Zacytuj

1. Ploeg M, Aben KK, Kiemeney LA. The present and future burden of urinary bladder cancer in the world. World J Urol. 2009;27(3):289-93.10.1007/s00345-009-0383-3269432319219610Search in Google Scholar

2. Murta-Nascimento C, Schmitz-Dräger BJ, Zeegers MP, Kogevinas G, Steineck M, Real FX, Malats N. Epidemiology of urinary bladder cancer: from tumor development to patient’s death. World J Urol. 2007;25:285-9510.1007/s00345-007-0168-517530260Search in Google Scholar

3. Aggarwal N, Sloane BF. Сathepsin B: multiple roles in cancer. Proteomics Clin Appl. 2014;8(5-6):427-37.10.1002/prca.201300105420594624677670Search in Google Scholar

4. Wolf K, Friedl P. Extracellular matrix determinants of proteolytic and non-proteolytic cell migration. Trends Cell Biol. 2011;21(12):736-44.10.1016/j.tcb.2011.09.00622036198Search in Google Scholar

5. Heutinck KM, Berge IJ, Hack CE, Hamann J, Rowshani AT. Serine proteases of the human immune system in health and disease. Mol Immunol. 2010;47(11-12):1943-5510.1016/j.molimm.2010.04.02020537709Search in Google Scholar

6. Hummel BC. Amodified spectrophotometric determination of chymotrypsin, trypsin and thrombin. Can J Biochem and Physiol. 1959;37:1393-9.10.1139/o59-157Search in Google Scholar

7. Nartykova VF, Paskhina TS. Unified method for determining the activity of α1-antitrypsin and α2-macroglobulin in serum (plasma) of human blood. Questions Med Chem. 1979;25(4):494-9.Search in Google Scholar

8. Nikolaichik VV, Moin VM, Kirasky VV. A method for the detection of “meddle-size molecules”. Lab Delo. 1993;10:11-8.Search in Google Scholar

9. Hoffman BD, Grashoff C, Schwartz MA. Dynamic molecular processes mediate cellular mechanotransduction. Nature. 2011;475:316-2310.1038/nature10316644968721776077Search in Google Scholar

10. Pranjol MZ, Gutowski N, Hannemann M, Whatmore J. The potential role of the proteases cathepsin D and cathepsin L in the progression and metastasis of epithelial ovarian cancer. Biomolecules. 2015;5(4):3260-79.10.3390/biom5043260469327726610586Search in Google Scholar

11. Wojtukiewicz MZ, Hempel D, Sierko E, Tucker SC, Honn KV. Protease-activated receptors (PARs)--biology and role in cancer invasion and metastasis. Cancer Metastasis Rev. 2015;34(4):775-96.10.1007/s10555-015-9599-4466121826573921Search in Google Scholar

12. Pavón MS, Arroyo-Solera I, Céspedes MV, Casanova I, León X, Mangues R. Silencing of plasminogen activator inhibitor-1 suppresses colorectal cancer progression and liver metastasis. Surgery. 2015;158(6):1704-13.10.1016/j.surg.2015.04.05326275833Search in Google Scholar

13. Mason SD, Joyce JA. Proteolytic networks in cancer. Trends Cell Biol. 2011;21(4):228-37.10.1016/j.tcb.2010.12.002384071521232958Search in Google Scholar

14. Ulrich D, Ulrich F, Unglaub F, Piatkowski A, Pallua N. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in patients with different types of scars and keloids. J Plast Reconstr Aesthet Surg. 2010;63(6):1015-21.10.1016/j.bjps.2009.04.02119464975Search in Google Scholar

15. Rakashanda S, Rana F, Rafiq S, Masood A, Amin S. Role of proteases in cancer: A review. Biotechnol Mol Biol Rev. 2012;7(4):90-101.10.5897/BMBR11.027Search in Google Scholar

16. Anariba DEI. Alpha1-Antitrypsin Deficiency. Medscape Reference. 2017. Available online at http://emedicine.medscape.com/article/295686-overview. Accessed February 2017.Search in Google Scholar

17. El-Akawi ZJ, Nusier MK, Sawalha DH. Alpha-1 antitrypsin genotypes in breast cancer patients. J Health Sci. 2008;54(4):493-6.10.1248/jhs.54.493Search in Google Scholar

18. Ahmed A Rehman, Haseeb Ahsan, Fahim HK. Alpha-2-macroglobulin: A physiological guardian. J Cell Physiol. 2013;228(8):1665-75.10.1002/jcp.2426623086799Search in Google Scholar

19. Ferrer IG, Marrero A, Xavier F, Gomis-Rüth, Goulas T. α2-Macroglobulins: Structure and Function. Macromolecular Protein Complexes. 2017;83:14983.Search in Google Scholar

20. Scherbina IN. The study of the diagnostic value of immunoregulatory proteins to assess the functional capacity of the fetoplacental complex with intrauterine infection. Br J Educ Scient Stud. 2016;1(23):833-8.Search in Google Scholar

21. Rehman AA, Ahsan H, Khan FH. Alpha-2-macroglobulin: a physiological guardian. J Cell Physiol. 2013;228:1665-75.10.1002/jcp.24266Search in Google Scholar

22. Zorin NA, Zorina VN, Zorina RM. Role of proteins of the macroglobulin family in regulation of tumor growth. Ontogenez. 2006;37(1):12-9.10.1134/S1062360406010024Search in Google Scholar

23. Lindner L, Hemdan NYA, Buchold M, Huse K, Bigl M, Oerlecke I, et al. α2-Macroglobulin inhibits the malignant properties of astrocytoma cells by impeding β-Catenin signaling. Ther Targets Chem Biol. 2010;70(1):277-87.10.1158/0008-5472.CAN-09-146220048078Search in Google Scholar

24. Korobov V, Bolesta I, Dika A, Korobova O, Savitsky V. Optical analysis of middle-molecular mass molecules of blood of individuals suffering from myocardial ischemia. Ukr J Phys Opt. 2012;3(1):35-42.10.3116/16091833/3/1/35/2002Search in Google Scholar

25. Chmielewski M, Cohen G, Wiecek A, Carrero J. The peptidic middle molecules: is a molecular weight doing the trick? Semin Nephrol. 2014;34:118-34.10.1016/j.semnephrol.2014.02.005Search in Google Scholar

26. Ishchuk TV, Raetska YaB, Savchuk OM, Ostapchenko LI. Changes blood protein composition under experimental chemical burns of esophageal development in rats. Biomed Res Ther. 2015;3(4):241-9.10.7603/s40730-015-0009-xSearch in Google Scholar

27. Nagoev BS, Nagoeva MK. Implication of middle-mass molecule peptides of blood plasma in assessment of intoxication syndrome in patients with bacterial tonsillitis. Vestn Otorinolaringol. 2016;6:41-4.Search in Google Scholar

eISSN:
2300-6676
ISSN:
2084-980X
Język:
Angielski
Częstotliwość wydawania:
4 razy w roku
Dziedziny czasopisma:
Medicine, Clinical Medicine, other, Pharmacology, Toxicology, Pharmacy