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Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin

science campus

Campus M, Flores M, Toldrá F.
GSID: ajxTF4M1weAJ
M Campus, M Flores, A Martinez, F Toldrá - Meat Science, 2008 - Elsevier

The effect of high pressure on sliced and vacuum packaged commercial dry-cured pork loin was determined by analysing the induced colour changes, the residual enzymatic activities of cathepsins, aminopeptidases and dipeptidilpeptidases and the changes in the content of …

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Campus, M., Flores, M., Martinez, A., & Toldrá, F. (2008). Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin. Meat Science, 80(4), 1174-1181.
Campus, Marco, et al. "Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin." Meat Science 80.4 (2008): 1174-1181.
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Serum cystatin C as a potential biomarker for the evaluation COPD.

International journal of clinical and experimental medicine

Zhang Y, Zhu Y, Wu Y, Wang G, Xie X, Ke R, Li S, Liu L, Fen W, Li F, Li F, Li M.
PMID: 25664059
Int J Clin Exp Med. 2014 Dec 15;7(12):5484-90. eCollection 2014.

BACKGROUND: Imbalance between protease-antiprotease plays an important role in the pathogenesis of chronic obstructive pulmonary disease (COPD). Cystatin C in circulating blood is a cysteine protease inhibitor and contributes to elastolysis and tissue destruction.OBJECTIVES: The aims of the present...

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Zhang Y, Zhu Y, Wu Y, et al. Serum cystatin C as a potential biomarker for the evaluation COPD. Int J Clin Exp Med. 2014;7(12):5484-90
Zhang, Y., Zhu, Y., Wu, Y., Wang, G., Xie, X., Ke, R., Li, S., Liu, L., Fen, W., Li, F., Li, F., & Li, M. (2014). Serum cystatin C as a potential biomarker for the evaluation COPD. International journal of clinical and experimental medicine, 7(12), 5484-90.
Zhang, Yonghong, et al. "Serum cystatin C as a potential biomarker for the evaluation COPD." International journal of clinical and experimental medicine vol. 7,12 (2014): 5484-90.
Zhang Y, Zhu Y, Wu Y, Wang G, Xie X, Ke R, Li S, Liu L, Fen W, Li F, Li F, Li M. Serum cystatin C as a potential biomarker for the evaluation COPD. Int J Clin Exp Med. 2014 Dec 15;7(12):5484-90. eCollection 2014. PMID: 25664059; PMCID: PMC4307506.
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Early breast cancer screening using iron/iron oxide-based nanoplatforms with sub-femtomolar limits of detection.

Beilstein journal of nanotechnology

Udukala DN, Wang H, Wendel SO, Malalasekera AP, Samarakoon TN, Yapa AS, Abayaweera G, Basel MT, Maynez P, Ortega R, Toledo Y, Bossmann L, Robinson C, Janik KE, Koper OB, Li P, Motamedi M, Higgins DA, Gadbury G, Zhu G, Troyer DL, Bossmann SH.
PMID: 27335730
Beilstein J Nanotechnol. 2016 Mar 07;7:364-373. doi: 10.3762/bjnano.7.33. eCollection 2016.

Proteases, including matrix metalloproteinases (MMPs), tissue serine proteases, and cathepsins (CTS) exhibit numerous functions in tumor biology. Solid tumors are characterized by changes in protease expression levels by tumor and surrounding tissue. Therefore, monitoring protease levels in tissue samples...

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Udukala DN, Wang H, Wendel SO, et al. Early breast cancer screening using iron/iron oxide-based nanoplatforms with sub-femtomolar limits of detection. Beilstein J Nanotechnol. 2016;7:364-373doi: 10.3762/bjnano.7.33.
Udukala, D. N., Wang, H., Wendel, S. O., Malalasekera, A. P., Samarakoon, T. N., Yapa, A. S., Abayaweera, G., Basel, M. T., Maynez, P., Ortega, R., Toledo, Y., Bossmann, L., Robinson, C., Janik, K. E., Koper, O. B., Li, P., Motamedi, M., Higgins, D. A., Gadbury, G., Zhu, G., Troyer, D. L., & Bossmann, S. H. (2016). Early breast cancer screening using iron/iron oxide-based nanoplatforms with sub-femtomolar limits of detection. Beilstein journal of nanotechnology, 7364-373. https://doi.org/10.3762/bjnano.7.33
Udukala, Dinusha N, et al. "Early breast cancer screening using iron/iron oxide-based nanoplatforms with sub-femtomolar limits of detection." Beilstein journal of nanotechnology vol. 7 (2016): 364-373. doi: https://doi.org/10.3762/bjnano.7.33
Udukala DN, Wang H, Wendel SO, Malalasekera AP, Samarakoon TN, Yapa AS, Abayaweera G, Basel MT, Maynez P, Ortega R, Toledo Y, Bossmann L, Robinson C, Janik KE, Koper OB, Li P, Motamedi M, Higgins DA, Gadbury G, Zhu G, Troyer DL, Bossmann SH. Early breast cancer screening using iron/iron oxide-based nanoplatforms with sub-femtomolar limits of detection. Beilstein J Nanotechnol. 2016 Mar 07;7:364-373. doi: 10.3762/bjnano.7.33. eCollection 2016. PMID: 27335730; PMCID: PMC4901534.
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Matricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor Cells.

