Jentsch Bernhard (25 results)

Condition: 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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Condition: 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 proteinżprotein 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.

Condition: New. In.

Condition: New. In.

Taschenbuch. Condition: 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]hartmann[at]springer[dot]com | Anbieter: preigu.

Buch. Condition: 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.

Taschenbuch. Condition: 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.

Condition: New. pp. 208.

Hardcover. Condition: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

Paperback. Condition: Brand New. reprint edition. 207 pages. 9.00x6.00x0.49 inches. In Stock.

Hardcover. Condition: Brand New. 1st edition. 190 pages. 8.25x6.00x0.75 inches. In Stock.

Paperback. Condition: Like New. Like New. book.

Leather Bound. Condition: New. Language: German. Language: German. Presenting an Exquisite Leather-Bound Edition, expertly crafted with Original Natural Leather that gracefully adorns the spine and corners. The allure continues with Golden Leaf Printing that adds a touch of elegance, while Hand Embossing on the rounded spine lends an artistic flair. This masterpiece has been meticulously reprinted in 2024, utilizing the invaluable guidance of the original edition published many years ago in 1897. The contents of this book are presented in classic black and white. Its durability is ensured through a meticulous sewing binding technique, enhancing its longevity. Imprinted on top-tier quality paper. A team of professionals has expertly processed each page, delicately preserving its content without alteration. Due to the vintage nature of these books, every page has been manually restored for legibility. However, in certain instances, occasional blurriness, missing segments, or faint black spots might persist. We sincerely hope for your understanding of the challenges we faced with these books. Recognizing their significance for readers seeking insight into our historical treasure, we've diligently restored and reissued them. Our intention is to offer this valuable resource once again. We eagerly await your feedback, hoping that you'll find it appealing and will generously share your thoughts and recommendations. Lang: - German, Pages: - 52, Print on Demand. If it is a multi-volume set, then it is only a single volume. We are specialised in Customisation of books, if you wish to opt different color leather binding, you may contact us. This service is chargeable. Product Disclaimer: Kindly be informed that, owing to the inherent nature of leather as a natural material, minor discolorations or textural variations may be perceptible. Explore the FOLIO EDITION (12x19 Inches): Available Upon Request. 52 52.

Leatherbound. Condition: NEW. BOOKS ARE EXEMPT FROM IMPORT DUTIES AND TARIFFS; NO EXTRA CHARGES APPLY. Leatherbound edition. Condition: New. Leather Binding on Spine and Corners with Golden leaf printing on spine. Bound in genuine leather with Satin ribbon page markers and Spine with raised gilt bands. Pages: 52. A perfect gift for your loved ones. Reprinted from 1897 edition. NO changes have been made to the original text. This is NOT a retyped or an ocr'd reprint. Illustrations, Index, if any, are included in black and white. Each page is checked manually before printing. As this print on demand book is reprinted from a very old book, there could be some missing or flawed pages, but we always try to make the book as complete as possible. Fold-outs, if any, are not part of the book. If the original book was published in multiple volumes then this reprint is of only one volume, not the whole set. IF YOU WISH TO ORDER PARTICULAR VOLUME OR ALL THE VOLUMES YOU CAN CONTACT US. Resized as per current standards. Sewing binding for longer life, where the book block is actually sewn (smythe sewn/section sewn) with thread before binding which results in a more durable type of binding. Language: German Pages: 52.

Condition: new. Questo è un articolo print on demand.

Taschenbuch. Condition: 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.

Buch. Condition: 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.

Condition: 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.- .

Gebunden. Condition: 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.- .

Taschenbuch. Condition: 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.- Transcriptional 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.

Buch. Condition: 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.- Transcriptional 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.

Condition: New. Print on Demand pp. 208 38 Illus. (32 Col.).

Condition: New. PRINT ON DEMAND pp. 208.