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Volumn 54, Issue 9, 2014, Pages 1117-1139

Nanomechanical Characteristics of Meat and Its Constituents Postmortem: A Review

Author keywords

atomic force microscopy; enzyme; myofibrils; nanomechanical properties; Stiffness; tenderness; ultrastructural

Indexed keywords

ATOMIC FORCE MICROSCOPY; COLLAGEN; ENZYMES; MUSCLE; STIFFNESS;

EID: 84893533945     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408398.2011.627518     Document Type: Article
Times cited : (9)

References (178)
  • 1
    • 33750100539 scopus 로고    scopus 로고
    • Transverse stiffness of myofibrils of skeletal and cardiac muscles studied by atomic force microscopy
    • Akiyama, N., Ohnuki, Y., Kunioka, Y., Saeki, Y. and Yamada, T. 2006. Transverse stiffness of myofibrils of skeletal and cardiac muscles studied by atomic force microscopy. J. Physiol. Sci, 56 (2): 145-151.
    • (2006) J. Physiol. Sci , vol.56 , Issue.2 , pp. 145-151
    • Akiyama, N.1    Ohnuki, Y.2    Kunioka, Y.3    Saeki, Y.4    Yamada, T.5
  • 2
    • 33747811148 scopus 로고    scopus 로고
    • 3D structure of relaxed fish muscle myosin filaments by single particle analysis
    • AL-Khayat, H. A., Morris, E. P., Kensler, R. W. and Squire, J. M. 2006. 3D structure of relaxed fish muscle myosin filaments by single particle analysis. J. Struct. Biol, 155: 202-217.
    • (2006) J. Struct. Biol , vol.155 , pp. 202-217
    • AL-Khayat, H.A.1    Morris, E.P.2    Kensler, R.W.3    Squire, J.M.4
  • 3
    • 77049086542 scopus 로고    scopus 로고
    • Effect of protein level in commercial diets on pork meat quality
    • Alonso, V., Campo, M. d. M., Provincial, L., Roncalés, P. and Beltrán, J. A. 2010. Effect of protein level in commercial diets on pork meat quality. Meat Sci, 85 (1): 7-14.
    • (2010) Meat Sci , vol.85 , Issue.1 , pp. 7-14
    • Alonso, V.1    Campo, M.D.M.2    Provincial, L.3    Roncalés, P.4    Beltrán, J.A.5
  • 4
    • 0041525992 scopus 로고    scopus 로고
    • Effects of the terminal sire type and sex on pork muscle cathepsins (B, B+L and H), cysteine proteinase inhibitors and lipolytic enzyme activities
    • Armero, E., Barbosa, J. A., Toldra, F., Baselga, M. and Pla, M. 1999. Effects of the terminal sire type and sex on pork muscle cathepsins (B, B+L and H), cysteine proteinase inhibitors and lipolytic enzyme activities. Meat Sci, 51 (2): 185-189.
    • (1999) Meat Sci , vol.51 , Issue.2 , pp. 185-189
    • Armero, E.1    Barbosa, J.A.2    Toldra, F.3    Baselga, M.4    Pla, M.5
  • 5
    • 9644291525 scopus 로고    scopus 로고
    • Cleavage of desmin by cysteine proteases: Calpains and cathepsin B
    • Baron, C. P., Jacobsen, S. and Purslow, P. P. 2004. Cleavage of desmin by cysteine proteases: Calpains and cathepsin B. Meat Sci, 68 (3): 447-456.
    • (2004) Meat Sci , vol.68 , Issue.3 , pp. 447-456
    • Baron, C.P.1    Jacobsen, S.2    Purslow, P.P.3
  • 6
    • 0032152137 scopus 로고    scopus 로고
    • Changes in the calpains and calpastatin during postmortem storage of bovine muscle
    • Boehm, M. L., Kendall, T. L., Thompson, V. F. and Goll, D. E. 1998. Changes in the calpains and calpastatin during postmortem storage of bovine muscle. J. Anim. Sci, 76 (9): 2415
    • (1998) J. Anim. Sci , vol.76 , Issue.9 , pp. 2415
    • Boehm, M.L.1    Kendall, T.L.2    Thompson, V.F.3    Goll, D.E.4
  • 9
    • 73249115945 scopus 로고    scopus 로고
    • Bovine cathepsin D activity under high pressure
    • Buckow, R., Truong, B. Q. and Versteeg, C. 2010. Bovine cathepsin D activity under high pressure. Food Chem, 120 (2): 474-481.
    • (2010) Food Chem , vol.120 , Issue.2 , pp. 474-481
    • Buckow, R.1    Truong, B.Q.2    Versteeg, C.3
  • 10
    • 35048874768 scopus 로고    scopus 로고
    • Nanomechanics of collagen fibrils under varying cross-link densities: Atomistic and continuum studies
    • Buehler, M. J. 2008. Nanomechanics of collagen fibrils under varying cross-link densities: Atomistic and continuum studies. J. Mech. Behav. Biomed. Mater, 1 (1): 59-67.
    • (2008) J. Mech. Behav. Biomed. Mater , vol.1 , Issue.1 , pp. 59-67
    • Buehler, M.J.1
  • 11
    • 0033167920 scopus 로고    scopus 로고
    • Imaging and force-distance analysis of human fibroblasts in vitro by atomic force microscopy
    • Bushell, G. R., Cahill, C., Clarke, F. M., Gibson, C. T., Myhra, S. and Watson, G. S. 1999. Imaging and force-distance analysis of human fibroblasts in vitro by atomic force microscopy. Cytometry, 36 (3): 254-264.
    • (1999) Cytometry , vol.36 , Issue.3 , pp. 254-264
    • Bushell, G.R.1    Cahill, C.2    Clarke, F.M.3    Gibson, C.T.4    Myhra, S.5    Watson, G.S.6
  • 12
    • 0037208092 scopus 로고    scopus 로고
    • Relationship of texture profile analysis and Warner-Bratzler shear force with sensory characteristics of beef rib steaks
    • Caine, W. R., Aalhus, J. L., Best, D. R., Dugan, M. E. R. and Jeremiah, L. E. 2003. Relationship of texture profile analysis and Warner-Bratzler shear force with sensory characteristics of beef rib steaks. Meat Sci, 64 (4): 333-339.
    • (2003) Meat Sci , vol.64 , Issue.4 , pp. 333-339
    • Caine, W.R.1    Aalhus, J.L.2    Best, D.R.3    Dugan, M.E.R.4    Jeremiah, L.E.5
  • 13
    • 0000068721 scopus 로고
    • Relationships among calcium-dependent protease, cathepsins B and H, meat tenderness and the response of muscle to aging
    • Calkins, C. R. and Seideman, S. C. 1988. Relationships among calcium-dependent protease, cathepsins B and H, meat tenderness and the response of muscle to aging. J. Anim. Sci, 66: 1186-1193.
    • (1988) J. Anim. Sci , vol.66 , pp. 1186-1193
    • Calkins, C.R.1    Seideman, S.C.2
  • 14
    • 35348931228 scopus 로고    scopus 로고
    • Effect of postmortem storage on activity of {micro}-and m-calpain in five bovine muscles
    • Camou, J. P., Marchello, J. A., Thompson, V. F., Mares, S. W. and Goll, D. E. 2007a. Effect of postmortem storage on activity of {micro}-and m-calpain in five bovine muscles. J. Anim. Sci, 85 (10): 2670-2681.
    • (2007) J. Anim. Sci , vol.85 , Issue.10 , pp. 2670-2681
    • Camou, J.P.1    Marchello, J.A.2    Thompson, V.F.3    Mares, S.W.4    Goll, D.E.5
  • 15
    • 37049025981 scopus 로고    scopus 로고
    • Isolation and characterization of {micro}-calpain, m-calpain, and calpastatin from postmortem muscle. I. Initial steps
    • Camou, J. P., Mares, S. W., Marchello, J. A., Vazquez, R., Taylor, M., Thompson, V. F. and Goll, D. E. 2007b. Isolation and characterization of {micro}-calpain, m-calpain, and calpastatin from postmortem muscle. I. Initial steps. J. Anim. Sci., 85 (12): 3400-3414.
    • (2007) J. Anim. Sci. , vol.85 , Issue.12 , pp. 3400-3414
    • Camou, J.P.1    Mares, S.W.2    Marchello, J.A.3    Vazquez, R.4    Taylor, M.5    Thompson, V.F.6    Goll, D.E.7
  • 16
    • 0034392670 scopus 로고    scopus 로고
    • Assessment of breed type and ageing time effects on beef meat quality using two different texture devices
    • Campo, M. M., Santolaria, P., Sañudo, C., Lepetit, J., Olleta, J. L., Panea, B. and Albertí, P. 2000. Assessment of breed type and ageing time effects on beef meat quality using two different texture devices. Meat Sci, 55: 371-378.
    • (2000) Meat Sci , vol.55 , pp. 371-378
    • Campo, M.M.1    Santolaria, P.2    Sañudo, C.3    Lepetit, J.4    Olleta, J.L.5    Panea, B.6    Albertí, P.7
  • 17
    • 21544469987 scopus 로고    scopus 로고
    • Degradation of myofibrillar proteins by a myofibril-bound serine proteinase in the skeletal muscle of crucian carp (Carasius auratus)
    • Cao, M. J., Jiang, X. J., Zhong, H. C., Zhang, Z. J. and Su, W. J. 2006. Degradation of myofibrillar proteins by a myofibril-bound serine proteinase in the skeletal muscle of crucian carp (Carasius auratus). Food Chem, 94 (1): 7-13.
    • (2006) Food Chem , vol.94 , Issue.1 , pp. 7-13
    • Cao, M.J.1    Jiang, X.J.2    Zhong, H.C.3    Zhang, Z.J.4    Su, W.J.5
  • 18
    • 33748798523 scopus 로고    scopus 로고
    • Effect of oxidation, pH, and ionic strength on calpastatin inhibition of {micro}-and m-calpain
    • Carlin, K. R., Huff-Lonergan, E., Rowe, L. J. and Lonergan, S. M. 2006. Effect of oxidation, pH, and ionic strength on calpastatin inhibition of {micro}-and m-calpain. J. Ani. Sci, 84 (4): 925-937.
