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Volumn 19, Issue 4, 2007, Pages 547-564

Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (Review)

Author keywords

Biomarker; Mass spectrometry; Muscular dystrophy; Peptide mass fingerprinting; Proteomics; Skeletal muscle aging

Indexed keywords

BIOLOGICAL MARKER; MUSCLE PROTEIN;

EID: 34247881871     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.19.4.547     Document Type: Review
Times cited : (43)

References (142)
  • 1
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • DOI 10.1146/annurev.biochem.70.1.437
    • Mann M, Hendrickson RC and Pandey A: Analysis of proteins and proteomes by mass spectrometry. Annu Rev Biochem 70: 437-473, 2001. (Pubitemid 32662217)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 3
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R and Mann M: Mass spectrometry-based proteomics. Nature 422: 198-207, 2003.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 4
    • 85016229161 scopus 로고    scopus 로고
    • Large-scale protein identification using mass spectrometry
    • Lin D, Tabb DL and Yates JR III: Large-scale protein identification using mass spectrometry. Biochim Biophys Acta 1646: 1-10, 2003.
    • (2003) Biochim Biophys Acta , vol.1646 , pp. 1-10
    • Lin, D.1    Tabb, D.L.2    Yates III, J.R.3
  • 6
    • 19444363756 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomic profiling
    • DOI 10.1093/bfgp/4.1.27, Proteomics Tools-Advances and Applications
    • Yan W and Chen SS: Mass spectrometry-based quantitative proteomic profiling. Brief Funct Genomic Proteomic 4: 27-38, 2005. (Pubitemid 40724165)
    • (2005) Briefings in Functional Genomics and Proteomics , vol.4 , Issue.1 , pp. 27-38
    • Yan, W.1    Chen, S.S.2
  • 7
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong SE and Mann M: Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 1: 252-262, 2005.
    • (2005) Nat Chem Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 8
    • 26444456180 scopus 로고    scopus 로고
    • Application of mass spectrometry in proteomics
    • Guerrera IC and Kleiner O: Application of mass spectrometry in proteomics. Biosci Rep 25: 71-93, 2005.
    • (2005) Biosci Rep , vol.25 , pp. 71-93
    • Guerrera, I.C.1    Kleiner, O.2
  • 9
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B and Aebersold R: Mass spectrometry and protein analysis. Science 312: 212-217, 2006.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 10
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg A, Weiss W and Dunn MJ: Current two-dimensional electrophoresis technology for proteomics. Proteomics 4: 3665-3685, 2004.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 11
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • DOI 10.1038/nbt0303-262
    • Wu CC and Yates JR III: The application of mass spectrometry to membrane proteomics. Nat Biotechnol 21: 262-267, 2003. (Pubitemid 36314809)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 12
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M and Jensen ON: Proteomic analysis of post-translational modifications. Nat Biotechnol 21: 255-261, 2003.
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 13
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches
    • Seo J and Lee KJ: Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J Biochem Mol Biol 37: 35-44, 2004. (Pubitemid 38402572)
    • (2004) Journal of Biochemistry and Molecular Biology , vol.37 , Issue.1 , pp. 35-44
    • Seo, J.1    Lee, K.-J.2
  • 14
    • 1042275615 scopus 로고    scopus 로고
    • Modification-specific proteomics: Characterization of post-translational modifications by mass spectrometry
    • DOI 10.1016/j.cbpa.2003.12.009
    • Jensen ON: Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry. Curr Opin Chem Biol 8: 33-41, 2004. (Pubitemid 38201475)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.1 , pp. 33-41
    • Jensen, O.N.1
  • 17
    • 61549140696 scopus 로고
    • The scientific basis of myology
    • McGraw-Hill Inc., New York
    • Engel AG and Franzini-Armstrong C: The scientific basis of myology. In: Basic and Clinical Myology. Vol. 1, McGraw-Hill Inc., New York, pp1-735, 1994.
    • (1994) Basic and Clinical Myology , vol.1 , pp. 1-735
    • Engel, A.G.1    Franzini-Armstrong, C.2
  • 18
    • 0035116376 scopus 로고    scopus 로고
    • Historical perspectives: Plasticity of mammalian skeletal muscle
    • Pette D: Historical perspectives: plasticity of mammalian skeletal muscle. J Appl Physiol 90: 1119-1124, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 1119-1124
    • Pette, D.1
  • 19
    • 0036690310 scopus 로고    scopus 로고
    • The adaptive potential of skeletal muscle fibers
    • Pette D: The adaptive potential of skeletal muscle fibers. Can J Appl Physiol 27: 423-448, 2002.
    • (2002) Can J Appl Physiol , vol.27 , pp. 423-448
    • Pette, D.1
  • 20
    • 0037610288 scopus 로고    scopus 로고
    • Molecular basis of skeletal muscle plasticity - From gene to form and function
    • Fluck M and Hoppeler H: Molecular basis of skeletal muscle plasticity - from gene to form and function. Rev Physiol Biochem Pharmacol 146: 159-216, 2003.
