M.J., Herrick R.E., Prietto N., Baldwin K.M. Microgravity-induced transformations of myosin isoforms and contractile properties of skeletal muscle. J Appl Physiol 1996, 81:123-132.
    • (1996) J Appl Physiol , vol.81 , pp. 123-132
    • Caiozzo, V.J.1    Haddad, F.2    Baker, M.J.3    Herrick, R.E.4    Prietto, N.5    Baldwin, K.M.6
  • 53
    • 31344475538 scopus 로고    scopus 로고
    • 2-D protein maps of rat gastrocnemius and soleus muscles: a tool for muscle plasticity assessment
    • Gelfi C., Vigano A., De Palma S., Ripamonti M., Begum S., Cerretelli P., et al. 2-D protein maps of rat gastrocnemius and soleus muscles: a tool for muscle plasticity assessment. Proteomics 2006, 6:321-340.
    • (2006) Proteomics , vol.6 , pp. 321-340
    • Gelfi, C.1    Vigano, A.2    De Palma, S.3    Ripamonti, M.4    Begum, S.5    Cerretelli, P.6
  • 54
    • 0026443844 scopus 로고
    • Thermogenic response to epinephrine in the forearm and abdominal subcutaneous adipose tissue
    • Simonsen L., Bulow J., Madsen J., Christensen N.J. Thermogenic response to epinephrine in the forearm and abdominal subcutaneous adipose tissue. Am J Physiol 1992, 263:E850-E855.
    • (1992) Am J Physiol , vol.263
    • Simonsen, L.1    Bulow, J.2    Madsen, J.3    Christensen, N.J.4
  • 55
    • 0022065787 scopus 로고
    • Contribution of BAT and skeletal muscle to thermogenesis induced by ephedrine in man
    • Astrup A., Bulow J., Madsen J., Christensen N.J. Contribution of BAT and skeletal muscle to thermogenesis induced by ephedrine in man. Am J Physiol 1985, 248:E507-E515.
    • (1985) Am J Physiol , vol.248
    • Astrup, A.1    Bulow, J.2    Madsen, J.3    Christensen, N.J.4
  • 56
    • 46349110454 scopus 로고    scopus 로고
    • Human skeletal muscle mitochondrial uncoupling is associated with cold induced adaptive thermogenesis
    • Wijers S.L., Schrauwen P., Saris W.H., van Marken Lichtenbelt W.D. Human skeletal muscle mitochondrial uncoupling is associated with cold induced adaptive thermogenesis. PLoS ONE 2008, 3:e1777.
    • (2008) PLoS ONE , vol.3
    • Wijers, S.L.1    Schrauwen, P.2    Saris, W.H.3    van Marken Lichtenbelt, W.D.4
  • 58
    • 0036434239 scopus 로고    scopus 로고
    • Prediction of body weight changes caused by changes in energy balance
    • Christiansen E., Garby L. Prediction of body weight changes caused by changes in energy balance. Eur J Clin Invest 2002, 32:826-830.
    • (2002) Eur J Clin Invest , vol.32 , pp. 826-830
    • Christiansen, E.1    Garby, L.2
  • 59
    • 70949099713 scopus 로고    scopus 로고
    • Proteomic investigation of changes in human vastus lateralis muscle in response to interval-exercise training
    • Holloway K.V., O'Gorman M., Woods P., Morton J.P., Evans L., Cable N.T., et al. Proteomic investigation of changes in human vastus lateralis muscle in response to interval-exercise training. Proteomics 2009, 9:5155-5174.
    • (2009) Proteomics , vol.9 , pp. 5155-5174
    • Holloway, K.V.1    O'Gorman, M.2    Woods, P.3    Morton, J.P.4    Evans, L.5    Cable, N.T.6
  • 60
    • 37749021969 scopus 로고    scopus 로고
    • Similar metabolic adaptations during exercise after low volume sprint interval and traditional endurance training in humans
    • Burgomaster K.A., Howarth K.R., Phillips S.M., Rakobowchuk M., Macdonald M.J., McGee S.L., et al. Similar metabolic adaptations during exercise after low volume sprint interval and traditional endurance training in humans. J Physiol 2008, 586:151-160.
    • (2008) J Physiol , vol.586 , pp. 151-160
    • Burgomaster, K.A.1    Howarth, K.R.2    Phillips, S.M.3    Rakobowchuk, M.4    Macdonald, M.J.5    McGee, S.L.6
  • 61
    • 52449135519 scopus 로고    scopus 로고
    • Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise
    • Burniston J.G. Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise. Biochim Biophys Acta 2008, 1784:1077-1086.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1077-1086
    • Burniston, J.G.1
  • 62
    • 24944591029 scopus 로고    scopus 로고
    • Exercise-related novel gene is involved in myoblast differentiation
    • Takahashi M., Kubota S. Exercise-related novel gene is involved in myoblast differentiation. Biomed Res 2005, 26:79-85.
