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Protein degradation . Vol. 4 The ubiquitin-proteasome system and disease / / edited by R. John Mayer, Aaron Ciechanover, Martin Rechsteiner
| Protein degradation . Vol. 4 The ubiquitin-proteasome system and disease / / edited by R. John Mayer, Aaron Ciechanover, Martin Rechsteiner |
| Pubbl/distr/stampa | Weinheim, Germany : , : WILEY-VCH Verlag GmbH & Co. KGaA, , 2008 |
| Descrizione fisica | 1 online resource (260 p.) |
| Disciplina |
572.76
612.3/98 |
| Collana | Protein Degradation |
| Soggetto topico |
Proteins - Metabolism
Ubiquitin |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-283-14037-3
9786613140371 3-527-62023-0 3-527-62030-3 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin Signaling and Cancer Pathogenesis; 1.1 Introduction; 1.1.1 Ubiquitin Signaling Networks; 1.1.2 Ubiquitin-like Proteins; 1.2 Ubiquitin in Cancer Pathogenesis; 1.2.1 Ubiquitin in Cell Cycle Control; 1.2.2 Ubiquitin in the NF-κB Pathway; 1.2.3 Ubiquitin as a Signal in DNA Repair; 1.2.3.1 p53 Pathway; 1.2.3.2 BRCA1 and FANCD2; 1.2.3.3 PCNA and TLS Polymerases; 1.2.4 Ubiquitin Networks in Angiogenesis; 1.2.5 Ubiquitin Networks in Receptor Endocytosis; 1.3 Targeting Ubiquitin Networks in Cancers
1.3.1 Targeting Interactions between E3s and their Substrates1.3.2 Targeting the Proteasome; 1.3.3 Other Approaches; 1.4 Conclusions and Future Perspectives; 2 Regulation of the p53 Tumor-suppressor Protein by Ubiquitin and Ubiquitin-like Molecules; 2.1 Functional Domains of p53; 2.2 The Family of Ubiquitin-like Molecules; 2.3 E3 Ligases for p53; 2.4 Modification of p53 with Ubiquitin; 2.5 Requirements for Mdm2-mediated Ubiquitination of p53; 2.6 Regulation of p53 Ubiquitination; 2.6.1 E2 Conjugating Enzymes; 2.6.2 Interacting Proteins; 2.6.3 By Other Post-translational Modifications 2.7 De-ubiquitination of p532.8 SUMO-1/sentrin/smpt3; 2.9 NEDD8/Rub1; 2.10 Therapeutic Intervention through the Ubiquitin Pathway; 3 The Ubiquitin-Proteasome System in Epstein-Barr Virus Infection and Oncogenesis; 3.1 Introduction; 3.2 Viral Interference with the Ubiquitin-Proteasome System; 3.3 The EBV Life Cycle; 3.4 EBV and the Ubiquitin-Proteasome System; 3.4.1 EBNA1; 3.4.2 EBNA6 (EBNA3C); 3.4.3 LMP1; 3.4.4 LMP2; 3.4.5 BZLF1 (Zta) and BRLF1 (Rta); 3.4.6 BPLF1; 3.5 EBV-associated Malignancies; 3.6 Concluding Remarks; 4 HECT Ubiquitin-protein Ligases in Human Disease; 4.1 Introduction 4.2 Definition of HECT E3s4.3 Human HECT E3s and their Role in Disease; 4.4 E6-AP; 4.4.1 E6-AP and Cervical Cancer (Cancer of the Uterine Cervix); 4.4.2 E6-AP and Angelman Syndrome; 4.5 HECTH9; 4.6 HECT E3s with WW Domains; 4.6.1 Nedd4/Nedd4-2; 4.6.1.1 Nedd4/Nedd4-2 and Liddle's Syndrome; 4.6.1.2 Nedd4 and Retrovirus Budding; 4.6.2 Itch and the Immune Response; 4.6.3 Smurfs; 4.6.3.1 Smurfs and Cancer; 4.6.3.2 Smurfs and Bone Homeostasis; 4.7 Concluding Remarks; 5 Ubiquitin-independent Mechanisms of Substrate Recognition and Degradation by the Proteasome; 5.1 Introduction 5.2 Ubiquitin-independent Proteasome Substrates5.2.1 Ornithine Decarboxylase; 5.2.2 p21(Waf1/Cip1); 5.2.3 Retinoblastoma Protein; 5.2.4 p53 and p73; 5.2.5 Human Thymidylate Synthase; 5.2.6 Rpn4; 5.2.7 NF-κB and IκBα; 5.2.8 Steroid Receptor Co-activator-3; 5.2.9 c-Jun; 5.3 Mechanisms of Ubiquitin-independent Degradation; 5.4 Conclusion; 6 Endoplasmic Reticulum Protein Quality Control and Degradation; 6.1 Introduction; 6.2 ER-import, Folding and the Unfolded Protein Response; 6.3 General Principles and Components of ERQD (Endoplasmic Reticulum Quality Control and Protein Degradation) 6.4 Mechanism of ERQD |
| Record Nr. | UNINA-9910144007703321 |