    • (2003) Rev Physiol Biochem Pharmacol , vol.146 , pp. 159-216
    • Fluck, M.1    Hoppeler, H.2
  • 21
    • 0030914822 scopus 로고    scopus 로고
    • Electron microscopic study of long-term denervated rat skeletal muscle
    • DOI 10.1002/(SICI)1097-0185(199707)248:3<355::AID-AR8>3.0.CO;2-O
    • Lu DX, Huang SK and Carlson BM: Electron microscopic study of long-term denervated rat skeletal muscle. Anat Rec 248: 355-365, 1997. (Pubitemid 27280142)
    • (1997) Anatomical Record , vol.248 , Issue.3 , pp. 355-365
    • Lu, D.-X.1    Huang, S.-K.2    Carlson, B.M.3
  • 22
    • 0035006873 scopus 로고    scopus 로고
    • Transitions of muscle fiber phenotypic profiles
    • Pette D and Staron RS: Transitions of muscle fiber phenotypic profiles. Histochem Cell Biol 115: 359-372, 2001. (Pubitemid 32467749)
    • (2001) Histochemistry and Cell Biology , vol.115 , Issue.5 , pp. 359-372
    • Pette, D.1    Staron, R.S.2
  • 24
    • 0142218511 scopus 로고    scopus 로고
    • Gene expression in muscle in response to exercise
    • DOI 10.1023/A:1026041228041
    • Goldspink G: Gene expression in muscle in response to exercise. J Muscle Res Cell Motil 24: 121-126, 2003. (Pubitemid 37323615)
    • (2003) Journal of Muscle Research and Cell Motility , vol.24 , Issue.2-3 , pp. 121-126
    • Goldspink, G.1
  • 26
    • 0037023852 scopus 로고    scopus 로고
    • Proteomic analysis of striated muscle
    • Isfort RJ: Proteomic analysis of striated muscle. J Chromatogr B 771: 155-165, 2002.
    • (2002) J Chromatogr B , vol.771 , pp. 155-165
    • Isfort, R.J.1
  • 28
    • 4444351485 scopus 로고    scopus 로고
    • Evaluation of an integrated strategy for proteomic profiling of skeletal muscle
    • LeBihan MC, Tarelli E and Coulton GR: Evaluation of an integrated strategy for proteomic profiling of skeletal muscle. Proteomics 4: 2739-2753, 2004.
    • (2004) Proteomics , vol.4 , pp. 2739-2753
    • LeBihan, M.C.1    Tarelli, E.2    Coulton, G.R.3
  • 30
    • 0035997273 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization-tandem mass spectrometry with high resolution and sensitivity for identification and characterization of proteins
    • Bienvenut WV, Deon C, Pasquarello C, Campbell JM, Sanchez JC, Vestal ML and Hochstrasser DF: Matrix-assisted laser desorption/ionization-tandem mass spectrometry with high resolution and sensitivity for identification and characterization of proteins. Proteomics 2: 868-876, 2002.
    • (2002) Proteomics , vol.2 , pp. 868-876
    • Bienvenut, W.V.1    Deon, C.2    Pasquarello, C.3    Campbell, J.M.4    Sanchez, J.C.5    Vestal, M.L.6    Hochstrasser, D.F.7
  • 31
    • 33644788060 scopus 로고    scopus 로고
    • Peptide mass fingerprinting: Protein identification using MALDI-TOF mass spectrometry
    • Webster J and Oxley D: Peptide mass fingerprinting: protein identification using MALDI-TOF mass spectrometry. Methods Mol Biol 310: 227-240, 2005.
    • (2005) Methods Mol Biol , vol.310 , pp. 227-240
    • Webster, J.1    Oxley, D.2
  • 32
    • 0025379205 scopus 로고
    • Comprehensive computerized 2D gel protein databases offer a global approach to the study of the mammalian cell
    • Celis JE, Honore B, Bauw G and Vandekerckhove J: Comprehensive computerized 2D gel protein databases offer a global approach to the study of the mammalian cell. Bioessays 12: 93-97, 1990.
    • (1990) Bioessays , vol.12 , pp. 93-97
    • Celis, J.E.1    Honore, B.2    Bauw, G.3    Vandekerckhove, J.4
  • 34
    • 33646102225 scopus 로고    scopus 로고
    • Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle
    • Doran P, Dowling P, Donoghue P, Buffini M and Ohlendieck K: Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle. Biochim Biophys Acta 1764: 773-785, 2006.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 773-785
    • Doran, P.1    Dowling, P.2    Donoghue, P.3    Buffini, M.4    Ohlendieck, K.5
  • 35
    • 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 and Ohlendieck K: Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics 6: 4610-4621, 2006.
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 36
    • 0025368249 scopus 로고
    • Analysis of protein digests by capillary high-performance liquid chromatography and on-line fast atom bombardment mass spectrometry
    • Henzel WJ, Bourell JH and Stults JT: Analysis of protein digests by capillary high-performance liquid chromatography and on-line fast atom bombardment mass spectrometry. Anal Biochem 187: 228-233, 1990.
    • (1990) Anal Biochem , vol.187 , pp. 228-233
    • Henzel, W.J.1    Bourell, J.H.2    Stults, J.T.3
  • 37
    • 0042386240 scopus 로고    scopus 로고
    • Protein identification: The origins of peptide mass fingerprinting
    • Henzel WJ, Watanabe C and Stults JT: Protein identification: the origins of peptide mass fingerprinting. J Am Soc Mass Spectrom 14: 931-942, 2003.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 931-942
    • Henzel, W.J.1    Watanabe, C.2    Stults, J.T.3
  • 42
    • 20744446463 scopus 로고    scopus 로고
    • An effective skeletal muscle prefractionation method to remove abundant structural proteins for optimized two-dimensional gel electrophoresis
    • Jarrold B, DeMuth J, Greis K, Burt T and Wang F: An effective skeletal muscle prefractionation method to remove abundant structural proteins for optimized two-dimensional gel electrophoresis. Electrophoresis 26: 2269-2278, 2005.