    • (2005) Biomed Res , vol.26 , pp. 79-85
    • Takahashi, M.1    Kubota, S.2
  • 63
    • 33748888361 scopus 로고    scopus 로고
    • A proteomic analysis of the acute effects of high-intensity exercise on skeletal muscle proteins in fasted rats
    • Guelfi K.J., Casey T.M., Giles J.J., Fournier P.A., Arthur P.G. A proteomic analysis of the acute effects of high-intensity exercise on skeletal muscle proteins in fasted rats. Clin Exp Pharmacol Physiol 2006, 33:952-957.
    • (2006) Clin Exp Pharmacol Physiol , vol.33 , pp. 952-957
    • Guelfi, K.J.1    Casey, T.M.2    Giles, J.J.3    Fournier, P.A.4    Arthur, P.G.5
  • 64
    • 79955475309 scopus 로고    scopus 로고
    • Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise
    • (Electronic publication ahead of print)
    • Gandra P.G., Valente R.H., Perales J., Pacheco A.G., Macedo D.V. Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise. Scand J Med Sci Sports 2010, (Electronic publication ahead of print).
    • (2010) Scand J Med Sci Sports
    • Gandra, P.G.1    Valente, R.H.2    Perales, J.3    Pacheco, A.G.4    Macedo, D.V.5
  • 65
    • 77956441071 scopus 로고    scopus 로고
    • A DIGE proteomic analysis for high-intensity exercise-trained rat skeletal muscle
    • Yamaguchi W., Fujimoto E., Higuchi M., Tabata I. A DIGE proteomic analysis for high-intensity exercise-trained rat skeletal muscle. J Biochem 2010, 148:327-333.
    • (2010) J Biochem , vol.148 , pp. 327-333
    • Yamaguchi, W.1    Fujimoto, E.2    Higuchi, M.3    Tabata, I.4
  • 67
    • 0033927851 scopus 로고    scopus 로고
    • Skeletal muscle mass and distribution in 468 men and women aged 18-88yr
    • Janssen I., Heymsfield S.B., Wang Z.M., Ross R. Skeletal muscle mass and distribution in 468 men and women aged 18-88yr. J Appl Physiol 2000, 89:81-88.
    • (2000) J Appl Physiol , vol.89 , pp. 81-88
    • Janssen, I.1    Heymsfield, S.B.2    Wang, Z.M.3    Ross, R.4
  • 68
    • 0032812431 scopus 로고    scopus 로고
    • Specific strength and voluntary muscle activation in young and elderly women and men
    • Kent-Braun J.A., Ng A.V. Specific strength and voluntary muscle activation in young and elderly women and men. J Appl Physiol 1999, 87:22-29.
    • (1999) J Appl Physiol , vol.87 , pp. 22-29
    • Kent-Braun, J.A.1    Ng, A.V.2
  • 70
    • 0030934826 scopus 로고    scopus 로고
    • Effects of aging on shortening velocity and myosin isoform composition in single human skeletal muscle cells
    • Larsson L., Li X., Frontera W.R. Effects of aging on shortening velocity and myosin isoform composition in single human skeletal muscle cells. Am J Physiol 1997, 272:C638-C649.
    • (1997) Am J Physiol , vol.272
    • Larsson, L.1    Li, X.2    Frontera, W.R.3
  • 72
    • 0028863055 scopus 로고
    • Human aging, muscle mass, and fiber type composition
    • Spec No:11-6
    • Lexell J. Human aging, muscle mass, and fiber type composition. J Gerontol A Biol Sci Med Sci 1995, 50. Spec No:11-6.
    • (1995) J Gerontol A Biol Sci Med Sci , vol.50
    • Lexell, J.1
  • 73
    • 0026592838 scopus 로고
    • Aging and muscle function
    • Aoyagi Y., Shephard R.J. Aging and muscle function. Sports Med 1992, 14:376-396.
    • (1992) Sports Med , vol.14 , pp. 376-396
    • Aoyagi, Y.1    Shephard, R.J.2
  • 74
    • 0025358143 scopus 로고
    • Histochemical and enzymatic characteristics of skeletal muscle in master athletes
    • Coggan A.R., Spina R.J., Rogers M.A., King D.S., Brown M., Nemeth P.M., et al. Histochemical and enzymatic characteristics of skeletal muscle in master athletes. J Appl Physiol 1990, 68:1896-1901.
