메뉴 건너뛰기




Volumn 75, Issue 14, 2012, Pages 4275-4289

"Muscle to meat" molecular events and technological transformations: The proteomics insight

Author keywords

Farm animals; Meat; Muscle proteins; Proteomics

Indexed keywords

ACTIN; ALDEHYDE REDUCTASE; ALPHA CRYSTALLIN; BETA ENOLASE; CALPAIN; CALPASTATIN; CONNECTIN; CREATINE KINASE; DESMIN; ENOLASE; FILAMIN; HEAT SHOCK PROTEIN 27; MUSCLE PROTEIN; MYOSIN; NEBULIN; TROPONIN T; UNCLASSIFIED DRUG;

EID: 84863818735     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.04.011     Document Type: Review
Times cited : (122)

References (86)
  • 1
    • 13344269000 scopus 로고    scopus 로고
    • From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis
    • Wilkins M.R., Pasquali C., Appel R.D., Ou K., Golaz O., Sanchez J.C., et al. From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis. Biotechnology (N Y) 1996, 14:61-65.
    • (1996) Biotechnology (N Y) , vol.14 , pp. 61-65
    • Wilkins, M.R.1    Pasquali, C.2    Appel, R.D.3    Ou, K.4    Golaz, O.5    Sanchez, J.C.6
  • 2
    • 34250634816 scopus 로고    scopus 로고
    • Application of proteomics to understand the molecular mechanisms behind meat quality
    • Hollung K., Veiseth E., Jia X., Faergestad E.M., Hildrum K.I. Application of proteomics to understand the molecular mechanisms behind meat quality. Meat Sci 2007, 77:97-104.
    • (2007) Meat Sci , vol.77 , pp. 97-104
    • Hollung, K.1    Veiseth, E.2    Jia, X.3    Faergestad, E.M.4    Hildrum, K.I.5
  • 5
    • 77954387385 scopus 로고    scopus 로고
    • Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization
    • Huff Lonergan E., Zhang W., Lonergan S.M. Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization. Meat Sci 2010, 86:184-195.
    • (2010) Meat Sci , vol.86 , pp. 184-195
    • Huff Lonergan, E.1    Zhang, W.2    Lonergan, S.M.3
  • 6
    • 35948989676 scopus 로고    scopus 로고
    • New frontiers in understanding drip loss in pork: recent insights on the role of postmortem muscle biochemistry
    • Huff-Lonergan E., Lonergan S.M. New frontiers in understanding drip loss in pork: recent insights on the role of postmortem muscle biochemistry. J Anim Breed Genet 2007, 124:19-26.
    • (2007) J Anim Breed Genet , vol.124 , pp. 19-26
    • Huff-Lonergan, E.1    Lonergan, S.M.2
  • 7
    • 34250654900 scopus 로고    scopus 로고
    • Mechanisms controlling pork quality development: the biochemistry controlling postmortem energy metabolism
    • Scheffler T.L., Gerrard D.E. Mechanisms controlling pork quality development: the biochemistry controlling postmortem energy metabolism. Meat Sci 2007, 77:7-16.
    • (2007) Meat Sci , vol.77 , pp. 7-16
    • Scheffler, T.L.1    Gerrard, D.E.2
  • 8
    • 70449633060 scopus 로고    scopus 로고
    • Production systems and influence on eating quality of pork
    • Bonneau M., Lebret B. Production systems and influence on eating quality of pork. Meat Sci 2009, 84:293-300.
    • (2009) Meat Sci , vol.84 , pp. 293-300
    • Bonneau, M.1    Lebret, B.2
  • 9
    • 45849131266 scopus 로고    scopus 로고
    • Animal welfare at markets and during transport and slaughter
    • Gregory N.G. Animal welfare at markets and during transport and slaughter. Meat Sci 2008, 80:2-11.
    • (2008) Meat Sci , vol.80 , pp. 2-11
    • Gregory, N.G.1
  • 10
    • 77956904525 scopus 로고    scopus 로고
    • Effect of unloading, lairage, pig handling, stunning and season on pH of pork
    • Van de Perre V., Permentier L., De Bie S., Verbeke G., Geers R. Effect of unloading, lairage, pig handling, stunning and season on pH of pork. Meat Sci 2010, 86:931-937.
    • (2010) Meat Sci , vol.86 , pp. 931-937
    • Van de Perre, V.1    Permentier, L.2    De Bie, S.3    Verbeke, G.4    Geers, R.5
  • 12
    • 2942529230 scopus 로고    scopus 로고
    • Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Bouley J., Chambon C., Picard B. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2004, 4:1811-1824.
    • (2004) Proteomics , vol.4 , pp. 1811-1824
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 14
    • 33745854852 scopus 로고    scopus 로고
    • Changes in enzymes associated with energy metabolism during the early post mortem period in longissimus thoracis bovine muscle analyzed by proteomics
    • Jia X., Hildrum K.I., Westad F., Kummen E., Aass L., Hollung K. Changes in enzymes associated with energy metabolism during the early post mortem period in longissimus thoracis bovine muscle analyzed by proteomics. J Proteome Res 2006, 5:1763-1769.