Frontiers in pharmacology

Ricard-Blum S, Vallet SD.
PMID: 26869928
Front Pharmacol. 2016 Feb 04;7:11. doi: 10.3389/fphar.2016.00011. eCollection 2016.

The extracellular matrix (ECM) is a source of bioactive fragments called matricryptins or matrikines resulting from the proteolytic cleavage of extracellular proteins (e.g., collagens, elastin, and laminins) and proteoglycans (e.g., perlecan). Matrix metalloproteinases (MMPs), cathepsins, and bone-morphogenetic protein-1 release...

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Ricard-Blum S, Vallet SD. Matricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor Cells. Front Pharmacol. 2016;7:11doi: 10.3389/fphar.2016.00011.
Ricard-Blum, S., & Vallet, S. D. (2016). Matricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor Cells. Frontiers in pharmacology, 711. https://doi.org/10.3389/fphar.2016.00011
Ricard-Blum, Sylvie, and Vallet, Sylvain D. "Matricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor Cells." Frontiers in pharmacology vol. 7 (2016): 11. doi: https://doi.org/10.3389/fphar.2016.00011
Ricard-Blum S, Vallet SD. Matricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor Cells. Front Pharmacol. 2016 Feb 04;7:11. doi: 10.3389/fphar.2016.00011. eCollection 2016. PMID: 26869928; PMCID: PMC4740388.
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Antigen expression on recurrent meningioma cells.

Radiology and oncology

Vranic A.
PMID: 22933900
Radiol Oncol. 2010 Jun;44(2):107-12. doi: 10.2478/v10019-010-0028-6. Epub 2010 May 24.

INTRODUCTION: Meningiomas are intracranial brain tumours that frequently recur. Recurrence rates up to 20% in 20 years for benign meningiomas, up to 80% for atypical meningiomas and up to 100% for malignant meningiomas, have been reported. The most important...

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Vranic A. Antigen expression on recurrent meningioma cells. Radiol Oncol. 2010;44(2):107-12doi: 10.2478/v10019-010-0028-6.
Vranic, A. (2010). Antigen expression on recurrent meningioma cells. Radiology and oncology, 44(2), 107-12. https://doi.org/10.2478/v10019-010-0028-6
Vranic, Andrej. "Antigen expression on recurrent meningioma cells." Radiology and oncology vol. 44,2 (2010): 107-12. doi: https://doi.org/10.2478/v10019-010-0028-6
Vranic A. Antigen expression on recurrent meningioma cells. Radiol Oncol. 2010 Jun;44(2):107-12. doi: 10.2478/v10019-010-0028-6. Epub 2010 May 24. PMID: 22933900; PMCID: PMC3423683.
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Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors.

Acta pharmaceutica Sinica. B

Siklos M, BenAissa M, Thatcher GR.
PMID: 26713267
Acta Pharm Sin B. 2015 Nov;5(6):506-19. doi: 10.1016/j.apsb.2015.08.001. Epub 2015 Sep 26.

Cysteine proteases continue to provide validated targets for treatment of human diseases. In neurodegenerative disorders, multiple cysteine proteases provide targets for enzyme inhibitors, notably caspases, calpains, and cathepsins. The reactive, active-site cysteine provides specificity for many inhibitor designs over...