    • (1990) J Appl Physiol , vol.68 , pp. 1896-1901
    • Coggan, A.R.1    Spina, R.J.2    Rogers, M.A.3    King, D.S.4    Brown, M.5    Nemeth, P.M.6
  • 76
    • 0036262770 scopus 로고    scopus 로고
    • Effects of aging on human skeletal muscle myosin heavy-chain mRNA content and protein isoform expression
    • Marx J.O., Kraemer W.J., Nindl B.C., Larsson L. Effects of aging on human skeletal muscle myosin heavy-chain mRNA content and protein isoform expression. J Gerontol A Biol Sci Med Sci 2002, 57:B232-B238.
    • (2002) J Gerontol A Biol Sci Med Sci , vol.57
    • Marx, J.O.1    Kraemer, W.J.2    Nindl, B.C.3    Larsson, L.4
  • 77
    • 0034996561 scopus 로고    scopus 로고
    • Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise
    • Balagopal P., Schimke J.C., Ades P., Adey D., Nair K.S. Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise. Am J Physiol Endocrinol Metab 2001, 280:E203-E208.
    • (2001) Am J Physiol Endocrinol Metab , vol.280
    • Balagopal, P.1    Schimke, J.C.2    Ades, P.3    Adey, D.4    Nair, K.S.5
  • 78
    • 0031889998 scopus 로고    scopus 로고
    • Lipofuscin: mechanisms of formation and increase with age
    • Terman A., Brunk U.T. Lipofuscin: mechanisms of formation and increase with age. APMIS 1998, 106:265-276.
    • (1998) APMIS , vol.106 , pp. 265-276
    • Terman, A.1    Brunk, U.T.2
  • 79
    • 0034029252 scopus 로고    scopus 로고
    • L-Type Ca(2+) channel charge movement and intracellular Ca(2+) in skeletal muscle fibers from aging mice
    • Wang Z.M., Messi M.L., Delbono O. L-Type Ca(2+) channel charge movement and intracellular Ca(2+) in skeletal muscle fibers from aging mice. Biophys J 2000, 78:1947-1954.
    • (2000) Biophys J , vol.78 , pp. 1947-1954
    • Wang, Z.M.1    Messi, M.L.2    Delbono, O.3
  • 81
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function
    • Sweeney H.L., Bowman B.F., Stull J.T. Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function. Am J Physiol 1993, 264:C1085-C1095.
    • (1993) Am J Physiol , vol.264
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 82
    • 0036286168 scopus 로고    scopus 로고
    • Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction
    • Davis J.S., Satorius C.L., Epstein N.D. Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction. Biophys J 2002, 83:359-370.
    • (2002) Biophys J , vol.83 , pp. 359-370
    • Davis, J.S.1    Satorius, C.L.2    Epstein, N.D.3
  • 83
    • 0036095636 scopus 로고    scopus 로고
    • Phosphorylation of the regulatory light chains of myosin affects Ca2+ sensitivity of skeletal muscle contraction
    • Szczesna D., Zhao J., Jones M., Zhi G., Stull J., Potter J.D. Phosphorylation of the regulatory light chains of myosin affects Ca2+ sensitivity of skeletal muscle contraction. J Appl Physiol 2002, 92:1661-1670.
    • (2002) J Appl Physiol , vol.92 , pp. 1661-1670
    • Szczesna, D.1    Zhao, J.2    Jones, M.3    Zhi, G.4    Stull, J.5    Potter, J.D.6
  • 84
    • 0024661091 scopus 로고
    • Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle
    • Godt R.E., Nosek T.M. Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle. J Physiol 1989, 412:155-180.
    • (1989) J Physiol , vol.412 , pp. 155-180
    • Godt, R.E.1    Nosek, T.M.2
  • 87
    • 65349118124 scopus 로고    scopus 로고
    • Comparative proteomic profile of rat sciatic nerve and gastrocnemius muscle tissues in ageing by 2-D DIGE
    • Capitanio D., Vasso M., Fania C., Moriggi M., Vigano A., Procacci P., et al. Comparative proteomic profile of rat sciatic nerve and gastrocnemius muscle tissues in ageing by 2-D DIGE. Proteomics 2009, 9:2004-2020.
    • (2009) Proteomics , vol.9 , pp. 2004-2020
    • Capitanio, D.1    Vasso, M.2    Fania, C.3    Moriggi, M.4    Vigano, A.5    Procacci, P.6
  • 88
    • 78049354620 scopus 로고    scopus 로고
    • Long term bed rest with and without vibration exercise countermeasures: effects on human muscle protein dysregulation
    • Moriggi M., Vasso M., Fania C., Capitanio D., Bonifacio G., Salanova M., et al. Long term bed rest with and without vibration exercise countermeasures: effects on human muscle protein dysregulation. Proteomics 2010, 10:3756-3774.