    • (2006) J Proteome Res , vol.5 , pp. 1763-1769
    • Jia, X.1    Hildrum, K.I.2    Westad, F.3    Kummen, E.4    Aass, L.5    Hollung, K.6
  • 15
    • 34547142184 scopus 로고    scopus 로고
    • Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period
    • Jia X., Ekman M., Grove H., Faergestad E.M., Aass L., Hildrum K.I., et al. Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period. J Proteome Res 2007, 6:2720-2731.
    • (2007) J Proteome Res , vol.6 , pp. 2720-2731
    • Jia, X.1    Ekman, M.2    Grove, H.3    Faergestad, E.M.4    Aass, L.5    Hildrum, K.I.6
  • 16
    • 32944454622 scopus 로고    scopus 로고
    • Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis
    • Jia X., Hollung K., Therkildsen M., Hildrum K.I., Bendixen E. Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis. Proteomics 2006, 6:936-944.
    • (2006) Proteomics , vol.6 , pp. 936-944
    • Jia, X.1    Hollung, K.2    Therkildsen, M.3    Hildrum, K.I.4    Bendixen, E.5
  • 17
    • 22144489165 scopus 로고    scopus 로고
    • The use of proteomics in meat science
    • Bendixen E. The use of proteomics in meat science. Meat Sci 2005, 71:138-149.
    • (2005) Meat Sci , vol.71 , pp. 138-149
    • Bendixen, E.1
  • 18
    • 33845716734 scopus 로고    scopus 로고
    • Postmortem changes in bovine troponin T isoforms on two-dimensional electrophoretic gel analyzed using mass spectrometry and western blotting: the limited fragmentation into basic polypeptides
    • Muroya S., Ohnishi-Kameyama M., Oe M., Nakajima I., Chikuni K. Postmortem changes in bovine troponin T isoforms on two-dimensional electrophoretic gel analyzed using mass spectrometry and western blotting: the limited fragmentation into basic polypeptides. Meat Sci 2007, 75:506-514.
    • (2007) Meat Sci , vol.75 , pp. 506-514
    • Muroya, S.1    Ohnishi-Kameyama, M.2    Oe, M.3    Nakajima, I.4    Chikuni, K.5
  • 19
    • 36749014526 scopus 로고    scopus 로고
    • Muscle proteome and meat eating qualities of longissimus thoracis of "Blonde d'Aquitaine" young bulls: a central role of HSP27 isoforms
    • Morzel M., Terlouw C., Chambon C., Micol D., Picard B. Muscle proteome and meat eating qualities of longissimus thoracis of "Blonde d'Aquitaine" young bulls: a central role of HSP27 isoforms. Meat Sci 2008, 78:297-304.
    • (2008) Meat Sci , vol.78 , pp. 297-304
    • Morzel, M.1    Terlouw, C.2    Chambon, C.3    Micol, D.4    Picard, B.5
  • 20
    • 52049123066 scopus 로고    scopus 로고
    • Proteins in longissimus muscle of Korean native cattle and their relationship to meat quality
    • Kim N.K., Cho S., Lee S.H., Park H.R., Lee C.S., Cho Y.M., et al. Proteins in longissimus muscle of Korean native cattle and their relationship to meat quality. Meat Sci 2008, 80:1068-1073.
    • (2008) Meat Sci , vol.80 , pp. 1068-1073
    • Kim, N.K.1    Cho, S.2    Lee, S.H.3    Park, H.R.4    Lee, C.S.5    Cho, Y.M.6
  • 21
    • 67650541787 scopus 로고    scopus 로고
    • Peroxiredoxin-6-a potential protein marker for meat tenderness in bovine longissimus thoracis muscle
    • Jia X., Veiseth-Kent E., Grove H., Kuziora P., Aass L., Hildrum K.I., et al. Peroxiredoxin-6-a potential protein marker for meat tenderness in bovine longissimus thoracis muscle. J Anim Sci 2009, 87:2391-2399.
    • (2009) J Anim Sci , vol.87 , pp. 2391-2399
    • Jia, X.1    Veiseth-Kent, E.2    Grove, H.3    Kuziora, P.4    Aass, L.5    Hildrum, K.I.6
  • 22
    • 67149116805 scopus 로고    scopus 로고
    • Functional proteomic analysis predicts beef tenderness and the tenderness differential
    • Zapata I., Zerby H.N., Wick M. Functional proteomic analysis predicts beef tenderness and the tenderness differential. J Agric Food Chem 2009, 57:4956-4963.
    • (2009) J Agric Food Chem , vol.57 , pp. 4956-4963
    • Zapata, I.1    Zerby, H.N.2    Wick, M.3
  • 23
    • 72449156073 scopus 로고    scopus 로고
    • Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization
    • Laville E., Sayd T., Morzel M., Blinet S., Chambon C., Lepetit J., et al. Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization. J Agric Food Chem 2009, 57:10755-10764.
