ADP-Ribosylation of Proteins

Inhaltsverzeichnis

I Poly-ADP-Ribosylation Reactions (F. R. Althaus).- 1 Poly(ADP-Ribose): Structure, Properties, and Quantification.- 1.1 Structure and Physicochemical Properties.- 1.2 Detection and Quantification of Poly(ADP-Ribose) in Biological Material.- References.- 2 Poly(ADP-Ribose) Biosynthesis.- 2.1 Natural Occurrence of Poly-ADP-Ribosylation Activity in Different Species, Tissues, and Cell Types.- 2.2 Subcellular Distribution of Poly-ADP-Ribosylation Activity.- 2.3 Purified Poly(ADP-Ribose) Polymerase.- 2.3.1 Physicochemical Properties.- 2.3.2 Domain Structure.- 2.3.3 Enzymological Properties.- References.- 3 Poly(ADP-Ribose) Catabolism.- 3.1 Enzymes Involved in Poly(ADP-Ribose) Catabolism.- 3.2 Factors Affecting Poly(ADP-Ribose) Catabolism.- References.- 4 Nuclear Acceptor Proteins for Poly(ADP-Ribose) and the Functional Consequences of Poly-ADP-Ribosylation on the Acceptor Species.- 4.1 Acceptor Proteins Identified in Reconstituted in Vitro Systems Involving Purified Poly(ADP-Ribose) Polymerase.- 4.2 Acceptor Proteins Identified in “Broken Cell” Systems or Polynucleosomal Preparations.- 4.3 Acceptor Proteins Which Have Been Identified in Intact Cells.- References.- 5 Poly-ADP-Ribosylation and Chromatin Organization.- 5.1 Introductory Comments.- 5.2 Electron Microscopy Investigations of Poly(ADP-Ribose)-Modified Chromatin.- 5.3 Biochemical Analyses of Poly(ADP-Ribose)-Modified Chromatin.- 5.4 Characterization of Sites Adjacent to Poly-ADP-Ribosylation in Bulk Chromatin.- References.- 6 Poly-ADP-Ribosylation in the Recovery of Mammalian Cells from DNA Damage.- 6.1 Introduction.- 6.2 DNA Damage, Activation of Poly(ADP-Ribose) Polymerase, and NAD Depletion in Mammalian Cells.- 6.3 Inhibitors of Poly(ADP-Ribose) Polymerase in the Investigation of the Role of Poly-ADP-Ribosylation Reactions in DNA-Excision Repair.- 6.3.1 Specificity of Poly(ADP-Ribose) Polymerase Inhibitors.- 6.3.2 Inhibitor Protocols Used.- 6.3.3 Consequences of Inhibited Poly(ADP-Ribose) Biosynthesis on Specific Reaction Steps in DNA-Excision Repair of Mammalian Cells.- 6.4 Effects of ADP-Ribosylation Inhibitors on the Clonal Survival of Carcinogen-Treated Cells.- 6.5 The Effects of ADP-Ribosylation Inhibitors on Chromosome Stability.- 6.6 Conclusions and Perspectives.- References.- 7 Poly(ADP-Ribose), DNA Synthesis, and Cell Cycle Progression.- 7.1 Proliferative Activity, Cell Cycle Progression, and Chromatin-Associated ADP-Ribosylation Activity.- 7.2 Poly-ADP-Ribosylation and DNA Synthesis in Isolated Nuclei.- 7.3 In Vitro Effects of Poly(ADP-Ribose) on Enzymes Acting on DNA.- References.- 8 Poly(ADP-Ribose), Cellular Differentiation, and Gene Expression.- 8.1 Introduction.- 8.2 Poly-ADP-Ribosylation in Differentiating Tissues and Cells.- 8.3 Evidence Derived from Inhibitor Studies.- 8.4 Possible Mechanism(s) of Poly(ADP-Ribose) Involvement in RNA Metabolism and Gene Expression.- References.- 9 Poly(ADP-Ribose) in Inherited Human Diseases and Experimental Disease Models.- 9.1 Glutamyl Ribose-5-Phosphate Storage Disease — A Hereditary Defect in the Catabolism of Poly(ADP-Ribosyl)ated Proteins.- 9.2 Collagen Vascular Diseases.- 9.2.1 Systemic Lupus Erythematosus (SLE).- 9.2.2 Other Collagen Vascular Diseases.- 9.3 Diseases Associated with Disorders of DNA Repair.- 9.3.1 Xeroderma Pigmentosum (XP).- 9.3.2 Ataxia Teleangiectasia (AT).- 9.3.3 Fanconi’s Anemia (FA).- 9.4 Experimental Diabetes.- 9.5 Neoplastic Transformation in Vitro and in Vivo.- 9.5.1 In Vitro Transformation Systems.- 9.5.2 Transformation in Vivo.- References.- II Mono-ADP-Ribosylation Reactions (Ch. Richter).