    • (2010) Proteomics , vol.10 , pp. 3756-3774
    • Moriggi, M.1    Vasso, M.2    Fania, C.3    Capitanio, D.4    Bonifacio, G.5    Salanova, M.6
  • 90
    • 38049091591 scopus 로고    scopus 로고
    • Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization
    • Udaka J., Ohmori S., Terui T., Ohtsuki I., Ishiwata S., Kurihara S., et al. Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization. J Gen Physiol 2008, 131:33-41.
    • (2008) J Gen Physiol , vol.131 , pp. 33-41
    • Udaka, J.1    Ohmori, S.2    Terui, T.3    Ohtsuki, I.4    Ishiwata, S.5    Kurihara, S.6
  • 91
    • 33646081053 scopus 로고    scopus 로고
    • Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures
    • Hoshijima M. Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures. Am J Physiol Heart Circ Physiol 2006, 290:H1313-H1325.
    • (2006) Am J Physiol Heart Circ Physiol , vol.290
    • Hoshijima, M.1
  • 92
    • 0036248674 scopus 로고    scopus 로고
    • Proteomic analysis of rat soleus muscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy
    • Isfort R.J., Wang F., Greis K.D., Sun Y., Keough T.W., Farrar R.P., et al. Proteomic analysis of rat soleus muscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy. Proteomics 2002, 2:543-550.
    • (2002) Proteomics , vol.2 , pp. 543-550
    • Isfort, R.J.1    Wang, F.2    Greis, K.D.3    Sun, Y.4    Keough, T.W.5    Farrar, R.P.6
  • 94
    • 32944477616 scopus 로고    scopus 로고
    • A proteomic assessment of muscle contractile alterations during unloading and reloading
    • Seo Y., Lee K., Park K., Bae K., Choi I. A proteomic assessment of muscle contractile alterations during unloading and reloading. J Biochem 2006, 139:71-80.
    • (2006) J Biochem , vol.139 , pp. 71-80
    • Seo, Y.1    Lee, K.2    Park, K.3    Bae, K.4    Choi, I.5
  • 95
    • 52649085309 scopus 로고    scopus 로고
    • A DIGE approach for the assessment of rat soleus muscle changes during unloading: effect of acetyl-L-carnitine supplementation
    • Moriggi M., Cassano P., Vasso M., Capitanio D., Fania C., Musicco C., et al. A DIGE approach for the assessment of rat soleus muscle changes during unloading: effect of acetyl-L-carnitine supplementation. Proteomics 2008, 8:3588-3604.
    • (2008) Proteomics , vol.8 , pp. 3588-3604
    • Moriggi, M.1    Cassano, P.2    Vasso, M.3    Capitanio, D.4    Fania, C.5    Musicco, C.6
  • 96
    • 0032810984 scopus 로고    scopus 로고
    • Skeletal muscle injury induced by eccentric muscle action: muscle proteins as markers of muscle fiber injury
    • Sorichter S., Puschendorf B., Mair J. Skeletal muscle injury induced by eccentric muscle action: muscle proteins as markers of muscle fiber injury. Exerc Immunol Rev 1999, 5:5-21.
    • (1999) Exerc Immunol Rev , vol.5 , pp. 5-21
    • Sorichter, S.1    Puschendorf, B.2    Mair, J.3
  • 98
    • 33846410247 scopus 로고    scopus 로고
    • Quantitative analysis of complex peptide mixtures using FTMS and differential mass spectrometry
    • Meng F., Wiener M.C., Sachs J.R., Burns C., Verma P., Paweletz C.P., et al. Quantitative analysis of complex peptide mixtures using FTMS and differential mass spectrometry. J Am Soc Mass Spectrom 2007, 18:226-233.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 226-233
    • Meng, F.1    Wiener, M.C.2    Sachs, J.R.3    Burns, C.4    Verma, P.5    Paweletz, C.P.6
  • 99
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H., Li X.J., Martin D.B., Aebersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 2003, 21:660-666.
