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Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase.

Meat science

Etherington DJ, Taylor MA, Dransfield E.
PMID: 22056115
Meat Sci. 1987;20(1):1-18. doi: 10.1016/0309-1740(87)90046-5.

The conditioning times for beef, calf, lamb, pig and chicken M. pectoralis profundus were determined from extensibility measurements at 15°C. Extracts from the same muscle from these animals and also rabbit were assayed for free and total cathepsin activities...

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Etherington DJ, Taylor MA, Dransfield E. Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase. Meat Sci. 1987;20(1):1-18doi: 10.1016/0309-1740(87)90046-5.
Etherington, D. J., Taylor, M. A., & Dransfield, E. (1987). Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase. Meat science, 20(1), 1-18. https://doi.org/10.1016/0309-1740(87)90046-5
Etherington, D J, et al. "Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase." Meat science vol. 20,1 (1987): 1-18. doi: https://doi.org/10.1016/0309-1740(87)90046-5
Etherington DJ, Taylor MA, Dransfield E. Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase. Meat Sci. 1987;20(1):1-18. doi: 10.1016/0309-1740(87)90046-5. PMID: 22056115.
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Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle.

Meat science

Etherington DJ, Taylor MA, Wakefield DK, Cousins A, Dransfield E.
PMID: 22055511
Meat Sci. 1990;28(2):99-109. doi: 10.1016/0309-1740(90)90034-4.

Control, electrically stimulated (ES) and glycogen-depleted (GD) chicken muscles were conditioned at 15°C with continuous mechanical testing for extensibility. The ES and GD muscles went into rigor 3·6 and 2·8 h earlier, respectively, than control muscle. At 24h post-rigor...

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Etherington DJ, Taylor MA, Wakefield DK, et al. Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle. Meat Sci. 1990;28(2):99-109doi: 10.1016/0309-1740(90)90034-4.
Etherington, D. J., Taylor, M. A., Wakefield, D. K., Cousins, A., & Dransfield, E. (1990). Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle. Meat science, 28(2), 99-109. https://doi.org/10.1016/0309-1740(90)90034-4
Etherington, D J, et al. "Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle." Meat science vol. 28,2 (1990): 99-109. doi: https://doi.org/10.1016/0309-1740(90)90034-4
Etherington DJ, Taylor MA, Wakefield DK, Cousins A, Dransfield E. Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle. Meat Sci. 1990;28(2):99-109. doi: 10.1016/0309-1740(90)90034-4. PMID: 22055511.
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Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef.

Meat science

Dransfield E, Etherington DJ, Taylor MA.
PMID: 22059511
Meat Sci. 1992;31(1):75-84. doi: 10.1016/0309-1740(92)90073-D.

Levels of calpains I and II, cathepsins B and L and β-glucuronidase were determined in extracts of electrically stimulated and control beef M. Pectoralis profundus stored at temperatures between 0 and 30°C and varied to avoid muscle shortening. The...

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Dransfield E, Etherington DJ, Taylor MA. Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef. Meat Sci. 1992;31(1):75-84doi: 10.1016/0309-1740(92)90073-D.
Dransfield, E., Etherington, D. J., & Taylor, M. A. (1992). Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef. Meat science, 31(1), 75-84. https://doi.org/10.1016/0309-1740(92)90073-D
Dransfield, E, et al. "Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef." Meat science vol. 31,1 (1992): 75-84. doi: https://doi.org/10.1016/0309-1740(92)90073-D
Dransfield E, Etherington DJ, Taylor MA. Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef. Meat Sci. 1992;31(1):75-84. doi: 10.1016/0309-1740(92)90073-D. PMID: 22059511.
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The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation.

Meat science

Thomas AR, Gondoza H, Hoffman LC, Oosthuizen V, Naudé RJ.
PMID: 22061124
Meat Sci. 2004 May;67(1):113-20. doi: 10.1016/j.meatsci.2003.10.001.

As very little research has been conducted on ostrich meat tenderisation, this study aims at investigating the roles of the proteasome and cathepsins B, L, H, and D in the tenderisation process. The enzyme activities in meat from eight...

