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Looking at the proteases from a simple perspective
Author(s) -
Castro Helena C.,
Abreu Paula A.,
Geraldo Reinaldo B.,
Martins Rita C.A.,
dos Santos Ruben,
Loureiro Natália I.V.,
Cabral Lúcio M.,
Rodrigues Carlos R.
Publication year - 2011
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.1091
Subject(s) - proteases , protease , trypanosoma cruzi , matrix metalloproteinase , thrombin , protease inhibitor (pharmacology) , biology , enzyme , biochemistry , chemistry , human immunodeficiency virus (hiv) , immunology , computer science , parasite hosting , platelet , world wide web , antiretroviral therapy , viral load
Proteases have received enormous interest from the research and medical communities because of their significant roles in several human diseases. Some examples include the involvement of thrombin in thrombosis, HIV‐1 protease in Acquired Immune Deficiency Syndrome, cruzain in Trypanosoma cruzi infection, and membrane‐type 1 matrix metalloproteinase in tumor invasion and metastasis. Many efforts has been undertaken to design effective inhibitors featuring potent inhibitory activity, specificity, and metabolic stability to those proteases involved in such pathologies. Protease inhibitors usually target the active site, but some of them act by other inhibitory mechanisms. The understanding of the structure‐function relationships of proteases and inhibitors has an impact on new inhibitor drugs designing. In this paper, the structures of four proteases (thrombin, HIV‐protease, cruzain, and a matrix metalloproteinase) are briefly reviewed, and used as examples of the importance of proteases for the development of new treatment strategies, leading to a longer and healthier life. Copyright © 2011 John Wiley & Sons, Ltd.