Interacting Protein Domains: Their Role in Signal and Energy Transduction: Nato ASI Subseries H:, cartea 102
Editat de Ludwig Heilmeyeren Limba Engleză Paperback – 16 sep 2011
Din seria Nato ASI Subseries H:
- 18%
Preț: 916.80 lei -
Preț: 378.21 lei - 15%
Preț: 618.50 lei - 15%
Preț: 618.50 lei - 15%
Preț: 618.03 lei - 15%
Preț: 617.72 lei -
Preț: 378.05 lei - 15%
Preț: 625.88 lei - 15%
Preț: 615.52 lei - 18%
Preț: 911.78 lei - 15%
Preț: 630.59 lei - 15%
Preț: 630.59 lei - 15%
Preț: 627.93 lei - 15%
Preț: 625.09 lei - 15%
Preț: 629.85 lei - 15%
Preț: 627.01 lei - 15%
Preț: 649.47 lei - 18%
Preț: 920.88 lei - 18%
Preț: 924.09 lei - 5%
Preț: 1057.56 lei - 5%
Preț: 362.13 lei - 15%
Preț: 625.75 lei - 15%
Preț: 619.75 lei - 15%
Preț: 630.29 lei - 18%
Preț: 926.05 lei - 15%
Preț: 623.39 lei - 5%
Preț: 703.21 lei - 15%
Preț: 627.93 lei - 18%
Preț: 922.85 lei - 18%
Preț: 930.75 lei - 18%
Preț: 916.93 lei - 15%
Preț: 627.31 lei - 15%
Preț: 625.75 lei - 5%
Preț: 353.69 lei - 5%
Preț: 1061.78 lei - 18%
Preț: 916.19 lei - 15%
Preț: 626.82 lei - 15%
Preț: 627.79 lei - 15%
Preț: 630.91 lei - 18%
Preț: 924.99 lei - 15%
Preț: 640.81 lei - 15%
Preț: 617.89 lei - 15%
Preț: 621.03 lei - 15%
Preț: 626.68 lei - 15%
Preț: 638.15 lei - 15%
Preț: 625.88 lei - 15%
Preț: 621.03 lei - 15%
Preț: 623.70 lei - 15%
Preț: 631.70 lei
Preț: 616.28 lei
Preț vechi: 725.04 lei
-15%
Puncte Express: 924
Carte tipărită la comandă
Livrare economică 11-25 august
Livrare prin curier în România Termenul estimat este afișat lângă disponibilitate.
Transport gratuit pentru acest produs Plată online sau ramburs, în funcție de opțiunile comenzii.
Retur gratuit în 14 zile Comandă securizată și suport în română.
Specificații
ISBN-13: 9783642645839
ISBN-10: 3642645836
Pagini: 308
Ilustrații: X, 292 p.
Dimensiuni: 155 x 235 x 16 mm
Greutate: 0.44 kg
Ediția:Softcover reprint of the original 1st ed. 1997
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Nato ASI Subseries H:
Locul publicării:Berlin, Heidelberg, Germany
ISBN-10: 3642645836
Pagini: 308
Ilustrații: X, 292 p.
Dimensiuni: 155 x 235 x 16 mm
Greutate: 0.44 kg
Ediția:Softcover reprint of the original 1st ed. 1997
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Nato ASI Subseries H:
Locul publicării:Berlin, Heidelberg, Germany
Public țintă
ResearchCuprins
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 NeuronalIsoform 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 theFunction of the Different Phosphoforms, of Cardiac Troponin I.
Caracteristici
Presents the newest methods and results of general interest to biochemists