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Thomas AR, Gondoza H, Hoffman LC, et al. The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation. Meat Sci. 2004;67(1):113-20doi: 10.1016/j.meatsci.2003.10.001.
Thomas, A. R., Gondoza, H., Hoffman, L. C., Oosthuizen, V., & Naudé, R. J. (2004). The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation. Meat science, 67(1), 113-20. https://doi.org/10.1016/j.meatsci.2003.10.001
Thomas, Adele R, et al. "The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation." Meat science vol. 67,1 (2004): 113-20. doi: https://doi.org/10.1016/j.meatsci.2003.10.001
Thomas AR, Gondoza H, Hoffman LC, Oosthuizen V, Naudé RJ. The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation. Meat Sci. 2004 May;67(1):113-20. doi: 10.1016/j.meatsci.2003.10.001. PMID: 22061124.
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Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells.

Anemia

Keegan PM, Surapaneni S, Platt MO.
PMID: 22550569
Anemia. 2012;2012:201781. doi: 10.1155/2012/201781. Epub 2012 Apr 09.

Sickle cell disease is a genetic disease that increases systemic inflammation as well as the risk of pediatric strokes, but links between sickle-induced inflammation and arterial remodeling are not clear. Cathepsins are powerful elastases and collagenases secreted by endothelial...

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Keegan PM, Surapaneni S, Platt MO. Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells. Anemia. 2012;2012:201781doi: 10.1155/2012/201781.
Keegan, P. M., Surapaneni, S., & Platt, M. O. (2012). Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells. Anemia, 2012201781. https://doi.org/10.1155/2012/201781
Keegan, Philip M, et al. "Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells." Anemia vol. 2012 (2012): 201781. doi: https://doi.org/10.1155/2012/201781
Keegan PM, Surapaneni S, Platt MO. Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells. Anemia. 2012;2012:201781. doi: 10.1155/2012/201781. Epub 2012 Apr 09. PMID: 22550569; PMCID: PMC3328887.
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Proteinases and their inhibitors in liver cancer.

World journal of hepatology

Puxbaum V, Mach L.
PMID: 21160962
World J Hepatol. 2009 Oct 31;1(1):28-34. doi: 10.4254/wjh.v1.i1.28.

Proteinases are known to be involved in many cancer-related processes, particularly in the breakdown of extracellular matrix barriers in the course of tumor invasion and metastasis. In this review we summarize the current knowledge about the role of the...

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Puxbaum V, Mach L. Proteinases and their inhibitors in liver cancer. World J Hepatol. 2009;1(1):28-34doi: 10.4254/wjh.v1.i1.28.
Puxbaum, V., & Mach, L. (2009). Proteinases and their inhibitors in liver cancer. World journal of hepatology, 1(1), 28-34. https://doi.org/10.4254/wjh.v1.i1.28
Puxbaum, Verena, and Mach, Lukas. "Proteinases and their inhibitors in liver cancer." World journal of hepatology vol. 1,1 (2009): 28-34. doi: https://doi.org/10.4254/wjh.v1.i1.28
Puxbaum V, Mach L. Proteinases and their inhibitors in liver cancer. World J Hepatol. 2009 Oct 31;1(1):28-34. doi: 10.4254/wjh.v1.i1.28. PMID: 21160962; PMCID: PMC2998952.
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Reduction of mutant huntingtin accumulation and toxicity by lysosomal cathepsins D and B in neurons.

Molecular neurodegeneration

Liang Q, Ouyang X, Schneider L, Zhang J.
PMID: 21631942
Mol Neurodegener. 2011 Jun 01;6:37. doi: 10.1186/1750-1326-6-37.

BACKGROUND: Huntington's disease is caused by aggregation of mutant huntingtin (mHtt) protein containing more than a 36 polyQ repeat. Upregulation of macroautophagy was suggested as a neuroprotective strategy to degrade mutant huntingtin. However, macroautophagy initiation has been shown to...