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Siklos M, BenAissa M, Thatcher GR. Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors. Acta Pharm Sin B. 2015;5(6):506-19doi: 10.1016/j.apsb.2015.08.001.
Siklos, M., BenAissa, M., & Thatcher, G. R. (2015). Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors. Acta pharmaceutica Sinica. B, 5(6), 506-19. https://doi.org/10.1016/j.apsb.2015.08.001
Siklos, Marton, et al. "Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors." Acta pharmaceutica Sinica. B vol. 5,6 (2015): 506-19. doi: https://doi.org/10.1016/j.apsb.2015.08.001
Siklos M, BenAissa M, Thatcher GR. Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors. Acta Pharm Sin B. 2015 Nov;5(6):506-19. doi: 10.1016/j.apsb.2015.08.001. Epub 2015 Sep 26. PMID: 26713267; PMCID: PMC4675809.
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Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes.

Frontiers in chemistry

Löser R, Pietzsch J.
PMID: 26157794
Front Chem. 2015 Jun 23;3:37. doi: 10.3389/fchem.2015.00037. eCollection 2015.

Papain-like cysteine proteases bear an enormous potential as drug discovery targets for both infectious and systemic human diseases. The considerable progress in this field over the last two decades has also raised interest in the visualization of these enzymes...

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Löser R, Pietzsch J. Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes. Front Chem. 2015;3:37doi: 10.3389/fchem.2015.00037.
Löser, R., & Pietzsch, J. (2015). Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes. Frontiers in chemistry, 337. https://doi.org/10.3389/fchem.2015.00037
Löser, Reik, and Pietzsch, Jens. "Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes." Frontiers in chemistry vol. 3 (2015): 37. doi: https://doi.org/10.3389/fchem.2015.00037
Löser R, Pietzsch J. Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes. Front Chem. 2015 Jun 23;3:37. doi: 10.3389/fchem.2015.00037. eCollection 2015. PMID: 26157794; PMCID: PMC4477214.
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Cathepsin B and D are Localized at the Surface of Human Breast Cancer Cells.

Pathology oncology research : POR

Sameni M, Elliott E, Ziegler G, Fortgens PH, Dennison C, Sloane BF.
PMID: 11173567
Pathol Oncol Res. 1995;1(1):43-53. doi: 10.1007/BF02893583.

Alterations in trafficking of cathepsins B and D have been reported in human and animal tumors. In MCF10 human breast epithelial cells, altered trafficking of cathepsin B occurs during their progression from a preneoplastic to neoplastic state. We now...

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Sameni M, Elliott E, Ziegler G, et al. Cathepsin B and D are Localized at the Surface of Human Breast Cancer Cells. Pathol Oncol Res. 1995;1(1):43-53doi: 10.1007/BF02893583.
Sameni, M., Elliott, E., Ziegler, G., Fortgens, P. H., Dennison, C., & Sloane, B. F. (1995). Cathepsin B and D are Localized at the Surface of Human Breast Cancer Cells. Pathology oncology research : POR, 1(1), 43-53. https://doi.org/10.1007/BF02893583
Sameni, Mansoureh, et al. "Cathepsin B and D are Localized at the Surface of Human Breast Cancer Cells." Pathology oncology research : POR vol. 1,1 (1995): 43-53. doi: https://doi.org/10.1007/BF02893583
Sameni M, Elliott E, Ziegler G, Fortgens PH, Dennison C, Sloane BF. Cathepsin B and D are Localized at the Surface of Human Breast Cancer Cells. Pathol Oncol Res. 1995;1(1):43-53. doi: 10.1007/BF02893583. PMID: 11173567.
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[Mechanisms of joint destruction in rheumatoid arthritis].

Clinical calcium

Sohen S.
PMID: 15775076
Clin Calcium. 2003 Feb;13(2):154-7. doi: CliCa0302154157.

A variety of destructive enzymes are secreted by pannnus. Prominent among these are the various matrix metalloproteinases (MMPs) and cathepsins. These enzymes act upon collagen and the proteoglycan matrix, thereby destroying the central structure of articular cartilage. Other destructive...

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Sohen S. [Mechanisms of joint destruction in rheumatoid arthritis]. Clin Calcium. 2003;13(2):154-7doi: CliCa0302154157.
Sohen, S. (2003). [Mechanisms of joint destruction in rheumatoid arthritis]. Clinical calcium, 13(2), 154-7. https://doi.org/CliCa0302154157
Sohen, Satoshi. "[Mechanisms of joint destruction in rheumatoid arthritis]." Clinical calcium vol. 13,2 (2003): 154-7. doi: https://doi.org/CliCa0302154157
Sohen S. [Mechanisms of joint destruction in rheumatoid arthritis]. Clin Calcium. 2003 Feb;13(2):154-7. doi: CliCa0302154157. Japanese. PMID: 15775076.
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Immunotoxicity of gallium arsenide on antigen presentation: comparative study of intratracheal and intraperitoneal exposure routes.

