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Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System
Autore Mayer R. John
Pubbl/distr/stampa Hoboken, : Wiley, 2008
Descrizione fisica 1 online resource (254 p.)
Disciplina 572.76
612.3/98
Altri autori (Persone) CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Cell Physiology
Proteins - Metabolism
Proteins - metabolism
Proteins --Metabolism
Ubiquitin
Ubiquitin - physiology
Animal Biochemistry
Human Anatomy & Physiology
Health & Biological Sciences
Soggetto genere / forma Electronic books.
ISBN 1-282-37219-X
9786612372193
3-527-62022-2
3-527-62029-X
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin: A New Player in the Peroxisome Field; 1.1 Introduction; 1.2 Matrix Protein Import into Peroxisomes is Mediated by Cycling Receptors; 1.3 Pex5p is Monoubiquitinated in Wild-type Cells, but Polyubiquitinated in Late-acting pex Mutants; 1.4 Ubiquitination of Pex18p; 1.5 Role for the RING Finger and AAA Peroxins in Pex5p Ubiquitination and Recycling; 1.6 Pex5p Monoubiquitination: A Role in Receptor Recycling; 1.7 Conclusions/Future Prospects; Acknowledgements; References
2 The Ubiquitin Proteasome System and Muscle Development2.1 Introduction; 2.2 Muscle Histology; 2.3 UPS and Developing Muscle; 2.3.1 Ubiquitin-dependent Degradation of MyoD; 2.3.2 Degradation of MyoD by SCF(MAFbx); 2.3.3 Other Muscle Regulatory Factors; 2.4 UPS and Organizing Muscle; 2.4.1 Ozz-E3-dependent β-Catenin Regulation in the Muscle; 2.4.2 Regulation of Myosin Assembly by CHN-1 and UFD-2; 2.5 UPS and Muscle Destruction or Degeneration; 2.5.1 N-end Rule and Muscle Atrophy; 2.5.2 MuRFs, E3 Enzymes in Atrophying Muscles; 2.5.3 Atrogin-1/MAFbx Function in Muscle Atrophy
2.5.4 Activation of Muscle-atrophy Pathways2.6 Concluding Remarks; References; 3 The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development; 3.1 Introduction; 3.2 The Plant COP9 Signalosome; 3.3 CSN Involvement in the Ubiquitin-Proteasome Pathway; 3.4 Plant CSN Biochemical Activities; 3.4.1 Deneddylation; 3.4.2 Subcellular Partitioning; 3.5 CSN Functions in Plant Development; 3.5.1 Floral Development; 3.5.2 Responses to Plant Hormones; 3.5.3 Disease Resistance; 3.5.4 Photomorphogenesis; 3.6 Conclusions; References
4 Ubiquitin and Protein Sorting to the Lysosome4.1 Introduction; 4.2 Identification of Ubiquitin as an Endosomal Sorting Signal; 4.3 Ubiquitin-mediated Sorting at the Endosome: The MVB Sorting Machinery; 4.3.1 Endosome-associated Ubiquitin Interacting Domains: Structure and Function; 4.3.2 The Hrs-STAM Complex and the Endosomal Clathrin Coat; 4.3.3 GGA and Tom1: Alternative Sorting Adapters?; 4.3.4 The ESCRT Machinery; 4.3.5 Vps4-SKD1; 4.4 Ubiquitin Ligases and Endosomal Sorting; 4.4.1 Nedd4 Family; 4.4.2 c-Cbl; 4.5 Endosomal DUBs; 4.5.1 Ubp1 and Ubp2; 4.5.2 Doa4; 4.5.3 UBPY; 4.5.4 AMSH
4.6 Polyubiquitin Linkages and Endocytosis4.6.1 Proteasome Involvement in Endocytic Sorting; 4.6.2 K63-linked Ubiquitin; 4.7 Future Directions; Acknowledgements; References; 5 ISG15-dependent Regulation; 5.1 Introduction and Overview; 5.2 The Discovery of ISG15; 5.3 Structure and Properties of the ISG15 Protein; 5.4 The ISG15 Conjugation Pathway; 5.4.1 Activation of ISG15 by UbE1L; 5.4.2 UbcH8 is an ISG15-specific Conjugating Enzyme; 5.4.3 Candidate ISG15-specific Ligases; 5.5 Regulation of Intracellular ISG15 Pools; 5.6 Functional Roles for ISG15; 5.6.1 ISG15 as an Extracellular Cytokine
5.6.2 Role of ISG15 in the Antiviral Response
Record Nr. UNINA-9910144008003321
Mayer R. John  
Hoboken, : Wiley, 2008
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System
Autore Mayer R. John
Pubbl/distr/stampa Hoboken, : Wiley, 2008
Descrizione fisica 1 online resource (254 p.)