    • (2005) Electrophoresis , vol.26 , pp. 2269-2278
    • Jarrold, B.1    DeMuth, J.2    Greis, K.3    Burt, T.4    Wang, F.5
  • 43
    • 61549140696 scopus 로고
    • The scientific basis of myology
    • McGraw-Hill Inc., New York
    • Engel AG and Franzini-Armstrong C: The scientific basis of myology. In: Basic and Clinical Myology. Vol. 2, McGraw-Hill Inc., New York, pp1130-1937, 1994.
    • (1994) Basic and Clinical Myology , vol.2 , pp. 1130-1937
    • Engel, A.G.1    Franzini-Armstrong, C.2
  • 46
    • 0037341605 scopus 로고    scopus 로고
    • Sarcopenia - Consequences, mechanisms, and potential therapies
    • Greenlund LJS and Nair KS: Sarcopenia - consequences, mechanisms, and potential therapies. Mech Ageing Dev 124: 287-299, 2003.
    • (2003) Mech Ageing Dev , vol.124 , pp. 287-299
    • Greenlund, L.J.S.1    Nair, K.S.2
  • 47
    • 0035235432 scopus 로고    scopus 로고
    • The role of ion-regulatory membrane proteins of excitation-contraction coupling and relaxation in inherited muscle diseases
    • Froemming GR and Ohlendieck K: The role of ion-regulatory membrane proteins of excitation-contraction coupling and relaxation in inherited muscle diseases. Front Biosci 6: D65-D74, 2001.
    • (2001) Front Biosci , vol.6
    • Froemming, G.R.1    Ohlendieck, K.2
  • 48
    • 0032034970 scopus 로고    scopus 로고
    • 2+- regulatory membrane proteins in normal, stimulated and pathological skeletal muscle fibres (Review)
    • 2+-regulatory membrane proteins in normal, stimulated and pathological skeletal muscle fibres (Review). Int J Mol Med 1: 677-697, 1998.
    • (1998) Int J Mol Med , vol.1 , pp. 677-697
    • Murray, B.E.1    Froemming, G.R.2    Maguire, P.B.3    Ohlendieck, K.4
  • 49
    • 78650323785 scopus 로고    scopus 로고
    • Malignant hyperthermia: A pharmacogenetic disease of excitation- contraction coupling
    • Ohlendieck K: Malignant hyperthermia: a pharmacogenetic disease of excitation-contraction coupling. Curr Trends Neurol 1: 101-108, 2005.
    • (2005) Curr Trends Neurol , vol.1 , pp. 101-108
    • Ohlendieck, K.1
  • 50
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME and Minden JS: Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18: 2071-2077, 1997. (Pubitemid 27501267)
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 51
    • 0032884023 scopus 로고    scopus 로고
    • Difference gel electrophoresis
    • Unlu M: Difference gel electrophoresis. Biochem Soc Trans 27: 547-549, 1999.
    • (1999) Biochem Soc Trans , vol.27 , pp. 547-549
    • Unlu, M.1
  • 53
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • DOI 10.1007/s00216-005-3126-3
    • Marouga R, David S and Hawkins E: The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal Bioanal Chem 382: 669-678, 2005. (Pubitemid 40890994)
    • (2005) Analytical and Bioanalytical Chemistry , vol.382 , Issue.3 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 54
    • 25144518100 scopus 로고    scopus 로고
    • Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation
    • Donoghue P, Doran P, Dowling P and Ohlendieck K: Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation. Biochim Biophys Acta 1752: 166-176, 2005.
    • (2005) Biochim Biophys Acta , vol.1752 , pp. 166-176
    • Donoghue, P.1    Doran, P.2    Dowling, P.3    Ohlendieck, K.4
  • 55
    • 0025653451 scopus 로고
    • Cellular and molecular diversities of mammalian skeletal muscle fibers
    • Pette D and Staron RS: Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol 116: 1-76, 1990.
    • (1990) Rev Physiol Biochem Pharmacol , vol.116 , pp. 1-76
    • Pette, D.1    Staron, R.S.2
  • 57
    • 0035106676 scopus 로고    scopus 로고
    • Native skeletal muscle dihydropyridine receptor exists as a supramolecular triad complex
    • Froemming GR and Ohlendieck K: Native skeletal muscle dihydropyridine receptor exists as a supramolecular triad complex. Cell Mol Life Sci 58: 312-320, 2001.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 312-320
    • Froemming, G.R.1    Ohlendieck, K.2
  • 58
  • 59
    • 0032934834 scopus 로고
    • Self-aggregation of triadin in the sarcoplasmic reticulum of rabbit skeletal muscle
    • Froemming GR, Murray BE and Ohlendieck K: Self-aggregation of triadin in the sarcoplasmic reticulum of rabbit skeletal muscle. Biochim Biophys Acta 1418: 197-205, 1990.
    • (1990) Biochim Biophys Acta , vol.1418 , pp. 197-205
    • Froemming, G.R.1    Murray, B.E.2    Ohlendieck, K.3
  • 60
    • 0035294573 scopus 로고    scopus 로고
    • Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Yan JX, Harry RA, Wait R, Welson SY, Emery PW, Preedy V and Dunn MJ: Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 1: 424-434, 2001.
    • (2001) Proteomics , vol.1 , pp. 424-434
    • Yan, J.X.1    Harry, R.A.2    Wait, R.3    Welson, S.Y.4    Emery, P.W.5    Preedy, V.6    Dunn, M.J.7
  • 61
    • 2942529230 scopus 로고    scopus 로고
    • Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Bouley J, Chambon C and Picard B: Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 4: 1811-1824, 2004.