    • (2006) J. Ani. Sci , vol.84 , Issue.4 , pp. 925-937
    • Carlin, K.R.1    Huff-Lonergan, E.2    Rowe, L.J.3    Lonergan, S.M.4
  • 19
    • 0942300360 scopus 로고    scopus 로고
    • Effect of Duroc content, sex and ageing period on meat and eating quality attributes of pork loin
    • Channon, H. A., Kerr, M. G. and Walker, P. J. 2004. Effect of Duroc content, sex and ageing period on meat and eating quality attributes of pork loin. Meat Sci, 66 (4): 881-888.
    • (2004) Meat Sci , vol.66 , Issue.4 , pp. 881-888
    • Channon, H.A.1    Kerr, M.G.2    Walker, P.J.3
  • 20
  • 21
    • 0142200868 scopus 로고    scopus 로고
    • Effect of proteolytic enzyme activity and heating on the mechanical properties of bovine single muscle fibres
    • Christensen, M., Larsen, L. M., Ertbjerg, P. and Purslow, P. P. 2004. Effect of proteolytic enzyme activity and heating on the mechanical properties of bovine single muscle fibres. Meat Sci, 66 (2): 361-369.
    • (2004) Meat Sci , vol.66 , Issue.2 , pp. 361-369
    • Christensen, M.1    Larsen, L.M.2    Ertbjerg, P.3    Purslow, P.P.4
  • 22
    • 0035545466 scopus 로고    scopus 로고
    • Effect of rate of pH decline on muscle enzyme activities in two pig lines
    • Claeys, E., De Smet, S., Demeyer, D., Geers, R. and Buys, N. 2001. Effect of rate of pH decline on muscle enzyme activities in two pig lines. Meat Sci, 57 (3): 257-263.
    • (2001) Meat Sci , vol.57 , Issue.3 , pp. 257-263
    • Claeys, E.1    De Smet, S.2    Demeyer, D.3    Geers, R.4    Buys, N.5
  • 23
    • 0036783749 scopus 로고    scopus 로고
    • Apparent elastic modulus and hysteresis of skeletal muscle cells throughout differentiation
    • Collinsworth, A. M., Zhang, S., Kraus, W. E. and Truskey, G. A. 2002. Apparent elastic modulus and hysteresis of skeletal muscle cells throughout differentiation. Am. J. Physiol. Cell Physiol, 283 (4): C1219-C1227.
    • (2002) Am. J. Physiol. Cell Physiol , vol.283 , Issue.4
    • Collinsworth, A.M.1    Zhang, S.2    Kraus, W.E.3    Truskey, G.A.4
  • 24
    • 84987279299 scopus 로고
    • Palatibility of individual muscles from ovine leg steaks as related to chemical and histological traits
    • Cross, H. R., Smith, G. C. and Carpenter, Z. L. 1972. Palatibility of individual muscles from ovine leg steaks as related to chemical and histological traits. J. Food Sci, 37: 282-285.
    • (1972) J. Food Sci , vol.37 , pp. 282-285
    • Cross, H.R.1    Smith, G.C.2    Carpenter, Z.L.3
  • 25
    • 84985162754 scopus 로고
    • Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle
    • Culler, R. D., Parrish, F. C. Jr, Smith, G. C. and Cross, H. R. 1978. Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle. J. Food Sci, 43 (4): 1177-1180.
    • (1978) J. Food Sci , vol.43 , Issue.4 , pp. 1177-1180
    • Culler, R.D.1    Parrish Jr., F.C.2    Smith, G.C.3    Cross, H.R.4
  • 26
    • 45849109920 scopus 로고    scopus 로고
    • Meat quality assessment using biophysical methods related to meat structure
    • Damez, J. L. and Clerjon, S. 2008. Meat quality assessment using biophysical methods related to meat structure. Meat Sci, 80 (1): 132-149.
    • (2008) Meat Sci , vol.80 , Issue.1 , pp. 132-149
    • Damez, J.L.1    Clerjon, S.2
  • 27
    • 0017101439 scopus 로고
    • A Ca2+ ion-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
    • Dayton, W. R., Goll, D. E., Zeece, M. G., Robson, R. M. and Reville, W. J. 1976. A Ca2+ ion-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry, 15 (10): 2150-2158.
    • (1976) Biochemistry , vol.15 , Issue.10 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 28
    • 0019879743 scopus 로고
    • A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium-requiring form of the protease
    • Dayton, W. R., Schollmeyer, J. V., Lepley, R. A. and Cortés, L. R. 1981. A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium-requiring form of the protease. Biochim. Biophys. Acta, 659 (1): 48-61.
    • (1981) Biochim. Biophys. Acta , vol.659 , Issue.1 , pp. 48-61
    • Dayton, W.R.1    Schollmeyer, J.V.2    Lepley, R.A.3    Cortés, L.R.4
  • 29
    • 22544487759 scopus 로고    scopus 로고
    • Imaging and elasticity measurements of the sarcolemma of fully differentiated skeletal muscle fibres
    • Defranchi, E., Bonaccurso, E., Tedesco, M., Canato, M., Pavan, E., Raiteri, R. and Reggiani, C. 2005. Imaging and elasticity measurements of the sarcolemma of fully differentiated skeletal muscle fibres. Microsc. Res. Tech, 67 (1): 27-35.
    • (2005) Microsc. Res. Tech , vol.67 , Issue.1 , pp. 27-35
    • Defranchi, E.1    Bonaccurso, E.2    Tedesco, M.3    Canato, M.4    Pavan, E.5    Raiteri, R.6    Reggiani, C.7
  • 30
    • 11444251857 scopus 로고    scopus 로고
    • A comparison between two methods (Warner-Bratzler and texture profile analysis) for testing either raw meat or cooked meat
    • de Huidobro, F. R., Miguel, E., Blázquez, B. and Onega, E. 2005. A comparison between two methods (Warner-Bratzler and texture profile analysis) for testing either raw meat or cooked meat. Meat Sci., 69 (3): 527-536.
    • (2005) Meat Sci. , vol.69 , Issue.3 , pp. 527-536
    • de Huidobro, F.R.1    Miguel, E.2    Blázquez, B.3    Onega, E.4
  • 32
    • 0035430563 scopus 로고    scopus 로고
    • Properties of myofibril-bound calpain activity in longissimus muscle of callipyge and normal sheep
    • Delgado, E. F., Geesink, G. H., Marchello, J. A., Goll, D. E. and Koohmaraie, M. 2001b. Properties of myofibril-bound calpain activity in longissimus muscle of callipyge and normal sheep. J. Anim. Sci, 79: 2097-2107.
    • (2001) J. Anim. Sci , vol.79 , pp. 2097-2107
    • Delgado, E.F.1    Geesink, G.H.2    Marchello, J.A.3    Goll, D.E.4    Koohmaraie, M.5
  • 34
    • 0033145074 scopus 로고    scopus 로고
    • Immunoblot analysis of calpastatin degradation: Evidence for cleavage by calpain in postmortem muscle
    • Doumit, M. E. and Koohmaraie, M. 1999. Immunoblot analysis of calpastatin degradation: Evidence for cleavage by calpain in postmortem muscle. J. Anim. Sci, 77: 1467-1473.
    • (1999) J. Anim. Sci , vol.77 , pp. 1467-1473
    • Doumit, M.E.1    Koohmaraie, M.2
  • 35
    • 0002741564 scopus 로고
    • Modeling post-mortem tenderization-III: Role of calpain I in conditioning
    • Dransfield, E. 1992. Modeling post-mortem tenderization-III: Role of calpain I in conditioning. Meat Sci, 31: 85-94.
    • (1992) Meat Sci , vol.31 , pp. 85-94
    • Dransfield, E.1
  • 37
    • 21244496302 scopus 로고    scopus 로고
    • Apoptosis in muscle atrophy: Relevance to sarcopenia
    • Dupont-Versteegden, E. E. 2005. Apoptosis in muscle atrophy: Relevance to sarcopenia. Exp. Gerontol, 40 (6): 473-481.
    • (2005) Exp. Gerontol , vol.40 , Issue.6 , pp. 473-481
    • Dupont-Versteegden, E.E.1
  • 38
    • 84985084292 scopus 로고
    • Effect of collagen levels and sarcomere shortening on muscle tenderness
    • Dutson, T. R., Hostetler, R. L. and Carpenter, Z. L. 1976. Effect of collagen levels and sarcomere shortening on muscle tenderness. J. Food Sci, 41 (4): 863-866.
    • (1976) J. Food Sci , vol.41 , Issue.4 , pp. 863-866
    • Dutson, T.R.1    Hostetler, R.L.2    Carpenter, Z.L.3
  • 39
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw, W. C., Martins, L. M. and Kaufmann, S. H. 1999. Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem, 68 (1): 383-424.
    • (1999) Annu. Rev. Biochem , vol.68 , Issue.1 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 40
    • 4544264684 scopus 로고    scopus 로고
    • Myotubes differentiate optimally on substrates with tissue-like stiffness: Pathological implications for soft or stiff microenvironments
    • Engler, A. J., Griffin, M. A., Sen, S., Bonnemann, C. G., Sweeney, H. L. and Discher, D. E. 2004. Myotubes differentiate optimally on substrates with tissue-like stiffness: Pathological implications for soft or stiff microenvironments. J. Cell Biol, 166 (6): 877
    • (2004) J. Cell Biol , vol.166 , Issue.6 , pp. 877
    • Engler, A.J.1    Griffin, M.A.2    Sen, S.3    Bonnemann, C.G.4    Sweeney, H.L.5    Discher, D.E.6
  • 42
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • Finer, J. T., Simmons, R. M. and Spudich, J. A. 1994. Single myosin molecule mechanics: Piconewton forces and nanometre steps. Nature, 368 (6467): 113-119.