Disciplina 572.76
612.3/98
Altri autori (Persone) CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Cell Physiology
Proteins - Metabolism
Proteins - metabolism
Proteins --Metabolism
Ubiquitin
Ubiquitin - physiology
Animal Biochemistry
Human Anatomy & Physiology
Health & Biological Sciences
ISBN 1-282-37219-X
9786612372193
3-527-62022-2
3-527-62029-X
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin: A New Player in the Peroxisome Field; 1.1 Introduction; 1.2 Matrix Protein Import into Peroxisomes is Mediated by Cycling Receptors; 1.3 Pex5p is Monoubiquitinated in Wild-type Cells, but Polyubiquitinated in Late-acting pex Mutants; 1.4 Ubiquitination of Pex18p; 1.5 Role for the RING Finger and AAA Peroxins in Pex5p Ubiquitination and Recycling; 1.6 Pex5p Monoubiquitination: A Role in Receptor Recycling; 1.7 Conclusions/Future Prospects; Acknowledgements; References
2 The Ubiquitin Proteasome System and Muscle Development2.1 Introduction; 2.2 Muscle Histology; 2.3 UPS and Developing Muscle; 2.3.1 Ubiquitin-dependent Degradation of MyoD; 2.3.2 Degradation of MyoD by SCF(MAFbx); 2.3.3 Other Muscle Regulatory Factors; 2.4 UPS and Organizing Muscle; 2.4.1 Ozz-E3-dependent β-Catenin Regulation in the Muscle; 2.4.2 Regulation of Myosin Assembly by CHN-1 and UFD-2; 2.5 UPS and Muscle Destruction or Degeneration; 2.5.1 N-end Rule and Muscle Atrophy; 2.5.2 MuRFs, E3 Enzymes in Atrophying Muscles; 2.5.3 Atrogin-1/MAFbx Function in Muscle Atrophy
2.5.4 Activation of Muscle-atrophy Pathways2.6 Concluding Remarks; References; 3 The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development; 3.1 Introduction; 3.2 The Plant COP9 Signalosome; 3.3 CSN Involvement in the Ubiquitin-Proteasome Pathway; 3.4 Plant CSN Biochemical Activities; 3.4.1 Deneddylation; 3.4.2 Subcellular Partitioning; 3.5 CSN Functions in Plant Development; 3.5.1 Floral Development; 3.5.2 Responses to Plant Hormones; 3.5.3 Disease Resistance; 3.5.4 Photomorphogenesis; 3.6 Conclusions; References
4 Ubiquitin and Protein Sorting to the Lysosome4.1 Introduction; 4.2 Identification of Ubiquitin as an Endosomal Sorting Signal; 4.3 Ubiquitin-mediated Sorting at the Endosome: The MVB Sorting Machinery; 4.3.1 Endosome-associated Ubiquitin Interacting Domains: Structure and Function; 4.3.2 The Hrs-STAM Complex and the Endosomal Clathrin Coat; 4.3.3 GGA and Tom1: Alternative Sorting Adapters?; 4.3.4 The ESCRT Machinery; 4.3.5 Vps4-SKD1; 4.4 Ubiquitin Ligases and Endosomal Sorting; 4.4.1 Nedd4 Family; 4.4.2 c-Cbl; 4.5 Endosomal DUBs; 4.5.1 Ubp1 and Ubp2; 4.5.2 Doa4; 4.5.3 UBPY; 4.5.4 AMSH
4.6 Polyubiquitin Linkages and Endocytosis4.6.1 Proteasome Involvement in Endocytic Sorting; 4.6.2 K63-linked Ubiquitin; 4.7 Future Directions; Acknowledgements; References; 5 ISG15-dependent Regulation; 5.1 Introduction and Overview; 5.2 The Discovery of ISG15; 5.3 Structure and Properties of the ISG15 Protein; 5.4 The ISG15 Conjugation Pathway; 5.4.1 Activation of ISG15 by UbE1L; 5.4.2 UbcH8 is an ISG15-specific Conjugating Enzyme; 5.4.3 Candidate ISG15-specific Ligases; 5.5 Regulation of Intracellular ISG15 Pools; 5.6 Functional Roles for ISG15; 5.6.1 ISG15 as an Extracellular Cytokine
5.6.2 Role of ISG15 in the Antiviral Response
Record Nr. UNINA-9910830200703321
Mayer R. John  
Hoboken, : Wiley, 2008
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System
Autore Mayer R. John
Pubbl/distr/stampa Hoboken, : Wiley, 2008
Descrizione fisica 1 online resource (254 p.)