    • (2004) Proteomics , vol.4 , pp. 1811-1824
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 64
    • 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 and Gelfi C: Comparison of protein expression in human deltoideus and vastus lateralis muscles using two-dimensional gel electrophoresis. Proteomics 5: 2577-2586, 2005.
    • (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
  • 65
    • 0041663955 scopus 로고    scopus 로고
    • Study of human laryngeal muscle protein using two-dimensional electrophoresis and mass spectrometry
    • DOI 10.1002/pmic.200300454
    • Li ZB, Lehar M, Braga N, Westra W, Liu LH and Flint PW: Study of human laryngeal muscle protein using two-dimensional electrophoresis and mass spectrometry. Proteomics 3: 1325-1334, 2003. (Pubitemid 36929555)
    • (2003) Proteomics , vol.3 , Issue.7 , pp. 1325-1334
    • Li, Z.-B.1    Lehar, M.2    Braga, N.3    Westra, W.4    Liu, L.-H.5    Flint, P.W.6
  • 66
    • 8744309971 scopus 로고    scopus 로고
    • Differential expression profiling of the proteomes and their mRNAs in porcine white and red skeletal muscles
    • Kim NK, Joh JH, Park HR, Kim OH, Park BY and Lee CS: Differential expression profiling of the proteomes and their mRNAs in porcine white and red skeletal muscles. Proteomics 4: 3422-3428, 2004.
    • (2004) Proteomics , vol.4 , pp. 3422-3428
    • Kim, N.K.1    Joh, J.H.2    Park, H.R.3    Kim, O.H.4    Park, B.Y.5    Lee, C.S.6
  • 67
    • 33748357119 scopus 로고    scopus 로고
    • Proteomic analysis of fast and slow muscles from normal and kyphoscoliotic mice using protein arrays, 2-DE and MS
    • DOI 10.1002/pmic.200500746
    • Le Bihan MC, Hou Y, Harris N, Tarelli E and Coulton GR: Proteomic analysis of fast and slow muscles from normal and kyphoscoliotic mice using protein arrays, 2-DE and MS. Proteomics 6: 4646-4661, 2006. (Pubitemid 44336978)
    • (2006) Proteomics , vol.6 , Issue.16 , pp. 4646-4661
    • Le Bihan, M.-C.1    Hou, Y.2    Harris, N.3    Tarelli, E.4    Coulton, G.R.5
  • 69
    • 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 and Wait R: 2-D protein maps of rat gastrocnemius and soleus muscles: a tool for muscle plasticity assessment. Proteomics 6: 321-340, 2006.
    • (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    Wait, R.7
  • 70
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner F, Foster LJ, Campanaro S, Valle G and Mann M: Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol Cell Proteomics 5: 608-619, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 71
    • 3042815335 scopus 로고    scopus 로고
    • Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry
    • DOI 10.1074/mcp.M400024-MCP200
    • Cieniewski-Bernard C, Bastide B, Lefebvre T, Lemoine J, Mounier Y and Michalski JC: Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry. Mol Cell Proteomics 3: 577-585, 2004. (Pubitemid 38878517)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.6 , pp. 577-585
    • Cieniewski-Bernard, C.1    Bastide, B.2    Lefebvre, T.3    Lemoine, J.4    Mounier, Y.5    Michalski, J.-C.6
  • 72
    • 2642568030 scopus 로고    scopus 로고
    • The proteome of chicken skeletal muscle: Changes in soluble protein expression during growth in a layer strain
    • DOI 10.1002/pmic.200300716
    • Doherty MK, McLean L, Hayter JR, Pratt JM, Robertson DH, El-Shafei A, Gaskell SJ and Beynon RJ: The proteome of chicken skeletal muscle: changes in soluble protein expression during growth in a layer strain. Proteomics 4: 2082-2093, 2004. (Pubitemid 38880373)
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 2082-2093
    • Doherty, M.K.1    McLean, L.2    Hayter, J.R.3    Pratt, J.M.4    Robertson, D.H.L.5    El-Shafei, A.6    Gaskell, S.J.7    Beynon, R.J.8
  • 74
    • 24944591029 scopus 로고    scopus 로고
    • Exercise-related novel gene is involved in myoblast differentiation
    • DOI 10.2220/biomedres.26.79
    • Takahashi M and Kubota S: Exercise-related novel gene is involved in myoblast differentiation. Biomed Res 26: 79-85, 2005. (Pubitemid 41519992)
    • (2005) Biomedical Research , vol.26 , Issue.2 , pp. 79-85
    • Takahashi, M.1    Kubota, S.2
  • 75
    • 13844310828 scopus 로고    scopus 로고
    • Proteomic analysis of bovine skeletal muscle hypertrophy
    • DOI 10.1002/pmic.200400925
    • Bouley J, Meunier B, Chambon C, De Smet S, Hocquette JF and Picard B: Proteomic analysis of bovine skeletal muscle hypertrophy. Proteomics 5: 490-500, 2005. (Pubitemid 40262066)
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 490-500
    • Bouley, J.1    Meunier, B.2    Chambon, C.3    De Smet, S.4    Hocquette, J.F.5    Picard, B.6
  • 76
    • 33645082204 scopus 로고    scopus 로고
    • Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis
    • Kjaersgard IV, Norrelykke MR and Jessen F: Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis. Proteomics 6: 1606-1618, 2006.