    • (2003) Nat Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 100
    • 20144383119 scopus 로고    scopus 로고
    • High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry
    • Zhang H., Yi E.C., Li X.J., Mallick P., Kelly-Spratt K.S., Masselon C.D., et al. High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry. Mol Cell Proteomics 2005, 4:144-155.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 144-155
    • Zhang, H.1    Yi, E.C.2    Li, X.J.3    Mallick, P.4    Kelly-Spratt, K.S.5    Masselon, C.D.6
  • 101
    • 42549137898 scopus 로고    scopus 로고
    • Serum protein profiling in mice: identification of Factor XIIIa as a potential biomarker for muscular dystrophy
    • Alagaratnam S., Mertens B.J., Dalebout J.C., Deelder A.M., van Ommen G.J., den Dunnen J.T., et al. Serum protein profiling in mice: identification of Factor XIIIa as a potential biomarker for muscular dystrophy. Proteomics 2008, 8:1552-1563.
    • (2008) Proteomics , vol.8 , pp. 1552-1563
    • Alagaratnam, S.1    Mertens, B.J.2    Dalebout, J.C.3    Deelder, A.M.4    van Ommen, G.J.5    den Dunnen, J.T.6
  • 102
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP
    • Doran P., Martin G., Dowling P., Jockusch H., Ohlendieck K. Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics 2006, 6:4610-4621.
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 103
    • 31344467095 scopus 로고    scopus 로고
    • Proteomic investigation of the molecular pathophysiology of dysferlinopathy
    • De Palma S., Morandi L., Mariani E., Begum S., Cerretelli P., Wait R., et al. Proteomic investigation of the molecular pathophysiology of dysferlinopathy. Proteomics 2006, 6:379-385.
    • (2006) Proteomics , vol.6 , pp. 379-385
    • De Palma, S.1    Morandi, L.2    Mariani, E.3    Begum, S.4    Cerretelli, P.5    Wait, R.6
  • 104
  • 105
    • 17344365600 scopus 로고    scopus 로고
    • Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy
    • Liu J., Aoki M., Illa I., Wu C., Fardeau M., Angelini C., et al. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nat Genet 1998, 20:31-36.
    • (1998) Nat Genet , vol.20 , pp. 31-36
    • Liu, J.1    Aoki, M.2    Illa, I.3    Wu, C.4    Fardeau, M.5    Angelini, C.6
  • 106
    • 0038629355 scopus 로고    scopus 로고
    • Protein and gene analyses of dysferlinopathy in a large group of Japanese muscular dystrophy patients
    • Tagawa K., Ogawa M., Kawabe K., Yamanaka G., Matsumura T., Goto K., et al. Protein and gene analyses of dysferlinopathy in a large group of Japanese muscular dystrophy patients. J Neurol Sci 2003, 211:23-28.
    • (2003) J Neurol Sci , vol.211 , pp. 23-28
    • Tagawa, K.1    Ogawa, M.2    Kawabe, K.3    Yamanaka, G.4    Matsumura, T.5    Goto, K.6
  • 107
    • 0037738510 scopus 로고    scopus 로고
    • Defective membrane repair in dysferlin-deficient muscular dystrophy
    • Bansal D., Miyake K., Vogel S.S., Groh S., Chen C.C., Williamson R., et al. Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 2003, 423:168-172.
    • (2003) Nature , vol.423 , pp. 168-172
    • Bansal, D.1    Miyake, K.2    Vogel, S.S.3    Groh, S.4    Chen, C.C.5    Williamson, R.6
  • 108
    • 13244284886 scopus 로고    scopus 로고
    • Ultrastructural changes in dysferlinopathy support defective membrane repair mechanism
    • Cenacchi G., Fanin M., De Giorgi L.B., Angelini C. Ultrastructural changes in dysferlinopathy support defective membrane repair mechanism. J Clin Pathol 2005, 58:190-195.
    • (2005) J Clin Pathol , vol.58 , pp. 190-195
    • Cenacchi, G.1    Fanin, M.2    De Giorgi, L.B.3    Angelini, C.4
  • 110
    • 0344391975 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments
    • Ono S. Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments. Biochemistry 2003, 42:13363-13370.
    • (2003) Biochemistry , vol.42 , pp. 13363-13370
    • Ono, S.1
  • 112
    • 0037118064 scopus 로고    scopus 로고
    • The Wnt/calcium pathway activates NF-AT and promotes ventral cell fate in Xenopus embryos
    • Saneyoshi T., Kume S., Amasaki Y., Mikoshiba K. The Wnt/calcium pathway activates NF-AT and promotes ventral cell fate in Xenopus embryos. Nature 2002, 417:295-299.
