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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 | ||
| ||
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 | ||
| ||
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 | ||
| ||
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 | ||
| ||
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-9910841650903321 |
| Weinheim, : Wiley-VCH, c2005 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein degradation in health and disease
| Protein degradation in health and disease |
| Pubbl/distr/stampa | Amsterdam ; ; New York : , : Excerpta Medica, , 1980 |
| Descrizione fisica | 1 online resource (430 pages) : illustrations |
| Disciplina | 616.3/995 |
| Collana | Ciba Foundation symposium |
| Soggetto topico |
Proteins - Metabolism
Proteolytic enzymes Physiology, Pathological |
| ISBN |
1-280-78393-1
9786613694324 0-470-72058-1 0-470-71826-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Degradation in Health and Disease; Contents; Discussion; Introduction: the classification of proteinases; Discussion; Lysosomal cysteine proteinases; Discussion; Cathepsin D: the lysosomal aspartic proteinase; Discussion; Human leucocyte elastase and cathepsin G: structural and functional characteristics; Discussion; Human collagenases: comparative and immunolocalization studies; Discussion; Proteinases in connective tissue breakdown; Discussion; Cellular mechanisms of proteinase release from inflammatory cells and the degradation of extracellular proteins; Discussion
Inactivation of cytosol enzymes by a liver membrane protein; Discussion; Lysosomes and protein degradation; Discussion; Insights into mechanisms of intracellular protein turnover from studies on pinocytosis; Discussion; Turnover and degradation of mitochondria and their proteins; Discussion; Protein degradation in cells in culture; Discussion; Regulation of protein breakdown in hepatocyte monolayers; Discussion; A possible role for neutral proteolysis in the degradation of intracellular proteins; Discussion; Studies of the ATP dependence of protein degradation in cells and cell extracts Discussion; Coordination of protein synthesis and degradation; Discussion; General discussion Sites of protein degradation; Application of liver perfusion as an in vitro model in studies of intracellular protein degradation; Protein degradation and the regulation of protein balance in muscle; Discussion; Protein degradation in metabolic and nutritional disorders; Discussion; Proteinase inhibitors in severe inflammatory processes (septic shock and experimental endotoxaemia): biochemical, pathophysiological and therapeutic aspects; Discussion; Neutral proteinases of leucocytes and the inflammatory process; Discussion; Final general discussion; Concluding remarks; Index of contributors; Subject index |
| Record Nr. | UNINA-9910144657103321 |
| Amsterdam ; ; New York : , : Excerpta Medica, , 1980 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein degradation in health and disease
| Protein degradation in health and disease |
| Pubbl/distr/stampa | Amsterdam ; ; New York : , : Excerpta Medica, , 1980 |
| Descrizione fisica | 1 online resource (430 pages) : illustrations |
| Disciplina | 616.3/995 |
| Collana | Ciba Foundation symposium |
| Soggetto topico |
Proteins - Metabolism
Proteolytic enzymes Physiology, Pathological |
| ISBN |
1-280-78393-1
9786613694324 0-470-72058-1 0-470-71826-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Degradation in Health and Disease; Contents; Discussion; Introduction: the classification of proteinases; Discussion; Lysosomal cysteine proteinases; Discussion; Cathepsin D: the lysosomal aspartic proteinase; Discussion; Human leucocyte elastase and cathepsin G: structural and functional characteristics; Discussion; Human collagenases: comparative and immunolocalization studies; Discussion; Proteinases in connective tissue breakdown; Discussion; Cellular mechanisms of proteinase release from inflammatory cells and the degradation of extracellular proteins; Discussion
