LEADER 05384nam 2200673 450 001 9910830864303321 005 20230721030215.0 010 $a1-283-14037-3 010 $a9786613140371 010 $a3-527-62023-0 010 $a3-527-62030-3 035 $a(CKB)1000000000376042 035 $a(EBL)481471 035 $a(SSID)ssj0000354689 035 $a(PQKBManifestationID)11251831 035 $a(PQKBTitleCode)TC0000354689 035 $a(PQKBWorkID)10313583 035 $a(PQKB)11345541 035 $a(MiAaPQ)EBC481471 035 $a(OCoLC)212142247 035 $a(EXLCZ)991000000000376042 100 $a20160819h20082008 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aProtein degradation$hVol. 4$iThe ubiquitin-proteasome system and disease /$fedited by R. John Mayer, Aaron Ciechanover, Martin Rechsteiner 210 1$aWeinheim, Germany :$cWILEY-VCH Verlag GmbH & Co. KGaA,$d2008. 210 4$dİ2008 215 $a1 online resource (260 p.) 225 1 $aProtein Degradation ;$vv.8 300 $aDescription based upon print version of record. 311 $a3-527-31436-9 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aProtein 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-?B 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 327 $a1.3.1 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 327 $a2.7 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 327 $a4.2 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 327 $a5.2 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-?B and I?B?; 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) 327 $a6.4 Mechanism of ERQD 330 $aThis final volume in the series focuses on malfunctions of the ubiquitin-proteasome system and their role in human disease. The editors and authors represent unmatched expertise, comprising virtually all the top scientists in the field, including the pioneers of protein degradation research.From the contents:* Ubiquitin and cancer * Ubiquitin and liver cancer* Muscle atrophy* Aggresomes and human disease* Parkin and neurodegeneration* Chronic neurodegenerative diseases* Parkinson's disease* Ubiquitin and viruses* Druggability of the ubiquitin-proteas 410 0$aProtein Degradation 606 $aProteins$xMetabolism 606 $aUbiquitin 615 0$aProteins$xMetabolism. 615 0$aUbiquitin. 676 $a572.76 676 $a612.3/98 702 $aMayer$b R. J. 702 $aCiechanover$b Aaron J. 702 $aRechsteiner$b Martin 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910830864303321 996 $aProtein degradation$94049972 997 $aUNINA