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The ubiquitin-proteasome proteolytic system [[electronic resource] ] : from classical biochemistry to human diseases / / editors, Aaron J. Ciechanover, Maria G. Masucci
| The ubiquitin-proteasome proteolytic system [[electronic resource] ] : from classical biochemistry to human diseases / / editors, Aaron J. Ciechanover, Maria G. Masucci |
| Pubbl/distr/stampa | New Jersey, : World Scientific, c2002 |
| Descrizione fisica | 1 online resource (242 p.) |
| Disciplina | 612/.01575 |
| Altri autori (Persone) |
CiechanoverAaron J
MasucciMaria G |
| Collana | Recent advances in human biology |
| Soggetto topico |
Ubiquitin
Proteolytic enzymes Proteins - Metabolism |
| Soggetto genere / forma | Electronic books. |
| ISBN | 981-277-687-7 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Contents ; Preface ; The Ubiquitin System and Some of Its Roles in Cell Cycle Control ; References ; The Ubiquitin System and the N-End Rule Pathway ; Summary ; The Ubiquitin System ; The N-End Rule Pathway ; Physical Association of Ubiquitin Ligases and the 26S Proteasome
Peptide Import and the N-End Rule Pathway The N-End Rule Pathway and Fidelity of Chromosome Segregation ; Concluding Remarks ; References ; Phosphorylation-Dependent Substrate Recognition in Ubiquitin-Mediated Proteolysis ; Abstract Modular Protein Interaction Domains Regulate Dynamic Cellular Behaviour Protein-Protein Interactions Determine Specificity in Ubiquitin-Mediated Proteolysis ; Cdk Activity and the Control of DNA Replication ; Discovery of SCF Ubiquitin Ligases Phosphorylation-Dependent Substrate Recognition by SCF Complexes Conservation of SCF Function in the Cell Cycle ; The Cdc4 Phospho-Degron ; Multi-Site Phosphorylation and Ultrasensitivity ; The Sicl-Cdc4 Interaction: Theoretical Considerations ; Discussion ; Prospects ; References The 26S Proteasome: A Supramolecular Assembly Designed for Controlled Proteolysis Introduction ; Structural Features of the 26S Proteasome ; Conclusions ; References ; Mechanisms and Regulation of Ubiquitin-Mediated Limited Processing of the NF-kBa Precursor Protein p105 ; Summary Introduction |
| Record Nr. | UNINA-9910450813603321 |
| New Jersey, : World Scientific, c2002 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
The ubiquitin-proteasome proteolytic system [[electronic resource] ] : from classical biochemistry to human diseases / / editors, Aaron J. Ciechanover, Maria G. Masucci
| The ubiquitin-proteasome proteolytic system [[electronic resource] ] : from classical biochemistry to human diseases / / editors, Aaron J. Ciechanover, Maria G. Masucci |
| Pubbl/distr/stampa | New Jersey, : World Scientific, c2002 |
| Descrizione fisica | 1 online resource (242 p.) |
| Disciplina | 612/.01575 |
| Altri autori (Persone) |
CiechanoverAaron J
MasucciMaria G |
| Collana | Recent advances in human biology |
| Soggetto topico |
Ubiquitin
Proteolytic enzymes Proteins - Metabolism |
| ISBN | 981-277-687-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Contents ; Preface ; The Ubiquitin System and Some of Its Roles in Cell Cycle Control ; References ; The Ubiquitin System and the N-End Rule Pathway ; Summary ; The Ubiquitin System ; The N-End Rule Pathway ; Physical Association of Ubiquitin Ligases and the 26S Proteasome
Peptide Import and the N-End Rule Pathway The N-End Rule Pathway and Fidelity of Chromosome Segregation ; Concluding Remarks ; References ; Phosphorylation-Dependent Substrate Recognition in Ubiquitin-Mediated Proteolysis ; Abstract Modular Protein Interaction Domains Regulate Dynamic Cellular Behaviour Protein-Protein Interactions Determine Specificity in Ubiquitin-Mediated Proteolysis ; Cdk Activity and the Control of DNA Replication ; Discovery of SCF Ubiquitin Ligases Phosphorylation-Dependent Substrate Recognition by SCF Complexes Conservation of SCF Function in the Cell Cycle ; The Cdc4 Phospho-Degron ; Multi-Site Phosphorylation and Ultrasensitivity ; The Sicl-Cdc4 Interaction: Theoretical Considerations ; Discussion ; Prospects ; References The 26S Proteasome: A Supramolecular Assembly Designed for Controlled Proteolysis Introduction ; Structural Features of the 26S Proteasome ; Conclusions ; References ; Mechanisms and Regulation of Ubiquitin-Mediated Limited Processing of the NF-kBa Precursor Protein p105 ; Summary Introduction |
| Record Nr. | UNINA-9910777054103321 |
| New Jersey, : World Scientific, c2002 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
The ubiquitin-proteasome proteolytic system [[electronic resource] ] : from classical biochemistry to human diseases / / editors, Aaron J. Ciechanover, Maria G. Masucci
| The ubiquitin-proteasome proteolytic system [[electronic resource] ] : from classical biochemistry to human diseases / / editors, Aaron J. Ciechanover, Maria G. Masucci |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | New Jersey, : World Scientific, c2002 |
| Descrizione fisica | 1 online resource (242 p.) |
| Disciplina | 612/.01575 |
| Altri autori (Persone) |
CiechanoverAaron J
MasucciMaria G |
| Collana | Recent advances in human biology |
| Soggetto topico |
Ubiquitin
Proteolytic enzymes Proteins - Metabolism |
| ISBN | 981-277-687-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Contents ; Preface ; The Ubiquitin System and Some of Its Roles in Cell Cycle Control ; References ; The Ubiquitin System and the N-End Rule Pathway ; Summary ; The Ubiquitin System ; The N-End Rule Pathway ; Physical Association of Ubiquitin Ligases and the 26S Proteasome
Peptide Import and the N-End Rule Pathway The N-End Rule Pathway and Fidelity of Chromosome Segregation ; Concluding Remarks ; References ; Phosphorylation-Dependent Substrate Recognition in Ubiquitin-Mediated Proteolysis ; Abstract Modular Protein Interaction Domains Regulate Dynamic Cellular Behaviour Protein-Protein Interactions Determine Specificity in Ubiquitin-Mediated Proteolysis ; Cdk Activity and the Control of DNA Replication ; Discovery of SCF Ubiquitin Ligases Phosphorylation-Dependent Substrate Recognition by SCF Complexes Conservation of SCF Function in the Cell Cycle ; The Cdc4 Phospho-Degron ; Multi-Site Phosphorylation and Ultrasensitivity ; The Sicl-Cdc4 Interaction: Theoretical Considerations ; Discussion ; Prospects ; References The 26S Proteasome: A Supramolecular Assembly Designed for Controlled Proteolysis Introduction ; Structural Features of the 26S Proteasome ; Conclusions ; References ; Mechanisms and Regulation of Ubiquitin-Mediated Limited Processing of the NF-kBa Precursor Protein p105 ; Summary Introduction |
| Record Nr. | UNINA-9910828735403321 |
| New Jersey, : World Scientific, c2002 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||