Inactivation of cytosol enzymes by a liver membrane protein; Discussion; Lysosomes and protein degradation; Discussion; Insights into mechanisms of intracellular protein turnover from studies on pinocytosis; Discussion; Turnover and degradation of mitochondria and their proteins; Discussion; Protein degradation in cells in culture; Discussion; Regulation of protein breakdown in hepatocyte monolayers; Discussion; A possible role for neutral proteolysis in the degradation of intracellular proteins; Discussion; Studies of the ATP dependence of protein degradation in cells and cell extracts Discussion; Coordination of protein synthesis and degradation; Discussion; General discussion Sites of protein degradation; Application of liver perfusion as an in vitro model in studies of intracellular protein degradation; Protein degradation and the regulation of protein balance in muscle; Discussion; Protein degradation in metabolic and nutritional disorders; Discussion; Proteinase inhibitors in severe inflammatory processes (septic shock and experimental endotoxaemia): biochemical, pathophysiological and therapeutic aspects; Discussion; Neutral proteinases of leucocytes and the inflammatory process; Discussion; Final general discussion; Concluding remarks; Index of contributors; Subject index |
| Record Nr. | UNISA-996206964103316 |
| Amsterdam ; ; New York : , : Excerpta Medica, , 1980 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Protein degradation in health and disease
| Protein degradation in health and disease |
| Pubbl/distr/stampa | Amsterdam ; ; New York : , : Excerpta Medica, , 1980 |
| Descrizione fisica | 1 online resource (430 pages) : illustrations |
| Disciplina | 616.3/995 |
| Collana | Ciba Foundation symposium |
| Soggetto topico |
Proteins - Metabolism
Proteolytic enzymes Physiology, Pathological |
| ISBN |
1-280-78393-1
9786613694324 0-470-72058-1 0-470-71826-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Degradation in Health and Disease; Contents; Discussion; Introduction: the classification of proteinases; Discussion; Lysosomal cysteine proteinases; Discussion; Cathepsin D: the lysosomal aspartic proteinase; Discussion; Human leucocyte elastase and cathepsin G: structural and functional characteristics; Discussion; Human collagenases: comparative and immunolocalization studies; Discussion; Proteinases in connective tissue breakdown; Discussion; Cellular mechanisms of proteinase release from inflammatory cells and the degradation of extracellular proteins; Discussion
Inactivation of cytosol enzymes by a liver membrane protein; Discussion; Lysosomes and protein degradation; Discussion; Insights into mechanisms of intracellular protein turnover from studies on pinocytosis; Discussion; Turnover and degradation of mitochondria and their proteins; Discussion; Protein degradation in cells in culture; Discussion; Regulation of protein breakdown in hepatocyte monolayers; Discussion; A possible role for neutral proteolysis in the degradation of intracellular proteins; Discussion; Studies of the ATP dependence of protein degradation in cells and cell extracts Discussion; Coordination of protein synthesis and degradation; Discussion; General discussion Sites of protein degradation; Application of liver perfusion as an in vitro model in studies of intracellular protein degradation; Protein degradation and the regulation of protein balance in muscle; Discussion; Protein degradation in metabolic and nutritional disorders; Discussion; Proteinase inhibitors in severe inflammatory processes (septic shock and experimental endotoxaemia): biochemical, pathophysiological and therapeutic aspects; Discussion; Neutral proteinases of leucocytes and the inflammatory process; Discussion; Final general discussion; Concluding remarks; Index of contributors; Subject index |
| Record Nr. | UNINA-9910819037703321 |
| Amsterdam ; ; New York : , : Excerpta Medica, , 1980 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein turnover [[electronic resource] /] / J.C. Waterlow
| Protein turnover [[electronic resource] /] / J.C. Waterlow |
| Autore | Waterlow J. C (John Conrad) |
| Pubbl/distr/stampa | Wallingford, UK ; ; Cambridge, MA, : CABI Pub., c2006 |
| Descrizione fisica | 1 online resource (313 p.) |
| Disciplina | 612.3/98 |
| Altri autori (Persone) | WaterlowJ. C (John Conrad) |
| Soggetto topico |
Proteins - Metabolism
Mammals - Physiology |
| ISBN |
1-280-73565-1
9786610735655 1-84593-084-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Contents; Foreword; Acknowledgements; 1 Basic Principles; 1.1 Definitions; 1.2 Notation; 1.3 Equivalence of Tracer and Tracee; 1.4 The Kinetics of Protein Turnover; 1.5 References; 2 Models and Their Analysis; 2.1 Models; 2.2 Compartmental Analysis; 2.3 Stochastic Analysis; 2.4 References; 3 Free Amino Acids: Their Pools, Kinetics and Transport; 3.1 Amino Acid Pools; 3.2 Nutritional Effects on the Free Amino Acid Pools; 3.3 Kinetics of Free Amino Acids; 3.4 Amino Acid Transport Across Cell Membranes; 3.5 Conclusion; 3.6 References; 4 Metabolism of Some Amino Acids; 4.1 Leucine; 4.2 Glycine