Disciplina 572.76
612.3/98
Altri autori (Persone) CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Cell Physiology
Proteins - Metabolism
Proteins - metabolism
Proteins --Metabolism
Ubiquitin
Ubiquitin - physiology
Animal Biochemistry
Human Anatomy & Physiology
Health & Biological Sciences
ISBN 1-282-37219-X
9786612372193
3-527-62022-2
3-527-62029-X
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin: A New Player in the Peroxisome Field; 1.1 Introduction; 1.2 Matrix Protein Import into Peroxisomes is Mediated by Cycling Receptors; 1.3 Pex5p is Monoubiquitinated in Wild-type Cells, but Polyubiquitinated in Late-acting pex Mutants; 1.4 Ubiquitination of Pex18p; 1.5 Role for the RING Finger and AAA Peroxins in Pex5p Ubiquitination and Recycling; 1.6 Pex5p Monoubiquitination: A Role in Receptor Recycling; 1.7 Conclusions/Future Prospects; Acknowledgements; References
2 The Ubiquitin Proteasome System and Muscle Development2.1 Introduction; 2.2 Muscle Histology; 2.3 UPS and Developing Muscle; 2.3.1 Ubiquitin-dependent Degradation of MyoD; 2.3.2 Degradation of MyoD by SCF(MAFbx); 2.3.3 Other Muscle Regulatory Factors; 2.4 UPS and Organizing Muscle; 2.4.1 Ozz-E3-dependent β-Catenin Regulation in the Muscle; 2.4.2 Regulation of Myosin Assembly by CHN-1 and UFD-2; 2.5 UPS and Muscle Destruction or Degeneration; 2.5.1 N-end Rule and Muscle Atrophy; 2.5.2 MuRFs, E3 Enzymes in Atrophying Muscles; 2.5.3 Atrogin-1/MAFbx Function in Muscle Atrophy
2.5.4 Activation of Muscle-atrophy Pathways2.6 Concluding Remarks; References; 3 The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development; 3.1 Introduction; 3.2 The Plant COP9 Signalosome; 3.3 CSN Involvement in the Ubiquitin-Proteasome Pathway; 3.4 Plant CSN Biochemical Activities; 3.4.1 Deneddylation; 3.4.2 Subcellular Partitioning; 3.5 CSN Functions in Plant Development; 3.5.1 Floral Development; 3.5.2 Responses to Plant Hormones; 3.5.3 Disease Resistance; 3.5.4 Photomorphogenesis; 3.6 Conclusions; References
4 Ubiquitin and Protein Sorting to the Lysosome4.1 Introduction; 4.2 Identification of Ubiquitin as an Endosomal Sorting Signal; 4.3 Ubiquitin-mediated Sorting at the Endosome: The MVB Sorting Machinery; 4.3.1 Endosome-associated Ubiquitin Interacting Domains: Structure and Function; 4.3.2 The Hrs-STAM Complex and the Endosomal Clathrin Coat; 4.3.3 GGA and Tom1: Alternative Sorting Adapters?; 4.3.4 The ESCRT Machinery; 4.3.5 Vps4-SKD1; 4.4 Ubiquitin Ligases and Endosomal Sorting; 4.4.1 Nedd4 Family; 4.4.2 c-Cbl; 4.5 Endosomal DUBs; 4.5.1 Ubp1 and Ubp2; 4.5.2 Doa4; 4.5.3 UBPY; 4.5.4 AMSH
4.6 Polyubiquitin Linkages and Endocytosis4.6.1 Proteasome Involvement in Endocytic Sorting; 4.6.2 K63-linked Ubiquitin; 4.7 Future Directions; Acknowledgements; References; 5 ISG15-dependent Regulation; 5.1 Introduction and Overview; 5.2 The Discovery of ISG15; 5.3 Structure and Properties of the ISG15 Protein; 5.4 The ISG15 Conjugation Pathway; 5.4.1 Activation of ISG15 by UbE1L; 5.4.2 UbcH8 is an ISG15-specific Conjugating Enzyme; 5.4.3 Candidate ISG15-specific Ligases; 5.5 Regulation of Intracellular ISG15 Pools; 5.6 Functional Roles for ISG15; 5.6.1 ISG15 as an Extracellular Cytokine
5.6.2 Role of ISG15 in the Antiviral Response
Record Nr. UNINA-9910841653603321
Mayer R. John  
Hoboken, : Wiley, 2008
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
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
Opac: Controlla la disponibilità qui
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
Opac: Controlla la disponibilità qui
Protein degradation . Volume 2 The Ubiquitin-proteasome system [[electronic resource] /] / R. John Mayer, Aaron Ciechanover, Martin Rechsteiner, eds
Protein degradation . Volume 2 The Ubiquitin-proteasome system [[electronic resource] /] / R. John Mayer, Aaron Ciechanover, Martin Rechsteiner, eds
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2006
Descrizione fisica 1 online resource (302 p.)