    • (2009) J Agric Food Chem , vol.57 , pp. 10755-10764
    • Laville, E.1    Sayd, T.2    Morzel, M.3    Blinet, S.4    Chambon, C.5    Lepetit, J.6
  • 24
    • 77953637963 scopus 로고    scopus 로고
    • Proteome changes in bovine longissimus thoracis muscle during the first 48h postmortem: shifts in energy status and myofibrillar stability
    • Bjarnadottir S.G., Hollung K., Faergestad E.M., Veiseth-Kent E. Proteome changes in bovine longissimus thoracis muscle during the first 48h postmortem: shifts in energy status and myofibrillar stability. J Agric Food Chem 2010, 58:7408-7414.
    • (2010) J Agric Food Chem , vol.58 , pp. 7408-7414
    • Bjarnadottir, S.G.1    Hollung, K.2    Faergestad, E.M.3    Veiseth-Kent, E.4
  • 25
    • 84863844092 scopus 로고    scopus 로고
    • Changes in protein abundance between tender and tough meat from bovine longissimus thoracis muscle assessed by iTRAQ and 2-DE analysis
    • Bjarnadottir S.G., Hollung K., Hoy M., Bendixen E., Codrea M.C., Veiseth-Kent E. Changes in protein abundance between tender and tough meat from bovine longissimus thoracis muscle assessed by iTRAQ and 2-DE analysis. J Anim Sci 2012, 90:1-9.
    • (2012) J Anim Sci , vol.90 , pp. 1-9
    • Bjarnadottir, S.G.1    Hollung, K.2    Hoy, M.3    Bendixen, E.4    Codrea, M.C.5    Veiseth-Kent, E.6
  • 26
    • 80555126736 scopus 로고    scopus 로고
    • Myosin light chain 1 release from myofibrillar fraction during postmortem aging is a potential indicator of proteolysis and tenderness of beef
    • Anderson M.J., Lonergan S.M., Huff-Lonergan E. Myosin light chain 1 release from myofibrillar fraction during postmortem aging is a potential indicator of proteolysis and tenderness of beef. Meat Sci 2012, 90:345-351.
    • (2012) Meat Sci , vol.90 , pp. 345-351
    • Anderson, M.J.1    Lonergan, S.M.2    Huff-Lonergan, E.3
  • 28
    • 79958714052 scopus 로고    scopus 로고
    • Proteome changes in the insoluble protein fraction of bovine longissimus dorsi muscle as a result of low-voltage electrical stimulation
    • Bjarnadottir S.G., Hollung K., Hoy M., Veiseth-Kent E. Proteome changes in the insoluble protein fraction of bovine longissimus dorsi muscle as a result of low-voltage electrical stimulation. Meat Sci 2011, 89:143-149.
    • (2011) Meat Sci , vol.89 , pp. 143-149
    • Bjarnadottir, S.G.1    Hollung, K.2    Hoy, M.3    Veiseth-Kent, E.4
  • 29
    • 84882582967 scopus 로고    scopus 로고
    • Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef
    • in press
    • Li C.B., Li J., Zhou G.H., Lametsch R., Ertbjerg P., Bruggemann D.A., et al. Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef. J Anim Sci 2012, in press.
    • (2012) J Anim Sci
    • Li, C.B.1    Li, J.2    Zhou, G.H.3    Lametsch, R.4    Ertbjerg, P.5    Bruggemann, D.A.6
  • 30
    • 69449090370 scopus 로고    scopus 로고
    • Proteome analysis of the m. longissimus dorsi between fattening stages in Hanwoo steer
    • Kim N.K., Lee S.H., Cho Y.M., Son E.S., Kim K.Y., Lee C.S., et al. Proteome analysis of the m. longissimus dorsi between fattening stages in Hanwoo steer. BMB Rep 2009, 42:433-438.
    • (2009) BMB Rep , vol.42 , pp. 433-438
    • Kim, N.K.1    Lee, S.H.2    Cho, Y.M.3    Son, E.S.4    Kim, K.Y.5    Lee, C.S.6
  • 31
    • 77952944632 scopus 로고    scopus 로고
    • Proteome differences associated with fat accumulation in bovine subcutaneous adipose tissues
    • Zhao Y.M., Basu U., Dodson M.V., Basarb J.A., Guan le L. Proteome differences associated with fat accumulation in bovine subcutaneous adipose tissues. Proteome Sci 2010, 8:14.
    • (2010) Proteome Sci , vol.8 , pp. 14
    • Zhao, Y.M.1    Basu, U.2    Dodson, M.V.3    Basarb, J.A.4    Guan le, L.5
  • 32
    • 84755161198 scopus 로고    scopus 로고
    • Differentially expressed proteins during fat accumulation in bovine skeletal muscle
    • Zhang Q., Lee H.G., Han J.A., Kim E.B., Kang S.K., Yin J., et al. Differentially expressed proteins during fat accumulation in bovine skeletal muscle. Meat Sci 2010, 86:814-820.