    • (2002) Nature , vol.417 , pp. 295-299
    • Saneyoshi, T.1    Kume, S.2    Amasaki, Y.3    Mikoshiba, K.4
  • 113
    • 0035929580 scopus 로고    scopus 로고
    • A novel myocyte-specific gene Midori promotes the differentiation of P19CL6 cells into cardiomyocytes
    • Hosoda T., Monzen K., Hiroi Y., Oka T., Takimoto E., Yazaki Y., et al. A novel myocyte-specific gene Midori promotes the differentiation of P19CL6 cells into cardiomyocytes. J Biol Chem 2001, 276:35978-35989.
    • (2001) J Biol Chem , vol.276 , pp. 35978-35989
    • Hosoda, T.1    Monzen, K.2    Hiroi, Y.3    Oka, T.4    Takimoto, E.5    Yazaki, Y.6
  • 115
    • 0034646141 scopus 로고    scopus 로고
    • AlphaB-crystallin immunolocalization yields new insights into inclusion body myositis
    • Banwell B.L., Engel A.G. AlphaB-crystallin immunolocalization yields new insights into inclusion body myositis. Neurology 2000, 54:1033-1041.
    • (2000) Neurology , vol.54 , pp. 1033-1041
    • Banwell, B.L.1    Engel, A.G.2
  • 116
    • 39649093167 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in inclusion body myositis
    • Hutchinson D.O., Jongbloed B. Two-dimensional gel electrophoresis in inclusion body myositis. J Clin Neurosci 2008, 15:440-444.
    • (2008) J Clin Neurosci , vol.15 , pp. 440-444
    • Hutchinson, D.O.1    Jongbloed, B.2
  • 119
    • 38649129756 scopus 로고    scopus 로고
    • The effects of shared peptides on protein quantitation in label-free proteomics by LC/MS/MS
    • Jin S., Daly D.S., Springer D.L., Miller J.H. The effects of shared peptides on protein quantitation in label-free proteomics by LC/MS/MS. J Proteome Res 2008, 7:164-169.
    • (2008) J Proteome Res , vol.7 , pp. 164-169
    • Jin, S.1    Daly, D.S.2    Springer, D.L.3    Miller, J.H.4
  • 121
    • 0033791932 scopus 로고    scopus 로고
    • Muscle abnormalities in juvenile dermatomyositis patients: P-31 magnetic resonance spectroscopy studies
    • Park J.H., Niermann K.J., Ryder N.M., Nelson A.E., Das A., Lawton A.R., et al. Muscle abnormalities in juvenile dermatomyositis patients: P-31 magnetic resonance spectroscopy studies. Arthritis Rheum 2000, 43:2359-2367.
    • (2000) Arthritis Rheum , vol.43 , pp. 2359-2367
    • Park, J.H.1    Niermann, K.J.2    Ryder, N.M.3    Nelson, A.E.4    Das, A.5    Lawton, A.R.6
  • 123
    • 77649298737 scopus 로고    scopus 로고
    • Interferon-stimulated gene 15 (ISG15) conjugates proteins in dermatomyositis muscle with perifascicular atrophy
    • Salajegheh M., Kong S.W., Pinkus J.L., Walsh R.J., Liao A., Nazareno R., et al. Interferon-stimulated gene 15 (ISG15) conjugates proteins in dermatomyositis muscle with perifascicular atrophy. Ann Neurol 2010, 67:53-63.
    • (2010) Ann Neurol , vol.67 , pp. 53-63
    • Salajegheh, M.1    Kong, S.W.2    Pinkus, J.L.3    Walsh, R.J.4    Liao, A.5    Nazareno, R.6
  • 124
    • 34948900717 scopus 로고    scopus 로고
    • Type I interferon-inducible gene expression in blood is present and reflects disease activity in dermatomyositis and polymyositis
    • Walsh R.J., Kong S.W., Yao Y., Jallal B., Kiener P.A., Pinkus J.L., et al. Type I interferon-inducible gene expression in blood is present and reflects disease activity in dermatomyositis and polymyositis. Arthritis Rheum 2007, 56:3784-3792.
    • (2007) Arthritis Rheum , vol.56 , pp. 3784-3792
    • Walsh, R.J.1    Kong, S.W.2    Yao, Y.3    Jallal, B.4    Kiener, P.A.5    Pinkus, J.L.6
  • 125
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan W., Krug R.M. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J 2001, 20:362-371.
    • (2001) EMBO J , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 126
    • 2442717751 scopus 로고    scopus 로고
    • The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein
    • Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W., Schulman B.A., et al. The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein. Proc Natl Acad Sci USA 2004, 101:7578-7582.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7578-7582
    • Zhao, C.1    Beaudenon, S.L.2    Kelley, M.L.3    Waddell, M.B.4    Yuan, W.5    Schulman, B.A.6
  • 127
    • 33645230779 scopus 로고    scopus 로고
    • Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells
    • Dastur A., Beaudenon S., Kelley M., Krug R.M., Huibregtse J.M. Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells. J Biol Chem 2006, 281:4334-4338.
