{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T06:18:39Z","timestamp":1779257919722,"version":"3.51.4"},"reference-count":42,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2012,3,1]],"date-time":"2012-03-01T00:00:00Z","timestamp":1330560000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"China Agriculture Research System"},{"DOI":"10.13039\/501100004608","name":"Natural Science Foundation of Jiangsu Province","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004608","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Meat Science"],"published-print":{"date-parts":[[2012,3]]},"DOI":"10.1016\/j.meatsci.2011.09.004","type":"journal-article","created":{"date-parts":[[2011,9,15]],"date-time":"2011-09-15T14:11:03Z","timestamp":1316095863000},"page":"536-542","source":"Crossref","is-referenced-by-count":32,"title":["Preliminary study on the effect of caspase-6 and calpain inhibitors on postmortem proteolysis of myofibrillar proteins in chicken breast muscle"],"prefix":"10.1016","volume":"90","author":[{"given":"Ming","family":"Huang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Feng","family":"Huang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hanjun","family":"Ma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinglian","family":"Xu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guanghong","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.meatsci.2011.09.004_bb0005","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1007\/s00217-010-1296-5","article-title":"Postmortem muscle cells die through apoptosis","volume":"231","author":"Becila","year":"2010","journal-title":"European Food Research and Technology"},{"issue":"13","key":"10.1016\/j.meatsci.2011.09.004_bb0010","doi-asserted-by":"crossref","first-page":"5229","DOI":"10.1021\/jf063372l","article-title":"New indicators of beef sensory quality revealed by expression of specific genes","volume":"55","author":"Bernard","year":"2007","journal-title":"Journal of Agricultural and Food Chemistry"},{"issue":"6","key":"10.1016\/j.meatsci.2011.09.004_bb0015","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1023\/A:1020668923852","article-title":"Oxygen deprivation induced cell death: An update","volume":"7","author":"Brunelle","year":"2002","journal-title":"Apoptosis"},{"issue":"10","key":"10.1016\/j.meatsci.2011.09.004_bb0020","doi-asserted-by":"crossref","first-page":"3439","DOI":"10.2527\/jas.2009-2412","article-title":"Morphological and biochemical assessment of apoptosis in different skeletal muscles of bulls during conditioning","volume":"88","author":"Cao","year":"2010","journal-title":"Journal of Animal Science"},{"issue":"9","key":"10.1016\/j.meatsci.2011.09.004_bb0025","doi-asserted-by":"crossref","first-page":"6848","DOI":"10.1074\/jbc.M212021200","article-title":"Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis","volume":"278","author":"Chen","year":"2003","journal-title":"Journal of Biological Chemistry"},{"issue":"3","key":"10.1016\/j.meatsci.2011.09.004_bb0030","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.meatsci.2010.10.002","article-title":"Effects of camptothecin, etoposide and Ca2+ on caspase-3 activity and myofibrillar disruption of chicken during postmortem ageing","volume":"87","author":"Chen","year":"2011","journal-title":"Meat Science"},{"issue":"10","key":"10.1016\/j.meatsci.2011.09.004_bb0035","doi-asserted-by":"crossref","first-page":"2134","DOI":"10.1016\/j.biocel.2005.03.010","article-title":"Ca2+-dependent proteolysis in muscle wasting","volume":"37","author":"Costelli","year":"2005","journal-title":"The International Journal of Biochemistry & Cell Biology"},{"issue":"Pt 4","key":"10.1016\/j.meatsci.2011.09.004_bb0040","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1093\/brain\/awh033","article-title":"Desmin myopathy","volume":"127","author":"Goldfarb","year":"2004","journal-title":"Brain"},{"issue":"8","key":"10.1016\/j.meatsci.2011.09.004_bb0045","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/j.tifs.2006.01.011","article-title":"Meat ageing: Reconsideration of the current concept","volume":"17","author":"Herrera-Mendez","year":"2006","journal-title":"Trends in Food Science and Technology"},{"issue":"2","key":"10.1016\/j.meatsci.2011.09.004_bb0050","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0309-1740(01)00068-7","article-title":"Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle","volume":"59","author":"Hopkins","year":"2001","journal-title":"Meat Science"},{"issue":"2","key":"10.1016\/j.meatsci.2011.09.004_bb0055","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1071\/AR01079","article-title":"Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat","volume":"53","author":"Hopkins","year":"2002","journal-title":"Australian Journal of Agricultural Research"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0060","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.foodchem.2008.11.095","article-title":"Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging","volume":"115","author":"Huang","year":"2009","journal-title":"Food