Disciplina 572.76
612.3/98
Altri autori (Persone) MayerR. J
CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Proteins - Metabolism
Ubiquitin
Soggetto genere / forma Electronic books.
ISBN 1-282-37220-3
9786612372209
3-527-62021-4
3-527-62036-2
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Molecular Chaperones and the Ubiquitin-Proteasome System; 1.1 Introduction; 1.2 A Biomedical Perspective; 1.3 Molecular Chaperones: Mode of Action and Cellular Functions; 1.3.1 The Hsp70 Family; 1.3.2 The Hsp90 Family; 1.3.3 The Small Heat Shock Proteins; 1.3.4 Chaperonins; 1.4 Chaperones: Central Players During Protein Quality Control; 1.5 Chaperones and Protein Degradation; 1.6 The CHIP Ubiquitin Ligase: A Link Between Folding and Degradation Systems
1.7 Other Proteins That May Influence the Balance Between Chaperone-assisted Folding and Degradation1.8 Further Considerations; 1.9 Conclusions; References; 2 Molecular Dissection of Autophagy in the Yeast Saccharomyces cerevisiae; 2.1 Introduction; 2.2 Vacuoles as a Lytic Compartment in Yeast; 2.3 Discovery of Autophagy in Yeast; 2.4 Genetic Dissection of Autophagy; 2.5 Characterization of Autophagy-defective Mutants; 2.6 Cloning of ATG Genes; 2.7 Further Genes Required for Autophagy; 2.8 Selectivity of Proteins Degraded; 2.9 Induction of Autophagy; 2.10 Membrane Dynamics During Autophagy
2.11 Monitoring Methods of Autophagy in the Yeast S. cerevisiae2.12 Function of Atg Proteins; 2.12.1 The Atg12 Protein Conjugation System; 2.12.2 The Atg8 System; 2.12.3 The Atg1 Kinase Complex; 2.12.4 Autophagy-specific PI3 Kinase Complex; 2.12.5 Other Atg Proteins; 2.13 Site of Atg Protein Functioning: The Pre-autophagosomal Structure; 2.14 Atg Proteins in Higher Eukaryotes; 2.15 Atg Proteins as Markers for Autophagy in Mammalian Cells; 2.16 Physiological Role of Autophagy in Multicellular Organisms; 2.17 Perspectives; References
3 Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes3.1 Introduction; 3.2 The Proteasome as an Essential Component of Intracellular Proteolysis; 3.3 Proteasome Structure, Function, and Localization; 3.4 Proteasome Inhibitors as Tools to Study Proteasome Function; 3.4.1 Peptide Aldehydes; 3.4.2 Lactacystin; 3.4.3 Peptide Epoxyketones; 3.4.4 Cyclic Peptides; 3.4.5 Peptide Boronates; 3.4.6 Peptide Vinyl Sulfones; 3.4.7 Peptide Vinyl Sulfones as Proteasomal Activity Probes
3.4.8 Future Directions in the Development of Inhibitors of the Proteasome's Proteolytic Activities3.5 Assessing the Biological Role of the Proteasome With Inhibitors and Probes; 3.6 Proteasome-associated Components: The Role of N-glycanase; 3.7 A Link Between Proteasomal Proteolysis and Deubiquitination; 3.7.1 Reversal of Ub Modification; 3.7.2 Ubiquitin-specific Proteases; 3.7.3 USP Reactive Probes Correlate USP Activity With Proteasomal Proteolysis; 3.8 Future Developments and Final Remarks; Acknowledgments; Abbreviations; References
4 MEKK1: Dual Function as a Protein Kinase and a Ubiquitin Protein Ligase
Record Nr. UNINA-9910144008303321
Weinheim, : Wiley-VCH, c2006
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Protein degradation . Volume 2 The Ubiquitin-proteasome system [[electronic resource] /] / R. John Mayer, Aaron Ciechanover, Martin Rechsteiner, eds
Protein degradation . Volume 2 The Ubiquitin-proteasome system [[electronic resource] /] / R. John Mayer, Aaron Ciechanover, Martin Rechsteiner, eds
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2006
Descrizione fisica 1 online resource (302 p.)
