Proteases structure function (38 resultados)

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Hardback or Cased Book. Condición: New. Proteases: From Basic Structure to Function to Drug Design as Targeted Therapy. Book.

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Condición: Good. This is an ex-library book and may have the usual library/used-book markings inside.This book has hardback covers. In good all round condition. Dust jacket in good condition. Please note the Image in this listing is a stock photo and may not match the covers of the actual item,900grams, ISBN:0306326957.…

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Paperback. Condición: Brand New. 364 pages. 9.70x6.70x0.80 inches. In Stock.

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Taschenbuch. Condición: Neu. Druck auf Anfrage Neuware - Printed after ordering - In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been pub lished. Their coverage of acid proteases has been limited, mainly due to the lack of significant new information on the structure of these enzymes. In the last four years, however, the primary and tertiary structures of a number of acid proteases have been deter mined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that the 'Conference on Acid Proteases: Structure, Function, and Biology' was organized. It took place at the University of Oklahoma on November 21-24, 1976. This book is a collection of the main lectures delivered at the Conference. Acid Proteases, by definition refers to a group of proteases having an optimal pH in acidic solutions. The classic examples are pepsin and chymosin. Some catalytic features are obviously shared by these proteases, most notably, their inhibition by pepstatin. The use of active center-directed inactivators such as diazoacetyl norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has shown that two catalytic aspartyl residues are present in most of these enzymes. These apparent cornmon features have prompted the suggestion by several investigators to name this group of enzymes 'aspartyl proteases' or 'carboxyl proteases'.…

Buch. Condición: Neu. Druck auf Anfrage Neuware - Printed after ordering - Proteolysis is an irreversible posttranslational modification affecting each and every protein from its biosynthesis to its degradation. Limited proteolysis regulates targeting and activity throughout the lifetime of proteins. Balancing proteolysis is therefore crucial for physiological homeostasis. Control mechanisms include proteolytic maturation of zymogens resulting in active proteases and the shut down of proteolysis by counteracting endogenous protease inhibitors. Beyond the protein level, proteolytic enzymes are involved in key decisions during development that determine life and death from single cells to adult individuals. In particular, we are becoming aware of the subtle role that proteases play in signaling events within proteolysis networks, in which the enzymes act synergistically and form alliances in a web-like fashion. Proteases come in different flavors. At least five families of mechanistically distinct enzymes and even more inhibitor families are known to date, many family members are still to be studied in detail. We have learned a lot about the diversity of the about 600 proteases in the human genome and begin to understand their physiological roles in the degradome. However, there are still many open questions regarding their actions in pathophysiology. It is in this area where the development of small molecule inhibitors as therapeutic agents is extremely promising. Approaching proteolysis as the most important, irreversible post-translational protein modification essentially requires an integrated effort of complementary research disciplines. In fact, proteolytic enzymes seem as diverse as the scientists working with these intriguing proteins. This book reflects the efforts of many in this exciting field of research where team and network formations are essential to move ahead.…

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Buch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - In the two last decades, proteases have constituted one of the primary and important targets in drug discovery. The U.S. FDA has approved more than 12 protease therapies in the last 10 years, and a number of next-generation or completely new proteases are under clinical development. Protease inhibition strategies are one of the fastest expanding areas in the field of of drugs that show considerable promise. This Special Issue will focus on the recent advances in the discovery and development of protease inhibitors, covering the synthesis of protease inhibitors, the design of new chemical entities acting as inhibitors of special/particular types of proteases, and their mode of actions (Frolova et al. 2020; Slapak et al. 2020; Künnapuu et al. 2021). In addition, the new applications of these interesting compounds/biomolecules and their limitations have been discussed and described (Wang et al. 2020; Barto¿ová-Sojková et al. 2021).…