Chemistry"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0065","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.foodchem.2011.02.062","article-title":"The effect of active caspase-3 on degradation of chicken myofibrillar proteins and structure of myofibrils","volume":"128","author":"Huang","year":"2011","journal-title":"Food Chemistry"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0070","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.meatsci.2010.05.004","article-title":"Biochemistry of postmortem muscle\u2014Lessons on mechanisms of meat tenderization","volume":"86","author":"Huff-Lonergan","year":"2010","journal-title":"Meat Science"},{"issue":"10","key":"10.1016\/j.meatsci.2011.09.004_bb0080","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.2527\/jas.2006-163","article-title":"Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle","volume":"84","author":"Kemp","year":"2006","journal-title":"Journal of Animal Science"},{"issue":"8","key":"10.1016\/j.meatsci.2011.09.004_bb0075","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1017\/S1751731108002310","article-title":"The effect of recombinant caspase 3 on myofibrillar proteins in porcine skeletal muscle","volume":"2","author":"Kemp","year":"2008","journal-title":"Animal"},{"issue":"3","key":"10.1016\/j.meatsci.2011.09.004_bb0085","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.meatsci.2005.12.009","article-title":"Comparison of the relative expression of caspase isoforms in different porcine skeletal muscles","volume":"73","author":"Kemp","year":"2006","journal-title":"Meat Science"},{"issue":"5","key":"10.1016\/j.meatsci.2011.09.004_bb0090","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1093\/oxfordjournals.jbchem.a022197","article-title":"Involvement of both caspase-like proteases and serine proteases in apoptotic cell death induced by ricin, modeccin, diphtheria toxin, and pseudomonas toxin","volume":"124","author":"Komatsu","year":"1998","journal-title":"Journal of Biochemistry"},{"issue":"Supplement 1","key":"10.1016\/j.meatsci.2011.09.004_bb0095","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/0309-1740(96)00065-4","article-title":"Biochemical factors regulating the toughening and tenderization processes of meat","volume":"43","author":"Koohmaraie","year":"1996","journal-title":"Meat Science"},{"issue":"5","key":"10.1016\/j.meatsci.2011.09.004_bb0100","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1111\/j.1365-2621.1988.tb09251.x","article-title":"Role of Ca-dependent proteases and lysosomal enzymes in postmortem changes in bovine skeletal muscle","volume":"53","author":"Koohmaraie","year":"1988","journal-title":"Journal of Food Science"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0105","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.meatsci.2006.04.025","article-title":"Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system","volume":"74","author":"Koohmaraie","year":"2006","journal-title":"Meat Science"},{"key":"10.1016\/j.meatsci.2011.09.004_bb0110","first-page":"69","article-title":"The biological basis of meat tenderness and potential genetic approaches for its control and prediction","volume":"48","author":"Koohmaraie","year":"1995","journal-title":"Proceedings of the Reciprocal Meat Conference"},{"issue":"22","key":"10.1016\/j.meatsci.2011.09.004_bb0115","doi-asserted-by":"crossref","first-page":"10755","DOI":"10.1021\/jf901949r","article-title":"Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization","volume":"57","author":"Laville","year":"2009","journal-title":"Journal of Agricultrual Food Chemistry"},{"issue":"4","key":"10.1016\/j.meatsci.2011.09.004_bb0120","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.2527\/2004.8241195x","article-title":"Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles","volume":"82","author":"Melody","year":"2004","journal-title":"Journal of Animal Science"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0125","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0309-1740(01)00175-9","article-title":"Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing","volume":"61","author":"Mestre Prates","year":"2002","journal-title":"Meat Science"},{"issue":"12","key":"10.1016\/j.meatsci.2011.09.004_bb0130","doi-asserted-by":"crossref","first-page":"3062","DOI":"10.2527\/2001.79123062x","article-title":"Consumer thresholds for establishing the value of beef tenderness","volume":"79","author":"Miller","year":"2001","journal-title":"Journal of Animal Science"},{"issue":"6","key":"10.1016\/j.meatsci.2011.09.004_bb0135","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.2527\/1993.7161471x","article-title":"Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers","volume":"71","author":"Morgan","year":"1993","journal-title":"Journal of Animal Science"},{"issue":"28","key":"10.1016\/j.meatsci.2011.09.004_bb0140","doi-asserted-by":"crossref","first-page":"16443","DOI":"10.1074\/jbc.271.28.16443","article-title":"The