2010, ISBN: 3642098800

[EAN: 9783642098802], Neubuch, [SC: 14.99], [PU: Springer Berlin Heidelberg], POST-TRANSLATIONALMODIFICATIONS; PROTEASOME; ENZYMES; THERAPY, Druck auf Anfrage Neuware - Printed after orde… Meer...

[EAN: 9783642098802], Neubuch, [SC: 14.99], [PU: Springer Berlin Heidelberg], POST-TRANSLATIONALMODIFICATIONS; PROTEASOME; ENZYMES; THERAPY, Druck auf Anfrage Neuware - Printed after ordering - The ubiquitin system has two major functions in eukaryotic cells: it r- ulates protein degradation, which is essential for normal cellular fu- tion and for the removal of potentially harmful, damaged, or misfolded proteins, and it controls protein activity by regulating protein protein interactions and subcellullar localization. The ubiquitin system is thus involved in processes as diverse as cell cycle progression, signal tra- duction, gene transcription, and DNA repair. Not surprisingly, defects in the ubiquitin system have been linked with numerous diseases such as cancer, in ammation, central nervous system disorders, and metabolic dysfunction. Ubiquitin is a highly conserved 76-amino acid protein which is transferred to its target protein in an ATP-dependent manner. This post-translational modi cation takes place in a hierarchical, three-step fashion involving an E1 ubiquitin-activating enzyme, an E2 ubiquit- conjugating enzyme, and an E3 ubiquitin ligase. Substrate speci city is predominantly controlled by members of a large family of E3 - zymes, which form complexes with the proteins that will be modi ed. This ultimately leads to the covalent attachment of the C-terminus of ubiquitin to usually an -amino group of a lysine residue in the targeted protein. Additional ubiquitin transfer to lysine-48 of ubiquitin itself will form a polyubiquitin chain, which usually targets the conjugate for degradation by the proteasome. By contrast, mono- or polyubiquityla- VI Preface tion involving lysine-63 is normally involved in the control of protein activity. Ubiquitylation can be reverted by deubiquitylating enzymes, of which approximately 95 exist in mammals. 208 pp. Englisch, Books<

2010, ISBN: 3642098800

[EAN: 9783642098802], Neubuch, [SC: 14.99], [PU: Springer Berlin Heidelberg], POST-TRANSLATIONALMODIFICATIONS; PROTEASOME; ENZYMES; THERAPY, Druck auf Anfrage Neuware - Printed after orde… Meer...

[EAN: 9783642098802], Neubuch, [SC: 14.99], [PU: Springer Berlin Heidelberg], POST-TRANSLATIONALMODIFICATIONS; PROTEASOME; ENZYMES; THERAPY, Druck auf Anfrage Neuware - Printed after ordering - The ubiquitin system has two major functions in eukaryotic cells: it r- ulates protein degradation, which is essential for normal cellular fu- tion and for the removal of potentially harmful, damaged, or misfolded proteins, and it controls protein activity by regulating protein protein interactions and subcellullar localization. The ubiquitin system is thus involved in processes as diverse as cell cycle progression, signal tra- duction, gene transcription, and DNA repair. Not surprisingly, defects in the ubiquitin system have been linked with numerous diseases such as cancer, in ammation, central nervous system disorders, and metabolic dysfunction. Ubiquitin is a highly conserved 76-amino acid protein which is transferred to its target protein in an ATP-dependent manner. This post-translational modi cation takes place in a hierarchical, three-step fashion involving an E1 ubiquitin-activating enzyme, an E2 ubiquit- conjugating enzyme, and an E3 ubiquitin ligase. Substrate speci city is predominantly controlled by members of a large family of E3 - zymes, which form complexes with the proteins that will be modi ed. This ultimately leads to the covalent attachment of the C-terminus of ubiquitin to usually an -amino group of a lysine residue in the targeted protein. Additional ubiquitin transfer to lysine-48 of ubiquitin itself will form a polyubiquitin chain, which usually targets the conjugate for degradation by the proteasome. By contrast, mono- or polyubiquityla- VI Preface tion involving lysine-63 is normally involved in the control of protein activity. Ubiquitylation can be reverted by deubiquitylating enzymes, of which approximately 95 exist in mammals., Books<

2010, ISBN: 9783642098802

Springer, Taschenbuch, Auflage: Softcover reprint of hardcover 1st ed. 2009, 208 Seiten, Publiziert: 2010-11-25T00:00:01Z, Produktgruppe: Buch, Hersteller-Nr.: 7 black & white illustratio… Meer...

Springer, Taschenbuch, Auflage: Softcover reprint of hardcover 1st ed. 2009, 208 Seiten, Publiziert: 2010-11-25T00:00:01Z, Produktgruppe: Buch, Hersteller-Nr.: 7 black & white illustrations, 32 colour, 0.55 kg, Medizin, Kategorien, Bücher, Medizinbedarf & Geräte, Wörterbücher & Nachschlagewerke, Medizin & Gesundheitsdienste, Fachbücher, Anatomie, Grundlagen, Chemie, Naturwissenschaften & Technik, Ingenieurwissenschaft & Technik, Allgemein, Biologie, Biowissenschaften, Jentsch, Stefan, Haendler, Bernhard, Springer, 2010<

ISBN: 9783642098802

Paperback, [PU: Springer-Verlag Berlin and Heidelberg GmbH & Co. KG], The ubiquitin system plays an essential role in numerous cellular processes by controlling protein stability and func… Meer...

Paperback, [PU: Springer-Verlag Berlin and Heidelberg GmbH & Co. KG], The ubiquitin system plays an essential role in numerous cellular processes by controlling protein stability and function. A deregulation of this system has been reported in various pathologies including cancer, neurodegenerative diseases and immune disorders. This book presents the developments in this field., Biochemistry<

2010, ISBN: 3642098800

gebonden uitgave

Softcover reprint of hardcover 1st ed. 2009 Kartoniert / Broschiert Medizin, allgemein, Medizinische Chemie, Pharmazeutische Chemie, Post-translationalmodifications; Proteasome; enzymes… Meer...

Softcover reprint of hardcover 1st ed. 2009 Kartoniert / Broschiert Medizin, allgemein, Medizinische Chemie, Pharmazeutische Chemie, Post-translationalmodifications; Proteasome; enzymes; therapy, mit Schutzumschlag 11, [PU:Springer Berlin Heidelberg; Springer-Verlag GmbH]<