    • (2006) J Biol Chem , vol.281 , pp. 4334-4338
    • Dastur, A.1    Beaudenon, S.2    Kelley, M.3    Krug, R.M.4    Huibregtse, J.M.5
  • 129
    • 31544460359 scopus 로고    scopus 로고
    • Elevated expression of ISG15 in tumor cells interferes with the ubiquitin/26S proteasome pathway
    • Desai S.D., Haas A.L., Wood L.M., Tsai Y.C., Pestka S., Rubin E.H., et al. Elevated expression of ISG15 in tumor cells interferes with the ubiquitin/26S proteasome pathway. Cancer Res 2006, 66:921-928.
    • (2006) Cancer Res , vol.66 , pp. 921-928
    • Desai, S.D.1    Haas, A.L.2    Wood, L.M.3    Tsai, Y.C.4    Pestka, S.5    Rubin, E.H.6
  • 130
    • 0032469474 scopus 로고    scopus 로고
    • Mechanisms of insulin resistance in non-oxidative glucose metabolism: the role of glycogen synthase
    • Beck-Nielsen H. Mechanisms of insulin resistance in non-oxidative glucose metabolism: the role of glycogen synthase. J Basic Clin Physiol Pharmacol 1998, 9:255-279.
    • (1998) J Basic Clin Physiol Pharmacol , vol.9 , pp. 255-279
    • Beck-Nielsen, H.1
  • 131
    • 0024348996 scopus 로고
    • Early metabolic defects in persons at increased risk for non-insulin-dependent diabetes mellitus
    • Eriksson J., Franssila-Kallunki A., Ekstrand A., Saloranta C., Widen E., Schalin C., et al. Early metabolic defects in persons at increased risk for non-insulin-dependent diabetes mellitus. N Engl J Med 1989, 321:337-343.
    • (1989) N Engl J Med , vol.321 , pp. 337-343
    • Eriksson, J.1    Franssila-Kallunki, A.2    Ekstrand, A.3    Saloranta, C.4    Widen, E.5    Schalin, C.6
  • 132
    • 0025860114 scopus 로고
    • Reduced glycogen synthase activity in skeletal muscle from obese patients with and without type 2 (non-insulin-dependent) diabetes mellitus
    • Damsbo P., Vaag A., Hother-Nielsen O., Beck-Nielsen H. Reduced glycogen synthase activity in skeletal muscle from obese patients with and without type 2 (non-insulin-dependent) diabetes mellitus. Diabetologia 1991, 34:239-245.
    • (1991) Diabetologia , vol.34 , pp. 239-245
    • Damsbo, P.1    Vaag, A.2    Hother-Nielsen, O.3    Beck-Nielsen, H.4
  • 133
    • 0036788293 scopus 로고    scopus 로고
    • Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes
    • Kelley D.E., He J., Menshikova E.V., Ritov V.B. Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes. Diabetes 2002, 51:2944-2950.
    • (2002) Diabetes , vol.51 , pp. 2944-2950
    • Kelley, D.E.1    He, J.2    Menshikova, E.V.3    Ritov, V.B.4
  • 134
    • 0029867177 scopus 로고    scopus 로고
    • Insulin resistance associated with maternally inherited diabetes and deafness
    • Gebhart S.S., Shoffner J.M., Koontz D., Kaufman A., Wallace D. Insulin resistance associated with maternally inherited diabetes and deafness. Metabolism 1996, 45:526-531.
    • (1996) Metabolism , vol.45 , pp. 526-531
    • Gebhart, S.S.1    Shoffner, J.M.2    Koontz, D.3    Kaufman, A.4    Wallace, D.5
  • 135
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace D.C. Mitochondrial diseases in man and mouse. Science 1999, 283:1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 136
    • 0033223479 scopus 로고    scopus 로고
    • Achieving breastfeeding success. Simple solutions to common concerns
    • Anderson C.M. Achieving breastfeeding success. Simple solutions to common concerns. Adv Nurse Pract 1999, 7:67-69.
    • (1999) Adv Nurse Pract , vol.7 , pp. 67-69
    • Anderson, C.M.1
  • 137
    • 0028967724 scopus 로고
    • Increased expression of mitochondrial-encoded genes in skeletal muscle of humans with diabetes mellitus
    • Antonetti D.A., Reynet C., Kahn C.R. Increased expression of mitochondrial-encoded genes in skeletal muscle of humans with diabetes mellitus. J Clin Invest 1995, 95:1383-1388.