    • (2006) Proteomics , vol.6 , pp. 1606-1618
    • Kjaersgard, I.V.1    Norrelykke, M.R.2    Jessen, F.3
  • 78
    • 1842848790 scopus 로고    scopus 로고
    • Proteomic analysis of secreted muscle components: Search for factors involved in neuromuscular synapse formation
    • Gajendran N, Frey JR, Lefkovits I, Kuhn L, Fountoulakis M, Krapfenbauer K and Brenner HR: Proteomic analysis of secreted muscle components: search for factors involved in neuromuscular synapse formation. Proteomics 2: 1601-1615, 2002.
    • (2002) Proteomics , vol.2 , pp. 1601-1615
    • Gajendran, N.1    Frey, J.R.2    Lefkovits, I.3    Kuhn, L.4    Fountoulakis, M.5    Krapfenbauer, K.6    Brenner, H.R.7
  • 79
    • 0036248674 scopus 로고    scopus 로고
    • Proteomic analysis of rat soleus muscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy
    • Isfort RJ, Wang F, Greis KD, Sun Y, Keough TW, Farrar RP, Bodine SC and Anderson NL: Proteomic analysis of rat soleus muscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy. Proteomics 2: 543-550, 2002.
    • (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    Bodine, S.C.7    Anderson, N.L.8
  • 81
    • 0142182391 scopus 로고    scopus 로고
    • Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity
    • Ge Y, Molloy MP, Chamberlain JS and Andrews PC: Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity. Proteomics 3: 1895-1903, 2003.
    • (2003) Proteomics , vol.3 , pp. 1895-1903
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 82
    • 4444267191 scopus 로고    scopus 로고
    • Differential expression of the skeletal muscle proteome in mdx mice at different ages
    • DOI 10.1002/elps.200406013
    • Ge Y, Molloy MP, Chamberlain JS and Andrews PC: Differential expression of the skeletal muscle proteome in mdx mice at different ages. Electrophoresis 25: 2576-2585, 2004. (Pubitemid 39193668)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2576-2585
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 84
    • 0242321030 scopus 로고    scopus 로고
    • Proteomic identification of age-dependent protein nitration in rat skeletal muscle
    • DOI 10.1016/S0891-5849(03)00500-8
    • Kanski J, Alterman MA and Schoneich C: Proteomic identification of age-dependent protein nitration in rat skeletal muscle. Free Radic Biol Med 35: 1229-1239, 2003. (Pubitemid 37357248)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.10 , pp. 1229-1239
    • Kanski, J.1    Alterman, M.A.2    Schoneich, C.3
  • 85
    • 21244457292 scopus 로고    scopus 로고
    • Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry
    • Kanski J, Hong SJ and Schoneich C: Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine- containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry. J Biol Chem 280: 24261-24266, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 24261-24266
    • Kanski, J.1    Hong, S.J.2    Schoneich, C.3
  • 86
    • 0037289173 scopus 로고    scopus 로고
    • Comparative proteomics: Characterization of a two-dimensional gel electrophoresis system to study the effect of aging on mitochondrial proteins
    • Chang J, Van Remmen H, Cornell J, Richardson A and Ward WF: Comparative proteomics: characterization of a two-dimensional gel electrophoresis system to study the effect of aging on mitochondrial proteins. Mech Ageing Dev 124: 33-41, 2003.
    • (2003) Mech Ageing Dev , vol.124 , pp. 33-41
    • Chang, J.1    Van Remmen, H.2    Cornell, J.3    Richardson, A.4    Ward, W.F.5
  • 87
    • 21744437938 scopus 로고    scopus 로고
    • Differential proteome analysis of aging in rat skeletal muscle
    • DOI 10.1096/fj.04-3084fje
    • Piec I, Listrat A, Alliot J, Chambon C, Taylor RG and Bechet D: Differential proteome analysis of aging in rat skeletal muscle. FASEB J 19: 1143-1145, 2005. (Pubitemid 40946445)
    • (2005) FASEB Journal , vol.19 , Issue.9 , pp. 1143-1145
    • Piec, I.1    Listrat, A.2    Alliot, J.3    Chambon, C.4    Taylor, R.G.5    Bechet, D.6
  • 89
    • 0037160782 scopus 로고    scopus 로고
    • The muscular dystrophies
    • Emery AE: The muscular dystrophies. Lancet 359: 687-695, 2002.
    • (2002) Lancet , vol.359 , pp. 687-695
    • Emery, A.E.1
  • 90
    • 0027470203 scopus 로고
    • The structural and functional diversity of dystrophin
    • Ahn AH and Kunkel LM: The structural and functional diversity of dystrophin. Nat Genet 3: 283-291, 1993.
    • (1993) Nat Genet , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 91
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn RD and Campbell KP: Molecular basis of muscular dystrophies. Muscle Nerve 23: 1456-1471, 2000.
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 92
    • 0035891532 scopus 로고    scopus 로고
    • Role of nitric oxide in the pathogenesis of muscular dystrophies: A 'two hit' hypothesis of the cause of muscle necrosis
    • Rando TA: Role of nitric oxide in the pathogenesis of muscular dystrophies: a 'two hit' hypothesis of the cause of muscle necrosis. Microsc Res Tech 55: 223-235, 2001.
    • (2001) Microsc Res Tech , vol.55 , pp. 223-235
    • Rando, T.A.1
  • 93
    • 0030026119 scopus 로고    scopus 로고
    • Towards an understanding of the dystrophinglycoprotein complex: Linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton
    • Ohlendieck K: Towards an understanding of the dystrophinglycoprotein complex: linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton. Eur J Cell Biol 69: 1-10, 1996.