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Liang Q, Ouyang X, Schneider L, et al. Reduction of mutant huntingtin accumulation and toxicity by lysosomal cathepsins D and B in neurons. Mol Neurodegener. 2011;6:37doi: 10.1186/1750-1326-6-37.
Liang, Q., Ouyang, X., Schneider, L., & Zhang, J. (2011). Reduction of mutant huntingtin accumulation and toxicity by lysosomal cathepsins D and B in neurons. Molecular neurodegeneration, 637. https://doi.org/10.1186/1750-1326-6-37
Liang, Qiuli, et al. "Reduction of mutant huntingtin accumulation and toxicity by lysosomal cathepsins D and B in neurons." Molecular neurodegeneration vol. 6 (2011): 37. doi: https://doi.org/10.1186/1750-1326-6-37
Liang Q, Ouyang X, Schneider L, Zhang J. Reduction of mutant huntingtin accumulation and toxicity by lysosomal cathepsins D and B in neurons. Mol Neurodegener. 2011 Jun 01;6:37. doi: 10.1186/1750-1326-6-37. PMID: 21631942; PMCID: PMC3164227.
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Cysteinyl cathepsins: multifunctional enzymes in cardiovascular disease.

Chonnam medical journal

Li X, Liu Z, Cheng Z, Cheng X.
PMID: 22977747
Chonnam Med J. 2012 Aug;48(2):77-85. doi: 10.4068/cmj.2012.48.2.77. Epub 2012 Aug 24.

Until recently, the role of lysosomal cysteine protease cathepsins in intracellular protein degradation was believed to be mainly restricted to scavenging. However, recent studies have revealed nontraditional roles for cysteine protease cathepsins in the extracellular space during the development...

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Li X, Liu Z, Cheng Z, et al. Cysteinyl cathepsins: multifunctional enzymes in cardiovascular disease. Chonnam Med J. 2012;48(2):77-85doi: 10.4068/cmj.2012.48.2.77.
Li, X., Liu, Z., Cheng, Z., & Cheng, X. (2012). Cysteinyl cathepsins: multifunctional enzymes in cardiovascular disease. Chonnam medical journal, 48(2), 77-85. https://doi.org/10.4068/cmj.2012.48.2.77
Li, Xiang, et al. "Cysteinyl cathepsins: multifunctional enzymes in cardiovascular disease." Chonnam medical journal vol. 48,2 (2012): 77-85. doi: https://doi.org/10.4068/cmj.2012.48.2.77
Li X, Liu Z, Cheng Z, Cheng X. Cysteinyl cathepsins: multifunctional enzymes in cardiovascular disease. Chonnam Med J. 2012 Aug;48(2):77-85. doi: 10.4068/cmj.2012.48.2.77. Epub 2012 Aug 24. PMID: 22977747; PMCID: PMC3434795.
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Cysteine Protease Cathepsins in Atherosclerosis and Abdominal Aortic Aneurysm.

Clinical reviews in bone and mineral metabolism

Sjöberg S, Shi GP.
PMID: 22505840
Clin Rev Bone Miner Metab. 2011 Jun 01;9(2):138-147. doi: 10.1007/s12018-011-9098-2. Epub 2011 Jun 18.

Extracellular matrix remodeling is an important mechanism in the initiation and progression of cardiovascular diseases. Cysteine protease cathepsins are among the important proteases that affect major events in the pathogenesis of atherosclerosis and abdominal aortic aneurysm, including smooth muscle...

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Sjöberg S, Shi GP. Cysteine Protease Cathepsins in Atherosclerosis and Abdominal Aortic Aneurysm. Clin Rev Bone Miner Metab. 2011;9(2):138-147doi: 10.1007/s12018-011-9098-2.
Sjöberg, S., & Shi, G. P. (2011). Cysteine Protease Cathepsins in Atherosclerosis and Abdominal Aortic Aneurysm. Clinical reviews in bone and mineral metabolism, 9(2), 138-147. https://doi.org/10.1007/s12018-011-9098-2
Sjöberg, Sara, and Shi, Guo-Ping. "Cysteine Protease Cathepsins in Atherosclerosis and Abdominal Aortic Aneurysm." Clinical reviews in bone and mineral metabolism vol. 9,2 (2011): 138-147. doi: https://doi.org/10.1007/s12018-011-9098-2
Sjöberg S, Shi GP. Cysteine Protease Cathepsins in Atherosclerosis and Abdominal Aortic Aneurysm. Clin Rev Bone Miner Metab. 2011 Jun 01;9(2):138-147. doi: 10.1007/s12018-011-9098-2. Epub 2011 Jun 18. PMID: 22505840; PMCID: PMC3324310.
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Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle.