    • (1994) Nature , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 43
    • 77949568631 scopus 로고    scopus 로고
    • Association between cathepsin L (CTSL) and cathepsin S (CTSS) polymorphisms and meat production and carcass traits in Italian Large White pigs
    • Fontanesi, L., Speroni, C., Buttazzoni, L., Scotti, E., Costa, L. N., Davoli, R. and Russo, V. 2010. Association between cathepsin L (CTSL) and cathepsin S (CTSS) polymorphisms and meat production and carcass traits in Italian Large White pigs. Meat Sci, 85 (2): 331-338.
    • (2010) Meat Sci , vol.85 , Issue.2 , pp. 331-338
    • Fontanesi, L.1    Speroni, C.2    Buttazzoni, L.3    Scotti, E.4    Costa, L.N.5    Davoli, R.6    Russo, V.7
  • 44
    • 69549123868 scopus 로고    scopus 로고
    • Effect of finishing and ageing time on quality attributes of loin from the meat of Holstein-Fresian cull cows
    • Franco, D., Bispo, E., González, L., Vázquez, J. A. and Moreno, T. 2009. Effect of finishing and ageing time on quality attributes of loin from the meat of Holstein-Fresian cull cows. Meat Sci, 83 (3): 484-491.
    • (2009) Meat Sci , vol.83 , Issue.3 , pp. 484-491
    • Franco, D.1    Bispo, E.2    González, L.3    Vázquez, J.A.4    Moreno, T.5
  • 45
    • 0003167746 scopus 로고
    • Titin content of beef in relation to tenderness
    • Fritz, J. D., Mitchell, M. C., Marsh, B. B. and Greaser, M. L. 1993. Titin content of beef in relation to tenderness. Meat Sci, 33 (1): 41-50.
    • (1993) Meat Sci , vol.33 , Issue.1 , pp. 41-50
    • Fritz, J.D.1    Mitchell, M.C.2    Marsh, B.B.3    Greaser, M.L.4
  • 46
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior, P. and Salvesen, G. S. 2004. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J, 384 (Pt 2): 201-232.
    • (2004) Biochem. J , vol.384 , Issue.Pt 2 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 47
    • 66149128872 scopus 로고    scopus 로고
    • Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains
    • Garcia, T. I., Oberhauser, A. F. and Braun, W. 2009. Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains. Proteins, 75 (3): 706-718.
    • (2009) Proteins , vol.75 , Issue.3 , pp. 706-718
    • Garcia, T.I.1    Oberhauser, A.F.2    Braun, W.3
  • 48
    • 0033208806 scopus 로고    scopus 로고
    • Effect of calpastatin on degradation of myofibrillar proteins by mu-calpain under postmortem conditions
    • Geesink, G. H. and Koohmaraie, M. 1999a. Effect of calpastatin on degradation of myofibrillar proteins by mu-calpain under postmortem conditions. J. Anim. Sci, 77 (10): 2685
    • (1999) J. Anim. Sci , vol.77 , Issue.10 , pp. 2685
    • Geesink, G.H.1    Koohmaraie, M.2
  • 49
    • 0033142812 scopus 로고    scopus 로고
    • Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage
    • Geesink, G. H. and Koohmaraie, M. 1999b. Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage. J. Anim. Sci, 77 (6): 1490-1501.
    • (1999) J. Anim. Sci , vol.77 , Issue.6 , pp. 1490-1501
    • Geesink, G.H.1    Koohmaraie, M.2
  • 50
    • 0034264486 scopus 로고    scopus 로고
    • Ionic strength-induced inactivation of mu-calpain in postmortem muscle
    • Geesink, G. H. and Koohmaraie, M. 2000. Ionic strength-induced inactivation of mu-calpain in postmortem muscle. J. Anim. Sci, 78 (9): 2336-2343.
    • (2000) J. Anim. Sci , vol.78 , Issue.9 , pp. 2336-2343
    • Geesink, G.H.1    Koohmaraie, M.2
  • 51
    • 33749402662 scopus 로고    scopus 로고
    • {micro}-Calpain is essential for postmortem proteolysis of muscle proteins
    • Geesink, G. H., Kuchay, S., Chishti, A. H. and Koohmaraie, M. 2006. {micro}-Calpain is essential for postmortem proteolysis of muscle proteins. J. Anim. Sci, 84 (10): 2834-2840.
    • (2006) J. Anim. Sci , vol.84 , Issue.10 , pp. 2834-2840
    • Geesink, G.H.1    Kuchay, S.2    Chishti, A.H.3    Koohmaraie, M.4
  • 52
    • 33646015361 scopus 로고    scopus 로고
    • Calpain 3/p94 is not involved in postmortem proteolysis
    • Geesink, G. H., Taylor, R. G. and Koohmaraie, M. 2005. Calpain 3/p94 is not involved in postmortem proteolysis. J. Anim. Sci, 83 (7): 1646
    • (2005) J. Anim. Sci , vol.83 , Issue.7 , pp. 1646
    • Geesink, G.H.1    Taylor, R.G.2    Koohmaraie, M.3
  • 53
    • 27144453667 scopus 로고    scopus 로고
    • Effect of selection for growth rate on the ageing of myofibrils, meat texture properties and the muscle proteolytic potential of m. longissimus in rabbits
    • Gil, M., Ramírez, J. A., Pla, M., Ariño, B., Hernández, P., Pascual, M., Blasco, A., Guerrero, L., Hajós, G., Szerdahelyi, E. N. and Oliver, M. Á. 2006. Effect of selection for growth rate on the ageing of myofibrils, meat texture properties and the muscle proteolytic potential of m. longissimus in rabbits. Meat Sci, 72 (1): 121-129.
    • (2006) Meat Sci , vol.72 , Issue.1 , pp. 121-129
    • Gil, M.1    Ramírez, J.A.2    Pla, M.3    Ariño, B.4    Hernández, P.5    Pascual, M.6    Blasco, A.7    Guerrero, L.8    Hajós, G.9    Szerdahelyi, E.N.10    Oliver, M.Á.11
  • 55
    • 0000666240 scopus 로고
    • Post-mortem changes in physical and chemical properties of bovine muscle
    • Goll, D. E., Henderson, D. W. and Kline, E. A. 1964. Post-mortem changes in physical and chemical properties of bovine muscle. J. Food Sci, 29: 590-596.
    • (1964) J. Food Sci , vol.29 , pp. 590-596
    • Goll, D.E.1    Henderson, D.W.2    Kline, E.A.3
  • 57
    • 33646005836 scopus 로고    scopus 로고
    • Substrate rigidity regulates the formation and maintenance of tissues
    • Guo, W. H., Frey, M. T., Burnham, N. A. and Wang, Y. L. 2006. Substrate rigidity regulates the formation and maintenance of tissues. Biophys. J, 90: 2213-2220.
    • (2006) Biophys. J , vol.90 , pp. 2213-2220
    • Guo, W.H.1    Frey, M.T.2    Burnham, N.A.3    Wang, Y.L.4
  • 58
    • 0842287487 scopus 로고    scopus 로고
    • Mechanisms of apoptosis in the heart
    • Gustafsson, Å. and Gottlieb, R. A. 2003. Mechanisms of apoptosis in the heart. J. Clin. Immunol, 23 (6): 447-459.
    • (2003) J. Clin. Immunol , vol.23 , Issue.6 , pp. 447-459
    • Gustafsson, A.1    Gottlieb, R.A.2
  • 59
    • 1642586149 scopus 로고    scopus 로고
    • Breakdown of large proteoglycans in bovine intramuscular connective tissue early postmortem
    • Hannesson, K. O., Pederson, M. E., Ofstad, R. and Kolset, S. O. 2003. Breakdown of large proteoglycans in bovine intramuscular connective tissue early postmortem. J. Muscle Food, 14: 301-318.
    • (2003) J. Muscle Food , vol.14 , pp. 301-318
    • Hannesson, K.O.1    Pederson, M.E.2    Ofstad, R.3    Kolset, S.O.4
  • 61
    • 84981849345 scopus 로고
    • Factors affecting collagen solubility in bovine muscles
    • Herring, H. K., Cassens, R. G. and Briskey, E. J. 1967. Factors affecting collagen solubility in bovine muscles. J. Food Sci, 32: 534-538.
    • (1967) J. Food Sci , vol.32 , pp. 534-538
    • Herring, H.K.1    Cassens, R.G.2    Briskey, E.J.3
  • 62
    • 0000416924 scopus 로고
    • Further studies on bovine muscle tenderness as influenced by carcass position, sarcomere length, and fiber diameter
    • Herring, H. K., Cassens, R. G. and Rriskey, E. J. 1965. Further studies on bovine muscle tenderness as influenced by carcass position, sarcomere length, and fiber diameter. J. Food Sci, 30 (6): 1049-1054.
    • (1965) J. Food Sci , vol.30 , Issue.6 , pp. 1049-1054
    • Herring, H.K.1    Cassens, R.G.2    Rriskey, E.J.3
  • 63
    • 84981854165 scopus 로고
    • The solubility of intramuscular collagen in meat animals of various ages
    • Hill, F. 1966. The solubility of intramuscular collagen in meat animals of various ages. J. Food Sci, 31: 161-166.
    • (1966) J. Food Sci , vol.31 , pp. 161-166
    • Hill, F.1
  • 64
    • 0028126638 scopus 로고
    • Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T
    • Ho, C. Y., Stromer, M. H. and Robson, R. M. 1994. Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie, 76 (5): 369-375.
    • (1994) Biochimie , vol.76 , Issue.5 , pp. 369-375
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 65
    • 0030183591 scopus 로고    scopus 로고
    • Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle
    • Ho, C. Y., Stromer, M. H. and Robson, R. M. 1996. Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle. J. Anim. Sci, 74 (7): 1563-1575.