- 10 Signal Transduction.- 10.1 Introduction.- 10.2 Guanine Nucleotide-Binding Regulatory Proteins Involved in Signal Transduction.- 10.3 Adenylate Cyclase.- 10.4 Transducin.- 10.5 Receptor-Stimulated Phosphodiesterase Stimulation and Calcium Mobilization.- 10.6 The ras Gene Product.- References.- 11 Cholera Toxin.- 11.1 The Discovery of Cholera Toxin.- 11.2 The Structure of Cholera Toxin.- 11.3 Interaction with the Receptor.- 11.4 Membrane Penetration and Processing.- 11.5 Enzymatic Activities of Cholera Toxin: NAD + Hydrolysis and ADP-Ribosyltransfer.- 11.6 Activation of Adenylate Cyclase.- 11.7 Cofactor Requirement for ADP-Ribosylation of Adenylate Cyclase.- 11.8 ADP-Ribosylation of Transducin.- 11.9 Minor Protein Substrates of Cholera Toxin.- References.- 12 Pertussis Toxin.- 12.1 The Discovery of Pertussis Toxin.- 12.2 The Structure of Pertussis Toxin.- 12.3 Pertussis Toxin Activation and Processing.- 12.4 Pertussis Toxin-Sensitive Cells.- 12.5 Pertussis Toxin-Catalyzed ADP-Ribosylation of a Membrane Protein: Unique Modification of the Receptor-Adenylate Cyclase Signal Transduction.- 12.6 The Inhibitory Guanine Nucleotide-Binding Protein.- 12.7 How Does Pertussis Toxin Inhibit Adenylate Cyclase?.- 12.8 Pertussis Toxin: A Useful Tool in Cell Biology.- 12.8.1 Phospholipase Activation and Ca2+ Mobilization.- 12.8.2 Muscarinic and Other Receptors.- 12.8.3 Transducin.- 12.9 Novel Target Proteins of Pertussis Toxin.- References.- 13 Diphtheria Toxin.- 13.1 General Characteristics.- 13.2 Uptake of Diphtheria Toxin into the Cytosol.- 13.2.1 Structural and Functional Relationships.- 13.2.2 The Receptor.- 13.2.3 The Entry Mechanism.- 13.3 The ADP-Ribosylation Activity.- 13.4 Structural Studies.- References.- 14 Cellular Transferases.- 14.1 Introduction.- 14.2 ADP-Ribosyltransferases from Erythrocytes.- 14.3 ADP-Ribosylation of Elongation Factor-2 by a Cellular ADP-Ribosyltransferase.- 14.4 Nuclear ADP-Ribosyltransferases.- 14.5 ADP-Ribosyltransferase of Rat Hepatic Tissue.- 14.6 ADP-Ribosyltransferase of Xenopus laevis.- 14.7 Thyroid Membrane ADP-Ribosyltransferase Activity.- 14.8 ADP-Ribosylation of Renal Brush Border Membrane Proteins.- 14.9 ADP-Ribosyltransferase Activity in Skeletal Muscle.- 14.10 ADP-Ribosyltransferase Activity in Testicular Cells.- 14.11 ADP-Ribosyltransferase Activity in Cholinergic Nerve Terminals.- 14.12 ADP-Ribosyltransferase Activity in Rat Islets of Langerhans.- 14.13 ADP-Ribosylation of Stress-Inducible and Glucose-Regulated Proteins.- 14.14 ADP-Ribosylation in Adipocyte Plasma Membranes.- 14.15 Possible Function of Cellular ADP-Ribosyltransferases.- 14.16 Reversible Regulation of the Fe Protein of Nitrogenase from Rhodospirillum rubrum by ADP-Ribosylation.- References.- 15 Mitochondria.- 15.1 Introduction.- 15.2 Mitochondria and Ca2+.- 15.3 Oxidation and Hydrolysis of Mitochondrial Pyridine Nucleotides Parallel Ca2+ Release.- 15.4 Mitochondrial ADP-Ribosylation.- 15.4.1 ADP-Ribosylation in Mitochondrial Extracts.- 15.4.2 ADP-Ribosylation in the Inner Mitochondrial Membrane.- References.- 16 The Bond.- 16.1 Introduction.- 16.2 Ester-Specific ADP-Ribosylation.- 16.3 Diphthamide-Specific ADP-Ribosylation.- 16.4 Arginine-Specific ADP-Ribosylation.- 16.5 Cysteine-Specific ADP-Ribosylation.- 16.6 ADP-Ribosylation at Unknown Acceptor Sites.- 16.6.1 Studies with Eukaryotic Cells.- 16.6.2 Prokaryotic Systems.- 16.7 Nonenzymatic ADP-Ribosylation.- 16.8 Release of ADP-Ribose from Acceptor Sites.- 16.8.1 Enzymatic Processing.- 16.8.2 Chemical Release and Analysis.- 16.9 Proteins Modified by ADP-Ribose in Vivo.- References.
Band 37

