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Aspartic proteinases --- Congresses --- ASPARTIC PROTEINASES --- PHYSIOLOGY
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Aspartic proteinases --- Aspartic Proteinases --- Congresses. --- genetics --- congresses. --- physiology --- Congresses --- Aspartic proteinases - Congresses. --- Genetics --- Physiology
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Serpins constitute a superfamily of proteins that possess a unique tertiary structure and mechanism of proteinase inhibition. In humans, serpins constitute 10% of the plasma proteins and are best known as critical regulators of both the thrombotic and fibrinolytic systems. Serpins also participate in the regulation of the complement cascade, angiogenesis, tumor metastasis, apoptosis and innate immunity. Considering the importance of these molecules in regulating proteolytic cascades, it is not surprising to find that loss- and gain-of-function mutations result in significant human diseases. Ma
Serpins. --- Serpins --- Serine proteinases --- Physiological effect. --- Inhibitors
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The book details the synthesis of molecules designed to inhibit the hepatitis C virus (HCV) NS3 serine protease and the human aspartic protease BACE-1. It explores the relationships between potential inhibitors and the targeted enzymes while discussing the class of enzymes known as proteases. The book also discusses why such enzymes can be regarded as suitable targets for developing drugs to combat diseases. It presents the results of the design and synthesis of linear and macrocyclic NS3 protease inhibitors containing a novel trisubstituted cyclopentane moiety as an N-acyl-(4 bioisostere. The book is intended for researchers and students in the field of medicinal chemistry and drug design.
Aspartic Proteinases. --- Hepatitis C Virus. --- Enzyme Inhibitors.
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Cystatins. --- Cysteine proteinases --- Cystatin superfamily --- Proteins --- Inhibitors. --- Inhibitors
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Antiviral agents --- Viral proteinases --- Testing --- Congresses. --- Inhibitors --- Congresses.
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Serine proteinases --- Serpins --- Protein Kinases --- Inhibitors. --- Physiological effect.
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Cysteine proteinases --- Cysteine --- Endopeptidases --- Protease Inhibitors --- Congresses --- Inhibitors --- antagonists & inhibitors
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In Calpain Methods and Protocols, John S. Elce and a seasoned team of principal investigators present a set of proven and easily followed protocols for studying calpain. The methods include in vitro techniques for the detection, expression, purification, and assay of µ- and m-calpain, supplemented with a wide range of system and tissue models for studying both the physiological functions and the effects of inhibitors on calpain. The systems used include neural tissue, kidney, liver, the eye, and membrane fusion in muscle and erythrocytes, each in connection with hypoxia or other injury. Among the analytical techniques employed are casein zymography, immunofluorescence, and calpain activity assays. The authors also examine specific substrates that have been proposed for the calpains. Highly practical and readily repeatable, Calpain Methods and Protocols offers investigators involved in basic and clinically oriented calpain research a gold-standard collection of powerful experimental tools for discovering the nature and function of calpains.
Calpain --- Cysteine proteinases. --- Proteinase --- Calcium-dependent cysteine proteinase --- Cysteine proteinases --- Neurosciences. --- Neural sciences --- Neurological sciences --- Neuroscience --- Medical sciences --- Nervous system
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