| Weinheim, Germany : , : WILEY-VCH Verlag GmbH & Co. KGaA, , 2008 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein degradation . Vol. 4 The ubiquitin-proteasome system and disease / / edited by R. John Mayer, Aaron Ciechanover, Martin Rechsteiner
| Protein degradation . Vol. 4 The ubiquitin-proteasome system and disease / / edited by R. John Mayer, Aaron Ciechanover, Martin Rechsteiner |
| Pubbl/distr/stampa | Weinheim, Germany : , : WILEY-VCH Verlag GmbH & Co. KGaA, , 2008 |
| Descrizione fisica | 1 online resource (260 p.) |
| Disciplina |
572.76
612.3/98 |
| Collana | Protein Degradation |
| Soggetto topico |
Proteins - Metabolism
Ubiquitin |
| ISBN |
1-283-14037-3
9786613140371 3-527-62023-0 3-527-62030-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin Signaling and Cancer Pathogenesis; 1.1 Introduction; 1.1.1 Ubiquitin Signaling Networks; 1.1.2 Ubiquitin-like Proteins; 1.2 Ubiquitin in Cancer Pathogenesis; 1.2.1 Ubiquitin in Cell Cycle Control; 1.2.2 Ubiquitin in the NF-κB Pathway; 1.2.3 Ubiquitin as a Signal in DNA Repair; 1.2.3.1 p53 Pathway; 1.2.3.2 BRCA1 and FANCD2; 1.2.3.3 PCNA and TLS Polymerases; 1.2.4 Ubiquitin Networks in Angiogenesis; 1.2.5 Ubiquitin Networks in Receptor Endocytosis; 1.3 Targeting Ubiquitin Networks in Cancers
1.3.1 Targeting Interactions between E3s and their Substrates1.3.2 Targeting the Proteasome; 1.3.3 Other Approaches; 1.4 Conclusions and Future Perspectives; 2 Regulation of the p53 Tumor-suppressor Protein by Ubiquitin and Ubiquitin-like Molecules; 2.1 Functional Domains of p53; 2.2 The Family of Ubiquitin-like Molecules; 2.3 E3 Ligases for p53; 2.4 Modification of p53 with Ubiquitin; 2.5 Requirements for Mdm2-mediated Ubiquitination of p53; 2.6 Regulation of p53 Ubiquitination; 2.6.1 E2 Conjugating Enzymes; 2.6.2 Interacting Proteins; 2.6.3 By Other Post-translational Modifications 2.7 De-ubiquitination of p532.8 SUMO-1/sentrin/smpt3; 2.9 NEDD8/Rub1; 2.10 Therapeutic Intervention through the Ubiquitin Pathway; 3 The Ubiquitin-Proteasome System in Epstein-Barr Virus Infection and Oncogenesis; 3.1 Introduction; 3.2 Viral Interference with the Ubiquitin-Proteasome System; 3.3 The EBV Life Cycle; 3.4 EBV and the Ubiquitin-Proteasome System; 3.4.1 EBNA1; 3.4.2 EBNA6 (EBNA3C); 3.4.3 LMP1; 3.4.4 LMP2; 3.4.5 BZLF1 (Zta) and BRLF1 (Rta); 3.4.6 BPLF1; 3.5 EBV-associated Malignancies; 3.6 Concluding Remarks; 4 HECT Ubiquitin-protein Ligases in Human Disease; 4.1 Introduction 4.2 Definition of HECT E3s4.3 Human HECT E3s and their Role in Disease; 4.4 E6-AP; 4.4.1 E6-AP and Cervical Cancer (Cancer of the Uterine Cervix); 4.4.2 E6-AP and Angelman Syndrome; 4.5 HECTH9; 4.6 HECT E3s with WW Domains; 4.6.1 Nedd4/Nedd4-2; 4.6.1.1 Nedd4/Nedd4-2 and Liddle's Syndrome; 4.6.1.2 Nedd4 and Retrovirus Budding; 4.6.2 Itch and the Immune Response; 4.6.3 Smurfs; 4.6.3.1 Smurfs and Cancer; 4.6.3.2 Smurfs and Bone Homeostasis; 4.7 Concluding Remarks; 5 Ubiquitin-independent Mechanisms of Substrate Recognition and Degradation by the Proteasome; 5.1 Introduction 5.2 Ubiquitin-independent Proteasome Substrates5.2.1 Ornithine Decarboxylase; 5.2.2 p21(Waf1/Cip1); 5.2.3 Retinoblastoma Protein; 5.2.4 p53 and p73; 5.2.5 Human Thymidylate Synthase; 5.2.6 Rpn4; 5.2.7 NF-κB and IκBα; 5.2.8 Steroid Receptor Co-activator-3; 5.2.9 c-Jun; 5.3 Mechanisms of Ubiquitin-independent Degradation; 5.4 Conclusion; 6 Endoplasmic Reticulum Protein Quality Control and Degradation; 6.1 Introduction; 6.2 ER-import, Folding and the Unfolded Protein Response; 6.3 General Principles and Components of ERQD (Endoplasmic Reticulum Quality Control and Protein Degradation) 6.4 Mechanism of ERQD |
| Record Nr. | UNINA-9910830864303321 |
| Weinheim, Germany : , : WILEY-VCH Verlag GmbH & Co. KGaA, , 2008 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||