    • (1996) Eur J Cell Biol , vol.69 , pp. 1-10
    • Ohlendieck, K.1
  • 94
    • 0034737602 scopus 로고    scopus 로고
    • Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton JM and Steinhardt RA: Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. J Biol Chem 275: 9452-9460, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 9452-9460
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 95
    • 0034468908 scopus 로고    scopus 로고
    • How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton JM and Steinhardt RA: How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. Trends Cardiovasc Med 10: 268-272, 2000.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 268-272
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 96
    • 33645728070 scopus 로고    scopus 로고
    • The pathophysiological role of impaired calcium handling in muscular dystrophy
    • Winder SJ (ed). Landes Bioscience, Georgetown, TX
    • Ohlendieck K: The pathophysiological role of impaired calcium handling in muscular dystrophy. In: Molecular Mechanisms of Muscular Dystrophies. Winder SJ (ed). Landes Bioscience, Georgetown, TX, pp183-192, 2006.
    • (2006) Molecular Mechanisms of Muscular Dystrophies , pp. 183-192
    • Ohlendieck, K.1
  • 97
    • 33645730485 scopus 로고    scopus 로고
    • Sparks, signals and shock absorbers: How dystrophin loss causes muscular dystrophy
    • Batchelor CL and Winder SJ: Sparks, signals and shock absorbers: how dystrophin loss causes muscular dystrophy. Trends Cell Biol 16: 198-205, 2006.
    • (2006) Trends Cell Biol , vol.16 , pp. 198-205
    • Batchelor, C.L.1    Winder, S.J.2
  • 99
    • 38349178972 scopus 로고    scopus 로고
    • Naturally protected muscle phenotypes: Development of novel treatment strategies for Duchenne muscular dystrophy
    • Dowling P, Doran P, Lohan J, Culligan K and Ohlendieck K: Naturally protected muscle phenotypes: Development of novel treatment strategies for Duchenne muscular dystrophy. Basic Appl Myol 14: 169-178, 2004.
    • (2004) Basic Appl Myol , vol.14 , pp. 169-178
    • Dowling, P.1    Doran, P.2    Lohan, J.3    Culligan, K.4    Ohlendieck, K.5
  • 100
    • 0036021778 scopus 로고    scopus 로고
    • Functional characteristics of dystrophic skeletal muscle: Insights from animal models
    • Watchko JF, O'Day TL and Hoffman EP: Functional characteristics of dystrophic skeletal muscle: insights from animal models. J Appl Physiol 93: 407-417, 2002.
    • (2002) J Appl Physiol , vol.93 , pp. 407-417
    • Watchko, J.F.1    O'Day, T.L.2    Hoffman, E.P.3
  • 103
    • 0026328022 scopus 로고
    • Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice
    • Ohlendieck K and Campbell KP: Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J Cell Biol 115: 1685-1694, 1991.
    • (1991) J Cell Biol , vol.115 , pp. 1685-1694
    • Ohlendieck, K.1    Campbell, K.P.2
  • 105
    • 0023091942 scopus 로고
    • The mutant mdx: Inherited myopathy in the mouse
    • Torres LFB and Duchen LW: The mutant mdx: inherited myopathy in the mouse. Brain 110: 269-299, 1987.
    • (1987) Brain , vol.110 , pp. 269-299
    • Torres, L.F.B.1    Duchen, L.W.2
  • 106
    • 0026032731 scopus 로고
    • Decreased osmotic stability of dystrophin-less muscle cells from mdx mouse
    • Menke A and Jockusch H: Decreased osmotic stability of dystrophin-less muscle cells from mdx mouse. Nature 349: 69-71, 1991.
    • (1991) Nature , vol.349 , pp. 69-71
    • Menke, A.1    Jockusch, H.2
  • 107
    • 0033695935 scopus 로고    scopus 로고
    • Contraction-induced injury to single permeabilized muscle fibers from mdx, transgenic mdx, and control mice
    • Lynch GS, Rafael JA, Chamberlain JS and Faulkner JA: Contraction-induced injury to single permeabilized muscle fibers from mdx, transgenic mdx, and control mice. Am J Physiol Cell Physiol 279: C1290-C1294, 2000.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Lynch, G.S.1    Rafael, J.A.2    Chamberlain, J.S.3    Faulkner, J.A.4
  • 108
    • 0035076160 scopus 로고    scopus 로고
    • Alteration of excitation-contraction coupling mechanism in extensor digitorum longus muscle fibres of dystrophic mdx mouse and potential efficacy of taurine
    • DeLuca A, Pierno S, Liantonio A, Cetrone M, Camerino C, Simonetti S, Papadia F and Camerino DC: Alteration of excitation-contraction coupling mechanism in extensor digitorum longus muscle fibres of dystrophic mdx mouse and potential efficacy of taurine. Br J Pharmacol 132: 1047-1054, 2001.
    • (2001) Br J Pharmacol , vol.132 , pp. 1047-1054
    • DeLuca, A.1    Pierno, S.2    Liantonio, A.3    Cetrone, M.4    Camerino, C.5    Simonetti, S.6    Papadia, F.7    Camerino, D.C.8
  • 109
    • 0036092560 scopus 로고    scopus 로고
    • Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle
    • Culligan K, Banville N, Dowling P and Ohlendieck K: Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle. J Appl Physiol 92: 435-445, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 435-445
    • Culligan, K.1    Banville, N.2    Dowling, P.3    Ohlendieck, K.4
  • 110
    • 2342614190 scopus 로고    scopus 로고
    • Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy
    • Dowling P, Doran P and Ohlendieck K: Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy. Biochem J 379: 479-488, 2004.