    • (1996) J. Anim. Sci , vol.74 , Issue.7 , pp. 1563-1575
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 66
    • 84959538627 scopus 로고    scopus 로고
    • Protein degradation postmortem and tenderization
    • In: Du M., McCormick R. J., editors Boca Raton, Boca Raton,: CRC Press
    • Hopkins, D. L. and Geesink, G. H. 2009. " Protein degradation postmortem and tenderization ". In Applied Muscle Biology and Meat Science, Edited by: Du, M. and McCormick, R. J. 149-173. Boca Raton: CRC Press.
    • (2009) Applied Muscle Biology and Meat Science , pp. 149-173
    • Hopkins, D.L.1    Geesink, G.H.2
  • 67
    • 0036013220 scopus 로고    scopus 로고
    • The relationship between post-mortem calcium concentration or pH and indicators of proteolysis in ovine muscle
    • Hopkins, D. L. and Thompson, J. M. 2002. The relationship between post-mortem calcium concentration or pH and indicators of proteolysis in ovine muscle. Meat Sci, 61 (4): 411-414.
    • (2002) Meat Sci , vol.61 , Issue.4 , pp. 411-414
    • Hopkins, D.L.1    Thompson, J.M.2
  • 68
    • 39449092496 scopus 로고    scopus 로고
    • In vitro study to evaluate the degradation of bovine muscle proteins post-mortem by proteasome and [mu]-calpain
    • Houbak, M. B., Ertbjerg, P. and Therkildsen, M. 2008. In vitro study to evaluate the degradation of bovine muscle proteins post-mortem by proteasome and [mu]-calpain. Meat Sc, 79 (1): 77-85.
    • (2008) Meat Sc , vol.79 , Issue.1 , pp. 77-85
    • Houbak, M.B.1    Ertbjerg, P.2    Therkildsen, M.3
  • 69
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle
    • Huff-Lonergan, E., Mitsuhashi, T., Beekman, D. D., Parrish, F. C. Jr, Olson, D. G. and Robson, R. M. 1996a. Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci, 74 (5): 993-1008.
    • (1996) J. Anim. Sci , vol.74 , Issue.5 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish Jr., F.C.4    Olson, D.G.5    Robson, R.M.6
  • 70
    • 0030122535 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and western blotting comparisons of purified myofibrils and whole muscle preparations for evaluating titin and nebulin in postmortem bovine muscle
    • Huff-Lonergan, E., Mitsuhashi, T., Parrish, F. C. Jr and Robson, R. M. 1996b. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and western blotting comparisons of purified myofibrils and whole muscle preparations for evaluating titin and nebulin in postmortem bovine muscle. J. Anim. Sci, 74 (4): 779-785.
    • (1996) J. Anim. Sci , vol.74 , Issue.4 , pp. 779-785
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Parrish Jr., F.C.3    Robson, R.M.4
  • 71
    • 0029285632 scopus 로고
    • Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle
    • Huff-Lonergan, E., Parrish, F. C. Jr and Robson, R. M. 1995. Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle. J. Anim. Sci, 73 (4): 1064-1073.
    • (1995) J. Anim. Sci , vol.73 , Issue.4 , pp. 1064-1073
    • Huff-Lonergan, E.1    Parrish Jr., F.C.2    Robson, R.M.3
  • 72
    • 77954387385 scopus 로고    scopus 로고
    • Biochemistry of postmortem muscle-Lessons on mechanisms of meat tenderization
    • Huff Lonergan, E., Zhang, W. and Lonergan, S. M. 2010. Biochemistry of postmortem muscle-Lessons on mechanisms of meat tenderization. Meat Sci, 86 (1): 184-195.
    • (2010) Meat Sci , vol.86 , Issue.1 , pp. 184-195
    • Huff Lonergan, E.1    Zhang, W.2    Lonergan, S.M.3
  • 73
    • 11444251857 scopus 로고    scopus 로고
    • A comparison between two methods (Warner-Bratzler and texture profile analysis) for testing either raw meat or cooked meat
    • Huidobrod., F. R., Miguel, E., Blázquez, B. and Onega, E. 2005. A comparison between two methods (Warner-Bratzler and texture profile analysis) for testing either raw meat or cooked meat. Meat Sci, 69: 527-536.
    • (2005) Meat Sci , vol.69 , pp. 527-536
    • Huidobrod, F.R.1    Miguel, E.2    Blázquez, B.3    Onega, E.4
  • 74
    • 0038267939 scopus 로고    scopus 로고
    • The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness
    • Hwang, I. H., Devine, C. E. and Hopkins, D. L. 2003. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness. Meat Sci, 65 (2): 677-691.
    • (2003) Meat Sci , vol.65 , Issue.2 , pp. 677-691
    • Hwang, I.H.1    Devine, C.E.2    Hopkins, D.L.3
  • 75
    • 0142200878 scopus 로고    scopus 로고
    • Does the newly discovered calpain 10 play a role in meat tenderization during post-mortem storage?
    • Ilian, M. A., Bekhit, A. E. D. A. and Bickerstaffe, R. 2004. Does the newly discovered calpain 10 play a role in meat tenderization during post-mortem storage?. Meat Sci, 66 (2): 317-327.
    • (2004) Meat Sci , vol.66 , Issue.2 , pp. 317-327
    • Ilian, M.A.1    Bekhit, A.E.D.A.2    Bickerstaffe, R.3
  • 77
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during Iinteraction with actin
    • Ishijima, A., Kojima, H., Funatsu, T., Tokunaga, M., Higuchi, H., Tanaka, H. and Yanagida, T. 1998. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during Iinteraction with actin. Cell, 92 (2): 161-171.
    • (1998) Cell , vol.92 , Issue.2 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 78
    • 0032110006 scopus 로고    scopus 로고
    • Contribution of muscle proteinases to meat tenderization
    • Jiang, S. T. 1998. Contribution of muscle proteinases to meat tenderization. Porc. Natl. Sci. Counc. Repub. China B, 22: 97-107.
    • (1998) Porc. Natl. Sci. Counc. Repub. China B , vol.22 , pp. 97-107
    • Jiang, S.T.1
  • 79
    • 0025469157 scopus 로고
    • Differences in cathepsin B + L and calcium dependent protease activity among breeds type and their relationship to beef tenderness
    • Johnson, M. H., Calkins, C. R., Huffman, R. D., Johnson, D. D. and Hargrove, D. D. 1990. Differences in cathepsin B + L and calcium dependent protease activity among breeds type and their relationship to beef tenderness. J. Anim. Sci, 68: 2371-2379.
    • (1990) J. Anim. Sci , vol.68 , pp. 2371-2379
    • Johnson, M.H.1    Calkins, C.R.2    Huffman, R.D.3    Johnson, D.D.4    Hargrove, D.D.5
  • 80
    • 0034399688 scopus 로고    scopus 로고
    • Changes in lysosomal enzyme activities and shear values of high pressure treated meat during ageing
    • Jung, S., Ghoul, M. and de Lamballerie-Anton, M. 2000. Changes in lysosomal enzyme activities and shear values of high pressure treated meat during ageing. Meat Sci, 56 (3): 239-246.
    • (2000) Meat Sci , vol.56 , Issue.3 , pp. 239-246
    • Jung, S.1    Ghoul, M.2    de Lamballerie-Anton, M.3
  • 82
    • 33846236014 scopus 로고    scopus 로고
    • Mechanical strength of sarcomere structures of skeletal myofibrils studied by submicromanipulation
    • Kayamori, T., Miyake, N., Akiyama, N., Aimi, M., Wakayama, J., Kunioka, Y. and Yamada, T. 2006. Mechanical strength of sarcomere structures of skeletal myofibrils studied by submicromanipulation. Cell Struct. Funct, 31 (2): 135-143.
    • (2006) Cell Struct. Funct , vol.31 , Issue.2 , pp. 135-143
    • Kayamori, T.1    Miyake, N.2    Akiyama, N.3    Aimi, M.4    Wakayama, J.5    Kunioka, Y.6    Yamada, T.7
  • 83
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L. and Bustamante, C. 1997. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science, 276 (5315): 1112-1116.
    • (1997) Science , vol.276 , Issue.5315 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 84
    • 33749376502 scopus 로고    scopus 로고
    • Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle
    • Kemp, C. M., Bardsley, R. G. and Parr, T. 2006a. Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle. J. Anim. Sci, 84 (10): 2841-2846.
    • (2006) J. Anim. Sci , vol.84 , Issue.10 , pp. 2841-2846
    • Kemp, C.M.1    Bardsley, R.G.2    Parr, T.3
  • 85
    • 33646506412 scopus 로고    scopus 로고
    • Comparison of the relative expression of caspase isoforms in different porcine skeletal muscles
    • Kemp, C. M., Parr, T., Bardsley, R. G. and Buttery, P. J. 2006b. Comparison of the relative expression of caspase isoforms in different porcine skeletal muscles. Meat Sci, 73 (3): 426-431.
    • (2006) Meat Sci , vol.73 , Issue.3 , pp. 426-431
    • Kemp, C.M.1    Parr, T.2    Bardsley, R.G.3    Buttery, P.J.4
  • 87
    • 0027356908 scopus 로고
    • Effect of pH and ionic strength on bovine m-calpain and calpastatin activity
    • Kendall, T. L., Koohmaraie, M., Arbona, J. R., Williams, S. E. and Young, L. L. 1993. Effect of pH and ionic strength on bovine m-calpain and calpastatin activity. J. Anim. Sci, 71: 96-104.
    • (1993) J. Anim. Sci , vol.71 , pp. 96-104
    • Kendall, T.L.1    Koohmaraie, M.2    Arbona, J.R.3    Williams, S.E.4    Young, L.L.5
  • 88
    • 0015383455 scopus 로고
    • Apoptosis, a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wylie, A. H. and Currie, A. R. 1972. Apoptosis, a basic biological phenomenon with wide-ranging implications in tissue kinetics. Brit. J. Cancer, 26: 239-257.