Disciplina 572.76
612.3/98
Altri autori (Persone) MayerR. J
CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Proteins - Metabolism
Ubiquitin
ISBN 1-282-37220-3
9786612372209
3-527-62021-4
3-527-62036-2
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Molecular Chaperones and the Ubiquitin-Proteasome System; 1.1 Introduction; 1.2 A Biomedical Perspective; 1.3 Molecular Chaperones: Mode of Action and Cellular Functions; 1.3.1 The Hsp70 Family; 1.3.2 The Hsp90 Family; 1.3.3 The Small Heat Shock Proteins; 1.3.4 Chaperonins; 1.4 Chaperones: Central Players During Protein Quality Control; 1.5 Chaperones and Protein Degradation; 1.6 The CHIP Ubiquitin Ligase: A Link Between Folding and Degradation Systems
1.7 Other Proteins That May Influence the Balance Between Chaperone-assisted Folding and Degradation1.8 Further Considerations; 1.9 Conclusions; References; 2 Molecular Dissection of Autophagy in the Yeast Saccharomyces cerevisiae; 2.1 Introduction; 2.2 Vacuoles as a Lytic Compartment in Yeast; 2.3 Discovery of Autophagy in Yeast; 2.4 Genetic Dissection of Autophagy; 2.5 Characterization of Autophagy-defective Mutants; 2.6 Cloning of ATG Genes; 2.7 Further Genes Required for Autophagy; 2.8 Selectivity of Proteins Degraded; 2.9 Induction of Autophagy; 2.10 Membrane Dynamics During Autophagy
2.11 Monitoring Methods of Autophagy in the Yeast S. cerevisiae2.12 Function of Atg Proteins; 2.12.1 The Atg12 Protein Conjugation System; 2.12.2 The Atg8 System; 2.12.3 The Atg1 Kinase Complex; 2.12.4 Autophagy-specific PI3 Kinase Complex; 2.12.5 Other Atg Proteins; 2.13 Site of Atg Protein Functioning: The Pre-autophagosomal Structure; 2.14 Atg Proteins in Higher Eukaryotes; 2.15 Atg Proteins as Markers for Autophagy in Mammalian Cells; 2.16 Physiological Role of Autophagy in Multicellular Organisms; 2.17 Perspectives; References
3 Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes3.1 Introduction; 3.2 The Proteasome as an Essential Component of Intracellular Proteolysis; 3.3 Proteasome Structure, Function, and Localization; 3.4 Proteasome Inhibitors as Tools to Study Proteasome Function; 3.4.1 Peptide Aldehydes; 3.4.2 Lactacystin; 3.4.3 Peptide Epoxyketones; 3.4.4 Cyclic Peptides; 3.4.5 Peptide Boronates; 3.4.6 Peptide Vinyl Sulfones; 3.4.7 Peptide Vinyl Sulfones as Proteasomal Activity Probes
3.4.8 Future Directions in the Development of Inhibitors of the Proteasome's Proteolytic Activities3.5 Assessing the Biological Role of the Proteasome With Inhibitors and Probes; 3.6 Proteasome-associated Components: The Role of N-glycanase; 3.7 A Link Between Proteasomal Proteolysis and Deubiquitination; 3.7.1 Reversal of Ub Modification; 3.7.2 Ubiquitin-specific Proteases; 3.7.3 USP Reactive Probes Correlate USP Activity With Proteasomal Proteolysis; 3.8 Future Developments and Final Remarks; Acknowledgments; Abbreviations; References
4 MEKK1: Dual Function as a Protein Kinase and a Ubiquitin Protein Ligase
Record Nr. UNINA-9910830458903321
Weinheim, : Wiley-VCH, c2006
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Protein degradation . Volume 2 The Ubiquitin-proteasome system [[electronic resource] /] / R. John Mayer, Aaron Ciechanover, Martin Rechsteiner, eds
Protein degradation . Volume 2 The Ubiquitin-proteasome system [[electronic resource] /] / R. John Mayer, Aaron Ciechanover, Martin Rechsteiner, eds
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2006
Descrizione fisica 1 online resource (302 p.)