    • (2004) Biochem J , vol.379 , pp. 479-488
    • Dowling, P.1    Doran, P.2    Ohlendieck, K.3
  • 111
    • 28544452497 scopus 로고    scopus 로고
    • Heat shock proteins and neuromuscular disease
    • Nishimura RN and Sharp FR: Heat shock proteins and neuromuscular disease. Muscle Nerve 32: 693-709, 2005.
    • (2005) Muscle Nerve , vol.32 , pp. 693-709
    • Nishimura, R.N.1    Sharp, F.R.2
  • 112
    • 0028813406 scopus 로고
    • Expression of heat-shock/stress proteins in Duchenne muscular dystrophy
    • Bornman L, Polla BS, Lotz BP and Gericke GS: Expression of heat-shock/stress proteins in Duchenne muscular dystrophy. Muscle Nerve 18: 23-31, 1995.
    • (1995) Muscle Nerve , vol.18 , pp. 23-31
    • Bornman, L.1    Polla, B.S.2    Lotz, B.P.3    Gericke, G.S.4
  • 113
    • 2442672776 scopus 로고    scopus 로고
    • Myoblast survival enhancement and transplantation success improvement by heat-shock treatment in mdx mice
    • Bouchentouf M, Benabdallah BF and Tremblay JP: Myoblast survival enhancement and transplantation success improvement by heat-shock treatment in mdx mice. Transplantation 77: 1349-1356, 2004.
    • (2004) Transplantation , vol.77 , pp. 1349-1356
    • Bouchentouf, M.1    Benabdallah, B.F.2    Tremblay, J.P.3
  • 115
    • 0028838732 scopus 로고
    • What is sarcopenia?
    • Evans WJ: What is sarcopenia? J Gerontol 50A: 5-8, 1995.
    • (1995) J Gerontol , vol.50 A , pp. 5-8
    • Evans, W.J.1
  • 118
    • 0033789444 scopus 로고    scopus 로고
    • Current status and perspectives of proteomics in aging research
    • Toda T: Current status and perspectives of proteomics in aging research. Exp Gerontol 35: 803-810, 2000.
    • (2000) Exp Gerontol , vol.35 , pp. 803-810
    • Toda, T.1
  • 119
    • 0033941589 scopus 로고    scopus 로고
    • Some new directions for research on the biology of aging
    • Martin GM: Some new directions for research on the biology of aging. Ann NY Acad Sci 908: 1-13, 2000.
    • (2000) Ann NY Acad Sci , vol.908 , pp. 1-13
    • Martin, G.M.1
  • 120
    • 0035033506 scopus 로고    scopus 로고
    • Proteome and proteomics for the research on protein alterations in aging
    • Toda T: Proteome and proteomics for the research on protein alterations in aging. Ann NY Acad Sci 928: 71-78, 2001.
    • (2001) Ann NY Acad Sci , vol.928 , pp. 71-78
    • Toda, T.1
  • 121
    • 0037653684 scopus 로고    scopus 로고
    • Proteomics in gerontological research
    • Schoneich C: Proteomics in gerontological research. Exp Gerontol 38: 473-481, 2003.
    • (2003) Exp Gerontol , vol.38 , pp. 473-481
    • Schoneich, C.1
  • 122
    • 0028921023 scopus 로고
    • Effects of ageing on the motor unit
    • Larsson L and Ansved T: Effects of ageing on the motor unit. Prog Neurobiol 45: 397-458, 1995.
    • (1995) Prog Neurobiol , vol.45 , pp. 397-458
    • Larsson, L.1    Ansved, T.2
  • 123
    • 0032425349 scopus 로고    scopus 로고
    • Age-associated changes in the innervation of muscle fibres and changes in the mechanical properties of motor units
    • Luff AR: Age-associated changes in the innervation of muscle fibres and changes in the mechanical properties of motor units. Ann NY Acad Sci 854: 92-101, 1998.
    • (1998) Ann NY Acad Sci , vol.854 , pp. 92-101
    • Luff, A.R.1
  • 124
    • 0031812237 scopus 로고    scopus 로고
    • The age-related motor disability: Underlying mechanisms in skeletal muscle at the motor unit, cellular and molecular level
    • Larsson L: The age-related motor disability: underlying mechanisms in skeletal muscle at the motor unit, cellular and molecular level. Acta Physiol Scand 163: S27-S29, 1998.
    • (1998) Acta Physiol Scand , vol.163
    • Larsson, L.1
  • 125
    • 38349114089 scopus 로고    scopus 로고
    • Denervation and the aging of skeletal muscle
    • Carlson BM: Denervation and the aging of skeletal muscle. Basic Appl Myol 14: 135-140, 2004.
    • (2004) Basic Appl Myol , vol.14 , pp. 135-140
    • Carlson, B.M.1
  • 126
    • 0031905072 scopus 로고    scopus 로고
    • Identical responses of fast muscle to sustained activity by low- Frequency stimulation in young and aging rats
    • Skorjanc D, Traub I and Pette D: Identical responses of fast muscle to sustained activity by low-frequency-stimulation in young and aging rats. J Appl Physiol 85: 437-441, 1998. (Pubitemid 28365808)
    • (1998) Journal of Applied Physiology , vol.85 , Issue.2 , pp. 437-441
    • Skorjanc, D.1    Traub, I.2    Pette, D.3
  • 127
    • 0347115997 scopus 로고    scopus 로고
    • Adaptive potentials of skeletal muscle in young and aging rats
    • Pette D and Skorjanc D: Adaptive potentials of skeletal muscle in young and aging rats. Int J Sport Nutr Exerc Metab 11: S3-S8, 2001.