ADP-Ribosylation of Proteins

Enzymology and Biological Significance

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ADP-Ribosylation of Proteins

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01.02.2012

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Springer Berlin

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238

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24,4/17/1,5 cm

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Details

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Taschenbuch

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01.02.2012

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Springer Berlin

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238

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24,4/17/1,5 cm

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Softcover reprint of the original 1st ed. 1987

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  • ADP-Ribosylation of Proteins
  • I Poly-ADP-Ribosylation Reactions (F. R. Althaus).- 1 Poly(ADP-Ribose): Structure, Properties, and Quantification.- 1.1 Structure and Physicochemical Properties.- 1.2 Detection and Quantification of Poly(ADP-Ribose) in Biological Material.- References.- 2 Poly(ADP-Ribose) Biosynthesis.- 2.1 Natural Occurrence of Poly-ADP-Ribosylation Activity in Different Species, Tissues, and Cell Types.- 2.2 Subcellular Distribution of Poly-ADP-Ribosylation Activity.- 2.3 Purified Poly(ADP-Ribose) Polymerase.- 2.3.1 Physicochemical Properties.- 2.3.2 Domain Structure.- 2.3.3 Enzymological Properties.- References.- 3 Poly(ADP-Ribose) Catabolism.- 3.1 Enzymes Involved in Poly(ADP-Ribose) Catabolism.- 3.2 Factors Affecting Poly(ADP-Ribose) Catabolism.- References.- 4 Nuclear Acceptor Proteins for Poly(ADP-Ribose) and the Functional Consequences of Poly-ADP-Ribosylation on the Acceptor Species.- 4.1 Acceptor Proteins Identified in Reconstituted in Vitro Systems Involving Purified Poly(ADP-Ribose) Polymerase.- 4.2 Acceptor Proteins Identified in “Broken Cell” Systems or Polynucleosomal Preparations.- 4.3 Acceptor Proteins Which Have Been Identified in Intact Cells.- References.- 5 Poly-ADP-Ribosylation and Chromatin Organization.- 5.1 Introductory Comments.- 5.2 Electron Microscopy Investigations of Poly(ADP-Ribose)-Modified Chromatin.- 5.3 Biochemical Analyses of Poly(ADP-Ribose)-Modified Chromatin.- 5.4 Characterization of Sites Adjacent to Poly-ADP-Ribosylation in Bulk Chromatin.- References.- 6 Poly-ADP-Ribosylation in the Recovery of Mammalian Cells from DNA Damage.- 6.1 Introduction.- 6.2 DNA Damage, Activation of Poly(ADP-Ribose) Polymerase, and NAD Depletion in Mammalian Cells.