Stefan jentsch (23 resultados)
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Librería: Antiquariat Kretzer, Kirchhain-Emsdorf, AlemaniaAntiquariat Kretzer
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Condición: Wie neu. XV, 190 Seiten. Mit 39 Abbildungen. Neuwertiges Exemplar. / As new. ISBN: 9783540851066 Sprache: Englisch Gewicht in Gramm: 990 8° (17,5-22,5 cm). Orig.-Pappband. [Hardcover / fest gebunden].
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Librería: Romtrade Corp., STERLING HEIGHTS, MI, Estados Unidos de AmericaRomtrade Corp.
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Condición: New. This is a Brand-new US Edition. This Item may be shipped from US or any other country as we have multiple locations worldwide.
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Librería: Basi6 International, Irving, TX, Estados Unidos de AmericaBasi6 International
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Librería: Buchpark, Trebbin, AlemaniaBuchpark
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Condición: Sehr gut. Zustand: Sehr gut | Sprache: Englisch | Produktart: Bücher | 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.
The Ubiquitin System in Health and Disease (Ernst Schering Foundation Symposium Proceedings, 2008/1)
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Librería: Ria Christie Collections, Uxbridge, Reino UnidoRia Christie Collections
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The Ubiquitin System in Health and Disease (Ernst Schering Foundation Symposium Proceedings, 2008/1)
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Librería: preigu, Osnabrück, Alemaniapreigu
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EUR 140,00
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Taschenbuch. Condición: Neu. The Ubiquitin System in Health and Disease | Stefan Jentsch (u. a.) | Taschenbuch | Ernst Schering Foundation Symposium Proceedings | xvi | Englisch | 2010 | Springer | EAN 9783642098802 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartma…nn[at]springer[dot]com | Anbieter: preigu.
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Buch. Condición: Neu. 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 activit…y 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.
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Librería: AHA-BUCH GmbH, Einbeck, AlemaniaAHA-BUCH GmbH
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Taschenbuch. Condición: Neu. 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.
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Librería: Books Puddle, New York, NY, Estados Unidos de AmericaBooks Puddle
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EUR 237,29
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Condición: New. pp. 208.
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Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books
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Hardcover. Condición: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
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Librería: Revaluation Books, Exeter, Reino UnidoRevaluation Books
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Paperback. Condición: Brand New. reprint edition. 207 pages. 9.00x6.00x0.49 inches. In Stock.
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Librería: Revaluation Books, Exeter, Reino UnidoRevaluation Books
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Hardcover. Condición: Brand New. 1st edition. 190 pages. 8.25x6.00x0.75 inches. In Stock.
The Ubiquitin System in Health and Disease (Ernst Schering Foundation Symposium Proceedings, 2008/1)
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Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books
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Librería: Brook Bookstore On Demand, Napoli, NA, ItaliaBrook Bookstore On Demand
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Condición: new. Questo è un articolo print on demand.
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Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, AlemaniaBuchWeltWeit Ludwig Meier e.K.
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Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -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 c…ontrols 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.
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Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, AlemaniaBuchWeltWeit Ludwig Meier e.K.
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Buch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -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.
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Librería: moluna, Greven, Alemaniamoluna
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Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Latest findings in the field of ubiquitin and proteasome researchBiochmemical, genetic and structural aspects are presented by top specialists to the fieldCrosstalk Between the SUMO and Ubiquitin Pathways.- A Tale of…Two Giant Proteases.- .
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Librería: moluna, Greven, Alemaniamoluna
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Gebunden. Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Latest findings in the field of ubiquitin and proteasome researchBiochmemical, genetic and structural aspects are presented by top specialists to the fieldCrosstalk Between the SUMO and Ubiquitin Pathways.-…A Tale of Two Giant Proteases.- .
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Librería: buchversandmimpf2000, Emtmannsberg, BAYE, Alemaniabuchversandmimpf2000
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Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Crosstalk Between the SUMO and Ubiquitin Pathways.- A Tale of Two Giant Proteases.- Molecular Genetics of the Ubiquitin-Proteasome System: Lessons from Yeast.- Less Is More: How Protein Degradation Regulates Muscle Development.- Transcr…iptional Control and the Ubiquitin-Proteasome System.- Ubiquitination of Myc: Proteasomal Degradation and Beyond.- Regulation of Apoptosis and Cytokinesis by the Anti-apoptotic E2/E3 Ubiquitin-Ligase BRUCE.- Dissecting Roles of Ubiquitination in the p53 Pathway.- Regulation of T Cell Differentiation and Allergic Responses by the E3 Ubiquitin Ligase Itch.- Approaches to Discovering Drugs that Regulate E3 Ubiquitin Ligases.- Inhibiting Hdm2 and Ubiquitin-Activating Enzyme: Targeting the Ubiquitin Conjugating System in Cancer.Springer-Verlag KG, Sachsenplatz 4-6, 1201 Wien 208 pp. Englisch.
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Buch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Crosstalk Between the SUMO and Ubiquitin Pathways.- A Tale of Two Giant Proteases.- Molecular Genetics of the Ubiquitin-Proteasome System: Lessons from Yeast.- Less Is More: How Protein Degradation Regulates Muscle Development.- Transcriptiona…l Control and the Ubiquitin-Proteasome System.- Ubiquitination of Myc: Proteasomal Degradation and Beyond.- Regulation of Apoptosis and Cytokinesis by the Anti-apoptotic E2/E3 Ubiquitin-Ligase BRUCE.- Dissecting Roles of Ubiquitination in the p53 Pathway.- Regulation of T Cell Differentiation and Allergic Responses by the E3 Ubiquitin Ligase Itch.- Approaches to Discovering Drugs that Regulate E3 Ubiquitin Ligases.- Inhibiting Hdm2 and Ubiquitin-Activating Enzyme: Targeting the Ubiquitin Conjugating System in Cancer.Springer-Verlag KG, Sachsenplatz 4-6, 1201 Wien 208 pp. Englisch.
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Librería: Majestic Books, Hounslow, Reino UnidoMajestic Books
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Condición: New. Print on Demand pp. 208 38 Illus. (32 Col.).
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Librería: Biblios, frankfurt am main, HESSE, AlemaniaBiblios
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Condición: New. PRINT ON DEMAND pp. 208.