    • (1972) Brit. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wylie, A.H.2    Currie, A.R.3
  • 89
    • 57249108033 scopus 로고    scopus 로고
    • Fatty acid composition and meat quality traits of organically reared Korean native black pigs
    • Kim, D. H., Seong, P. N., Cho, S. H., Kim, J. H., Lee, J. M., Jo, C. and Lim, D. G. 2009. Fatty acid composition and meat quality traits of organically reared Korean native black pigs. Livestock Sci, 120 (1-2): 96-102.
    • (2009) Livestock Sci , vol.120 , Issue.1-2 , pp. 96-102
    • Kim, D.H.1    Seong, P.N.2    Cho, S.H.3    Kim, J.H.4    Lee, J.M.5    Jo, C.6    Lim, D.G.7
  • 90
    • 0026510571 scopus 로고
    • Characterization and localization of -connectin (titin 1): An elastic protein isolated from rabbit skeletal muscle
    • Kimura, S., Matsuura, T., Ohtsuka, S., Nakauchi, Y., Matsuno, A. and Maruyama, K. 1992. Characterization and localization of -connectin (titin 1): An elastic protein isolated from rabbit skeletal muscle. J. Muscle Res. Cell M, 13 (1): 39-47.
    • (1992) J. Muscle Res. Cell M , vol.13 , Issue.1 , pp. 39-47
    • Kimura, S.1    Matsuura, T.2    Ohtsuka, S.3    Nakauchi, Y.4    Matsuno, A.5    Maruyama, K.6
  • 91
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A. and Yanagida, T. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature, 334: 74-76.
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 92
    • 0001619142 scopus 로고
    • Inhibition of postmortem tenderization in ovine carcasses through infusion of zinc
    • Koohmaraie, M. 1990. Inhibition of postmortem tenderization in ovine carcasses through infusion of zinc. J. Anim. Sci, 68: 1476-1483.
    • (1990) J. Anim. Sci , vol.68 , pp. 1476-1483
    • Koohmaraie, M.1
  • 93
    • 0026929966 scopus 로고
    • Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle mu-calpain
    • Koohmaraie, M. 1992a. Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle mu-calpain. J. Anim. Sci, 70: 3071-3080.
    • (1992) J. Anim. Sci , vol.70 , pp. 3071-3080
    • Koohmaraie, M.1
  • 94
    • 0027026199 scopus 로고
    • Ovine skeletal muscle multicatalytic proteinase complex (proteasome): Purification, characterization, and comparison of its effects on myofibrils with mu-calpains
    • Koohmaraie, M. 1992b. Ovine skeletal muscle multicatalytic proteinase complex (proteasome): Purification, characterization, and comparison of its effects on myofibrils with mu-calpains. J. Anim. Sci, 70 (12): 3697
    • (1992) J. Anim. Sci , vol.70 , Issue.12 , pp. 3697
    • Koohmaraie, M.1
  • 95
    • 0030305245 scopus 로고    scopus 로고
    • Biochemical factors regulating the toughening and tenderization process of meat
    • Koohmaraie, M. 1996. Biochemical factors regulating the toughening and tenderization process of meat. Meat Sci, 43: 193-201.
    • (1996) Meat Sci , vol.43 , pp. 193-201
    • Koohmaraie, M.1
  • 96
    • 0030330032 scopus 로고    scopus 로고
    • Meat toughening does not occur when rigor shortening is prevented
    • Koohmaraie, M., Doumit, M. E. and Wheeler, T. L. 1996. Meat toughening does not occur when rigor shortening is prevented. J. Anim. Sci, 74 (12): 2935-2942.
    • (1996) J. Anim. Sci , vol.74 , Issue.12 , pp. 2935-2942
    • Koohmaraie, M.1    Doumit, M.E.2    Wheeler, T.L.3
  • 97
    • 33745648075 scopus 로고    scopus 로고
    • Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system
    • Koohmaraie, M. and Geesink, G. H. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci, 74 (1): 34-43.
    • (2006) Meat Sci , vol.74 , Issue.1 , pp. 34-43
    • Koohmaraie, M.1    Geesink, G.H.2
  • 98
    • 0026248168 scopus 로고
    • Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride
    • Koohmaraie, M. and Whipple, G. 1991. Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. J. Anim. Sci, 69: 4449-4460.
    • (1991) J. Anim. Sci , vol.69 , pp. 4449-4460
    • Koohmaraie, M.1    Whipple, G.2
  • 99
    • 0026114381 scopus 로고
    • Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses
    • Koohmaraie, M., Whipple, G., Kretchmar, D. H., Crouse, J. D. and Mersmann, H. J. 1991. Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J. Anim. Sci, 69 (2): 617-624.
    • (1991) J. Anim. Sci , vol.69 , Issue.2 , pp. 617-624
    • Koohmaraie, M.1    Whipple, G.2    Kretchmar, D.H.3    Crouse, J.D.4    Mersmann, H.J.5
  • 100
    • 41649116913 scopus 로고    scopus 로고
    • Tensile properties of single desmin intermediate filaments
    • Kreplak, L., Herrmann, H. and Aebi, U. 2008. Tensile properties of single desmin intermediate filaments. Biophys. J, 94 (7): 2790-2799.
    • (2008) Biophys. J , vol.94 , Issue.7 , pp. 2790-2799
    • Kreplak, L.1    Herrmann, H.2    Aebi, U.3
  • 101
    • 0036313464 scopus 로고    scopus 로고
    • Changes in proteasome activity during postmortem aging of bovine muscle
    • Lamare, M., Taylor, R. G., Farout, L., Briand, Y. and Briand, M. 2002a. Changes in proteasome activity during postmortem aging of bovine muscle. Meat Sci, 61: 199-204.
    • (2002) Meat Sci , vol.61 , pp. 199-204
    • Lamare, M.1    Taylor, R.G.2    Farout, L.3    Briand, Y.4    Briand, M.5
  • 102
    • 0036313464 scopus 로고    scopus 로고
    • Changes in proteasome activity during postmortem aging of bovine muscle
    • Lamare, M., Taylor, R. G., Farout, L., Briand, Y. and Briand, M. 2002b. Changes in proteasome activity during postmortem aging of bovine muscle. Meat Sci, 61 (2): 199-204.
    • (2002) Meat Sci , vol.61 , Issue.2 , pp. 199-204
    • Lamare, M.1    Taylor, R.G.2    Farout, L.3    Briand, Y.4    Briand, M.5
  • 105
    • 33847145736 scopus 로고    scopus 로고
    • A theoretical approach of the relationship between collagen content, collagen cross-links and meat tenderness
    • Lepetit, J. 2007. A theoretical approach of the relationship between collagen content, collagen cross-links and meat tenderness. Meat Sci, 76: 147-159.
    • (2007) Meat Sci , vol.76 , pp. 147-159
    • Lepetit, J.1
  • 106
    • 52249084763 scopus 로고    scopus 로고
    • Collagen contribution to meat toughness: Theoretical aspects
    • Lepetit, J. 2008. Collagen contribution to meat toughness: Theoretical aspects. Meat Sci, 80: 960-967.
    • (2008) Meat Sci , vol.80 , pp. 960-967
    • Lepetit, J.1
  • 107
    • 0011046055 scopus 로고
    • The effect of conditioning on the strength of perimysial connective tissue dissected from cooked meat
    • Lewis, G. J., Purslow, P. P. and Rice, A. E. 1991. The effect of conditioning on the strength of perimysial connective tissue dissected from cooked meat. Meat Sci, 30: 1-12.
    • (1991) Meat Sci , vol.30 , pp. 1-12
    • Lewis, G.J.1    Purslow, P.P.2    Rice, A.E.3
  • 109
    • 21344495035 scopus 로고
    • Structural changes in endomysium and perimysium during postmortem ageing of chicken semitendinosus muscle-Contribution of intramuscular connective tissue to meat tenderisation
    • Liu, A., Nishimura, T. and Takahashi, K. 1994. Structural changes in endomysium and perimysium during postmortem ageing of chicken semitendinosus muscle-Contribution of intramuscular connective tissue to meat tenderisation. Meat Sci, 38: 315-328.
    • (1994) Meat Sci , vol.38 , pp. 315-328
    • Liu, A.1    Nishimura, T.2    Takahashi, K.3
  • 110
    • 0030140583 scopus 로고    scopus 로고
    • Relationship between structural properties of intramuscular connective tissue and toughness of various chicken skeletal muscles
    • Liu, A., Nishimura, T. and Takahashi, K. 1996. Relationship between structural properties of intramuscular connective tissue and toughness of various chicken skeletal muscles. Meat Sci, 43: 43-49.
    • (1996) Meat Sci , vol.43 , pp. 43-49
    • Liu, A.1    Nishimura, T.2    Takahashi, K.3
  • 111
    • 22144449926 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on μ- and m-calpain inhibition by calpastatin
    • Maddock, K. R., Huff Lonergan, E., Rowe, L. J. and Lonergan, S. M. 2005. Effect of pH and ionic strength on μ- and m-calpain inhibition by calpastatin. J. Anim. Sci, 83: 1370-1376.
    • (2005) J. Anim. Sci , vol.83 , pp. 1370-1376
    • Maddock, K.R.1    Huff Lonergan, E.2    Rowe, L.J.3    Lonergan, S.M.4
  • 112
    • 1542375185 scopus 로고    scopus 로고
    • Quantitative analysis of the viscoelastic properties of thin regions of fibroblasts using atomic force microscopy
    • Mahaffy, R. E., Park, S., Gerde, E., Kas, J. and Shih, S. K. 2004. Quantitative analysis of the viscoelastic properties of thin regions of fibroblasts using atomic force microscopy. Biophys. J, 86: 1777-1793.