- 6.3 Inhibitors of Poly(ADP-Ribose) Polymerase in the Investigation of the Role of Poly-ADP-Ribosylation Reactions in DNA-Excision Repair.- 6.3.1 Specificity of Poly(ADP-Ribose) Polymerase Inhibitors.- 6.3.2 Inhibitor Protocols Used.- 6.3.3 Consequences of Inhibited Poly(ADP-Ribose) Biosynthesis on Specific Reaction Steps in DNA-Excision Repair of Mammalian Cells.- 6.4 Effects of ADP-Ribosylation Inhibitors on the Clonal Survival of Carcinogen-Treated Cells.- 6.5 The Effects of ADP-Ribosylation Inhibitors on Chromosome Stability.- 6.6 Conclusions and Perspectives.- References.- 7 Poly(ADP-Ribose), DNA Synthesis, and Cell Cycle Progression.- 7.1 Proliferative Activity, Cell Cycle Progression, and Chromatin-Associated ADP-Ribosylation Activity.- 7.2 Poly-ADP-Ribosylation and DNA Synthesis in Isolated Nuclei.- 7.3 In Vitro Effects of Poly(ADP-Ribose) on Enzymes Acting on DNA.- References.- 8 Poly(ADP-Ribose), Cellular Differentiation, and Gene Expression.- 8.1 Introduction.- 8.2 Poly-ADP-Ribosylation in Differentiating Tissues and Cells.- 8.3 Evidence Derived from Inhibitor Studies.- 8.4 Possible Mechanism(s) of Poly(ADP-Ribose) Involvement in RNA Metabolism and Gene Expression.- References.- 9 Poly(ADP-Ribose) in Inherited Human Diseases and Experimental Disease Models.- 9.1 Glutamyl Ribose-5-Phosphate Storage Disease — A Hereditary Defect in the Catabolism of Poly(ADP-Ribosyl)ated Proteins.- 9.2 Collagen Vascular Diseases.- 9.2.1 Systemic Lupus Erythematosus (SLE).- 9.2.2 Other Collagen Vascular Diseases.- 9.3 Diseases Associated with Disorders of DNA Repair.- 9.3.1 Xeroderma Pigmentosum (XP).- 9.3.2 Ataxia Teleangiectasia (AT).- 9.3.3 Fanconi’s Anemia (FA).- 9.4 Experimental Diabetes.- 9.5 Neoplastic Transformation in Vitro and in Vivo.- 9.5.1 In Vitro Transformation Systems.- 9.5.2 Transformation in Vivo.- References.- II Mono-ADP-Ribosylation Reactions (Ch. Richter).- 10 Signal Transduction.- 10.1 Introduction.- 10.2 Guanine Nucleotide-Binding Regulatory Proteins Involved in Signal Transduction.- 10.3 Adenylate Cyclase.- 10.4 Transducin.- 10.5 Receptor-Stimulated Phosphodiesterase Stimulation and Calcium Mobilization.- 10.6 The ras Gene Product.- References.- 11 Cholera Toxin.- 11.1 The Discovery of Cholera Toxin.- 11.2 The Structure of Cholera Toxin.- 11.3 Interaction with the Receptor.- 11.4 Membrane Penetration and Processing.- 11.5 Enzymatic Activities of Cholera Toxin: NAD + Hydrolysis and ADP-Ribosyltransfer.- 11.6 Activation of Adenylate Cyclase.- 11.7 Cofactor Requirement for ADP-Ribosylation of Adenylate Cyclase.- 11.8 ADP-Ribosylation of Transducin.- 11.9 Minor Protein Substrates of Cholera Toxin.- References.- 12 Pertussis Toxin.- 12.1 The Discovery of Pertussis Toxin.- 12.2 The Structure of Pertussis Toxin.