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ADP-Ribosylation Reactions

Editat de Guy G. Poirier, Pierre Moreau
en Limba Engleză Paperback – 8 noi 2012
This monograph is dedicated to one of the discoverers of poly(ADP­ ribose), Professor Paul Mandel, from the Centre de Neurochimie in Strasbourg. We would like to congratulate him for his distinguished contributions to the field of poly(ADP-ribosyl)ation and express our gratitude for his support in the last years and particularly for his encouragement for the organization of this meeting. Poly(ADP-ribose) was discovered more than 25 years ago. Since then, excellent progress has been made on the study of the mechanisms of poly(ADP­ ribose) reaction. The last five years have been particularly exciting since the development of various molecular biology techniques has revealed the complex nature of this multifunctional enzyme. Looking at the contributions presented at this meeting, it becomes obvious that more work at the molecular level is needed. Most likely, these experiments will shed some light on the functions of poly(ADP-ribose), but further ~iophysical studies will still be required to fully understand this complex enzymatic system.
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Specificații

ISBN-13: 9781461264569
ISBN-10: 1461264561
Pagini: 452
Ilustrații: XXXVI, 410 p.
Dimensiuni: 155 x 235 x 24 mm
Greutate: 0.63 kg
Ediția:Softcover reprint of the original 1st ed. 1992
Editura: Springer
Colecția Springer
Locul publicării:New York, NY, United States

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Descriere

This monograph is dedicated to one of the discoverers of poly(ADP­ ribose), Professor Paul Mandel, from the Centre de Neurochimie in Strasbourg. We would like to congratulate him for his distinguished contributions to the field of poly(ADP-ribosyl)ation and express our gratitude for his support in the last years and particularly for his encouragement for the organization of this meeting. Poly(ADP-ribose) was discovered more than 25 years ago. Since then, excellent progress has been made on the study of the mechanisms of poly(ADP­ ribose) reaction. The last five years have been particularly exciting since the development of various molecular biology techniques has revealed the complex nature of this multifunctional enzyme. Looking at the contributions presented at this meeting, it becomes obvious that more work at the molecular level is needed. Most likely, these experiments will shed some light on the functions of poly(ADP-ribose), but further ~iophysical studies will still be required to fully understand this complex enzymatic system.