    • (2010) Meat Sci , vol.86 , pp. 814-820
    • Zhang, Q.1    Lee, H.G.2    Han, J.A.3    Kim, E.B.4    Kang, S.K.5    Yin, J.6
  • 33
    • 84863814973 scopus 로고    scopus 로고
    • Proteomics of meat color. In: Association AMS, editor. 64th Annual Reciprocal Meat Conference.
    • Suman SP, Joseph P. Proteomics of meat color. In: Association AMS, editor. 64th Annual Reciprocal Meat Conference 2011.
    • (2011)
    • Suman, S.P.1    Joseph, P.2
  • 34
    • 0037174398 scopus 로고    scopus 로고
    • Identification of protein degradation during post-mortem storage of pig meat
    • Lametsch R., Roepstorff P., Bendixen E. Identification of protein degradation during post-mortem storage of pig meat. J Agric Food Chem 2002, 50:5508-5512.
    • (2002) J Agric Food Chem , vol.50 , pp. 5508-5512
    • Lametsch, R.1    Roepstorff, P.2    Bendixen, E.3
  • 35
    • 1842584567 scopus 로고    scopus 로고
    • Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures
    • Morzel M., Chambon C., Hamelin M., Santé-Lhoutellier V., Sayd T., Monin G. Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures. Meat Sci 2004, 67:689-696.
    • (2004) Meat Sci , vol.67 , pp. 689-696
    • Morzel, M.1    Chambon, C.2    Hamelin, M.3    Santé-Lhoutellier, V.4    Sayd, T.5    Monin, G.6
  • 36
    • 5744228466 scopus 로고    scopus 로고
    • Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus
    • Hwang I.H., Park B.Y., Kim J.H., Cho S.H., Lee J.M. Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus. Meat Sci 2005, 69:79-91.
    • (2005) Meat Sci , vol.69 , pp. 79-91
    • Hwang, I.H.1    Park, B.Y.2    Kim, J.H.3    Cho, S.H.4    Lee, J.M.5
  • 38
    • 34447619884 scopus 로고    scopus 로고
    • Comparison of sarcoplasmic proteomes between two groups of pig muscles selected for shear force of cooked meat
    • Laville E., Sayd T., Terlouw C., Chambon C., Damon M., Larzul C., et al. Comparison of sarcoplasmic proteomes between two groups of pig muscles selected for shear force of cooked meat. J Agric Food Chem 2007, 55:5834-5841.
    • (2007) J Agric Food Chem , vol.55 , pp. 5834-5841
    • Laville, E.1    Sayd, T.2    Terlouw, C.3    Chambon, C.4    Damon, M.5    Larzul, C.6
  • 39
    • 80051549000 scopus 로고    scopus 로고
    • Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis
    • Bernevic B., Petre B.A., Galetskiy D., Werner C., Wicke M., Schellander K., et al. Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis. Int J Mass Spectrom 2011, 305:217-227.
    • (2011) Int J Mass Spectrom , vol.305 , pp. 217-227
    • Bernevic, B.1    Petre, B.A.2    Galetskiy, D.3    Werner, C.4    Wicke, M.5    Schellander, K.6
  • 40
    • 79952539233 scopus 로고    scopus 로고
    • Early post-mortem sarcoplasmic proteome of porcine muscle related to protein oxidation
    • Promeyrat A., Sayd T., Laville E., Chambon C., Lebret B., Gatellier P. Early post-mortem sarcoplasmic proteome of porcine muscle related to protein oxidation. Food Chem 2011, 127:1097-1104.
    • (2011) Food Chem , vol.127 , pp. 1097-1104
    • Promeyrat, A.1    Sayd, T.2    Laville, E.3    Chambon, C.4    Lebret, B.5    Gatellier, P.6
  • 41
    • 80053996537 scopus 로고    scopus 로고
    • Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences
    • Huang H., Larsen M.R., Karlsson A.H., Pomponio L., Costa L.N., Lametsch R. Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics 2011, 11:4063-4076.
    • (2011) Proteomics , vol.11 , pp. 4063-4076
    • Huang, H.1    Larsen, M.R.2    Karlsson, A.H.3    Pomponio, L.4    Costa, L.N.5    Lametsch, R.6
  • 43
    • 82355192275 scopus 로고    scopus 로고
    • Meat quality of the longissimus lumborum muscle of Casertana and Large White pigs: metabolomics and proteomics intertwined
    • D'Alessandro A., Marrocco C., Zolla V., D'Andrea M., Zolla L. Meat quality of the longissimus lumborum muscle of Casertana and Large White pigs: metabolomics and proteomics intertwined. J Proteomics 2011, 75:610-627.