- 12.3 Pertussis Toxin Activation and Processing.- 12.4 Pertussis Toxin-Sensitive Cells.- 12.5 Pertussis Toxin-Catalyzed ADP-Ribosylation of a Membrane Protein: Unique Modification of the Receptor-Adenylate Cyclase Signal Transduction.- 12.6 The Inhibitory Guanine Nucleotide-Binding Protein.- 12.7 How Does Pertussis Toxin Inhibit Adenylate Cyclase?.- 12.8 Pertussis Toxin: A Useful Tool in Cell Biology.- 12.8.1 Phospholipase Activation and Ca2+ Mobilization.- 12.8.2 Muscarinic and Other Receptors.- 12.8.3 Transducin.- 12.9 Novel Target Proteins of Pertussis Toxin.- References.- 13 Diphtheria Toxin.- 13.1 General Characteristics.- 13.2 Uptake of Diphtheria Toxin into the Cytosol.- 13.2.1 Structural and Functional Relationships.- 13.2.2 The Receptor.- 13.2.3 The Entry Mechanism.- 13.3 The ADP-Ribosylation Activity.- 13.4 Structural Studies.- References.- 14 Cellular Transferases.- 14.1 Introduction.- 14.2 ADP-Ribosyltransferases from Erythrocytes.- 14.3 ADP-Ribosylation of Elongation Factor-2 by a Cellular ADP-Ribosyltransferase.- 14.4 Nuclear ADP-Ribosyltransferases.- 14.5 ADP-Ribosyltransferase of Rat Hepatic Tissue.- 14.6 ADP-Ribosyltransferase of Xenopus laevis.- 14.7 Thyroid Membrane ADP-Ribosyltransferase Activity.- 14.8 ADP-Ribosylation of Renal Brush Border Membrane Proteins.- 14.9 ADP-Ribosyltransferase Activity in Skeletal Muscle.- 14.10 ADP-Ribosyltransferase Activity in Testicular Cells.- 14.11 ADP-Ribosyltransferase Activity in Cholinergic Nerve Terminals.- 14.12 ADP-Ribosyltransferase Activity in Rat Islets of Langerhans.- 14.13 ADP-Ribosylation of Stress-Inducible and Glucose-Regulated Proteins.- 14.14 ADP-Ribosylation in Adipocyte Plasma Membranes.- 14.15 Possible Function of Cellular ADP-Ribosyltransferases.- 14.16 Reversible Regulation of the Fe Protein of Nitrogenase from Rhodospirillum rubrum by ADP-Ribosylation.- References.- 15 Mitochondria.- 15.1 Introduction.- 15.2 Mitochondria and Ca2+.- 15.3 Oxidation and Hydrolysis of Mitochondrial Pyridine Nucleotides Parallel Ca2+ Release.- 15.4 Mitochondrial ADP-Ribosylation.- 15.4.1 ADP-Ribosylation in Mitochondrial Extracts.- 15.4.2 ADP-Ribosylation in the Inner Mitochondrial Membrane.- References.- 16 The Bond.- 16.1 Introduction.- 16.2 Ester-Specific ADP-Ribosylation.- 16.3 Diphthamide-Specific ADP-Ribosylation.- 16.4 Arginine-Specific ADP-Ribosylation.- 16.5 Cysteine-Specific ADP-Ribosylation.- 16.6 ADP-Ribosylation at Unknown Acceptor Sites.- 16.6.1 Studies with Eukaryotic Cells.- 16.6.2 Prokaryotic Systems.- 16.7 Nonenzymatic ADP-Ribosylation.- 16.8 Release of ADP-Ribose from Acceptor Sites.- 16.8.1 Enzymatic Processing.- 16.8.2 Chemical Release and Analysis.- 16.9 Proteins Modified by ADP-Ribose in Vivo.- References.