Listing 1 - 10 of 51 | << page >> |
Sort by
|
Choose an application
Choose an application
Choose an application
Proteinase --- Proteinase --- Proteinase --- Proteinase. --- Biotechnology. --- Inhibitors --- Biotechnology. --- Inhibitors.
Choose an application
Choose an application
Choose an application
Hepatitis C is an epidemic that affects about 200 million people worldwide. It is a liver inflammation caused by a virus of the flavivirus family. Depending on the country, hepatitis C does not have the same distribution within the population of the same country and between countries. HCV is transmitted through blood and all derived products, poorly sterilized material and re-use of needles. In the majority of cases a chronic phase installs that can progress to liver cirrhosis or cancer of the liver. HCV is a single-stranded positive-strand RNA virus. It is characterized by an important genetic polymorphism resulting in a varied genotype and a tropism immune and liver high. The degree of liver damage and type of genotype determines the decision to treat and support global infection. Pegylated dual is the classical treatment used mainly in countries with lower income. With the arrival of NS3/4A protease inhibitors, triple therapy replaces the dual therapy especially in genotype 1. One of the critical target for the replication process is the NS3/4A protease of HCV. Also a better understanding of the viral cycle development in testing effectives in vitro methods and characterization of NS3/4A viral protease, as potential target, has opened the door to the discovery of new molecules protease inhibitors. The first wave of its new drugs (boceprevir and telaprevir) which have been put on the market as early as 2011 are linear reversible covalent inhibitors. A second wave consists of non-covalent reversible inhibitors structure macrocyclic P1-P3 and P2-P4 either structure linear. Finally, other inhibitions strategies non peptidomimetrics are under investigations. L’hépatite C est une épidémie qui affecte environ 200 millions de personnes dans le monde. C’est une inflammation hépatique causée par un virus de la famille des flavivirus. L’hépatite C n’a pas la même distribution au sein de la population d’un même pays et entre les pays. Le VHC est transmis par le sang et tous les produits dérivés, les matériels ma stérilisés et les réutilisations des aiguilles. Dans la majorité des cas, une phase chronique s’installe pouvant évoluer vers une cirrhose hépatique, voire vers un cancer du foie. Le VHC est un virus à ARN monocaténaire à brin positif. Il est caractérisé par un polymorphisme génétique important se traduisant par un génotype varié et un tropisme hépatique et immunitaire élevé. Le degré de l’atteinte hépatique et le type de génotype conditionne la décision de traiter la prise en charge global de l’infection. La bithérapie pégylée est le traitement classique utilisé surtout dans les pays à moindre revenu. Ave l’arrivé des inhibiteurs de protéase NS3/4A, la trithérapie remplace la bithérapie particulièrement dans le génotype 1. L’une des cibles critiques est la protéase à sérine NS3/4A du VHC, impliquée dans la réplication. Aussi une meilleure compréhension du cycle viral par la mise au point de méthodes d’expérimentation in vitro efficaces et la caractérisation de la protéase NS3/4S, comme cible potentielle, a ouvert la porte à la découverte de nouvelles molécules antiprotéases. La première vague de ses nouveaux médicaments (bocéprévir et télaprévir) qui sont des inhibiteurs covalents linéaires réversibles. Une seconde vague est constitué par des inhibiteurs non covalents réversibles soit de structures macrocycliques P1-P3 ou P2-P4 soit de structure linéaires enfin d’autres stratégies d’inhibitions non peptidomimetiques sont en cours d’investigations.
Choose an application
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
Choose an application
Aphididae --- Aphididae --- Biopesticides --- Biopesticides --- Insecticides --- Insecticides --- Acyrthosiphon pisum --- Myzus persicae --- Myzus persicae --- Vicia faba --- Vicia faba --- Proteinase inhibitors --- Proteinase inhibitors
Choose an application
Enzymology --- Aspartic Acid Proteases. --- Metalloproteases. --- Peptide Hydrolases. --- Esteroproteases --- Peptidases --- Proteases --- Proteinases --- Proteolytic Enzymes --- Gene Products, pol --- Metallopeptidases --- Metalloproteinases --- Aspartyl Proteases --- Aspartic Acid Proteinases --- Aspartic Proteinases --- Aspartyl Proteinases --- Acid Proteases, Aspartic --- Proteases, Aspartic Acid --- Proteases, Aspartyl --- Proteinases, Aspartic --- Proteinases, Aspartic Acid --- Proteinases, Aspartyl --- Peptidase --- Peptide Hydrolase --- Protease --- Proteinase --- Proteolytic Enzyme --- Enzyme, Proteolytic --- Hydrolase, Peptide --- Metallopeptidase --- Metalloprotease --- Metalloproteinase --- Aspartic Acid Protease --- Aspartic Acid Proteinase --- Aspartic Proteinase --- Aspartyl Protease --- Aspartyl Proteinase --- Acid Protease, Aspartic --- Acid Proteinase, Aspartic --- Protease, Aspartic Acid --- Protease, Aspartyl --- Proteinase, Aspartic --- Proteinase, Aspartic Acid --- Proteinase, Aspartyl --- Aspartic Acid Proteases --- Metalloproteases --- Peptide Hydrolases
Choose an application
The chapters in this book thoroughly cover the structure, regulation, and function of matrix metalloproteinases, and provide information on the latest strategies to inhibit enzyme activity. This work will be an indispensable reference tool for investigators with an interest in extracellular matrix biology, matrix turnover, enzymology and biochemistry of proteinases, developmental biology, pathology, and therapeutic interventions.Key Features* Provides state-of-the-art information on a field with broad implications to many areas of biology* Includes detailed coverage of the stru
Metalloproteinases. --- Extracellular matrix proteins. --- Matrix proteins --- Metalloproteases --- Proteins --- Metalloenzymes --- Proteinase --- Extracellular matrix proteins --- Metalloproteinases
Listing 1 - 10 of 51 | << page >> |
Sort by
|