05384nam 2200673 450 991083086430332120230721030215.01-283-14037-397866131403713-527-62023-03-527-62030-3(CKB)1000000000376042(EBL)481471(SSID)ssj0000354689(PQKBManifestationID)11251831(PQKBTitleCode)TC0000354689(PQKBWorkID)10313583(PQKB)11345541(MiAaPQ)EBC481471(OCoLC)212142247(EXLCZ)99100000000037604220160819h20082008 uy 0engur|n|---|||||txtccrProtein degradationVol. 4The ubiquitin-proteasome system and disease /edited by R. John Mayer, Aaron Ciechanover, Martin RechsteinerWeinheim, Germany :WILEY-VCH Verlag GmbH & Co. KGaA,2008.©20081 online resource (260 p.)Protein Degradation ;v.8Description based upon print version of record.3-527-31436-9 Includes bibliographical references at the end of each chapters and index.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 Cancers1.3.1 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 Modifications2.7 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 Introduction4.2 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 Introduction5.2 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 ERQDThis final volume in the series focuses on malfunctions of the ubiquitin-proteasome system and their role in human disease. The editors and authors represent unmatched expertise, comprising virtually all the top scientists in the field, including the pioneers of protein degradation research.From the contents:* Ubiquitin and cancer * Ubiquitin and liver cancer* Muscle atrophy* Aggresomes and human disease* Parkin and neurodegeneration* Chronic neurodegenerative diseases* Parkinson's disease* Ubiquitin and viruses* Druggability of the ubiquitin-proteasProtein DegradationProteinsMetabolismUbiquitinProteinsMetabolism.Ubiquitin.572.76612.3/98Mayer R. J.Ciechanover Aaron J.Rechsteiner MartinMiAaPQMiAaPQMiAaPQBOOK9910830864303321Protein degradation4049972UNINA