Disciplina 572.76
612.3/98
Altri autori (Persone) MayerR. J
CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Proteins - Metabolism
Ubiquitin
ISBN 1-282-37220-3
9786612372209
3-527-62021-4
3-527-62036-2
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Molecular Chaperones and the Ubiquitin-Proteasome System; 1.1 Introduction; 1.2 A Biomedical Perspective; 1.3 Molecular Chaperones: Mode of Action and Cellular Functions; 1.3.1 The Hsp70 Family; 1.3.2 The Hsp90 Family; 1.3.3 The Small Heat Shock Proteins; 1.3.4 Chaperonins; 1.4 Chaperones: Central Players During Protein Quality Control; 1.5 Chaperones and Protein Degradation; 1.6 The CHIP Ubiquitin Ligase: A Link Between Folding and Degradation Systems
1.7 Other Proteins That May Influence the Balance Between Chaperone-assisted Folding and Degradation1.8 Further Considerations; 1.9 Conclusions; References; 2 Molecular Dissection of Autophagy in the Yeast Saccharomyces cerevisiae; 2.1 Introduction; 2.2 Vacuoles as a Lytic Compartment in Yeast; 2.3 Discovery of Autophagy in Yeast; 2.4 Genetic Dissection of Autophagy; 2.5 Characterization of Autophagy-defective Mutants; 2.6 Cloning of ATG Genes; 2.7 Further Genes Required for Autophagy; 2.8 Selectivity of Proteins Degraded; 2.9 Induction of Autophagy; 2.10 Membrane Dynamics During Autophagy
2.11 Monitoring Methods of Autophagy in the Yeast S. cerevisiae2.12 Function of Atg Proteins; 2.12.1 The Atg12 Protein Conjugation System; 2.12.2 The Atg8 System; 2.12.3 The Atg1 Kinase Complex; 2.12.4 Autophagy-specific PI3 Kinase Complex; 2.12.5 Other Atg Proteins; 2.13 Site of Atg Protein Functioning: The Pre-autophagosomal Structure; 2.14 Atg Proteins in Higher Eukaryotes; 2.15 Atg Proteins as Markers for Autophagy in Mammalian Cells; 2.16 Physiological Role of Autophagy in Multicellular Organisms; 2.17 Perspectives; References
3 Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes3.1 Introduction; 3.2 The Proteasome as an Essential Component of Intracellular Proteolysis; 3.3 Proteasome Structure, Function, and Localization; 3.4 Proteasome Inhibitors as Tools to Study Proteasome Function; 3.4.1 Peptide Aldehydes; 3.4.2 Lactacystin; 3.4.3 Peptide Epoxyketones; 3.4.4 Cyclic Peptides; 3.4.5 Peptide Boronates; 3.4.6 Peptide Vinyl Sulfones; 3.4.7 Peptide Vinyl Sulfones as Proteasomal Activity Probes
3.4.8 Future Directions in the Development of Inhibitors of the Proteasome's Proteolytic Activities3.5 Assessing the Biological Role of the Proteasome With Inhibitors and Probes; 3.6 Proteasome-associated Components: The Role of N-glycanase; 3.7 A Link Between Proteasomal Proteolysis and Deubiquitination; 3.7.1 Reversal of Ub Modification; 3.7.2 Ubiquitin-specific Proteases; 3.7.3 USP Reactive Probes Correlate USP Activity With Proteasomal Proteolysis; 3.8 Future Developments and Final Remarks; Acknowledgments; Abbreviations; References
4 MEKK1: Dual Function as a Protein Kinase and a Ubiquitin Protein Ligase
Record Nr. UNINA-9910840771303321
Weinheim, : Wiley-VCH, c2006
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Protein degradation . Volume 1 Ubiquitin and the chemistry of life [[electronic resource] /] / John Mayer, Aaron Ciechanover, Martin Rechsteiner (eds.)
Protein degradation . Volume 1 Ubiquitin and the chemistry of life [[electronic resource] /] / John Mayer, Aaron Ciechanover, Martin Rechsteiner (eds.)
Edizione [1st ed.]
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2005
Descrizione fisica 1 online resource (395 p.)
Disciplina 572.76
Altri autori (Persone) MayerR. J
CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Proteins - Metabolism
Ubiquitin
Soggetto genere / forma Electronic books.
