Isbn: 9781838804329 - ubiquitin: proteasome pathway (biochemistry, 18) (9 Ergebnisse)

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Buch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The ubiquitin-proteasome pathway consists of ubiquitin, substrate proteins, E1 enzymes, E2 enzymes, E3 enzymes, and proteasome, which acts in a series of enzymatic reaction chains to ubiquitinate substrate proteins such as surplus and misfolded proteins for degradation by the proteasome to maintain the balance between protein synthesis and degradation in a cell and tissue. Moreover, deubiquitinating enzymes can remove the attached ubiquitin chain, which results in a reverse ubiquitination-deubiquitination process involved in multiple biological processes in a cell and tissue. The changes of components in the ubiquitin-proteasome pathway are associated with multiple pathophysiological processes, such as cancers and neurodegenerative diseases. This book presents the new advances in concepts, analytical methodology, and application of ubiquitin-proteasome pathway for clarification of molecular mechanisms and discovery of new therapeutic targets and drugs in different diseases. 124 pp. Englisch.…

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Gebunden. Zustand: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. KlappentextrnrnThe ubiquitin-proteasome pathway consists of ubiquitin, substrate proteins, E1 enzymes, E2 enzymes, E3 enzymes, and proteasome, which acts in a series of enzymatic reaction chains to ubiquitinate substrate proteins such as surplus.…

Buch. Zustand: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The ubiquitin-proteasome pathway consists of ubiquitin, substrate proteins, E1 enzymes, E2 enzymes, E3 enzymes, and proteasome, which acts in a series of enzymatic reaction chains to ubiquitinate substrate proteins such as surplus and misfolded proteins for degradation by the proteasome to maintain the balance between protein synthesis and degradation in a cell and tissue. Moreover, deubiquitinating enzymes can remove the attached ubiquitin chain, which results in a reverse ubiquitination-deubiquitination process involved in multiple biological processes in a cell and tissue. The changes of components in the ubiquitin-proteasome pathway are associated with multiple pathophysiological processes, such as cancers and neurodegenerative diseases. This book presents the new advances in concepts, analytical methodology, and application of ubiquitin-proteasome pathway for clarification of molecular mechanisms and discovery of new therapeutic targets and drugs in different diseases.Books on Demand GmbH, Überseering 33, 22297 Hamburg 124 pp. Englisch.…

Buch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - The ubiquitin-proteasome pathway consists of ubiquitin, substrate proteins, E1 enzymes, E2 enzymes, E3 enzymes, and proteasome, which acts in a series of enzymatic reaction chains to ubiquitinate substrate proteins such as surplus and misfolded proteins for degradation by the proteasome to maintain the balance between protein synthesis and degradation in a cell and tissue. Moreover, deubiquitinating enzymes can remove the attached ubiquitin chain, which results in a reverse ubiquitination-deubiquitination process involved in multiple biological processes in a cell and tissue. The changes of components in the ubiquitin-proteasome pathway are associated with multiple pathophysiological processes, such as cancers and neurodegenerative diseases. This book presents the new advances in concepts, analytical methodology, and application of ubiquitin-proteasome pathway for clarification of molecular mechanisms and discovery of new therapeutic targets and drugs in different diseases.…

Buch. Zustand: Neu. Ubiquitin | Proteasome Pathway | Xianquan Zhan (u. a.) | Buch | Biochemistry, Volume 18 | Gebunden | Englisch | 2020 | IntechOpen | EAN 9781838804329 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.…