    • (2001) Int J Sport Nutr Exerc Metab , vol.11
    • Pette, D.1    Skorjanc, D.2
  • 128
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • Squier TS and Bigelow DJ: Protein oxidation and age-dependent alterations in calcium homeostasis. Front Biosci 5: 504-526, 2000.
    • (2000) Front Biosci , vol.5 , pp. 504-526
    • Squier, T.S.1    Bigelow, D.J.2
  • 129
    • 0036089622 scopus 로고    scopus 로고
    • Mitochondrial abnormalities are more frequent in muscles undergoing sarcopenia
    • Bua EA, McKiernan SH, Wanagat J, McKenzie D and Aiken JM: Mitochondrial abnormalities are more frequent in muscles undergoing sarcopenia. J Appl Physiol 92: 2617-2624, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 2617-2624
    • Bua, E.A.1    McKiernan, S.H.2    Wanagat, J.3    McKenzie, D.4    Aiken, J.M.5
  • 130
    • 0036081754 scopus 로고    scopus 로고
    • Apoptosis in skeletal muscle with aging
    • Dirks A and Leeuwenburgh C: Apoptosis in skeletal muscle with aging. Am J Physiol 282: R519-R527, 2002.
    • (2002) Am J Physiol , vol.282
    • Dirks, A.1    Leeuwenburgh, C.2
  • 131
    • 0035260493 scopus 로고    scopus 로고
    • Functional and metabolic consequences of sarcopenia
    • Vandervoort AA and Symons TB: Functional and metabolic consequences of sarcopenia. Can J Appl Physiol 26: 90-101, 2001.
    • (2001) Can J Appl Physiol , vol.26 , pp. 90-101
    • Vandervoort, A.A.1    Symons, T.B.2
  • 132
    • 0028874819 scopus 로고
    • Effects of aging on energy requirements and the control of food intake in men
    • Roberts SB: Effects of aging on energy requirements and the control of food intake in men. J Gerontol 50A: 101-106, 1995.
    • (1995) J Gerontol , vol.50 A , pp. 101-106
    • Roberts, S.B.1
  • 133
    • 0032413531 scopus 로고    scopus 로고
    • Age-related changes in the microcirculation of skeletal muscle
    • Degens H: Age-related changes in the microcirculation of skeletal muscle. Adv Exp Med Biol 454: 343-348, 1998. (Pubitemid 29005547)
    • (1998) Advances in Experimental Medicine and Biology , vol.454 , pp. 343-348
    • Degens, H.1
  • 134
    • 0030707838 scopus 로고    scopus 로고
    • Effects of aging on in vivo synthesis of skeletal muscle myosin heavy-chain and sarcoplasmic protein in humans
    • Balagopal P, Rooyackers OE, Adey DB, Ades PA and Nair KS: Effects of aging on in vivo synthesis of skeletal muscle myosin heavy-chain and sarcoplasmic protein in humans. Am J Physiol 273: E790-E800, 1997.
    • (1997) Am J Physiol , vol.273
    • Balagopal, P.1    Rooyackers, O.E.2    Adey, D.B.3    Ades, P.A.4    Nair, K.S.5
  • 135
    • 38349157693 scopus 로고    scopus 로고
    • Excitation-contraction uncoupling and sarcopenia
    • Ryan M and Ohlendieck K: Excitation-contraction uncoupling and sarcopenia. Basic Appl Myol 14: 141-154, 2004.
    • (2004) Basic Appl Myol , vol.14 , pp. 141-154
    • Ryan, M.1    Ohlendieck, K.2
  • 138
    • 0030861193 scopus 로고    scopus 로고
    • Early functional and biochemical adaptations to low-frequency stimulation of rabbit fast-twitch muscle
    • Hicks A, Ohlendieck K, Gopel SO and Pette D: Early functional and biochemical adaptations to low-frequency stimulation of rabbit fast-twitch muscle. Am J Physiol 273: C297-C305, 1997.
    • (1997) Am J Physiol , vol.273
    • Hicks, A.1    Ohlendieck, K.2    Gopel, S.O.3    Pette, D.4
  • 139
    • 0002360801 scopus 로고    scopus 로고
    • 2+-regulatory membrane proteins during the stimulation-induced fast-to-slow transition process
    • 2+-regulatory membrane proteins during the stimulation-induced fast-to-slow transition process. Basic Appl Myol 10: 99-106, 2000.
    • (2000) Basic Appl Myol , vol.10 , pp. 99-106
    • Ohlendieck, K.1
  • 141
    • 0034212222 scopus 로고    scopus 로고
    • 2+-regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle fibers
    • 2+-regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle fibers. Biochim Biophys Acta 1466: 151-168, 2000.
    • (2000) Biochim Biophys Acta , vol.1466 , pp. 151-168
    • Froemming, G.R.1    Murray, B.E.2    Harmon, S.3    Pette, D.4    Ohlendieck, K.5
  • 142
    • 0036227796 scopus 로고    scopus 로고
    • Muscular dystrophy into the new millennium
    • Emery AE: Muscular dystrophy into the new millennium. Neuromusc Disord 12: 343-349, 2002.
    • (2002) Neuromusc Disord , vol.12 , pp. 343-349
    • Emery, A.E.1


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