    • (2011) J Proteomics , vol.75 , pp. 610-627
    • D'Alessandro, A.1    Marrocco, C.2    Zolla, V.3    D'Andrea, M.4    Zolla, L.5
  • 44
    • 78649837277 scopus 로고    scopus 로고
    • Proteomics and transcriptomics investigation on longissimus muscles in Large White and Casertana pig breeds
    • Murgiano L., D'Alessandro A., Egidi M.G., Crisa A., Prosperini G., Timperio A.M., et al. Proteomics and transcriptomics investigation on longissimus muscles in Large White and Casertana pig breeds. J Proteome Res 2010, 9:6450-6466.
    • (2010) J Proteome Res , vol.9 , pp. 6450-6466
    • Murgiano, L.1    D'Alessandro, A.2    Egidi, M.G.3    Crisa, A.4    Prosperini, G.5    Timperio, A.M.6
  • 45
    • 34250670413 scopus 로고    scopus 로고
    • Identification of pork quality parameters by proteomics
    • van de Wiel D.F.M., Zhang W.L. Identification of pork quality parameters by proteomics. Meat Sci 2007, 77:46-54.
    • (2007) Meat Sci , vol.77 , pp. 46-54
    • van de Wiel, D.F.M.1    Zhang, W.L.2
  • 46
    • 0035606922 scopus 로고    scopus 로고
    • The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins
    • Kristensen L., Purslow P.P. The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. Meat Sci 2001, 58:17-23.
    • (2001) Meat Sci , vol.58 , pp. 17-23
    • Kristensen, L.1    Purslow, P.P.2
  • 47
    • 79951774411 scopus 로고    scopus 로고
    • Centrifugal drip is an accessible source for protein indicators of pork ageing and water-holding capacity
    • Di Luca A., Mullen A.M., Elia G., Davey G., Hamill R.M. Centrifugal drip is an accessible source for protein indicators of pork ageing and water-holding capacity. Meat Sci 2011, 88:261-270.
    • (2011) Meat Sci , vol.88 , pp. 261-270
    • Di Luca, A.1    Mullen, A.M.2    Elia, G.3    Davey, G.4    Hamill, R.M.5
  • 48
    • 0036024907 scopus 로고    scopus 로고
    • Effects of halothane genotype and pre-slaughter treatment on pig meat quality. Part 2. Physico-chemical traits of cured-cooked ham and sensory traits of cured-cooked and dry-cured hams
    • Fernandez X., Gilbert S., Vendeuvre J.L. Effects of halothane genotype and pre-slaughter treatment on pig meat quality. Part 2. Physico-chemical traits of cured-cooked ham and sensory traits of cured-cooked and dry-cured hams. Meat Sci 2002, 62:439-446.
    • (2002) Meat Sci , vol.62 , pp. 439-446
    • Fernandez, X.1    Gilbert, S.2    Vendeuvre, J.L.3
  • 49
    • 0036024908 scopus 로고    scopus 로고
    • Effects of halothane genotype and pre-slaughter treatment on pig meat quality. Part 1. Post mortem metabolism, meat quality indicators and sensory traits of m. longissimus lumborum
    • Fernandez X., Neyraud E., Astruc T., Sante V. Effects of halothane genotype and pre-slaughter treatment on pig meat quality. Part 1. Post mortem metabolism, meat quality indicators and sensory traits of m. longissimus lumborum. Meat Sci 2002, 62:429-437.
    • (2002) Meat Sci , vol.62 , pp. 429-437
    • Fernandez, X.1    Neyraud, E.2    Astruc, T.3    Sante, V.4
  • 51
    • 67149093426 scopus 로고    scopus 로고
    • Differences in pig muscle proteome according to HAL genotype: implications for meat quality defects
    • Laville E., Sayd T., Terlouw C., Blinet S., Pinguet J., Fillaut M., et al. Differences in pig muscle proteome according to HAL genotype: implications for meat quality defects. J Agric Food Chem 2009, 57:4913-4923.
    • (2009) J Agric Food Chem , vol.57 , pp. 4913-4923
    • Laville, E.1    Sayd, T.2    Terlouw, C.3    Blinet, S.4    Pinguet, J.5    Fillaut, M.6
  • 52
    • 44949286385 scopus 로고
    • Modelling of the formation of pale, soft and exudative meat: effects of chilling regime and rate and extent of glycolysis
    • Offer G. Modelling of the formation of pale, soft and exudative meat: effects of chilling regime and rate and extent of glycolysis. Meat Sci 1991, 30:157-184.
    • (1991) Meat Sci , vol.30 , pp. 157-184
    • Offer, G.1
  • 53
    • 33645976443 scopus 로고    scopus 로고
    • Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: implications on meat color development
    • Sayd T., Morzel M., Chambon C., Franck M., Figwer P., Larzul C., et al. Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: implications on meat color development. J Agric Food Chem 2006, 54:2732-2737.
    • (2006) J Agric Food Chem , vol.54 , pp. 2732-2737
    • Sayd, T.1    Morzel, M.2    Chambon, C.3    Franck, M.4    Figwer, P.5    Larzul, C.6
  • 54
    • 52249115647 scopus 로고    scopus 로고
    • The behaviour of the protein complex throughout the technological process in the production of cooked cold meats
    • Barbieri G., Rivaldi P. The behaviour of the protein complex throughout the technological process in the production of cooked cold meats. Meat Sci 2008, 80:1132-1137.
    • (2008) Meat Sci , vol.80 , pp. 1132-1137
    • Barbieri, G.1    Rivaldi, P.2
  • 55
    • 79959241187 scopus 로고    scopus 로고
    • Proteomic analysis of pork meat in the production of cooked ham
    • Pioselli B., Paredi G., Mozzarelli A. Proteomic analysis of pork meat in the production of cooked ham. Mol Biosyst 2011, 7:2252-2260.
    • (2011) Mol Biosyst , vol.7 , pp. 2252-2260
    • Pioselli, B.1    Paredi, G.2    Mozzarelli, A.3
  • 56
    • 79151484348 scopus 로고    scopus 로고
    • Proteomic analysis of semimembranosus and biceps femoris muscles from Bayonne dry-cured ham
    • Théron L., Sayd T., Pinguet J., Chambon C., Robert N., Santé-Lhoutellier V. Proteomic analysis of semimembranosus and biceps femoris muscles from Bayonne dry-cured ham. Meat Sci 2011, 88:82-90.
    • (2011) Meat Sci , vol.88 , pp. 82-90
    • Théron, L.1    Sayd, T.2    Pinguet, J.3    Chambon, C.4    Robert, N.5    Santé-Lhoutellier, V.6
  • 57
    • 11444259281 scopus 로고    scopus 로고
    • Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams
    • Di Luccia A., Picariello G., Cacace G., Scaloni A., Faccia M., Liuzzi V., et al. Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams. Meat Sci 2005, 69:479-491.
    • (2005) Meat Sci , vol.69 , pp. 479-491
    • Di Luccia, A.1    Picariello, G.2    Cacace, G.3    Scaloni, A.4    Faccia, M.5    Liuzzi, V.6
  • 58
    • 77954622848 scopus 로고    scopus 로고
    • Identification of small troponin T peptides generated in dry-cured ham
    • Mora L., Sentandreu M.A., Toldrá F. Identification of small troponin T peptides generated in dry-cured ham. Food Chem 2010, 123:691-697.
    • (2010) Food Chem , vol.123 , pp. 691-697
    • Mora, L.1    Sentandreu, M.A.2    Toldrá, F.3
  • 59
    • 0037208101 scopus 로고    scopus 로고
    • Survey of conditioning indicators for pork loins: changes in myofibrils, proteins and peptides during postmortem conditioning of vacuum-packed pork loins for 30days
    • Okumura T., Yamada R., Nishimura T. Survey of conditioning indicators for pork loins: changes in myofibrils, proteins and peptides during postmortem conditioning of vacuum-packed pork loins for 30days. Meat Sci 2003, 64:467-473.
    • (2003) Meat Sci , vol.64 , pp. 467-473
    • Okumura, T.1    Yamada, R.2    Nishimura, T.3
  • 61
    • 0037207445 scopus 로고    scopus 로고
    • Identification and significance of the N-terminal part of swine pyruvate kinase in aged Parma hams
    • Sforza S., Boni M., Ruozi R., Virgili R., Marchelli R. Identification and significance of the N-terminal part of swine pyruvate kinase in aged Parma hams. Meat Sci 2003, 63:57-61.
    • (2003) Meat Sci , vol.63 , pp. 57-61
    • Sforza, S.1    Boni, M.2    Ruozi, R.3    Virgili, R.4    Marchelli, R.5
  • 62
    • 79955046274 scopus 로고    scopus 로고
    • Proteomic profile of dry-cured ham relative to PRKAG3 or CAST genotype, level of salt and pastiness
    • Škrlep M., Čandek-Potokar M., Mandelc S., Javornik B., Gou P., Chambon C., et al. Proteomic profile of dry-cured ham relative to PRKAG3 or CAST genotype, level of salt and pastiness. Meat Sci 2011, 88:657-667.
    • (2011) Meat Sci , vol.88 , pp. 657-667
    • Škrlep, M.1    Čandek-Potokar, M.2    Mandelc, S.3    Javornik, B.4    Gou, P.5    Chambon, C.6
  • 63
    • 3543052953 scopus 로고    scopus 로고
    • UDP-glucose pyrophosphorylase is upregulated in carriers of the porcine RN-mutation in the AMP-activated protein kinase
    • Hedegaard J., Horn P., Lametsch R., Sondergaard Moller H., Roepstorff P., Bendixen C., et al. UDP-glucose pyrophosphorylase is upregulated in carriers of the porcine RN-mutation in the AMP-activated protein kinase. Proteomics 2004, 4:2448-2454.
    • (2004) Proteomics , vol.4 , pp. 2448-2454
    • Hedegaard, J.1    Horn, P.2    Lametsch, R.3    Sondergaard Moller, H.4    Roepstorff, P.5    Bendixen, C.6
  • 64
    • 2642568030 scopus 로고    scopus 로고
    • The proteome of chicken skeletal muscle: changes in soluble protein expression during growth in a layer strain
    • Doherty M.K., McLean L., Hayter J.R., Pratt J.M., Robertson D.H.L., El-Shafei A., et al. The proteome of chicken skeletal muscle: changes in soluble protein expression during growth in a layer strain. Proteomics 2004, 4:2082-2093.
    • (2004) Proteomics , vol.4 , pp. 2082-2093
    • Doherty, M.K.1    McLean, L.2    Hayter, J.R.3    Pratt, J.M.4    Robertson, D.H.L.5    El-Shafei, A.6
  • 65
    • 33646441029 scopus 로고    scopus 로고
    • Protein expression of pectoralis major muscle in chickens in response to dietary methionine status
    • Corzo A., Kidd M.T., Dozier W.A., Shack L.A., Burgess P.S.C. Protein expression of pectoralis major muscle in chickens in response to dietary methionine status. Br J Nutr 2006, 95:703-708.
    • (2006) Br J Nutr , vol.95 , pp. 703-708
    • Corzo, A.1    Kidd, M.T.2    Dozier, W.A.3    Shack, L.A.4    Burgess, P.S.C.5
  • 66
    • 80052664934 scopus 로고    scopus 로고
    • Functional genomics of the muscle response to restraint and transport in chickens
    • Hazard D., Fernandez X., Pinguet J., Chambon C., Letisse F., Portais J.C., et al. Functional genomics of the muscle response to restraint and transport in chickens. J Anim Sci 2011, 89:2717-2730.
    • (2011) J Anim Sci , vol.89 , pp. 2717-2730
    • Hazard, D.1    Fernandez, X.2    Pinguet, J.3    Chambon, C.4    Letisse, F.5    Portais, J.C.6
  • 67
    • 76349117911 scopus 로고    scopus 로고
    • Proteomic analysis of tenderness trait in Thai native and commercial broiler chicken muscles
    • Mekchay S., Teltathum T., Nakasathien S., Pongpaichan P. Proteomic analysis of tenderness trait in Thai native and commercial broiler chicken muscles. J Poult Sci 2010, 47:8-12.
    • (2010) J Poult Sci , vol.47 , pp. 8-12
    • Mekchay, S.1    Teltathum, T.2    Nakasathien, S.3    Pongpaichan, P.4
  • 68
    • 74049093200 scopus 로고    scopus 로고
    • Proteome changes in Thai indigenous chicken muscle during growth period
    • Eltathum T., Mekchay S. Proteome changes in Thai indigenous chicken muscle during growth period. Int J Biol Sci 2009, 5:679-685.
    • (2009) Int J Biol Sci , vol.5 , pp. 679-685
    • Eltathum, T.1    Mekchay, S.2
  • 71
    • 34548153081 scopus 로고    scopus 로고
    • De novo mass spectrometry sequencing and characterization of species-specific peptides from nucleoside diphosphate kinase B for the classification of commercial fish species belonging to the family merlucciidae
    • Carrera M., Cañas B., Piñeiro C., Vázquez J., Gallardo J.M. De novo mass spectrometry sequencing and characterization of species-specific peptides from nucleoside diphosphate kinase B for the classification of commercial fish species belonging to the family merlucciidae. J Proteome Res 2007, 6:3070-3080.
    • (2007) J Proteome Res , vol.6 , pp. 3070-3080
    • Carrera, M.1    Cañas, B.2    Piñeiro, C.3    Vázquez, J.4    Gallardo, J.M.5
  • 72
    • 33748317825 scopus 로고    scopus 로고
    • Identification of marker proteins for the adulteration of meat products with soybean proteins by multidimensional liquid chromatography-tandem mass spectrometry
    • Leitner A., Castro-Rubio F., Marina M.L., Lindner W. Identification of marker proteins for the adulteration of meat products with soybean proteins by multidimensional liquid chromatography-tandem mass spectrometry. J Proteome Res 2006, 5:2424-2430.
    • (2006) J Proteome Res , vol.5 , pp. 2424-2430
    • Leitner, A.1    Castro-Rubio, F.2    Marina, M.L.3    Lindner, W.4
  • 73
    • 79958748572 scopus 로고    scopus 로고
    • Proteomic approach for the detection of chicken mechanically recovered meat
    • Surowiec I., Koistinen K.M., Fraser P.D., Bramley P.M. Proteomic approach for the detection of chicken mechanically recovered meat. Meat Sci 2011, 89:233-237.
    • (2011) Meat Sci , vol.89 , pp. 233-237
    • Surowiec, I.1    Koistinen, K.M.2    Fraser, P.D.3    Bramley, P.M.4
  • 75
    • 79952819297 scopus 로고    scopus 로고
    • The role of rabbit meat as functional food
    • Dalle Zotte A., Szendro Z. The role of rabbit meat as functional food. Meat Sci 2011, 88:319-331.
    • (2011) Meat Sci , vol.88 , pp. 319-331
    • Dalle Zotte, A.1    Szendro, Z.2
  • 76
    • 67650429974 scopus 로고    scopus 로고
    • Establishment of a proteomic reference map for the gastrocnemius muscle in the rabbit (Oryctolagus cuniculus)
    • Almeida A.M., Campos A., van Harten S., Cardoso L.A., Coelho A.V. Establishment of a proteomic reference map for the gastrocnemius muscle in the rabbit (Oryctolagus cuniculus). Res Vet Sci 2009, 87:196-199.
    • (2009) Res Vet Sci , vol.87 , pp. 196-199
    • Almeida, A.M.1    Campos, A.2    van Harten, S.3    Cardoso, L.A.4    Coelho, A.V.5
  • 77
    • 77952053019 scopus 로고    scopus 로고
    • Proteomic investigation of the effects of weight loss in the gastrocnemius muscle of wild and NZW rabbits via 2D-electrophoresis and MALDI-TOF MS
    • Almeida A.M., Campos A., Francisco R., van Harten S., Cardoso L.A., Coelho A.V. Proteomic investigation of the effects of weight loss in the gastrocnemius muscle of wild and NZW rabbits via 2D-electrophoresis and MALDI-TOF MS. Anim Genet 2010, 41:260-272.
    • (2010) Anim Genet , vol.41 , pp. 260-272
    • Almeida, A.M.1    Campos, A.2    Francisco, R.3    van Harten, S.4    Cardoso, L.A.5    Coelho, A.V.6
  • 78
    • 84858838369 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the sarcoplasmic reticulum from rabbit skeletal muscle by on-membrane digestion
    • Staunton L., Ohlendieck K. Mass spectrometric characterization of the sarcoplasmic reticulum from rabbit skeletal muscle by on-membrane digestion. Protein Pept Lett 2012, 19:252-263.
    • (2012) Protein Pept Lett , vol.19 , pp. 252-263
    • Staunton, L.1    Ohlendieck, K.2
  • 79
    • 33846644523 scopus 로고    scopus 로고
    • Differential expression of sarcoplasmic proteins in four heterogeneous ovine skeletal muscles
    • Hamelin M., Sayd T., Chambon C., Bouix J., Bibe B., Milenkovic D., et al. Differential expression of sarcoplasmic proteins in four heterogeneous ovine skeletal muscles. Proteomics 2007, 7:271-280.
    • (2007) Proteomics , vol.7 , pp. 271-280
    • Hamelin, M.1    Sayd, T.2    Chambon, C.3    Bouix, J.4    Bibe, B.5    Milenkovic, D.6
  • 83
    • 21844483186 scopus 로고
    • Effect of electrical stimulation on post mortem biochemical characteristics and quality of longissimus dorsi thoracis muscle from buffalo (Bubalus bubalis)
    • Soares G.J., Areas J.A. Effect of electrical stimulation on post mortem biochemical characteristics and quality of longissimus dorsi thoracis muscle from buffalo (Bubalus bubalis). Meat Sci 1995, 41:369-379.
    • (1995) Meat Sci , vol.41 , pp. 369-379
    • Soares, G.J.1    Areas, J.A.2
  • 84
    • 50249118185 scopus 로고    scopus 로고
    • Comparison of fresh beef and camel meat proteolysis during cold storage
    • Soltanizadeh N., Kadivar M., Keramat J., Fazilati M. Comparison of fresh beef and camel meat proteolysis during cold storage. Meat Sci 2008, 80:892-895.
    • (2008) Meat Sci , vol.80 , pp. 892-895
    • Soltanizadeh, N.1    Kadivar, M.2    Keramat, J.3    Fazilati, M.4
  • 85
    • 80053211040 scopus 로고    scopus 로고
    • Effect of season on contractile and metabolic properties of desert camel muscle (Camelus dromedarius)
    • Abdelhadi O.M., Babiker S.A., Picard B., Jurie C., Jailler R., Hocquette J.F., et al. Effect of season on contractile and metabolic properties of desert camel muscle (Camelus dromedarius). Meat Sci 2012, 90:139-144.
    • (2012) Meat Sci , vol.90 , pp. 139-144
    • Abdelhadi, O.M.1    Babiker, S.A.2    Picard, B.3    Jurie, C.4    Jailler, R.5    Hocquette, J.F.6
  • 86
    • 33847104545 scopus 로고    scopus 로고
    • Influence of hunting-season stage and ripening conditions on nitrogen fractions and degradation of myofibrillar proteins in venison (Cervus elaphus) chorizo sausages
    • Ruiz A.G., Mariscal C., Soriano A. Influence of hunting-season stage and ripening conditions on nitrogen fractions and degradation of myofibrillar proteins in venison (Cervus elaphus) chorizo sausages. Meat Sci 2007, 76:74-85.
    • (2007) Meat Sci , vol.76 , pp. 74-85
    • Ruiz, A.G.1    Mariscal, C.2    Soriano, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.