Cellular Regulation by Protein Phosphorylation: Nato ASI Subseries H:, cartea 56
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Specificații
ISBN-13: 9783642751448
ISBN-10: 364275144X
Pagini: 524
Ilustrații: XIII, 501 p.
Dimensiuni: 170 x 242 x 28 mm
Greutate: 0.83 kg
Ediția:Softcover reprint of the original 1st ed. 1991
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Nato ASI Subseries H:
Locul publicării:Berlin, Heidelberg, Germany
ISBN-10: 364275144X
Pagini: 524
Ilustrații: XIII, 501 p.
Dimensiuni: 170 x 242 x 28 mm
Greutate: 0.83 kg
Ediția:Softcover reprint of the original 1st ed. 1991
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Nato ASI Subseries H:
Locul publicării:Berlin, Heidelberg, Germany
Public țintă
ResearchCuprins
I. Background and General Introduction.- Signal Integration in Phosphorylase Kinase.- Physical Approaches to Conformation and Assembly of Biological Macromolecules.- A Vibrational Raman Spectroscopic Study of Myosin and Myosin-Vanadate Interactions.- Phosphorylation and the Frequency Encoding of Signal-induced Calcium Oscillations.- II. Methodology.- Determination of Phosphorylated Amino Acids in Protein Sequences.- Back-Phosphorylation - a Sensitive Technique to Study Protein Phosphorylation in the Intact Heart.- Thermal Transitions in Cardiac Troponin and Its Subunits.- Dynamic Phosphorylation of a Small Chloroplast Protein Exhibiting So Far Undescribed Labelling Properties.- Identification of Phosphorylation Sites in the Nicotinic Acetylcholine Receptor by Edman Degradation and Mass Spectroscopy LC/MS and LC/MS/MS.- A Sensitive Colorimetric Assay for Protein Phosphatase Activity.- III. Structure - Function Relationship.- Protein Kinase Structure and Function: cAMP-Dependent Protein Kinase.- Expression in E. Coli of Mutated R Subunits of the cAMP-Dependent Protein Kinase From Dictyostelium Discoideum.- Expression of the -Subunit of Phosphorylase b Kinase in E. Coli.- Conformational and Shape Changes Associated with cAMP-Dependent Protein Kinase.- Crystallographic Studies of the Catalytic Subunit of cAMP-Dependent Protein Kinase.- 6-Phosphofructo 2-Kinase/Fructose 2,6-Bisphosphatase: Kinetic Changes Induced by Phosphorylation.- Enzymes Involved in the Reversible Phosphorylation in Microvessels of the Brain.- Covalent Modification of Creatine Kinase by ATP; Evidence for Autophosphorylation.- Two Adjacent Phosphoserines in Bovine, Rabbit and Human Cardiac Troponin I.- Characterisation of Thylakoid Membrane Protein Kinase by Affinity and Immunological Methods.- IV. CA 2+and Cyclic Nucleotide-Independent Phosphorylation.- A Diversity of Elements in the Protein Kinase C Signal Transduction Pathway.- “Independent” Protein Kinases: A Challenge to Canons.- Biphasic Activation of the S6 Kinase: Identification of Signalling Pathways.- Changes on the Electrophoretic Mobility of CD5 Molecules Induced by PKC-mediated Phosphorylation.- Opposing Effects of Protein Kinase C in IgE-dependent Exocytosis and InsP3 Formation.- Proteinphosphorylation in Platelets-Evidence for Increased Protein Kinase C Activity in Essential Hypertension.- Protein Phosphorylation in Luteal Membrane Fraction.- Purification of Bovine Brain Protein Kinase C Employing Metal Ion Dependent Properties.- Cardiac Protein Kinase C Isoenzymes: Phosphorylation of Phospholamban in Longitudinal and Junctional Sarcoplasmic Reticulum.- Characterization of the Phosphorylation Sites of 40S Ribosomal Protein S6.- V. Cyclic Nucleotide-Dependent Signalling.- G Protein Oncogenes.- A New Role for ? -Subunits of G-Proteins.- Conditions Favouring Phosphorylation Inhibit the Activation of Adenylate Cyclase in Human Platelet Membranes.- VI. Protein Tyrosine Phosphorylation.- Regulation of Tyrosine Kinases by Tyrosine Phosphorylation.- pp75: A Novel Tyrosine Phosphorylated Protein That Heralds Differentiation of HL-60 Cells.- Preliminary Biochemical Studies of a Drosophila Homolog of p60c-src.- Phosphoinositide Kinases and EGF Receptor Activation in Plasma Membranes of Tyrosine from A431 Cells.- Phosphorylation of Synaptophysin by the c-src Encoded Protein Tyrosine Kinase pp60c-src.- Altered Thymocyte Development Induced by Augmented Expression of p56lck.- VII. Protein Phosphatases.- Regulation and Regulatory Role of the Inactive ATP, Mg-dependent Protein Phosphatase (pp-1I).- Okadaic Acidfrom Laboratory Cultures of a Dinoflagellate Alga: Effects on Protein Phosphorylation in C3H10T1/2 Fibroblasts.- Regulation of Proto-oncogene Expression and Rate of Protein Synthesis by the Tumor Promoter Okadaic Acid.- The Use of ? Cyclodextrin in the Purification of Protein Phosphatase G from Rat Liver.- Characterization of a Human T-cell Protein Tyrosine Phosphatase Expressed in the Baculovirus System.- Inhibition of Tyrosine Protein Phosphatases from Muscle and Spleen by Nucleic Acids and Polyanions.- VIII. Control of Cellular Processes.- Biochemical Regulation of the CDC2 Protein Kinase.- Molecular and Biochemical Characterization of the Mitogen-activated S6 Kinase.- Protein Phosphorylation in the Nervous System.- Mitotic Control in Mammalian Cells, Positive and Negative Regulation by Protein Phosphorylation.- Regulation of Eukaryotic Translation by Protein Phosphorylation.- Regulation of Microfilament Assembly.- Stimulation of Human DNA Topoisomerase I by Protein Kinase C.- Protein Phosphorylation in Partially Synchronized Cell Suspension Culture of Alfalfa.- Phosphorylation of Elongation Factor Tu in vitro and in vivo.- About a Controversy Concerning the Existence of a Mitogen-responsive S6-Kinase (Late-eluting from DEAE-Sephacel).- Expression of Ferritin Messenger RNA in an in vitro Model of Human CD3-mediated T-Lymphocyte Activation.- Relaxation of Smooth Muscle at High Levels of Myosin Light Chain (MLC) Phosphorylation.- Evidence for Site- and Domain-specific Phosphorylation of the 145 kDa Neurofilament Subunit in vivo.- Tumor Necrosis Factor-induced Gene Expression and Cytotoxicity Share a Signal Transduction Pathway.- Protein Phosphorylation Is Involved in the Recognition of Pathogen-derived Signals by Plant Cells.- Effect of Membrane Modifiers onPolyphosphoinositide Synthesis in Rat Heart Sarcolemma.- Phosphorylation and Acylation of the Growth-related Murine Small Stress Protein P25.