CED-3\/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A","volume":"271","author":"Orth","year":"1996","journal-title":"The Journal of Biological Chemistry"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0145","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.meatsci.2006.05.010","article-title":"Revisiting the conversion of muscle into meat and the underlying mechanisms","volume":"74","author":"Ouali","year":"2006","journal-title":"Meat Science"},{"issue":"3","key":"10.1016\/j.meatsci.2011.09.004_bb0150","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0309-1740(00)00103-0","article-title":"Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes","volume":"57","author":"Prates","year":"2001","journal-title":"Meat Science"},{"issue":"2","key":"10.1016\/j.meatsci.2011.09.004_bb0155","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0309-1740(98)00113-2","article-title":"The effect of proteasome on myofibrillar structures in bovine skeletal muscle","volume":"51","author":"Robert","year":"1999","journal-title":"Meat Science"},{"issue":"6","key":"10.1016\/j.meatsci.2011.09.004_bb0160","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.vph.2007.01.006","article-title":"Cell suicide and caspases","volume":"46","author":"Rupinder","year":"2007","journal-title":"Vascular Pharmacology"},{"issue":"12","key":"10.1016\/j.meatsci.2011.09.004_bb0165","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/S0924-2244(02)00188-7","article-title":"Role of muscle endopeptidases and their inhibitors in meat tenderness","volume":"13","author":"Sentandreu","year":"2002","journal-title":"Trends in Food Science and Technology"},{"issue":"10","key":"10.1016\/j.meatsci.2011.09.004_bb0170","doi-asserted-by":"crossref","first-page":"7320","DOI":"10.1074\/jbc.M008363200","article-title":"Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis","volume":"276","author":"Slee","year":"2001","journal-title":"Journal of Biological Chemistry"},{"key":"10.1016\/j.meatsci.2011.09.004_bb0205","unstructured":"SPSS (1998). SPSS base 8.0 for windows. Chicago, IL: User's Guide. SPSS Inc."},{"issue":"15","key":"10.1016\/j.meatsci.2011.09.004_bb0175","doi-asserted-by":"crossref","first-page":"9677","DOI":"10.1074\/jbc.272.15.9677","article-title":"Substrate specificities of caspase family proteases","volume":"272","author":"Talanian","year":"1997","journal-title":"The Journal of Biological Chemistry"},{"issue":"5","key":"10.1016\/j.meatsci.2011.09.004_bb0180","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.2527\/1995.7351351x","article-title":"Is Z-disk degradation responsible for postmortem tenderization?","volume":"73","author":"Taylor","year":"1995","journal-title":"Journal of Animal Science"},{"issue":"1","key":"10.1016\/j.meatsci.2011.09.004_bb0185","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1038\/sj.cdd.4402059","article-title":"Caspase substrates","volume":"14","author":"Timmer","year":"2006","journal-title":"Cell Death and Differentiation"},{"issue":"4","key":"10.1016\/j.meatsci.2011.09.004_bb0210","doi-asserted-by":"crossref","first-page":"960","DOI":"10.2527\/jas.2007-0549","article-title":"Caspase 3 is not likely involved in the postmortem tenderization of beef muscle","volume":"86","author":"Underwood","year":"2008","journal-title":"Journal of Animal Science"},{"issue":"5","key":"10.1016\/j.meatsci.2011.09.004_bb0190","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.2527\/1994.7251209x","article-title":"Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility","volume":"72","author":"Uytterhaegen","year":"1994","journal-title":"Journal of Animal Science"},{"issue":"6","key":"10.1016\/j.meatsci.2011.09.004_bb0195","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.2527\/2001.7961502x","article-title":"Effect of postmortem storage on mu-calpain and m-calpain in ovine skeletal muscle","volume":"79","author":"Veiseth","year":"2001","journal-title":"Journal of Animal Science"},{"issue":"6","key":"10.1016\/j.meatsci.2011.09.004_bb0200","doi-asserted-by":"crossref","first-page":"2199","DOI":"10.1083\/jcb.107.6.2199","article-title":"Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line","volume":"107","author":"Wang","year":"1988","journal-title":"The Journal of Cell Biology"}],"container-title":["Meat Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0309174011003019?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0309174011003019?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,6,15]],"date-time":"2019-06-15T16:00:30Z","timestamp":1560614430000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0309174011003019"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,3]]},"references-count":42,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2012,3]]}},"alternative-id":["S0309174011003019"],"URL":"https:\/\/doi.org\/10.1016\/j.meatsci.2011.09.004","relation":{},"ISSN":["0309-1740"],"issn-type":[{"value":"0309-1740","type":"print"}],"subject":[],"published":{"date-parts":[[2012,3]]}}}