Journal of immunotoxicology

Hartmann CB, Harrison MT, McCoy KL.
PMID: 18958654
J Immunotoxicol. 2005 Jan 01;2(1):1-9. doi: 10.1080/15476910590930083.

Gallium arsenide (GaAs) is a semiconductor utilized in electronics and computer industries. GaAs exposure of animals causes local inflammation and systemic immune suppression. Mice were administered 2 to 200 mg/kg GaAs. On day 5, intratracheal instillation increased lung weights...

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Hartmann CB, Harrison MT, McCoy KL. Immunotoxicity of gallium arsenide on antigen presentation: comparative study of intratracheal and intraperitoneal exposure routes. J Immunotoxicol. 2005;2(1):1-9doi: 10.1080/15476910590930083.
Hartmann, C. B., Harrison, M. T., & McCoy, K. L. (2005). Immunotoxicity of gallium arsenide on antigen presentation: comparative study of intratracheal and intraperitoneal exposure routes. Journal of immunotoxicology, 2(1), 1-9. https://doi.org/10.1080/15476910590930083
Hartmann, Constance B, et al. "Immunotoxicity of gallium arsenide on antigen presentation: comparative study of intratracheal and intraperitoneal exposure routes." Journal of immunotoxicology vol. 2,1 (2005): 1-9. doi: https://doi.org/10.1080/15476910590930083
Hartmann CB, Harrison MT, McCoy KL. Immunotoxicity of gallium arsenide on antigen presentation: comparative study of intratracheal and intraperitoneal exposure routes. J Immunotoxicol. 2005 Jan 01;2(1):1-9. doi: 10.1080/15476910590930083. PMID: 18958654.
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PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration.

Cell communication and signaling : CCS

Chaitanya GV, Steven AJ, Babu PP.
PMID: 21176168
Cell Commun Signal. 2010 Dec 22;8:31. doi: 10.1186/1478-811X-8-31.

The normal function of poly (ADP-ribose) polymerase-1 (PARP-1) is the routine repair of DNA damage by adding poly (ADP ribose) polymers in response to a variety of cellular stresses. Recently, it has become widely appreciated that PARP-1 also participates...

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Chaitanya GV, Steven AJ, Babu PP. PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration. Cell Commun Signal. 2010;8:31doi: 10.1186/1478-811X-8-31.
Chaitanya, G. V., Steven, A. J., & Babu, P. P. (2010). PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration. Cell communication and signaling : CCS, 831. https://doi.org/10.1186/1478-811X-8-31
Chaitanya, Ganta Vijay, et al. "PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration." Cell communication and signaling : CCS vol. 8 (2010): 31. doi: https://doi.org/10.1186/1478-811X-8-31
Chaitanya GV, Steven AJ, Babu PP. PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration. Cell Commun Signal. 2010 Dec 22;8:31. doi: 10.1186/1478-811X-8-31. PMID: 21176168; PMCID: PMC3022541.
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Isolation and immunochemical characterization of human cystitis C.

Bosnian journal of basic medical sciences

Begić L, Berbić S.
PMID: 16212561
Bosn J Basic Med Sci. 2002 Dec;2(1):12-5. doi: 10.17305/bjbms.2002.3576.

Cystatin C is a natural inhibitor of the cysteine proteinases papain, and mammalian lysosomal cathepsins B, H, L and S. This protein is thought to serve an important physiological role as a local regulator of enzyme activity. The changes...

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Begić L, Berbić S. Isolation and immunochemical characterization of human cystitis C. Bosn J Basic Med Sci. 2002;2(1):12-5doi: 10.17305/bjbms.2002.3576.
Begić, L., & Berbić, S. (2002). Isolation and immunochemical characterization of human cystitis C. Bosnian journal of basic medical sciences, 2(1), 12-5. https://doi.org/10.17305/bjbms.2002.3576
Begić, Lejla, and Berbić, Selma. "Isolation and immunochemical characterization of human cystitis C." Bosnian journal of basic medical sciences vol. 2,1 (2002): 12-5. doi: https://doi.org/10.17305/bjbms.2002.3576
Begić L, Berbić S. Isolation and immunochemical characterization of human cystitis C. Bosn J Basic Med Sci. 2002 Dec;2(1):12-5. doi: 10.17305/bjbms.2002.3576. PMID: 16212561.
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Showing 1 to 12 of 306 entries