Meat science

Hopkins DL, Thompson JM.
PMID: 22062676
Meat Sci. 2001 Oct;59(2):175-85. doi: 10.1016/s0309-1740(01)00068-7.

To examine the effect of particular enzyme groups on tenderness specific cysteine protease inhibitors were injected into muscle early post-mortem. The protease enzyme inhibitor E-64 was injected into the m. longissimus thoracis et lumborum (LTL) on the right side...

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Hopkins DL, Thompson JM. Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle. Meat Sci. 2001;59(2):175-85doi: 10.1016/s0309-1740(01)00068-7.
Hopkins, D. L., & Thompson, J. M. (2001). Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle. Meat science, 59(2), 175-85. https://doi.org/10.1016/s0309-1740(01)00068-7
Hopkins, D L, and Thompson, J M. "Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle." Meat science vol. 59,2 (2001): 175-85. doi: https://doi.org/10.1016/s0309-1740(01)00068-7
Hopkins DL, Thompson JM. Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle. Meat Sci. 2001 Oct;59(2):175-85. doi: 10.1016/s0309-1740(01)00068-7. PMID: 22062676.
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miR-352 participates in the regulation of trypsinogen activation in pancreatic acinar cells by influencing the function of autophagic lysosomes.

Oncotarget

Song Z, Huang Y, Liu C, Lu M, Li Z, Sun B, Zhang W, Xue D.
PMID: 29541382
Oncotarget. 2018 Jan 13;9(13):10868-10879. doi: 10.18632/oncotarget.24220. eCollection 2018 Feb 16.

This study was performed to screen miRNAs and mRNAs that are differentially expressed during trypsinogen activation in acute pancreatitis and to verify their role in the process of trypsinogen activation. The function enrichment analysis showed that the functions of...

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Song Z, Huang Y, Liu C, et al. miR-352 participates in the regulation of trypsinogen activation in pancreatic acinar cells by influencing the function of autophagic lysosomes. Oncotarget. 2018;9(13):10868-10879doi: 10.18632/oncotarget.24220.
Song, Z., Huang, Y., Liu, C., Lu, M., Li, Z., Sun, B., Zhang, W., & Xue, D. (2018). miR-352 participates in the regulation of trypsinogen activation in pancreatic acinar cells by influencing the function of autophagic lysosomes. Oncotarget, 9(13), 10868-10879. https://doi.org/10.18632/oncotarget.24220
Song, Zonggong, et al. "miR-352 participates in the regulation of trypsinogen activation in pancreatic acinar cells by influencing the function of autophagic lysosomes." Oncotarget vol. 9,13 (2018): 10868-10879. doi: https://doi.org/10.18632/oncotarget.24220
Song Z, Huang Y, Liu C, Lu M, Li Z, Sun B, Zhang W, Xue D. miR-352 participates in the regulation of trypsinogen activation in pancreatic acinar cells by influencing the function of autophagic lysosomes. Oncotarget. 2018 Jan 13;9(13):10868-10879. doi: 10.18632/oncotarget.24220. eCollection 2018 Feb 16. PMID: 29541382; PMCID: PMC5834275.
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Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family.

Pflugers Archiv : European journal of physiology

Pungerčar J, Ivanovski G.
PMID: 28176093
Pflugers Arch. 2000 Jan;439:r116-r118. doi: 10.1007/s004240000112.

A cDNA encoding a novel human putative member of the papain family of cysteine peptidases has been cloned. The protease, named cathepsin P, is synthesized as a preproprotein. The presumed propeptide of 38 amino acids is followed by a...

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Pungerčar J, Ivanovski G. Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family. Pflugers Arch. 2000;439:r116-r118doi: 10.1007/s004240000112.
Pungerčar, J., & Ivanovski, G. (2000). Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family. Pflugers Archiv : European journal of physiology, 439r116-r118. https://doi.org/10.1007/s004240000112
Pungerčar, Jože, and Ivanovski, Gabriela. "Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family." Pflugers Archiv : European journal of physiology vol. 439 (2000): r116-r118. doi: https://doi.org/10.1007/s004240000112
Pungerčar J, Ivanovski G. Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family. Pflugers Arch. 2000 Jan;439:r116-r118. doi: 10.1007/s004240000112. PMID: 28176093.
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Showing 13 to 24 of 306 entries