4.3 Alanine4.4 Glutamine; 4.5 Glutamic acid; 4.6 Phenylalanine; 4.7 Arginine; 4.8 Methionine; 4.9 References; 5 The Precursor Problem; 5.1 Transfer-RNA as the Precursor for Synthesis; 5.2 A 'Reciprocal' Metabolite as Precursor; 5.3 A Rapidly Synthesized Protein as Precursor; 5.4 Conclusion; 5.5 References; 6 Precursor Method: Whole Body Protein Turnover Measured by the Precursor Method; 6.1 Background; 6.2 Outline of the Method; 6.3 Variability of Whole Body Synthesis Rates in Healthy Adults by the Precursor Method; 6.4 Sites of Administration and of Sampling; 6.5 Priming 6.6 The First-pass Effect6.7 Recycling; 6.8 Regional Turnover; 6.9 Measurement of Protein Turnover with Amino Acids other than Leucine; 6.10 Conclusion; 6.11 References; 7 Measurement of Whole Body Protein Turnover by the End-product Method; 7.1 History; 7.2 Theory; 7.3 Alternative End-products (EP); 7.4 Measurement of Flux with a Single End-product; 7.5 Behaviour of Different Amino Acids in the End-product Method: Choice of Glycine; 7.6 Comparisons of Different Protocols; 7.7 Summary of Measurements of Protein Synthesis in Normal Adults by the End-product Method; 7.8 Variability 7.9 Comparison of Synthesis Rates Measured by the End-product and Precursor Methods7.10 Comparison of Oxidation Rates by the Two Methods; 7.11 The Flux Ratio; 7.12 Kinetics Findings by the End-product Method; 7.13 Conclusion; 7.14 References; 8 Amino Acid Oxidation and Urea Metabolism; 8.1 Amino Acid Oxidation; 8.2 Metabolism of Urea; 8.3 References; 9 The Effects of Food and Hormones on Protein Turnover in the Whole Body and Regions; 9.1 The Immediate Effects of Food; 9.2 The Effects of Hormones on Protein Turnover in the Whole Body, Limb or Splanchnic Region; 9.3 References 10 Adaptation to Different Protein Intakes: Protein and Amino Acid Requirements10.1 Adaptation; 10.2 Requirements for Protein and Amino Acids; 10.3 References; 11 Physiological Determinants of Protein Turnover; 11.1 Body Size - the Contribution of Allometry; 11.2 Growth and its Cost; 11.3 The Effect of Muscular Activity and Immobility on Protein Turnover; 11.4 Conclusion; 11.5 References; 12 Whole Body Protein Turnover at Different Ages and in Pregnancy and Lactation; 12.1 Premature Infants; 12.2 Neonates; 12.3 Infants 6 months-2 years; 12.4 Older Children; 12.5 Pregnancy; 12.6 Lactation 12.7 The Elderly |
| Record Nr. | UNINA-9910446331103321 |
Waterlow J. C (John Conrad)
|
||
| Wallingford, UK ; ; Cambridge, MA, : CABI Pub., c2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein turnover / / sponsored by the Ciba Foundation
| Protein turnover / / sponsored by the Ciba Foundation |
| Pubbl/distr/stampa | Amsterdam : , : Associated Scientific Publishers, , 1973 |
| Descrizione fisica | 1 online resource (330 pages) : illustrations |
| Disciplina | 574.1/33 |
| Collana | Ciba Foundation symposium. New series |
| Soggetto topico |
Proteins - Metabolism
Nuclear medicine |
| ISBN |
1-280-78320-6
9786613693594 0-470-71992-3 0-470-71759-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Turnover; Contents; Chairman's introduction; The role of cell surface receptors in the transport and catabolism of immunoglobulins; Discussion; The role of the kidney in the metabolism of serum proteins; Discussion; Short-term determination of plasma protein turnover by a two-tracer technique using plasma only or plasma and urine data; Discussion; Acute-phase plasma proteins in wound healing; Discussion; Studies with a mass balance method of measuring fibrinogen synthesis; Discussion; Analysis of disappearance time-curves after single injection of labelled proteins; Discussion
The influence of amino acids and hepatotoxic agents on albumin synthesis, polysomal aggregation and RNA turnover Discussion; Regulatory factors in the synthesis of plasnia proteins by the isolated perfused rat liver; Discussion; Effects of intravenous neuraminidase on the turnover of fibrinogen; Discussion; Generation of 125I-labelled plasmin in dogs in response to venous injury; Discussion; The comparative effects of nutritional and hormonal factors on the synthesis of albumin, fibrinogen and transferrin; Discussion; IgM turnover in man; Discussion Complement in membranoproliferative (hypocomplementaemic) glomerulonephritis Discussion; Disorders of the complement and properdin systems; Discussion; General Discussion Criteria of viability in perfused livers; Index of Contributors; Subject Index |
| Record Nr. | UNISA-996206957203316 |
| Amsterdam : , : Associated Scientific Publishers, , 1973 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Soggetto topico
-
Proteins - Metabolism
(42)
- Ubiquitin (14)
- Proteolytic enzymes (6)
- Proteins - metabolism (5)
- Appetite stimulants (4)