    • (2004) Biophys. J , vol.86 , pp. 1777-1793
    • Mahaffy, R.E.1    Park, S.2    Gerde, E.3    Kas, J.4    Shih, S.K.5
  • 113
    • 0033484399 scopus 로고    scopus 로고
    • Electrical stimulation of pigs-effect on pH fall, meat quality and cathepsin B+L activity
    • Maribo, H., Ertbjerg, P., Andersson, M., Barton-Gade, P. and Møller, A. J. 1999. Electrical stimulation of pigs-effect on pH fall, meat quality and cathepsin B+L activity. Meat Sci, 52 (2): 179-187.
    • (1999) Meat Sci , vol.52 , Issue.2 , pp. 179-187
    • Maribo, H.1    Ertbjerg, P.2    Andersson, M.3    Barton-Gade, P.4    Møller, A.J.5
  • 114
    • 84981851390 scopus 로고
    • Studies in meat tenderness. III. The effects of cold shortening on tenderness
    • Marsh, B. B. and Leet, N. G. 1966. Studies in meat tenderness. III. The effects of cold shortening on tenderness. J. Food Sci, 31: 450-459.
    • (1966) J. Food Sci , vol.31 , pp. 450-459
    • Marsh, B.B.1    Leet, N.G.2
  • 115
    • 0034753596 scopus 로고    scopus 로고
    • Endothelial, cardiac muscle and skeletal muscle exhibit different viscous and elastic properties as determined by atomic force microscopy
    • Mathur, A. B., Collinsworth, A. M., Reichert, W. M., Kraus, W. E. and Truskey, G. A. 2001. Endothelial, cardiac muscle and skeletal muscle exhibit different viscous and elastic properties as determined by atomic force microscopy. J. Biomech, 34 (12): 1545-1553.
    • (2001) J. Biomech , vol.34 , Issue.12 , pp. 1545-1553
    • Mathur, A.B.1    Collinsworth, A.M.2    Reichert, W.M.3    Kraus, W.E.4    Truskey, G.A.5
  • 117
    • 0038196357 scopus 로고
    • Atomic force microscopy
    • Meyer, E. 1992. Atomic force microscopy. Prog. Surf. Sci, 41: 3-49.
    • (1992) Prog. Surf. Sci , vol.41 , pp. 3-49
    • Meyer, E.1
  • 118
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva, A., Kulke, M., Fernandez, J. M. and Linke, W. A. 2001. Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys. J, 80 (3): 1442-1451.
    • (2001) Biophys. J , vol.80 , Issue.3 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 119
    • 0029984843 scopus 로고    scopus 로고
    • Strength and lifetime of the bond between actin and skeletal muscle [alpha]-actinin studied with an optical trapping technique
    • Miyata, H., Yasuda, R. and Kinosita, K. 1996. Strength and lifetime of the bond between actin and skeletal muscle [alpha]-actinin studied with an optical trapping technique. Biochim. Biophys. Acta, 1290 (1): 83-88.
    • (1996) Biochim. Biophys. Acta , vol.1290 , Issue.1 , pp. 83-88
    • Miyata, H.1    Yasuda, R.2    Kinosita, K.3
  • 121
    • 77953921363 scopus 로고    scopus 로고
    • Molecular and biological factors affecting skeletal muscle cells after slaughtering and their impact on meat quality: A mini review
    • Mohanty, T. R., Park, K. M., Pramod, A. B., Kim, J. H., Choe, H. S. and Hwang, I. H. 2010. Molecular and biological factors affecting skeletal muscle cells after slaughtering and their impact on meat quality: A mini review. J. Muscle Foods, 21: 51-78.
    • (2010) J. Muscle Foods , vol.21 , pp. 51-78
    • Mohanty, T.R.1    Park, K.M.2    Pramod, A.B.3    Kim, J.H.4    Choe, H.S.5    Hwang, I.H.6
  • 122
    • 22544432237 scopus 로고    scopus 로고
    • Postmortem changes in myofibrillar proteins of goat skeletal muscles
    • Nagaraj, N. S., Anilakumar, K. R. and Santhanam, K. 2005. Postmortem changes in myofibrillar proteins of goat skeletal muscles. J. Food Biochem, 29 (2): 152-170.
    • (2005) J. Food Biochem , vol.29 , Issue.2 , pp. 152-170
    • Nagaraj, N.S.1    Anilakumar, K.R.2    Santhanam, K.3
  • 123
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid
    • Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A. and Yuan, J. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid. Nature, 403 (6765): 98-103.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 124
    • 0142249479 scopus 로고    scopus 로고
    • Gigantic variety: Expression patterns of titin isoforms in striated muscles and consequences for myofibrillar passive stiffness
    • Neagoe, C., Opitz, C. A., Makarenko, I. and Linke, W. A. 2003. Gigantic variety: Expression patterns of titin isoforms in striated muscles and consequences for myofibrillar passive stiffness. J. Muscle Res. Cell Motil, 24 (2): 175-189.
    • (2003) J. Muscle Res. Cell Motil , vol.24 , Issue.2 , pp. 175-189
    • Neagoe, C.1    Opitz, C.A.2    Makarenko, I.3    Linke, W.A.4
  • 125
    • 55349146638 scopus 로고    scopus 로고
    • Structural weakening of intramuscular connective tissue during postmortem aging of pork
    • Nishimura, T., Fang, S., Ito, T., Wakamatsu, J. and Takahashi, K. 2008. Structural weakening of intramuscular connective tissue during postmortem aging of pork. Anim. Sci. J, 79: 716-721.
    • (2008) Anim. Sci. J , vol.79 , pp. 716-721
    • Nishimura, T.1    Fang, S.2    Ito, T.3    Wakamatsu, J.4    Takahashi, K.5
  • 126
    • 0031992372 scopus 로고    scopus 로고
    • Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef
    • Nishimura, T., Liu, A., Hattori, A. and Takahashi, K. 1998. Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef. J. Anim. Sci, 76 (2): 528-532.
    • (1998) J. Anim. Sci , vol.76 , Issue.2 , pp. 528-532
    • Nishimura, T.1    Liu, A.2    Hattori, A.3    Takahashi, K.4
  • 127
    • 0029075829 scopus 로고
    • Unbinding force of a single motor molecule of muscle measured using optical tweezers
    • Nishizaka, T., Miyata, H., Yoshikawa, H., Ishiwata, S. and Kinosita, K. Jr. 1995. Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature, 377 (6546): 251-254.
    • (1995) Nature , vol.377 , Issue.6546 , pp. 251-254
    • Nishizaka, T.1    Miyata, H.2    Yoshikawa, H.3    Ishiwata, S.4    Kinosita Jr., K.5
  • 128
    • 0033884332 scopus 로고    scopus 로고
    • Characterization of single actomyosin rigor bonds: Load dependence of lifetime and mechanical properties
    • Nishizaka, T., Seo, R., Tadakuma, H., Kinosita, K. and Ishiwata, S. 2000. Characterization of single actomyosin rigor bonds: Load dependence of lifetime and mechanical properties. Biophys. J, 79 (2): 962-974.
    • (2000) Biophys. J , vol.79 , Issue.2 , pp. 962-974
    • Nishizaka, T.1    Seo, R.2    Tadakuma, H.3    Kinosita, K.4    Ishiwata, S.5
  • 129
    • 0031992319 scopus 로고    scopus 로고
    • Effects of age and tissue type on the calpain proteolytic system in turkey skeletal muscle
    • Northcutt, J. K., Pringle, T. D., Dickens, J. A., Buhr, R. J. and Young, L. L. 1998. Effects of age and tissue type on the calpain proteolytic system in turkey skeletal muscle. Poultry Sci., 77 (2): 367
    • (1998) Poultry Sci. , vol.77 , Issue.2 , pp. 367
    • Northcutt, J.K.1    Pringle, T.D.2    Dickens, J.A.3    Buhr, R.J.4    Young, L.L.5
  • 130
    • 0034052572 scopus 로고    scopus 로고
    • Morphology and transverse stiffness of drosophila myofibrils measured by atomic force microscopy
    • Nyland, L. R. and Maughan, D. W. 2000. Morphology and transverse stiffness of drosophila myofibrils measured by atomic force microscopy. Biophys. J, 78 (3): 1490-1497.
    • (2000) Biophys. J , vol.78 , Issue.3 , pp. 1490-1497
    • Nyland, L.R.1    Maughan, D.W.2
  • 132
    • 70350417132 scopus 로고    scopus 로고
    • Lateral mechanics of muscle fibers and its role in signaling
    • Ogneva, I. V., Lebedev, D. V. and Shenkman, B. S. 2009. Lateral mechanics of muscle fibers and its role in signaling. Biophysics, 54 (3): 365-369.
    • (2009) Biophysics , vol.54 , Issue.3 , pp. 365-369
    • Ogneva, I.V.1    Lebedev, D.V.2    Shenkman, B.S.3
  • 134
    • 84985046283 scopus 로고
    • Effect of postmortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle
    • Olson, D. G., Parrish, F. C. Jr, Dayton, W. R. and Goll, D. E. 1977. Effect of postmortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle. J. Food Sci, 42 (1): 117-124.
    • (1977) J. Food Sci , vol.42 , Issue.1 , pp. 117-124
    • Olson, D.G.1    Parrish Jr., F.C.2    Dayton, W.R.3    Goll, D.E.4
  • 136
    • 0033089932 scopus 로고    scopus 로고
    • Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine longissimus muscle
    • Parr, T., Sensky, P. L., Scothern, G. P., Bardsley, R. G., Buttery, P. J., Wood, J. D. and Warkup, C. 1999. Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine longissimus muscle. J. Anim. Sci, 77: 661-668.
    • (1999) J. Anim. Sci , vol.77 , pp. 661-668
    • Parr, T.1    Sensky, P.L.2    Scothern, G.P.3    Bardsley, R.G.4    Buttery, P.J.5    Wood, J.D.6    Warkup, C.7
  • 138
    • 1842455882 scopus 로고    scopus 로고
    • Effect of selection for growth rate on biochemical, quality and texture characteristics of meat from rabbits
    • Ramírez, J. A., Oliver, M. À., Pla, M., Guerrero, L., Ariño, B., Blasco, A., Pascual, M. and Gil, M. 2004. Effect of selection for growth rate on biochemical, quality and texture characteristics of meat from rabbits. Meat Sci, 67 (4): 617-624.
