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Life Sciences - Biochemistry & Biophysics | Interacting Protein Domains - Their Role in Signal and Energy Transduction

Interacting Protein Domains

Their Role in Signal and Energy Transduction

Proceedings of the NATO Advanced Study Institute on Structure and Function of Interacting Protein Domains in Signal and Energy Transduction, held at Acquafredda di Maratea, Italy, September 10-19, 1996

Series: Nato ASI Subseries H:, Vol. 102

Heilmeyer, Ludwig (Ed.)

Softcover reprint of the original 1st ed. 1997, X, 292 pp. 119 figs.

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  • About this book

  • * Presents the newest methods and results of general interest to biochemists
This is now the fourth time that protein phosphorylation has been the focus of a NATO Advanced Study Institute. The first meeting with the topic "Signal Trans­ duction and Protein Phosphorylation" was held on the island of Spezai, Greece, in September 1986. The second one took place in Chateau La Londe, France, in September 1989 on "Cellular Regulation by Protein Phosphorylation", the third one on " Tyrosine Phosphorylation/Dephosphorylation and Downstream Signaling" was in September 1992 in Maratea, Italy. The titles of these books clearly mirror the developments that have taken place in the last decade. Beginning with the recognition that protein phosphorylation is at the center of signaling -clearly established in 1990 -it became apparent that many cellular processes are regulated by this mode. A new focus then emerged when it was recognized that growth factors are bound to corresponding receptors trigger protein tyrosine phosphorylation which controls cell prolifera­ tion. This was the topic of the third meeting in this series. It is now evident that further progress depends on understanding the three dimensional structure of the proteins involved. It goes without saying, for example, that understanding the location of proteins by adaptor proteins is only possible on the basis of the three dimensional protein structure. Therefore, the fourth meeting in this series concentrated on the protein structure of signaling molecules as well as on the elucidation of the principles of protein domain interactions.

Content Level » Research

Keywords » ATP - Activation - Antigen - FTIR-Spektroskopie - Proteinphosphorylierung - Proteinstruktur - Vivo - cellular processes - enzymes - opioid - protein phosphorylation - proteins - regulation - translation - x-ray diffraction

Related subjects » Biochemistry & Biophysics - Cell Biology - Immunology - Molecular Medicine - Pharmacology & Toxicology

Table of contents 

I: Regulation by Reversible Protein Phosphorylation.- Control of Cellular Processes by Reversible Protein Phosphorylation.- From Phosphorylase to Phosphorylase Kinase.- Protein Kinase X: A Novel Human Protein Kinase Closely Related to the Catalytic Subunit of cAMP-Dependent Protein Kinase.- Interaction of Protein Kinase Ac from Ascaris Suum with Proteins and Peptides: Comparison with the Mammalian Enzyme.- II: Methodology.- Interaction Studies Using Biosensors.- Advances in Determination of Protein Structure by X-ray Diffraction Methods.- Spectroscopical Studies on the Interaction Between WW Domain and Proline-Rich Peptides.- Novel Microscope-Based Approaches for the Investigation of Protein-Protein Interactions in Signal Transduction.- Binding Studies with SH2 Domains from the Phosphotyrosine Kinase ZAP70 Using Surface Plasmon Resonance and Scintillation Proximity Assays.- Leucine Zipper Mediated Homodimerization of Autoantigen L7 Analyzed by Electrospray Ionization Mass Spectrometry and Yeast Two Hybrid Interactions.- Proteins at Work: Time-Resolved FTIR Studies of Bacteriorhodopsin and the GTP-Binding Protein 21.- III: Phospholipid Signaling.- Downstream Signaling from Phosphoinositide 3-Kinase.- Phosphoinositide-3-Kinase Mediated Activation of JNK by the ßPDGFR.- Regulation of Phospholipase C Isozymes.- Substrate Binding and Catalytic Mechanism in Phospholipase C from Bacillus Cereus.- Identification of Three Active Site Residues Involved in Substrate Binding by Human 43 kDa-D-myo-inositol 1,4,5-trisphosphate 5-phosphatase.- Structural Basis of Protein Ligand Interactions in the Pleckstrin Homology Domain.- IV: Tyrosine Phosphorylation and Downstream Signaling.- Cell Signaling by Tyrosine Phosphorylation: The Other Side of the Coin.- Binding Studies on the Neuronal Isoform of the Non-Receptor Protein Tyrosine Kinase pp60c-src, pp60c-srcN and Potential Target Proteins.- The Switch Cycle of the Ras Protein and Its Role in Signal Transduction.- In Vivo Quantitative Assessment of Ras/Raf Interaction Using the Two-Hybrid System.- In Vivo Analysis of c-Raf1 — 14-3-3 Interaction.- Signal Transduction Through the MAP Kinase Pathway.- Identification and Characterization of MKKX, a Novel Mammalian MAP Kinase Kinase.- Interleukin-1 Activates a Novel p54 MAP Kinase Kinase in Rabbit Liver.- The Protein Kinase B Family — Structure, Regulation and Function.- Regulation of p70s6k.- Rapamycin, FRAP and the Control of 5’TOP mRNA Translation.- Structure, Regulation and Targeting of Protein Phosphatase 2A.- The Constitutive Activation of MET, RON and SEA Genes Induces Different Biological Responses.- Nucleoside Diphosphate Kinase: Effect of the P100S Mutation on Activity and Quaternary Structure.- V: Regulatory Cascades.- Interaction of Adenylyl Cyclase Type 1 with ?? Subunits of Heterotrimeric G-Proteins.- Regulation of G-Protein Activation in Retinal Rods by Phosducin.- Selective Interactions of the Rat ?-Opioid Receptor and a Chimeric ?-Opioid Receptor Expressed in COS-7 Cells with Multiple G Proteins.- Structural Requirements for the EF-Tu-Directed Kinase.- Effect of the Phytotoxin Fusicoccin on Plant Plasma Membrane H+-ATPase Expressed in Yeast.- Organization and Putative Regulation of the Glucose-Specific Phosphotransferase System from Staphylococcus Carnosus.- VI: Regulation of Muscle Contraction.- Single Molecule Myosin Mechanics Measured Using Optical Trapping.- Studies on the ATP-Binding Site of Actin Using Site-Directed Mutagenesis.- Characterisation of the Actin-Binding Protein Insertin.- Cardiac Troponin.- Studies on the Function of the Different Phosphoforms, of Cardiac Troponin I.

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