Cuprins

1: Molecular Biology.- Structure and Function of the Human Poly(ADP-Ribose) Polymerase.- Cloning of Poly(ADP-Ribose) Polymerase cDNA from Lower Eukaryotes.- Molecular Biology of Human Nuclear NAD+: ADP-Ribosyl-transferase (Polymerizing).- Strategies for Studying the Functions of PADPRP Genes on Human Chromosomes 1 and 13.- Expression of the DNA-Binding Domain of Human Poly(ADP-Ribose) Polymerase as a Trans-Dominant Inhibitor of Poly(ADP-Ribosyl)ation in Transfected Eucaryotic Cell Lines.- Directed Mutagenesis of Glutamic Acid 988 of Poly(ADP-Ribose) Polymerase.- Chicken Poly(ADP-Ribose) Polymerase. Complete Protein Sequence Deduced from cDNA, Comparison with Mammalian Enzyme Sequences.- Nuclear Poly(ADPR) Polymerase Expression and Activity in Rat Astrocytes Culture: Effects of bFGF.- Molecular Cloning of the Rat Poly(ADP-Ribose) Polymerase Gene and Preliminary Characterization of its Promoter and 5’-Flanking Regions.- Structure and Organization of the Mouse pADPRT Gene.- Strategies for Expressing Analogs of PADPRP in Eukaryotic Cells.- Expression and Characterization of PADPRP and a Novel Glucocorticoid-PADPRP “Finger Swapped” Protein from Escherichia coil.- Tumor Promoters, But Not EGF, Increase Nuclear Poly(ADP-Ribose) Polymerase Gene Expression in Rat Hepatocytes Initiated in Utero with DMN and Cultured After Birth in Low-Calcium Synthetic Medium.- Expression of the Gene for Poly(ADP-Ribose) Polymerase and DNA Polymerase ß in Rat Tissues and in Proliferating Cells.- Expression of Poly(ADP-Ribose) Polymerase in Differentiating HL-60 Cells..- 2: Cancer, DNA Repair, and Metabolism.- A Novel Model of Enzymatic Repair of U.V.-Induced DNA Damage in Human Cells.- Poly(ADP-Ribose) Polymerase in Xenopus Laevis.- ADP-Ribosylation is Involved in the Integration of Exogenous DNA into the Mammalian Cell Genome, but is not Required for the Episomal Replication or Expression of Autonomously Replicating Plasmids.- Inhibitors of Poly(ADP-Ribose) Polymerase Block the Infection of Mammalian Cells by Retroviral Vectors.- Detection and Analysis of NAD Binding Proteins Including Poly(ADP-Ribose) Polymerase Immobilized on the Membrane.- An In Vitro Replication System for Autonomously Replicating Mammalian Origin-Enriched Sequences.- Variation in Poly(ADP-Ribose) Polymerase Activity and 2’, 5’-Oligoadenylates Core Concentration in Estrogen-Stimulated Uterus and Liver of Immature and Adult Rats.- Possible Involvement of Poly(ADP-Ribose) Polymerase in the Brain Function.- Inhibition of Interferon-?-Dependent Induction of Major Histocompatibility Complex Class II Antigen by Expressing Exogenous Poly(ADP-Ribose) Synthetase Gene.- ADP-Ribose Polymers Bind Specifically and Non-covalently to Histones.- Poly(3’-deoxy ADP-ribosyl)ation of Proteins in Liver Chromatin Isolated from Rats Fed with Hepatocarcinogens.- ADP-Ribose Polymer Metabolism: Implications for Human Nutrition.- Some Aspects of Nuclear and Cytoplasmic ADP-ribosylation. Biological and Pharmacological Perspectives.- DNA Base Excision Repair Stimulates Poly(ADP-Ribose) Synthesis.- Studies on Poly(ADP-Ribosyl)ation in DNA Amplification and Mammalian Longevity.- DNA Topoisomerase I and Poly(ADP-Ribose) Polymerase in the Early Stages of Hepatocarcinogenesis.- Poly(ADP-Ribose) Polymerase Inhibitors Induce Murine Melanoma Cell Differentiation by a Mechanism Independent of Alterations in cAMP Levels and Protein Kinase A Activity.- Enhancement of Antimetabolite Cytoatoxicity by 3-Aminobenzamide in Chinese Hamster Ovary Cells is Independent of Poly(ADP-Ribose) Polymerase Inhibition.- Evidence for the Participation of Poly(ADP-Ribosyl)ation in Collagenase Gene Expression in Rabbit Synovial Fibroblasts after Treatment with Active Oxygen Released by Xantbin/Xanthinoxidase.- Enhancement of Oncogene-Mediated Transformation in Cloned Rat Embryo Fibroblast (CREF) Cells by 3-Anilnobenzamide.- Control of Procollagen Gene Transcription and Prolyl Hydroxylase Activity by Poly(ADP-Ribose).- Poly(ADP-Ribose) Synthesis in Lymphocytes of Systemic Lupus Erythematosus Patients.- Possible Involvement of Poly(ADP-Ribosyl)ation in Phenobarbital Promotion Activity in Rat Hepatocarcinogenesis.- 1-Methylnicotinamide Stimulates Cell Growth, Causes DNA Hypermethylation and Inhibits Induced Differentiation of Friend Erythroleukemia Cells.- 2-Aminobenzamide Antagonizes DNA De-methylation which Precedes Induced Differentiation of Friend Erythroleukemia Cells by N’-Methylnicotinamide.- ADP-Ribosylation of Rubisco in Lettuce Chloroplasts.- In Vivo Evidence in Humans of an Association Between ADP-Ribosylation Levels in Mononuclear Leukocytes and Immune Function.- Evaluation of the DNA Damage and Inhibition of DNA Repair Caused by the Benzamide Derivative Metoclopramide in Human Peripheral Mononuclear Leukocytes.- Nuclear ADP-Ribosyltranferase as Target Antigen in Chronic Graft-Versus-Host Disease.- Induction of Poly ADP-Ribosylation in Human Malignant Cells.- Proteolytic Cleavage of Poly(ADP-Ribose) Polymerase in Human Leukemia Cells Treated with Etoposide and Other Cytotoxic Agents.- ADP-Ribosylation of Topoisomerase II in Physiological Conditions.- Regulation of DNA Polymerase ß by Poly(ADP-Ribose) Polymerase.- Extensive Purification of Nuclear Poly(ADP-Ribose) Glycohydrolase.- Poly(ADP-Ribose) Polymerase and NMN Adenylyl-Transferase Interaction: Molecular and Immunological Studies.- Covalent Modification of Poly(ADP-Ribose) Polymerase by Reactive Benzamides.- Alterations in Repair of DNA Damage in Poly(ADP-Ribose) Polymerase Deficient Cell Lines.- 3: Enzymology.- Amino Acid Specific Modification of Poly(ADP-Ribose) Polymerase with Monomers and Polymers of ADP-Ribose.- Enzymatic Properties of Poly(ADP-Ribose) Polymerase and Poly(ADP-Ribose) Glycohydrolase on Chromatin.- A New “Transition-State” Inhibitor Specific for Poly(ADP-Ribose) Glycohydrolase.- Histones Affect Polymer Patterns Produced by Poly(ADP-Ribose) Polymerase.- Proteolytic Degradation of Poly(ADP-Ribose) Polymerase by Contaminating Proteases in Commercial Preparations of DNAse I.- Inactivation of the Polymerase but not the DNA Binding Function of ADPRT by Destabilization of one of its Zn2+ Coordination Centers by 6-Nitroso-1,2-Benzopyrone.- Conversion of Poly(ADP-Ribose) Polymerase Activity to NAD-Glycohydrolase During Retinoic Acid Induced Differentiation of HL60 Cells.- Improved Assays of Poly(ADP-Ribose) Metabolizing Enzymes.- Specific Inhibitors of Poly(ADP-Ribose) Synthetase.- Automodification and NADase Activity of Poly(ADP-Ribose) Polymerase.- The Poly(ADP-Ribose)-Protein Shuttle of Chromatin.- 4: Mono ADP-Ribosylation.- Endogenous Mono-ADP-Ribosylation of Wild-Type and Mutant Elongation Factor 2 in Eukaryotic Cells.- Heterogeneity of ADP-Ribosylation Reaction in Sulfolobus solfataricus.- A Novel C3-like ADP-Ribosyltransferase Produced by Clostridium limosum.- The 52 kDa ADP-Ribosylated Protein in the Rat Heart Plasma Membrane: Is it Gsa?.- Biochemical and Developmental Characterization of ADP-Ribosylation Factors A Family of 20 kDa Guanine Nucleotide-binding Proteins.- Nonenzymatic ADP-Ribosylation of Cysteine.- Molecular and Immunological Characterization of ADP-Ribosylarginine Hydrolases.- Characterization of the Family of Mammalian Genes Encoding ADP-Ribosylation Factors.- Purification and Characterisation of NAD: Arginine Mono ADP-Ribosyl Transferase from Chicken Erythrocytes; Identification of some Enzyme Inhibitors.- Target Proteins for Arginine Specific ADP-Ribosyltransferase in Chickens.- NAD+ Biosynthesis in Human Placenta: Characterization of Homogeneous NMN Adenylyltransferase.