    • (1995) J Clin Invest , vol.95 , pp. 1383-1388
    • Antonetti, D.A.1    Reynet, C.2    Kahn, C.R.3
  • 138
    • 0032792665 scopus 로고    scopus 로고
    • AMP-activated protein kinase, a metabolic master switch: possible roles in type 2 diabetes
    • Winder W.W., Hardie D.G. AMP-activated protein kinase, a metabolic master switch: possible roles in type 2 diabetes. Am J Physiol 1999, 277:E1-E10.
    • (1999) Am J Physiol , vol.277
    • Winder, W.W.1    Hardie, D.G.2
  • 139
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • Winder W.W., Holmes B.F., Rubink D.S., Jensen E.B., Chen M., Holloszy J.O. Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle. J Appl Physiol 2000, 88:2219-2226.
    • (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
  • 140
    • 0035957375 scopus 로고    scopus 로고
    • Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1
    • Michael L.F., Wu Z., Cheatham R.B., Puigserver P., Adelmant G., Lehman J.J., et al. Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1. Proc Natl Acad Sci USA 2001, 98:3820-3825.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3820-3825
    • Michael, L.F.1    Wu, Z.2    Cheatham, R.B.3    Puigserver, P.4    Adelmant, G.5    Lehman, J.J.6
  • 141
    • 0033538473 scopus 로고    scopus 로고
    • Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
    • Wu Z., Puigserver P., Andersson U., Zhang C., Adelmant G., Mootha V., et al. Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 1999, 98:115-124.
    • (1999) Cell , vol.98 , pp. 115-124
    • Wu, Z.1    Puigserver, P.2    Andersson, U.3    Zhang, C.4    Adelmant, G.5    Mootha, V.6
  • 142
    • 0035083645 scopus 로고    scopus 로고
    • Skeletal muscle lipid content and oxidative enzyme activity in relation to muscle fiber type in type 2 diabetes and obesity
    • He J., Watkins S., Kelley D.E. Skeletal muscle lipid content and oxidative enzyme activity in relation to muscle fiber type in type 2 diabetes and obesity. Diabetes 2001, 50:817-823.
    • (2001) Diabetes , vol.50 , pp. 817-823
    • He, J.1    Watkins, S.2    Kelley, D.E.3
  • 143
    • 77449155964 scopus 로고    scopus 로고
    • Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes
    • Hwang H., Bowen B.P., Lefort N., Flynn C.R., De Filippis E.A., Roberts C., et al. Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes. Diabetes 2010, 59:33-42.
    • (2010) Diabetes , vol.59 , pp. 33-42
    • Hwang, H.1    Bowen, B.P.2    Lefort, N.3    Flynn, C.R.4    De Filippis, E.A.5    Roberts, C.6
  • 145
    • 76949100689 scopus 로고    scopus 로고
    • Proteomic profiling of non-obese type 2 diabetic skeletal muscle
    • Mullen E., Ohlendieck K. Proteomic profiling of non-obese type 2 diabetic skeletal muscle. Int J Mol Med 2010, 25:445-458.
    • (2010) Int J Mol Med , vol.25 , pp. 445-458
    • Mullen, E.1    Ohlendieck, K.2
  • 146
    • 0018123653 scopus 로고
    • Activities of hepatic enzymes in spontaneous diabetes rats produced by selective breeding of normal Wistar rats
    • Kitahara A., Toyota T., Kakizaki M., Goto Y. Activities of hepatic enzymes in spontaneous diabetes rats produced by selective breeding of normal Wistar rats. Tohoku J Exp Med 1978, 126:7-11.
    • (1978) Tohoku J Exp Med , vol.126 , pp. 7-11
    • Kitahara, A.1    Toyota, T.2    Kakizaki, M.3    Goto, Y.4
  • 147
    • 77953507944 scopus 로고    scopus 로고
    • Comparative analysis of fat and muscle proteins in fenofibrate-fed type II diabetic OLETF rats: the fenofibrate-dependent expression of PEBP or C11orf59 protein
    • Hahm J.R., Ahn J.S., Noh H.S., Baek S.M., Ha J.H., Jung T.S., et al. Comparative analysis of fat and muscle proteins in fenofibrate-fed type II diabetic OLETF rats: the fenofibrate-dependent expression of PEBP or C11orf59 protein. BMB Rep 2010, 43:337-343.
    • (2010) BMB Rep , vol.43 , pp. 337-343
    • Hahm, J.R.1    Ahn, J.S.2    Noh, H.S.3    Baek, S.M.4    Ha, J.H.5    Jung, T.S.6


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