ISBN 1-280-52062-0
9786610520626
3-527-60586-X
3-527-60556-8
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Brief History of Protein Degradation and the Ubiquitin System; 1.1 Introductory Remarks; 1.2 Protein Degradation - Does It Exist?; 1.3 Discovery of the Role of Ubiquitin in Protein Degradation; 1.4 Identification of Enzymes of the Ubiquitin-mediated Proteolytic System; 1.5 Discovery of Some Basic Cellular Functions of the Ubiquitin System; 1.6 Concluding Remarks; References; 2 N-terminal Ubiquitination: No Longer Such a Rare Modification; Abstract; 2.1 Background; 2.2 Results; 2.3 Discussion; Acknowledgments; References
3 Evolutionary Origin of the Activation Step During Ubiquitin-dependent Protein DegradationAbbreviations; Abstract; 3.1 Introduction; 3.1.1 Activation of Ubiquitin and Ubiquitin-like Proteins; 3.1.2 Molybdenum Cofactor Biosynthesis; 3.2 The Crystal Structure of MoaD Reveals the Ubiquitin Fold; 3.3 Structural Studies of the MoeB-MoaD Complex; 3.3.1 Structure of MoeB; 3.3.2 The MoeB-MoaD Interface; 3.3.3 Structure of MoeB-MoaD with Bound ATP; 3.3.4 Structure of the MoaD Adenylate; 3.3.5 Fate of the Adenylate; 3.4 Structure of the NEDD8 Activator; 3.4.1 Overall Structure of the NEDD8-E1
3.4.2 Comparison with the MoaD-MoeB Complex3.4.3 Conformational Changes during the Formation of the Acyl Adenylate; Summary; Acknowledgments; References; 4 RING Fingers and Relatives: Determinators of Protein Fate; 4.1 Introduction and Overview; 4.1.1 Historical Perspective; 4.2 RING Fingers as E3s; 4.2.1 General Considerations; 4.2.2 Structural Analysis and Structure-Function Relationships; 4.2.2.1 RING finger-E2 Interactions; 4.2.3 Other Protein-Protein Interaction Motifs in RING finger Proteins; 4.2.4 Variations on the RING Finger; 4.2.5 High-order Structure of RINGs - TRIMs
4.3 RING Fingers in Cell Signaling4.3.1 Siahs; 4.3.2 IAPs; 4.3.3 TRAFs; 4.3.4 Cbls; 4.4 Multi RING finger Proteins; 4.4.1 Mindbomb and TRIADs; 4.4.2 Parkin and Parkinson's Disease; 4.4.2.1 Parkin Substrates; 4.4.2.2 Parkin Animal Models; 4.4.2.3 Possible Pathogenic Mechanisms in ARJP; 4.5 Regulation of p53 by Mdm2 and other RING finger Proteins; 4.5.1 Mdm2; 4.5.2 Pirh2; 4.5.3 MdmX; 4.5.4 Arf and Other Modulators of Mdm2 Activity; 4.5.5 Other Potential Mdm2 Substrates; 4.5.6 Mdm2 and Therapeutic Intervention in Cancer; 4.6 Conclusion - Perspective; Acknowledgments; References
5 Ubiquitin-conjugating Enzymes5.1 Introduction; 5.2 Historical Background; 5.3 What is an E2?; 5.4 Functional Diversity of Ubiquitin-conjugating Enzymes; 5.4.1 Functions Related to Proteasome Proteolysis; 5.4.2 Endocytosis and Trafficking; 5.4.3 Non-proteolytic Functions; 5.4.4 E2s of Uncertain Function; 5.4.5 E2 Enzymes and Disease; 5.5 E2 Enzymes Dedicated to Ubiquitin-like Proteins (UbLs); 5.6 The Biochemistry of E2 Enzymes; 5.6.1 E1 Interaction; 5.6.2 Interactions with Thiol-linked Ubiquitin; 5.6.3 E3 Interactions; 5.6.3.1 RING E3/E2 Interactions; 5.6.3.2 U-box E3/E2 Interactions
5.6.3.3 HECT E3/E2 Interactions
Record Nr. UNINA-9910144557303321
Weinheim, : Wiley-VCH, c2005
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Protein degradation . Volume 1 Ubiquitin and the chemistry of life [[electronic resource] /] / John Mayer, Aaron Ciechanover, Martin Rechsteiner (eds.)
Protein degradation . Volume 1 Ubiquitin and the chemistry of life [[electronic resource] /] / John Mayer, Aaron Ciechanover, Martin Rechsteiner (eds.)
Edizione [1st ed.]
Pubbl/distr/stampa Weinheim, : Wiley-VCH, c2005
Descrizione fisica 1 online resource (395 p.)
