메뉴 건너뛰기




Volumn 17, Issue 8, 2006, Pages 394-405

Meat ageing: Reconsideration of the current concept

Author keywords

Apoptosis; Calcium; Caspases; Meat ageing; Muscle; pH; Tenderness

Indexed keywords

ANIMAL CELL CULTURE; CALCIUM; ENZYMES; LIFE CYCLE; LIVING SYSTEMS STUDIES; MUSCLE; PH EFFECTS; RESEARCH AND DEVELOPMENT MANAGEMENT;

EID: 33744553092     PISSN: 09242244     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tifs.2006.01.011     Document Type: Review
Times cited : (169)

References (99)
  • 2
    • 18444366777 scopus 로고    scopus 로고
    • In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation
    • Arrigo A.P. In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation. Journal of Cellular Biochemistry 94 (2005) 241-246
    • (2005) Journal of Cellular Biochemistry , vol.94 , pp. 241-246
    • Arrigo, A.P.1
  • 4
    • 33744511679 scopus 로고    scopus 로고
    • Barnier, V. M. H. (1995). Determinants and predictors of beef tenderness. PhD thesis, University of Utrech, The Nederlands.
  • 5
    • 0023268643 scopus 로고
    • The cystatins: A new class of peptidase inhibitors
    • Barrett A.J. The cystatins: A new class of peptidase inhibitors. Trends in Biochemical Sciences 12 (1987) 193-196
    • (1987) Trends in Biochemical Sciences , vol.12 , pp. 193-196
    • Barrett, A.J.1
  • 6
    • 0141805544 scopus 로고    scopus 로고
    • Beere, H. M. (2001). Stressed to death: Regulation of apoptotic signaling pathways by the heat shock proteins. Science's STKE, 93, RE1.
  • 7
    • 3242879188 scopus 로고    scopus 로고
    • The stress of dying: The role of heat shock proteins in the regulation of apoptosis
    • Beere H.M. The stress of dying: The role of heat shock proteins in the regulation of apoptosis. Journal of Cell Science 117 (2004) 2641-2651
    • (2004) Journal of Cell Science , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 8
    • 26444495615 scopus 로고    scopus 로고
    • Death versus survival: Functional interaction between the apoptotic and stress-inducible heat shock protein pathways
    • Beere H.M. Death versus survival: Functional interaction between the apoptotic and stress-inducible heat shock protein pathways. The Journal of Clinical Investigation 115 (2005) 2633-2639
    • (2005) The Journal of Clinical Investigation , vol.115 , pp. 2633-2639
    • Beere, H.M.1
  • 9
    • 0022406394 scopus 로고
    • Purification and characterization of a low molecular weight cysteine proteinase inhibitor from bovine muscle
    • Bige L., Ouali A., and Valin C. Purification and characterization of a low molecular weight cysteine proteinase inhibitor from bovine muscle. Biochimica et Biophysica Acta 843 (1985) 269-275
    • (1985) Biochimica et Biophysica Acta , vol.843 , pp. 269-275
    • Bige, L.1    Ouali, A.2    Valin, C.3
  • 10
    • 17144403458 scopus 로고    scopus 로고
    • Programmed cell death via mitochondria: Different modes of dying
    • Bras M., Queenan B., and Susin S.A. Programmed cell death via mitochondria: Different modes of dying. Biochemistry (Moscow) 70 (2005) 231-239
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 231-239
    • Bras, M.1    Queenan, B.2    Susin, S.A.3
  • 11
    • 0030697996 scopus 로고    scopus 로고
    • Appearance of phosphatidylserine on apoptotic cells requires calcium-mediated nonspecific flip-flop and is enhanced by loss of the aminophospholipid translocase
    • Bratton D.L., Fadok V.A., Richter D.A., Kailey J.M., Guthrie L.A., and Henson P.M. Appearance of phosphatidylserine on apoptotic cells requires calcium-mediated nonspecific flip-flop and is enhanced by loss of the aminophospholipid translocase. The Journal of Biological Chemistry 272 (1997) 26159-26165
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 26159-26165
    • Bratton, D.L.1    Fadok, V.A.2    Richter, D.A.3    Kailey, J.M.4    Guthrie, L.A.5    Henson, P.M.6
  • 14
    • 0028800903 scopus 로고
    • Historic apoptosis
    • Clarke P.G.H., and Clarke S. Historic apoptosis. Nature 378 (1995) 230
    • (1995) Nature , vol.378 , pp. 230
    • Clarke, P.G.H.1    Clarke, S.2
  • 16
    • 33744531628 scopus 로고    scopus 로고
    • Damez, J. L., Clerjon, S., & Abouelkaram, S. (2005). Mesostructure assessed by alternating current spectroscopy during meat ageing, 51st International Congress of Meat Science and Technology, 2005, Baltimore, August 7-12.
  • 17
    • 33744525973 scopus 로고    scopus 로고
    • Damez, J. L., Lepetit, J., Desneux, L., Clerjon, S., & Favier, R. (2002). Non destructive assessment of meat ageing using electrical impedance anisotropy. 48th ICOMST, Rome, Italie (Vol. 1), (pp. 802-803).
  • 18
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • De Duve C., Pressman B.C., Gianetto R., Wattiaux R., and Appelmans F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochemical Journal 60 (1955) 604-617
    • (1955) Biochemical Journal , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 19
    • 0036931366 scopus 로고    scopus 로고
    • Caspases: Keys in the ignition of cell death
    • Denault J.-B., and Salvesen G.S. Caspases: Keys in the ignition of cell death. Chemical Reviews 102 (2002) 4489-4500
    • (2002) Chemical Reviews , vol.102 , pp. 4489-4500
    • Denault, J.-B.1    Salvesen, G.S.2
  • 20
    • 22344444732 scopus 로고    scopus 로고
    • The role of apoptosis in age-related skeletal muscle atrophy
    • Dirks A.J., and Leeuwenburgh C. The role of apoptosis in age-related skeletal muscle atrophy. Sports Medicine 35 (2005) 473-483
    • (2005) Sports Medicine , vol.35 , pp. 473-483
    • Dirks, A.J.1    Leeuwenburgh, C.2
  • 21
    • 0029859434 scopus 로고    scopus 로고
    • Cell death in C. elegans: Molecular insights into mechanisms conserved between nematodes and mammals
    • Driscoll M. Cell death in C. elegans: Molecular insights into mechanisms conserved between nematodes and mammals. Brain Pathology 6 (1996) 411-425
    • (1996) Brain Pathology , vol.6 , pp. 411-425
    • Driscoll, M.1
  • 22
    • 17044379501 scopus 로고    scopus 로고
    • Proteinaceous cysteine protease inhibitors
    • Dubin G. Proteinaceous cysteine protease inhibitors. Cellular and Molecular Life Sciences 62 (2005) 653-669
    • (2005) Cellular and Molecular Life Sciences , vol.62 , pp. 653-669
    • Dubin, G.1
  • 23
    • 33744514189 scopus 로고    scopus 로고
    • Dutaud, D. (1998). Quantification et caractérisation du proteasome 20S de muscle de bovin en relation avec l'attendrissage de la viande bovine. PhD thesis, Blaise Pascal University, Clermont-Ferrand, France.
  • 24
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw W.C., Martins L.M., and Kaufmann S.H. Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annual Review of Biochemistry 68 (1999) 383-424
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 25
    • 0026281041 scopus 로고
    • Muscle cell death. Ultrastructural differences between muscle cell necrosis and apoptosis
    • Fidzianska A., Kaminska A., and Glinka Z. Muscle cell death. Ultrastructural differences between muscle cell necrosis and apoptosis. Neuropatologia Polska 29 (1991) 19-28
    • (1991) Neuropatologia Polska , vol.29 , pp. 19-28
    • Fidzianska, A.1    Kaminska, A.2    Glinka, Z.3
  • 27
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease
    • Flower T.R., Chesnokova L.S., Froelich C.A., Dixon C., and Witt S.N. Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. Molecular Biology 351 5 (2005) 1081-1100
    • (2005) Molecular Biology , vol.351 , Issue.5 , pp. 1081-1100
    • Flower, T.R.1    Chesnokova, L.S.2    Froelich, C.A.3    Dixon, C.4    Witt, S.N.5
  • 28
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase-activity, specificity, activation, and inhibition
    • Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase-activity, specificity, activation, and inhibition. Biochemical Journal 384 (2004) 201-232
    • (2004) Biochemical Journal , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 29
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y., Sherman Y., and Ben-Sasson S.A. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. Journal of Cell Biology 119 (1992) 493-501
    • (1992) Journal of Cell Biology , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 32
  • 33
    • 20444430478 scopus 로고    scopus 로고
    • Green, D.R. (2005). Apoptotic pathways: ten minutes to dead. Cell, 121, 671-674.
  • 35
    • 21144461970 scopus 로고
    • Post mortem evolution of myofilament spacing and extracellular space in veal muscle
    • Guignot F., Vignon X., and Monin G. Post mortem evolution of myofilament spacing and extracellular space in veal muscle. Meat Science 33 (1993) 333-347
    • (1993) Meat Science , vol.33 , pp. 333-347
    • Guignot, F.1    Vignon, X.2    Monin, G.3
  • 37
    • 0001070415 scopus 로고
    • A neutral, calcium-activated proteinase from the soluble fraction of rat brain
    • Guroff G. A neutral, calcium-activated proteinase from the soluble fraction of rat brain. The Journal of Biological Chemistry 239 (1964) 149-155
    • (1964) The Journal of Biological Chemistry , vol.239 , pp. 149-155
    • Guroff, G.1
  • 38
    • 1542318100 scopus 로고    scopus 로고
    • Mitochondrial function in apoptotic neuronal cell death
    • Haeberlein S.L. Mitochondrial function in apoptotic neuronal cell death. Neurochemical Research 29 (2004) 521-530
    • (2004) Neurochemical Research , vol.29 , pp. 521-530
    • Haeberlein, S.L.1
  • 39
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • (review)
    • Hengartner M.O. The biochemistry of apoptosis. Nature 407 6805 (2000) 770-776 (review)
    • (2000) Nature , vol.407 , Issue.6805 , pp. 770-776
    • Hengartner, M.O.1
  • 40
    • 0023195510 scopus 로고
    • Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: Mechanism of interaction and the role of divalent cations
    • Ishiguro H., Higashiyama S., Namikawa C., Kunimatsu M., Takano E., Tanaka K., et al. Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: Mechanism of interaction and the role of divalent cations. Biochemistry 26 (1987) 2863-2870
    • (1987) Biochemistry , vol.26 , pp. 2863-2870
    • Ishiguro, H.1    Higashiyama, S.2    Namikawa, C.3    Kunimatsu, M.4    Takano, E.5    Tanaka, K.6
  • 41
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., and Currie A.R. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. British Journal of Cancer 26 (1972) 239-257
    • (1972) British Journal of Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 42
    • 84985145925 scopus 로고
    • Effect of calcium on isometric tension, glycolysis and tenderness of poultry breast meat
    • Khan A.W., and Kim Y.K. Effect of calcium on isometric tension, glycolysis and tenderness of poultry breast meat. Journal of Food Science 40 6 (1975) 1119-1121
    • (1975) Journal of Food Science , vol.40 , Issue.6 , pp. 1119-1121
    • Khan, A.W.1    Kim, Y.K.2
  • 43
    • 0031685364 scopus 로고    scopus 로고
    • Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer
    • Kos J., and Lah T.T. Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer. Oncology Reports 5 (1998) 1349-1361
    • (1998) Oncology Reports , vol.5 , pp. 1349-1361
    • Kos, J.1    Lah, T.T.2
  • 45
    • 0141454834 scopus 로고    scopus 로고
    • Evolution of the cellular stress proteome: From monophyletic origin to ubiquitous function
    • Kultz D. Evolution of the cellular stress proteome: From monophyletic origin to ubiquitous function. The Journal of Experimental Biology 206 (2003) 3119-3124
    • (2003) The Journal of Experimental Biology , vol.206 , pp. 3119-3124
    • Kultz, D.1
  • 46
    • 0036313464 scopus 로고    scopus 로고
    • Changes in proteasome activity during postmortem aging of bovine muscle
    • Lamare M., Taylor R.G., Farouta L., Briand Y., and Briand M. Changes in proteasome activity during postmortem aging of bovine muscle. Meat Science 61 (2002) 199-204
    • (2002) Meat Science , vol.61 , pp. 199-204
    • Lamare, M.1    Taylor, R.G.2    Farouta, L.3    Briand, Y.4    Briand, M.5
  • 48
    • 0035433172 scopus 로고    scopus 로고
    • Apoptosis of skeletal muscle cells and the pathogenesis of myositis: A perspective
    • Liu C.C., and Ahearn J.M. Apoptosis of skeletal muscle cells and the pathogenesis of myositis: A perspective. Current Rheumatology Reports 3 (2001) 325-333
    • (2001) Current Rheumatology Reports , vol.3 , pp. 325-333
    • Liu, C.C.1    Ahearn, J.M.2
  • 49
    • 0028891783 scopus 로고
    • Apoptosis, oncosis and necrosis. An overview of cell death
    • Majino G., and Jons I. Apoptosis, oncosis and necrosis. An overview of cell death. The American Journal of Pathology 146 (1995) 3-15
    • (1995) The American Journal of Pathology , vol.146 , pp. 3-15
    • Majino, G.1    Jons, I.2
  • 50
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin S.J., Reutelingsperger C.P., McGahon A.J., Rader J.A., van Schie R.C., LaFace D.M., et al. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl. The Journal of Experimental Medicine 182 (1995) 1545-1556
    • (1995) The Journal of Experimental Medicine , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3    Rader, J.A.4    van Schie, R.C.5    LaFace, D.M.6
  • 51
    • 0031286043 scopus 로고    scopus 로고
    • Proteasome from rabbit skeletal muscle: Some properties and effects on muscle proteins
    • Matsuishi M., and Okitani A. Proteasome from rabbit skeletal muscle: Some properties and effects on muscle proteins. Meat Science 45 (1997) 451-462
    • (1997) Meat Science , vol.45 , pp. 451-462
    • Matsuishi, M.1    Okitani, A.2
  • 53
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • Meier P., Finch A., and Evan G. Apoptosis in development. Nature 407 (2000) 796-801
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 54
    • 11444270251 scopus 로고    scopus 로고
    • Mishra, N. C., & Kumar, S. (2005). Apoptosis: A mitochondrial perspective on cell death. Indian Journal of Experimental Biology, 43, 25-34.
  • 56
    • 0022350512 scopus 로고
    • Genealogy of mammalian cysteine proteinase inhibitors. Common evolutionary origin of stefins, cystatins and kininogens
    • Muller-Esterl W., Fritz H., Kellermann J., Lottspeich F., Machleidt W., and Turk V. Genealogy of mammalian cysteine proteinase inhibitors. Common evolutionary origin of stefins, cystatins and kininogens. FEBS Letters 191 (1985) 221-226
    • (1985) FEBS Letters , vol.191 , pp. 221-226
    • Muller-Esterl, W.1    Fritz, H.2    Kellermann, J.3    Lottspeich, F.4    Machleidt, W.5    Turk, V.6
  • 57
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death and Differentiation 6 (1999) 1028-1042
    • (1999) Cell Death and Differentiation , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 58
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson D.W. From bench to clinic with apoptosis-based therapeutic agents. Nature 407 (2000) 810-816
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 59
    • 0002878025 scopus 로고
    • The structural basis of water-holding in meat. I. General principles and water uptake in meat processing
    • Offer G., and Knight P. The structural basis of water-holding in meat. I. General principles and water uptake in meat processing. Developments in Meat Science 4 (1988) 63-171
    • (1988) Developments in Meat Science , vol.4 , pp. 63-171
    • Offer, G.1    Knight, P.2
  • 60
    • 0002878025 scopus 로고
    • The structural basis of water-holding in meat. II. Drip losses
    • Offer G., and Knight P. The structural basis of water-holding in meat. II. Drip losses. Developments in Meat Science 4 (1988) 173-243
    • (1988) Developments in Meat Science , vol.4 , pp. 173-243
    • Offer, G.1    Knight, P.2
  • 62
    • 0032219241 scopus 로고    scopus 로고
    • Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure
    • Otsuka Y., Homma N., Shiga K., Ushiki J., Ikeuchib Y., and Suzukib A. Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure. Meat Science 49 (1998) 365-378
    • (1998) Meat Science , vol.49 , pp. 365-378
    • Otsuka, Y.1    Homma, N.2    Shiga, K.3    Ushiki, J.4    Ikeuchib, Y.5    Suzukib, A.6
  • 63
    • 0026539218 scopus 로고
    • Proteolytic and physicochemical mechanisms involved in meat texture development
    • Ouali A. Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie 74 (1992) 251-265
    • (1992) Biochimie , vol.74 , pp. 251-265
    • Ouali, A.1
  • 64
    • 33744511399 scopus 로고    scopus 로고
    • Ouali, A. (1999). Structure and biochemistry of muscle as related to meat texture, Proceedings of the 14th European symposium on the quality of poultry meat, Bologna, Vol. 1, 1999, (pp. 91-121).
  • 66
    • 0001603082 scopus 로고
    • Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles
    • Ouali A., and Talmant A. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Science 28 (1990) 331-348
    • (1990) Meat Science , vol.28 , pp. 331-348
    • Ouali, A.1    Talmant, A.2
  • 67
    • 0036479004 scopus 로고    scopus 로고
    • Mitochondria: Regulating the inevitable
    • Parone P.A., James D., and Martinou J.C. Mitochondria: Regulating the inevitable. Biochimie 84 (2002) 105-111
    • (2002) Biochimie , vol.84 , pp. 105-111
    • Parone, P.A.1    James, D.2    Martinou, J.C.3
  • 72
    • 18944385186 scopus 로고    scopus 로고
    • Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril
    • Raynaud F., Fernandez E., Coulis G., Aubry L., Vignon X., Bleimling N., et al. Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril. The FEBS Journal 272 (2005) 2578-2590
    • (2005) The FEBS Journal , vol.272 , pp. 2578-2590
    • Raynaud, F.1    Fernandez, E.2    Coulis, G.3    Aubry, L.4    Vignon, X.5    Bleimling, N.6
  • 77
    • 0017709822 scopus 로고    scopus 로고
    • Schwartz, W., & Bird, J. W. C. (1977). Degradation of myofibrillar proteins by cathepsins B and D. The Biochemical Journal, 167, 811-820.
  • 78
    • 0036986447 scopus 로고    scopus 로고
    • Role of muscle endopeptidases and their inhibitors in meat tenderness
    • Sentandreu M.A., Coulis G., and Ouali A. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology 13 12 (2002) 400-421
    • (2002) Trends in Food Science and Technology , vol.13 , Issue.12 , pp. 400-421
    • Sentandreu, M.A.1    Coulis, G.2    Ouali, A.3
  • 80
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Molecular Cell 9 (2002) 459-470
    • (2002) Molecular Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 81
    • 0034059284 scopus 로고    scopus 로고
    • Prognostic significance of cysteine proteinases cathepsins B and L and their endogenous inhibitors stefins A and B in patients with squamous cell carcinoma of the head and neck
    • Strojan P., Budihna M., Smid L., Svetic B., Vrhovec I., Kos J., et al. Prognostic significance of cysteine proteinases cathepsins B and L and their endogenous inhibitors stefins A and B in patients with squamous cell carcinoma of the head and neck. Clinical Cancer Research 6 (2000) 1052-1062
    • (2000) Clinical Cancer Research , vol.6 , pp. 1052-1062
    • Strojan, P.1    Budihna, M.2    Smid, L.3    Svetic, B.4    Vrhovec, I.5    Kos, J.6
  • 82
    • 2542448093 scopus 로고    scopus 로고
    • Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: More than just neighbourhood
    • Szabadkai G., and Rizzuto R. Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: More than just neighbourhood. FEBS Letters 567 (2004) 111-115
    • (2004) FEBS Letters , vol.567 , pp. 111-115
    • Szabadkai, G.1    Rizzuto, R.2
  • 84
    • 0036788751 scopus 로고    scopus 로고
    • Apoptosis and muscle fibre loss in neuromuscular disorders
    • Tews D.S. Apoptosis and muscle fibre loss in neuromuscular disorders. Neuromuscular Disorders 12 (2002) 613-622
    • (2002) Neuromuscular Disorders , vol.12 , pp. 613-622
    • Tews, D.S.1
  • 85
    • 25844513077 scopus 로고    scopus 로고
    • Muscle-fiber apoptosis in neuromuscular diseases
    • Tews D.S. Muscle-fiber apoptosis in neuromuscular diseases. Muscle and Nerve 32 (2005) 443-458
    • (2005) Muscle and Nerve , vol.32 , pp. 443-458
    • Tews, D.S.1
  • 86
    • 0942300420 scopus 로고    scopus 로고
    • The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation
    • Thomas A.R., Gondoza H., Hoffman L.C., Oosthuizen V., Ryno J., and Naude A. The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation. Meat Science 67 (2004) 113-120
    • (2004) Meat Science , vol.67 , pp. 113-120
    • Thomas, A.R.1    Gondoza, H.2    Hoffman, L.C.3    Oosthuizen, V.4    Ryno, J.5    Naude, A.6
  • 87
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1∼ processing in monocytes
    • Thornberry N.A., Bull H.G., Calaycay J.R., Chapman K.T., Howard A.D., Kostura M.J., et al. A novel heterodimeric cysteine protease is required for interleukin-1∼ processing in monocytes. Nature 356 (1992) 768-774
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5    Kostura, M.J.6
  • 88
    • 0022881701 scopus 로고
    • Human cysteine proteinases and their protein inhibitors stefins, cystatins an kininogens
    • Turk V., Brzin J., Kotnik M., Lenarcic B., Popovic T., Ritonja A., et al. Human cysteine proteinases and their protein inhibitors stefins, cystatins an kininogens. Biomedica Biochimica Acta 45 (1986) 1375-1384
    • (1986) Biomedica Biochimica Acta , vol.45 , pp. 1375-1384
    • Turk, V.1    Brzin, J.2    Kotnik, M.3    Lenarcic, B.4    Popovic, T.5    Ritonja, A.6
  • 89
    • 33744509171 scopus 로고    scopus 로고
    • Hocquette J.F., and Gigli S. (Eds), Wageningen Academic Publishers, Wageningen, The Netherlands (EAAP publication no. 112)
    • Veiseth E., and Koohmaraie M. In: Hocquette J.F., and Gigli S. (Eds). Beef tenderness: Significance of the calpain proteolytic system (2005), Wageningen Academic Publishers, Wageningen, The Netherlands 111-126 (EAAP publication no. 112)
    • (2005) Beef tenderness: Significance of the calpain proteolytic system , pp. 111-126
    • Veiseth, E.1    Koohmaraie, M.2
  • 90
    • 0024435232 scopus 로고
    • Ultrastructural localization of calcium in post-mortem bovine muscle: A cytochemical and X-ray microanalytical study
    • Vignon X., Beaulaton J., and Ouali A. Ultrastructural localization of calcium in post-mortem bovine muscle: A cytochemical and X-ray microanalytical study. The Histochemical Journal 21 7 (1989) 403-411
    • (1989) The Histochemical Journal , vol.21 , Issue.7 , pp. 403-411
    • Vignon, X.1    Beaulaton, J.2    Ouali, A.3
  • 91
    • 0019195859 scopus 로고
    • Cation-sensitive neutral endopeptidase: Isolation and specificity of the bovine pituitary enzyme
    • Wilk S., and Orlowski M. Cation-sensitive neutral endopeptidase: Isolation and specificity of the bovine pituitary enzyme. Journal of Neurochemistry 35 5 (1980) 1172-1182
    • (1980) Journal of Neurochemistry , vol.35 , Issue.5 , pp. 1172-1182
    • Wilk, S.1    Orlowski, M.2
  • 92
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie A.H. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284 (1980) 555-556
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 94
    • 0030068922 scopus 로고    scopus 로고
    • Evolutionary conservation of a genetic pathway of programmed cell death
    • Yuan J. Evolutionary conservation of a genetic pathway of programmed cell death. Journal of Cellular Biochemistry 60 (1996) 4-11
    • (1996) Journal of Cellular Biochemistry , vol.60 , pp. 4-11
    • Yuan, J.1
  • 95
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., and Horvitz H.M. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1-converting enzyme. Cell 75 (1993) 641-652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.M.5
  • 97
    • 33744545285 scopus 로고    scopus 로고
    • Zeece, M. G., Woods, T. L., Keen, M.A., & Reville, W.J. (1992). Role of proteinases and inhibitors in postmortem muscle protein degradation, Proceedings of the reciprocal meat conference, Colorado State University, Vol. 45, 1992, (pp. 51-61).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.