2009
DOI: 10.2174/187152009789056877
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Proteases as Anti-Cancer Targets - Molecular and Biological Basis for Development of Inhibitor-Like Drugs Against Cancer

Abstract: The systematic improvement of methods used for unraveling physiological and pathological role of proteases, as well as for elucidation of relevant hydrolase structures contributes to the progress in the area of new inhibitor-like drugs development. Many of protease inhibitors have entered clinics and are now successfully applied for the treatment of various systemic disorders caused by deregulation of physiological processes governed by proteolytic enzymes, including cardiovascular, neurodegenerative and infla… Show more

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Cited by 15 publications
(8 citation statements)
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“…The search for chemical compounds to inhibit these proteinases is a topic of constant interest for anti-cancer therapeutics [56,57]. Notably, the bone metastasis-specific proteins identified in our proteomic study are enriched with the regulators of these proteinases.…”
Section: Discussionmentioning
confidence: 93%
“…The search for chemical compounds to inhibit these proteinases is a topic of constant interest for anti-cancer therapeutics [56,57]. Notably, the bone metastasis-specific proteins identified in our proteomic study are enriched with the regulators of these proteinases.…”
Section: Discussionmentioning
confidence: 93%
“…Much effort is invested in determining which metalloproteases to target and in designing highly selective and potent protease inhibitors based on the structural characteristics of individual target metalloproteases (Coussens et al 2002;Bialas and Kafarski 2009;Dorman et al 2010;Overall and Kleifeld 2006). Several proteases of the serine catalytic type have also been targeted for the design of specific protease inhibitors for use in cancer treatment, including the urokinase plasminogen activator and matriptase (Abbenante and Fairlie 2005;Bialas and Kafarski 2009;Ulisse et al 2009). The broad-range microbial inhibitors of serine, cysteine and threonine proteases, leupeptin and antipain, were also shown to inhibit malignant transformation (Vaccari et al 1999) or tumourigenesis (Hozumi et al 1972).…”
Section: Cancermentioning
confidence: 99%
“…The broad-range microbial inhibitors of serine, cysteine and threonine proteases, leupeptin and antipain, were also shown to inhibit malignant transformation (Vaccari et al 1999) or tumourigenesis (Hozumi et al 1972). Threonine catalytic type proteolysis is present in proteasomes, and several chemical classes of natural and synthetic proteasome inhibitors have been considered as anticancer agents because of their preferential antiproliferative and proapoptotic activity on cancer cells (Kisselev and Goldberg 2001;Abbenante and Fairlie 2005;Bialas and Kafarski 2009;Cecarini et al 2011;Chen et al 2011).…”
Section: Cancermentioning
confidence: 99%
“…It was revealed that the inhibitor was extremely robust, resistant to proteolysis (no N-or C-ends) which, coupled to its high potency of inhibition for such proteinases as matripatse, thrombin, kallikrein 4 etc. made it an excellent candidate for use as a template for further development of drugs for therapy against cancer, thromboembolism and other proteinase-related human pathologies (Li, et al, 2007;Luckett et al, 1999;Swedberg et al, 2009;Białas & Kafarski, 2009) or agents for plant protection against pests and pathogens.…”
Section: Unique Low-molecular Weight Cyclic Trypsin Inhibitor From Sumentioning
confidence: 99%