Disciplina 572.76
Altri autori (Persone) MayerR. J
CiechanoverAaron J
RechsteinerMartin
Collana Protein Degradation
Soggetto topico Proteins - Metabolism
Ubiquitin
ISBN 1-280-52062-0
9786610520626
3-527-60586-X
3-527-60556-8
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Protein Degradation; Contents; Preface; List of Contributors; 1 Brief History of Protein Degradation and the Ubiquitin System; 1.1 Introductory Remarks; 1.2 Protein Degradation - Does It Exist?; 1.3 Discovery of the Role of Ubiquitin in Protein Degradation; 1.4 Identification of Enzymes of the Ubiquitin-mediated Proteolytic System; 1.5 Discovery of Some Basic Cellular Functions of the Ubiquitin System; 1.6 Concluding Remarks; References; 2 N-terminal Ubiquitination: No Longer Such a Rare Modification; Abstract; 2.1 Background; 2.2 Results; 2.3 Discussion; Acknowledgments; References
3 Evolutionary Origin of the Activation Step During Ubiquitin-dependent Protein DegradationAbbreviations; Abstract; 3.1 Introduction; 3.1.1 Activation of Ubiquitin and Ubiquitin-like Proteins; 3.1.2 Molybdenum Cofactor Biosynthesis; 3.2 The Crystal Structure of MoaD Reveals the Ubiquitin Fold; 3.3 Structural Studies of the MoeB-MoaD Complex; 3.3.1 Structure of MoeB; 3.3.2 The MoeB-MoaD Interface; 3.3.3 Structure of MoeB-MoaD with Bound ATP; 3.3.4 Structure of the MoaD Adenylate; 3.3.5 Fate of the Adenylate; 3.4 Structure of the NEDD8 Activator; 3.4.1 Overall Structure of the NEDD8-E1
3.4.2 Comparison with the MoaD-MoeB Complex3.4.3 Conformational Changes during the Formation of the Acyl Adenylate; Summary; Acknowledgments; References; 4 RING Fingers and Relatives: Determinators of Protein Fate; 4.1 Introduction and Overview; 4.1.1 Historical Perspective; 4.2 RING Fingers as E3s; 4.2.1 General Considerations; 4.2.2 Structural Analysis and Structure-Function Relationships; 4.2.2.1 RING finger-E2 Interactions; 4.2.3 Other Protein-Protein Interaction Motifs in RING finger Proteins; 4.2.4 Variations on the RING Finger; 4.2.5 High-order Structure of RINGs - TRIMs
4.3 RING Fingers in Cell Signaling4.3.1 Siahs; 4.3.2 IAPs; 4.3.3 TRAFs; 4.3.4 Cbls; 4.4 Multi RING finger Proteins; 4.4.1 Mindbomb and TRIADs; 4.4.2 Parkin and Parkinson's Disease; 4.4.2.1 Parkin Substrates; 4.4.2.2 Parkin Animal Models; 4.4.2.3 Possible Pathogenic Mechanisms in ARJP; 4.5 Regulation of p53 by Mdm2 and other RING finger Proteins; 4.5.1 Mdm2; 4.5.2 Pirh2; 4.5.3 MdmX; 4.5.4 Arf and Other Modulators of Mdm2 Activity; 4.5.5 Other Potential Mdm2 Substrates; 4.5.6 Mdm2 and Therapeutic Intervention in Cancer; 4.6 Conclusion - Perspective; Acknowledgments; References
5 Ubiquitin-conjugating Enzymes5.1 Introduction; 5.2 Historical Background; 5.3 What is an E2?; 5.4 Functional Diversity of Ubiquitin-conjugating Enzymes; 5.4.1 Functions Related to Proteasome Proteolysis; 5.4.2 Endocytosis and Trafficking; 5.4.3 Non-proteolytic Functions; 5.4.4 E2s of Uncertain Function; 5.4.5 E2 Enzymes and Disease; 5.5 E2 Enzymes Dedicated to Ubiquitin-like Proteins (UbLs); 5.6 The Biochemistry of E2 Enzymes; 5.6.1 E1 Interaction; 5.6.2 Interactions with Thiol-linked Ubiquitin; 5.6.3 E3 Interactions; 5.6.3.1 RING E3/E2 Interactions; 5.6.3.2 U-box E3/E2 Interactions
5.6.3.3 HECT E3/E2 Interactions
Record Nr. UNINA-9910830198003321
Weinheim, : Wiley-VCH, c2005
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui