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  • 1
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Enzymes -- Periodicals. ; Enzymes. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (525 pages)
    Edition: 3rd ed.
    ISBN: 9780080865959
    Series Statement: Issn Series
    DDC: 810.9868
    Language: English
    Note: Front Cover -- The Enzymes: Control by Phosphorylation -- Copyright Page -- Contents -- Preface -- Section I: Control of Specific Enzymes (Continued) -- Chapter 1. Enzymes of the Fructose 6-Phosphate-Fructose 1,6-Bisphosphate Substrate Cycle -- I. Introduction -- II. Purification of Hepatic 6-Phosphofructo-2-Kinase- Fructose-2,6-Bisphosphatase -- III. Assay of 6-Phosphofructo-2-Kinase Activity -- IV. Assay of Fructose-2,6-Bisphosphatase Activity -- V. Structural Properties -- VI. Catalytic Properties of Rat Liver 6-Phosphofructo-2-Kinase -- VII. Catalytic Properties of Rat Liver Fructose-2,6- Bisphosphatase -- VIII. Evidence for Two Catalytic Centers -- IX. Regulation of 6-Phosphofructo-2-Kinase- Fructose-2,6-Bisphophatase by Low-Molecular-Weight Effectors -- X. Regulation of 6-Phosphofructo-2-Kinase-Fructose-2,6- Bisphosphatase by Phosphorylation-Dephosphorylation -- XI. 6-Phosphofructo-1 -Kinase: Possible Role of Phosphorylation in the Control of Enzyme Activity -- XII. Fructose-l,6-Bisphosphatase: Possible Role of Phosphorylation in Control of Enzyme Activity -- XIII. Role of 6-Phosphofructo-2-Kinase-Fructose-2,6- Bisphosphatase in the Hormonal Control of Hepatic Gluconeogenesis and Glycolysis -- XIV. Summary and Overview -- References -- Chapter 2. Pyruvate Kinase -- I. Introduction -- II. Influence of Phosphorylation on the Kinetic Properties of Liver Pyruvate Kinase -- III. Influence of Phosphorylation on the Sensitivity of Liver Pyruvate Kinase to Proteolytic Enzymes -- IV. The Reaction of Cyclic AMP-Dependent Protein Kinase with Liver Pyruvate Kinase as Substrate -- V. Dephosphorylation of Liver Pyruvate Kinase with Phosphoprotein Phosphatases -- VI. Acute Hormonal Regulation of Liver Pyruvate Kinase in Vivo and in Intact Cells -- VII. Phosphorylation of Other Pyruvate Kinases -- VIII. Concluding Remarks -- References. , Chapter 3. Pyruvate Dehydrogenase -- I. Introduction -- II. Mammalian Pyruvate Dehydrogenase Complex -- III. Pyruvate Dehydrogenase Kinase -- IV. Pyruvate Dehydrogenase Phosphatase -- V. Regulation of Mammalian Pyruvate Dehydrogenase Complex -- VI. Comparison of Properties of Mitochondrial a-Ketoacid Dehydrogenase Kinases and Phosphatases -- References -- Chapter 4. Branched-Chain Ketoacid Dehydrogenase -- I. Introduction -- II. Animal Branched-Chain Ketoacid-Dehydrogenase Complex -- III. Regulation by Reversible Phosphorylation -- IV. Biological Significance of Reversible Phosphorylation -- V. Addendum -- References -- Chapter 5. Acetyl-Coenzyme A Carboxylase -- I. Introduction -- II. Structural Aspects and Regulation by Allosteric Effectors -- III. Short-Term Hormonal Regulation of Fatty Acid Synthesis Associated with Persistent Changes in Acetyl-CoA Carboxylase Activity -- IV. Early Evidence for the Regulation of Acetyl-CoA Carboxylase by Reversible Phosphorylation -- V. Effects of Hormones on the level of Phosphorylation of Acetyl-CoA Carboxylase within Intact Cell Preparations -- VI. Protein Kinases That Phosphorylate Acetyl -CoA Carboxylase -- VII. Protein Phosphatases That Act on Acetyl-CoA Carboxylase -- VIII. Concluding Remarks -- References -- Chapter 6. Hormone-Sensitive Lipase -- I. Introduction -- II. Properties -- II. Mechanism of Regulation of the Adipose Tissue Lipase -- IV. Possible Role as a Hormone-Activatable, Multifunctional Tissue Lipase -- V. Conclusions and Perspectives -- References -- Chapter 7. Hydroxymethylglutaryl- Coenzyme A Reductase -- I. Introduction -- II. Topology -- III. Multivalent Control -- IV. Reversible Phosphorylation in Vitro -- V. lntracellular Phosphorylation -- VI. Reversible Phosphorylation and Degradation -- References -- Chapter 8. Aromatic Amino Acid Hydroxylases -- I. Introduction. , II. Phenylalanine Hydroxylase -- III. Tyrosine Hydroxylase -- IV. Tryptophan Hydroxylase -- References -- Section II: Control of Biological Processes -- Chapter 9. Phosphorylation of Bra in Proteins -- I. Introduction -- II. Protein Kinases in the Brain -- III. Phosphoproteins in the Brain -- IV. Protein Phosphatases in the Brain -- V. Conclusion -- References -- Chapter 10. Regulation of Receptor Function -- I. Introduction and Perspectives -- II. The β-Adrenergic Receptor -- III. Rhodopsin -- IV. The Nicotinic Acetylcholine Receptor -- V. The Receptors for EGF and Insulin -- VI. Other Membrane Receptors -- References -- Chapter 11. Regulation of Ionic Channels -- I. Introduction -- II. Calcium Channels -- III. Potassium Channels -- IV. Acetylcholine Receptor -- V. Sodium Channels -- VI. Conclusions -- References -- Chapter 12. Regulation of Protein Synthesis -- I. Introduction -- II. Initiation of Protein Synthesis in Eukaryotic Cells -- III. Role of elF-2 in Eukaryotic Protein Chain Initiation and the Effect of elF-2α Phosphorylation -- IV. Heme-Regulated elF-2α Kinase -- V. dsRNA-Dependent elF-2α Kinase -- VI. Biological Significance of HRI and dsl -- VII. Guanine Nucleotide-Binding Proteins -- References -- Chapter 13. Regulation of Contractile Activity -- I. Introduction -- II. Regulation of Vertebrate Smooth-Muscle Myosin by Phosphorylation -- III. Role of Phosphorylation in Modulating Contractile Activity of Striated Muscle Proteins -- IV. Phosphorylation-Dependent Regulatory Systems in Invertebrate Muscles -- VI. Summary -- References -- Chapter 14. Protein Phosphorylation in Prokaryotes and Single-Celled Eukaryotes -- I. Introduction -- II. Protein Phosphorylation in Prokaryotes -- III. Protein Phosphorylation in Single-Celled Eukaryotes -- IV. General Comments -- References -- Author Index -- Subject Index.
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  • 2
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Enzymes -- Periodicals. ; Enzymes. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (623 pages)
    Edition: 3rd ed.
    ISBN: 9780080865942
    Series Statement: Issn Series
    DDC: 810.9868
    Language: English
    Note: Front Cover -- The Enzymes, Volume XVII -- Copyright Page -- Contents -- Preface -- Section I. Enzymology of Control by Phosphorylation -- Chapter 1. The Enzymology of Control by Phosphorylation -- I. Historical Aspects of Protein Phosphorylation -- II. Protein Phosphorylation-Dephosphorylation Reactions -- III. Classification of Protein Kinases and Phosphoprotein Phosphatases -- IV. Protein Phosphorylation and the Regulation of Biological Processes -- References -- Chapter 2. Cyclic Cascades and Metabolic Regulation -- I. Perspectives -- II. Features of Cyclic Cascade Systems -- III. Experimental Verification of the Cyclic Cascade Model -- IV. Energy Consumption -- V. Covalent Interconversion versus Simple Allosteric Control -- VI. Concluding Remarks -- References -- Chapter 3. Cyclic Nucleotide-Dependent Protein Kinases -- I. Introduction -- II. Purification -- III. Characterization and Physical Properties -- IV. Mechanism of Action -- V. Biological Role of Protein Kinases -- References -- Chapter 4. Calmodulin-Dependent Protein Kinases -- I. Introduction -- II. Myosin Light Chain Kinases -- III. Multifunctional Calmodulin-Dependent Protein Kinases -- References -- Chapter 5. Protein Kinase C -- I. Introduction -- II. Properties -- III. Biochemical Activation -- IV. Physiological Activation -- V. Action of Tumor Promoters -- VI. Inhibitors -- VII. Synergistic Roles with Calcium -- VIII. Growth Response and Down Regulation -- IX. Target Proteins and Catalytic Specificity -- X. Relation to Other Receptors -- XI. Conclusion -- References -- Chapter 6. Viral Oncogenes and Tyrosine Phosphorylation -- I. Introduction and Historical Perspective -- II. Individual Viral Protein-Tyrosine Kinases and Their Cellular Homologues -- III. Other Transformation-Related Tyrosine Phosphorylation Systems -- IV. General Properties of Protein-Tyrosine Kinases. , V. Cellular Substrates for Protein-Tyrosine Kinases -- VI. Conclusions -- References -- Chapter 7. The Insulin Receptor and Tyrosine Phosphorylation -- I. Introduction and Scope -- II. Structure of the Insulin Receptor and Its Relation to Other Tyrosine-Specific Protein Kinases -- III. Properties of Tyrosine-Specific Protein Kinases -- IV. Tyrosine Phosphorylation of Insulin Receptors and Other Proteins in the Intact Cell -- V. Regulation of Hormone Receptors by Multisite Phosphorylation -- VI. Evidence That Tyrosine Phosphorylation Is Physiologically Important -- VII. Conclusions -- References -- Chapter 8. Phosphoprotein Phosphatases -- I. Introduction and Historical Overview: The "PR Enzyme -- II. Classification of Protein Phosphatases -- III. Phosphatase Type 1 (Phosphorylase Phosphatase) -- IV. Phosphatase Type 2A -- V. Phosphatase Type 2B (Calcineurin) -- VI. Phosphatase Type 2C -- VII. Phosphotyrosyl-Protein Phosphatases -- References -- Section II. Control of Specific Enzymes -- Chapter 9. Glycogen Phosphorylase -- I. Introduction -- II. Enzymic Characteristics of Phosphorylase -- III. Molecular Structure -- IV. Substrate-Directed Control of Phosphorylation and Dephosphorylation -- V. Structural Consequences of Serine-14 Phosphorylation -- VI. Functional Results of the Phosphorylation of Serine-14 -- VII. Concluding Remarks -- References -- Chapter 10. Phosphorylase Kinase -- I. Introduction -- II. Physicochemical Properties -- III. Subunit Function and Interaction between Subunits -- IV. Catalytic Properties -- V. Regulation of Phosphorylase Kinase Activity by Allosteric Effectors -- VI. Proteolytic Activation of Phosphorylase Kinase -- VII. Covalent Regulation: In Vitro Studies -- VIII. Regulation of Phosphorylase Kinase in Intact Cells -- References -- Chapter 11. Muscle Glycogen Synthase -- I. Introduction. , II. Structure of Glycogen Synthase from Mammalian Skeletal Muscle -- III. Glycogen Synthase Kinases in Mammalian Skeletal Muscle -- IV. Effect of Phosphorylation on the Activity of Skeletal-Muscle Glycogen Synthase -- V. Synergism between Glycogen Synthase Kinase-3 and Glycogen Synthase Kinase-5 -- VI. The Glycogen Synthase Phosphatases in Skeletal Muscle -- VII. Phosphorylation State of Skeletal-Muscle Glycogen Synthase in Vivo -- VIII. Interpretation of in Vivo Phosphorylation Experiments -- References -- Chapter 12. Liver Glycogen Synthase -- I. Introduction -- II. Liver Glycogen Synthase -- III. Converting Enzymes -- IV. Phosphorylation of Liver Glycogen Synthase -- V. Comparative Enzymology of Glycogen Synthase -- VI. Control of Hepatic Glycogen Synthase -- VII. Conclusion -- References -- Author Index -- Subject Index.
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  • 3
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Treatment of PC12 pheochromocytoma cells with nerve growth factor (NGF) or bradykinin leads to the activation of extracellular signal-regulated kinases ERK1 and ERK2, two isozymes of microtubule-associated protein 2 (MAP) kinase that are present in numerous cell lines and regulated by diverse extracellular signals. The activation of MAP kinase is associated with its phosphorylation on tyro-sine and threonine residues, both of which are required for activity. In the present studies, we have identified a factor in extracts of PC12 cells treated with NGF or bradykinin, named MAP kinase activator, that, when reconstituted with inactive MAP kinase from untreated cells, dramatically increased MAP kinase activity. Activation of MAP kinase in vitro by this factor required MgATP and was associated with the phosphorylation of a 42- (ERK1) and 44-kDa (ERK2) polypeptide. Incorporation of 32P into ERK1 and ERK2 occurred primarily on tyrosine and threonine residues and was associated with a single tryptic peptide, which is identical to one whose phosphorylation is increased by treatment of intact PC12 cells with NGF. Thus, the MAP kinase activator identified in PC12 cells is likely to be a physiologically important intermediate in the signaling pathways activated by NGF and bradykinin. Moreover, stimulation of the activator by NGF and bradykinin suggests that tyrosine kinase receptors and guanine nucleotide-binding protein-coupled receptors are both capable of regulating these pathways.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 80 (1958), S. 2906-2907 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 6 (1967), S. 423-434 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 8049-8057 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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