    • (2004) Meat Sci , vol.67 , Issue.4 , pp. 617-624
    • Ramírez, J.A.1    Oliver, M.A.2    Pla, M.3    Guerrero, L.4    Ariño, B.5    Blasco, A.6    Pascual, M.7    Gil, M.8
  • 140
    • 0033478347 scopus 로고    scopus 로고
    • The effect of proteasome on myofibrillar structures in bovine skeletal muscle
    • Robert, N., Briand, M., Taylor, R. and Briand, Y. 1999. The effect of proteasome on myofibrillar structures in bovine skeletal muscle. Meat Sci, 51 (2): 149-153.
    • (1999) Meat Sci , vol.51 , Issue.2 , pp. 149-153
    • Robert, N.1    Briand, M.2    Taylor, R.3    Briand, Y.4
  • 142
    • 0033514379 scopus 로고    scopus 로고
    • Dimensional and mechanical dynamics of active and stable edges in motile fibroblasts investigated by using atomic force microscopy
    • Rotsch, C., Jacobson, K. and Radmacher, R. 1999. Dimensional and mechanical dynamics of active and stable edges in motile fibroblasts investigated by using atomic force microscopy. Proc. Natl. Acad. Sci., 96: 921-926.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 921-926
    • Rotsch, C.1    Jacobson, K.2    Radmacher, R.3
  • 143
    • 0034127331 scopus 로고    scopus 로고
    • Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: An atomic force microscopy study
    • Rotsch, C. and Manfred, R. 2000. Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: An atomic force microscopy study. Biophys. J, 78: 520-536.
    • (2000) Biophys. J , vol.78 , pp. 520-536
    • Rotsch, C.1    Manfred, R.2
  • 144
    • 7244260588 scopus 로고    scopus 로고
    • Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain
    • Rowe, L. J., Maddock, K. R., Lonergan, S. M. and Huff Lonergan, E. 2004. Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain. J. Anim. Sci, 82: 3254-3266.
    • (2004) J. Anim. Sci , vol.82 , pp. 3254-3266
    • Rowe, L.J.1    Maddock, K.R.2    Lonergan, S.M.3    Huff Lonergan, E.4
  • 145
    • 34247241609 scopus 로고    scopus 로고
    • Characterization of beef semimembranosus and adductor muscles from US and Mexican origin
    • Rubio, L. M. S., Méndez, M. R. D. and Huerta-Leidenz, N. 2007. Characterization of beef semimembranosus and adductor muscles from US and Mexican origin. Meat Sci, 76 (3): 438-443.
    • (2007) Meat Sci , vol.76 , Issue.3 , pp. 438-443
    • Rubio, L.M.S.1    Méndez, M.R.D.2    Huerta-Leidenz, N.3
  • 146
    • 0042384409 scopus 로고    scopus 로고
    • Changes in meat quality characteristics of bovine meat during the first 6 days post mortem
    • Ruiz d. H. F
    • Miguel, E., Onega, E. and Blázquez, B. 2003. Changes in meat quality characteristics of bovine meat during the first 6 days post mortem. Meat Sci, 65 (4): 1439-1446. Ruiz, d. H. F.
    • (2003) Meat Sci , vol.65 , Issue.4 , pp. 1439-1446
    • Miguel, E.1    Onega, E.2    Blázquez, B.3
  • 147
    • 0035090082 scopus 로고    scopus 로고
    • Caspase 3 expression correlates with skeletal muscle apoptosis in Duchenne and facioscapulo human muscular dystrophy. A potential target for pharmacological treatment?
    • Sandri, M., El Meslemani, A. H., Sandri, C., Schjerling, P., Vissing, K., Andersen, J. L., Rossini, K., Carraro, U. and Angelini, C. 2001. Caspase 3 expression correlates with skeletal muscle apoptosis in Duchenne and facioscapulo human muscular dystrophy. A potential target for pharmacological treatment?. J. Neuropathol. Exp. Neurol, 60 (3): 302-312.
    • (2001) J. Neuropathol. Exp. Neurol , vol.60 , Issue.3 , pp. 302-312
    • Sandri, M.1    El Meslemani, A.H.2    Sandri, C.3    Schjerling, P.4    Vissing, K.5    Andersen, J.L.6    Rossini, K.7    Carraro, U.8    Angelini, C.9
  • 148
    • 0036206684 scopus 로고    scopus 로고
    • Myofibril-bound serine protease and its endogenous inhibitor in mouse: Extraction, partial characterization and effect on myofibrils
    • Sangorrín, M. P., Martone, C. B. and Sánchez, J. J. 2002. Myofibril-bound serine protease and its endogenous inhibitor in mouse: Extraction, partial characterization and effect on myofibrils. Comp. Biochem. Physiol. B: Biochem. Mol. Biol, 131 (4): 713-723.
    • (2002) Comp. Biochem. Physiol. B: Biochem. Mol. Biol , vol.131 , Issue.4 , pp. 713-723
    • Sangorrín, M.P.1    Martone, C.B.2    Sánchez, J.J.3
  • 149
    • 0030902490 scopus 로고    scopus 로고
    • Axial rotation of sliding actin filaments revealed by single-fluorophore imaging
    • Sase, I., Miyata, H., Ishiwata, S. and Kinosita, J. K. 1997. Axial rotation of sliding actin filaments revealed by single-fluorophore imaging. Proc. Natl. Acad. Sci, 94: 5646-5650.
    • (1997) Proc. Natl. Acad. Sci , vol.94 , pp. 5646-5650
    • Sase, I.1    Miyata, H.2    Ishiwata, S.3    Kinosita, J.K.4
  • 150
    • 0031826531 scopus 로고    scopus 로고
    • The structure of interfibrillar proteoglycan bridge ('shape modules') in extracellular matrix of fibrous connective tissues and their stability in various chemical environments
    • Scott, J. E. and Thomlinson, A. M. 1998. The structure of interfibrillar proteoglycan bridge ('shape modules') in extracellular matrix of fibrous connective tissues and their stability in various chemical environments. J. Anat, 192: 391-405.
    • (1998) J. Anat , vol.192 , pp. 391-405
    • Scott, J.E.1    Thomlinson, A.M.2
  • 151
    • 0000641777 scopus 로고
    • Factors associated with tenderness in young beef
    • Seideman, S. C., Koohmaraie, M. and Crouse, J. D. 1987. Factors associated with tenderness in young beef. Meat Sci, 20 (4): 281-291.
    • (1987) Meat Sci , vol.20 , Issue.4 , pp. 281-291
    • Seideman, S.C.1    Koohmaraie, M.2    Crouse, J.D.3
  • 152
    • 0036986447 scopus 로고    scopus 로고
    • Role of muscle endopeptidases and their inhibitors in meat tenderness
    • Sentandreu, M. A., Coulis, G. and Ouali, A. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci. Technol, 13 (12): 400-421.
    • (2002) Trends Food Sci. Technol , vol.13 , Issue.12 , pp. 400-421
    • Sentandreu, M.A.1    Coulis, G.2    Ouali, A.3
  • 154
    • 84863231112 scopus 로고    scopus 로고
    • Cellular biomechanics investigated by atomic force microscopy
    • Montreal, Montreal,: Mcgill University, PhD
    • Smith, B. A. 2004. " Cellular biomechanics investigated by atomic force microscopy ". In Department of Physics, 260 Montreal: Mcgill University. PhD
    • (2004) Department of Physics , pp. 260
    • Smith, B.A.1
  • 155
    • 79960603497 scopus 로고    scopus 로고
    • Physiology and chemistry of edible muscle tissue
    • In: Damodaran S., Parkin K. L., Fennema O. R., editors Boca Raton, Boca Raton,: CRC Press
    • Strasberg, G., Xiong, Y. L. and Chiang, W. 2007. " Physiology and chemistry of edible muscle tissue ". In Fennema's Food Chemistry, Edited by: Damodaran, S., Parkin, K. L. and Fennema, O. R. 924-968. Boca Raton: CRC Press.
    • (2007) Fennema's Food Chemistry , pp. 924-968
    • Strasberg, G.1    Xiong, Y.L.2    Chiang, W.3
  • 156
    • 84893606285 scopus 로고    scopus 로고
    • Muscle structure and function
    • In: Du M., McCormick R. J., editors Boca Raton, Boca Raton,: CRC Press
    • Swartz, D. R., Greaser, M. L. and Cantino, M. E. 2009. " Muscle structure and function ". In Applied Muscle Biology and Meat Science, Edited by: Du, M. and McCormick, R. J. 1-195. Boca Raton: CRC Press.
    • (2009) Applied Muscle Biology and Meat Science , pp. 1-195
    • Swartz, D.R.1    Greaser, M.L.2    Cantino, M.E.3
  • 157
    • 0030305246 scopus 로고    scopus 로고
    • Structural weakening of skeletal muscle tissue during postmortem ageing of meat: The non-enzymatic mechanism of meat tenderization
    • Takahashi, K. 1996. Structural weakening of skeletal muscle tissue during postmortem ageing of meat: The non-enzymatic mechanism of meat tenderization. Meat Sci, 43: 67-80.
    • (1996) Meat Sci , vol.43 , pp. 67-80
    • Takahashi, K.1
  • 158
    • 0029298086 scopus 로고
    • Is Z-disk degradation responsible for postmortem tenderization?
    • Taylor, R. G., Geesink, G. H., Thompson, V. F., Koohmaraie, M. and Goll, D. E. 1995a. Is Z-disk degradation responsible for postmortem tenderization?. J. Anim. Sci, 73 (5): 1351-1367.
    • (1995) J. Anim. Sci , vol.73 , Issue.5 , pp. 1351-1367
    • Taylor, R.G.1    Geesink, G.H.2    Thompson, V.F.3    Koohmaraie, M.4    Goll, D.E.5
  • 159
    • 0032196716 scopus 로고    scopus 로고
    • Effects of postmortem storage on the ultrastructure of the endomysium and myofibrils in normal and callipyge longissimus
    • Taylor, R. G. and Koohmaraie, M. 1998. Effects of postmortem storage on the ultrastructure of the endomysium and myofibrils in normal and callipyge longissimus. J. Anim. Sci, 76 (11): 2811-2817.
    • (1998) J. Anim. Sci , vol.76 , Issue.11 , pp. 2811-2817
    • Taylor, R.G.1    Koohmaraie, M.2
  • 161
    • 0030305256 scopus 로고    scopus 로고
    • Biophysical aspects of meat tenderness
    • Tornberg, E. 1996. Biophysical aspects of meat tenderness. Meat Sci, 43: 175-191.
    • (1996) Meat Sci , vol.43 , pp. 175-191
    • Tornberg, E.1
  • 163
    • 42149127186 scopus 로고    scopus 로고
    • Caspase 3 is not likely involved in the postmortem tenderization of beef muscle
    • Underwood, K. R., Means, W. J. and Du, M. 2008. Caspase 3 is not likely involved in the postmortem tenderization of beef muscle. J. Anim. Sci, 86 (4): 960-966.
    • (2008) J. Anim. Sci , vol.86 , Issue.4 , pp. 960-966
    • Underwood, K.R.1    Means, W.J.2    Du, M.3
  • 164
    • 0028435234 scopus 로고
    • Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility
    • Uytterhaegen, L., Claeys, E. and Demeyer, D. 1994. Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility. J. Anim. Sci, 72 (5): 1209-1223.
    • (1994) J. Anim. Sci , vol.72 , Issue.5 , pp. 1209-1223
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.3
  • 165
    • 0035381015 scopus 로고    scopus 로고
    • Effect of postmortem storage on mu-calpain and m-calpain in ovine skeletal muscle
    • Veiseth, E., Shackelford, S. D., Wheeler, T. L. and Koohmaraie, M. 2001. Effect of postmortem storage on mu-calpain and m-calpain in ovine skeletal muscle. J. Anim. Sci, 70: 1502-1508.
    • (2001) J. Anim. Sci , vol.70 , pp. 1502-1508
    • Veiseth, E.1    Shackelford, S.D.2    Wheeler, T.L.3    Koohmaraie, M.4
  • 166
    • 0034456653 scopus 로고    scopus 로고
    • Atomic force microscopic evidence for Z-band as a rigid disc fixing the sarcomere structure of skeletal muscle
    • Wakayama, J., Yoshikawa, Y., Yasuike, T. and Yamada, T. 2000. Atomic force microscopic evidence for Z-band as a rigid disc fixing the sarcomere structure of skeletal muscle. Cell Struct. Funct, 25 (6): 361-365.
    • (2000) Cell Struct. Funct , vol.25 , Issue.6 , pp. 361-365
    • Wakayama, J.1    Yoshikawa, Y.2    Yasuike, T.3    Yamada, T.4
  • 167
    • 0030524816 scopus 로고    scopus 로고
    • The effects of the ultimate pH of meat on tenderness changes during aging
    • Watanabe, A., Daly, C. C. and Devine, C. E. 1996. The effects of the ultimate pH of meat on tenderness changes during aging. Meat Sci, 42 (1): 67-78.
    • (1996) Meat Sci , vol.42 , Issue.1 , pp. 67-78
    • Watanabe, A.1    Daly, C.C.2    Devine, C.E.3
  • 168
    • 0026950706 scopus 로고
    • The effect of postmortem time of injection and freezing on the effectiveness of calcium chloride for improving beef tenderness
    • Wheeler, T. L., Crouse, J. D. and Koohmaraie, M. 1992. The effect of postmortem time of injection and freezing on the effectiveness of calcium chloride for improving beef tenderness. J. Anim. Sci, 70: 3451-3457.
    • (1992) J. Anim. Sci , vol.70 , pp. 3451-3457
    • Wheeler, T.L.1    Crouse, J.D.2    Koohmaraie, M.3
  • 169
    • 0028432852 scopus 로고
    • Prerigor and postrigor changes in tenderness of ovine longissimus muscle
    • Wheeler, T. L. and Koohmaraie, M. 1994. Prerigor and postrigor changes in tenderness of ovine longissimus muscle. J. Anim. Sci, 72 (5): 1232-1238.
    • (1994) J. Anim. Sci , vol.72 , Issue.5 , pp. 1232-1238
    • Wheeler, T.L.1    Koohmaraie, M.2
  • 170
    • 0033195002 scopus 로고    scopus 로고
    • The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major
    • Wheeler, T. L. and Koohmaraie, M. 1999. The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. J. Anim. Sci, 77 (9): 2444-2451.
    • (1999) J. Anim. Sci , vol.77 , Issue.9 , pp. 2444-2451
    • Wheeler, T.L.1    Koohmaraie, M.2
  • 171
    • 0025667597 scopus 로고
    • Mechanisms association with the variation in tenderness of meat from Braman and Herford cattle
    • Wheeler, T. L., Savell, J. W., Cross, H. R., Lunt, D. K. and Smith, S. B. 1990. Mechanisms association with the variation in tenderness of meat from Braman and Herford cattle. J. Anat, 68: 4206-4220.
    • (1990) J. Anat , vol.68 , pp. 4206-4220
    • Wheeler, T.L.1    Savell, J.W.2    Cross, H.R.3    Lunt, D.K.4    Smith, S.B.5
  • 172
    • 0025485110 scopus 로고
    • Evaluation of attributes that affect longissimus muscle tenderness in Bos taurus and Bos indicus cattle
    • Whipple, G., Koohmaraie, M., Dikeman, M. E., Crouse, J. D., Hunt, M. C. and Klemm, R. D. 1990. Evaluation of attributes that affect longissimus muscle tenderness in Bos taurus and Bos indicus cattle. J. Anim. Sci, 68 (9): 2716-2728.
    • (1990) J. Anim. Sci , vol.68 , Issue.9 , pp. 2716-2728
    • Whipple, G.1    Koohmaraie, M.2    Dikeman, M.E.3    Crouse, J.D.4    Hunt, M.C.5    Klemm, R.D.6
  • 173
    • 0017724825 scopus 로고
    • Relationship between sarcomere length and active force in rabbit papillary muscle
    • Wohlfart, B., Grimm, A. F. and Edman, K. A. P. 1977. Relationship between sarcomere length and active force in rabbit papillary muscle. Acta Physiol. Scand, 101 (2): 155-164.
    • (1977) Acta Physiol. Scand , vol.101 , Issue.2 , pp. 155-164
    • Wohlfart, B.1    Grimm, A.F.2    Edman, K.A.P.3
  • 174
    • 0031782264 scopus 로고    scopus 로고
    • Mechanical properties of L929 fibroblasts measured by atomic force microscopy: Effects of anticytoskeletal drugs and membrane crosslinking
    • Wu, H. W., Kuhn, T. and Moy, V. N. 1998. Mechanical properties of L929 fibroblasts measured by atomic force microscopy: Effects of anticytoskeletal drugs and membrane crosslinking. Scanning, 20 (5): 389-397.
    • (1998) Scanning , vol.20 , Issue.5 , pp. 389-397
    • Wu, H.W.1    Kuhn, T.2    Moy, V.N.3
  • 175
    • 67650078502 scopus 로고    scopus 로고
    • Nanomechanics of full-length nebulin: An elastic strain gauge in the skeletal muscle sarcomere
    • Yadavalli, V. K., Forbes, J. G. and Wang, K. 2009. Nanomechanics of full-length nebulin: An elastic strain gauge in the skeletal muscle sarcomere. Langmuir, 25 (13): 7496-7505.
    • (2009) Langmuir , vol.25 , Issue.13 , pp. 7496-7505
    • Yadavalli, V.K.1    Forbes, J.G.2    Wang, K.3
  • 176
    • 84893620416 scopus 로고    scopus 로고
    • Molecular organizations of myofibrils of skeletal muscle studied by atomic force microscopy
    • In: Sugi H., editors New York, New York,: Kluwer Academic/Plenum Publisher
    • Yamada, T., Kunioka, Y., Jun'ichi Wakayama, M. A., Noguchi, Y., Akiyama, N. and Kayamori, T. 2003. " Molecular organizations of myofibrils of skeletal muscle studied by atomic force microscopy ". In Molecular and Cellular Aspects of Muscle Contraction, Edited by: Sugi, H. 285-294. New York: Kluwer Academic/Plenum Publisher.
    • (2003) Molecular and Cellular Aspects of Muscle Contraction , pp. 285-294
    • Yamada, T.1    Kunioka, Y.2    Jun'ichi Wakayama, M.A.3    Noguchi, Y.4    Akiyama, N.5    Kayamori, T.6
  • 177
    • 0033525792 scopus 로고    scopus 로고
    • Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy
    • Yoshikawa, Y., Yasuike, T., Yagi, A. and Yamada, T. 1999. Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy. Biochem. Biophys. Res. Commun, 256 (1): 13-19.
    • (1999) Biochem. Biophys. Res. Commun , vol.256 , Issue.1 , pp. 13-19
    • Yoshikawa, Y.1    Yasuike, T.2    Yagi, A.3    Yamada, T.4
  • 178
    • 3242675222 scopus 로고    scopus 로고
    • Stretch-induced nitric oxide modulates mechanical properties of skeletal muscle cells
    • Zhang, S., Kraus, W. E. and Truskey, G. A. 2004. Stretch-induced nitric oxide modulates mechanical properties of skeletal muscle cells. Am. J. Physiol, 287: C292-C299.
    • (2004) Am. J. Physiol , vol.287
    • Zhang, S.1    Kraus, W.E.2    Truskey, G.A.3


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