G Protein Pathways, Part B: G Proteins and Their Regulators

<p>Section I: Activation of G Proteins by Receptors or Other Regulators</p> <p>[1]: Analysis of G Protein Activation in Sf9 and Mammalian Cells by Agonist-Promoted [<SUP>35</SUP>S]GTPγS Binding</p> <p>[2]: Elucidating Kinetic and Thermodynamic Constants for Interaction of G Protein Subunits and Receptors by Surface Plasmon Resonance Spectroscopy</p> <p>[3]: Neuroanatomical Localization of Receptor-Activated G Proteins in Brain</p> <p>[4]: Design and Use of C-Terminal Minigene Vectors for Studying Role of Heterotrimeric G Proteins</p> <p>[5]: Dissecting Receptor–G Protein Specificity Using Gα Chimeras</p> <p>[6]: Use of Dominant Negative Mutations in Analysis of G Protein Function in Saccharomyces cerevisiae</p> <p>[7]: Functional Assays for Mammalian G-Protein-Coupled Receptors in Yeast</p> <p>[8]: Role of G Protein βγ Complex in Receptor–G Protein Interaction</p> <p>[9]: Phosducin Down-Regulation of G-Protein Coupling: Reconstitution of Phosducin Transducin of cGMP Cascade in Bovine Rod Photoreceptor Cells</p> <p>[10]: Analysis of Signal Transfer from Receptor to G<SUB>o</SUB>/G<SUB>i</SUB> in Different Membrane Environments and Receptor-Independent Activators of Brain G Protein</p> <p>[11]: Identification of Modulators of Mammalian G-Protein Signaling by Functional Screens in the Yeast Saccharomyces cerevisiae</p> <p>Section II: Isolation or Production of Native or Modified</p> <p>[12]: Expression of α Subunit of G<SUB>s</SUB> in Escherichia coli</p> <p>[13]: Purification of G Protein Isoforms G<SUB>OA</SUB> G<SUB>OC</SUB> from Bovine Brain</p> <p>[14]: Coexpression of Proteins with Methionine Aminopeptidase/or N-Myristoyltransferase in Escherichia coli to Increase Acylation Homogeneity of Protein Preparations</p> <p>[15]: Purification of G Protein βγ from Bovine Brain</p> <p>[16]: Separation and Analysis of G Protein γ Subunits</p> <p>[17]: Activity of Gγ Prenylcysteine Carboxyl Methyltransferase</p> <p>[18]: Preparation and Application of G Protein γ Subunit-Derived Peptides Incorporating a Photoactive Isoprenoid</p> <p>Section III: Functional Analysis of G Protein Subunits</p> <p>[19]: Expression and Functional Analysis of G Protein α Subunits in S49 Lymphoma Cells</p> <p>[20]: Mouse Gene Knockout Knockin Strategies in Application to α Subunits of G<SUB>i</SUB>/G<SUB>o</SUB> Family of G Proteins</p> <p>[21]: Determining Cellular Role of Gα<SUB>12</SUB></p> <p>[22]: Targeted, Regulatable Expression of Activated Heterotrimeric G Protein α Subunits in Transgenic Mice</p> <p>[23]: Inducible, Tissue-Specific Suppression of Heterotrimeric G Protein α Subunits in Vivo</p> <p>[24]: Construction of Replication Defective Adenovirus That Expresses Mutant Gα<SUB>s</SUB> Q227L</p> <p>[25]: Expression of Adenovirus-Directed Expression of Activated Gα<SUB>s</SUB> in Rat Hippocampal Slices</p> <p>[26]: Quench-Flow Kinetic Measurement of Individual Reactions of G-Protein-Catalyzed GTPase Cycle</p> <p>[27]: Analysis of Genomic Imprinting of G<SUB>s</SUB>α Gene</p> <p>[28]: Subcellular Localization of G Protein Subunits</p> <p>[29]: Fluorescence Approaches to Study G Protein Mechanisms</p> <p>[30]: Defining G Protein βγ Specificity for Effector Recognition</p> <p>[31]: Ribozyme-Mediated Suppression of G Protein γ Subunits</p> <p>Section IV: G Protein Structure and Identification</p> <p>[32]: Use of Scanning Mutagenesis to Delineate Structure–Function Relationships in G Protein α Subunits</p> <p>[33]: Development of G<SUB>s</SUB>-Selective Inhibitory Compounds</p> <p>[34]: Characterization of Deamidated G Protein Subunits</p> <p>[35]: Determining G Protein Heterotrimer Formation</p> <p>[36]: Use of Peptide Probes to Determine Function of Interaction Sites in G Protein Interactions with Effectors</p> <p>[37]: Protein Interaction Assays with G Proteins</p> <p>[38]: Evolutionary Traces of Functional Surfaces along G Protein Signaling Pathway</p> <p>[39]: Discovery of Ligands for βγ Subunits from Phage-Displayed Peptide Libraries</p> <p>[40]: Exploring Protein–Protein Interactions by Peptide Docking Protocols</p> <p>[41]: Structural Characterization of Intact G Protein γ Subunits by Mass Spectrometry</p> <p>Section V: RGS Proteins and Signal Termination</p> <p>[42]: Quantitative Assays for GTPase-Activating Proteins</p> <p>[43]: Analysis of RGS Proteins in Saccharomyces cerevisiae</p> <p>[44]: Purification of RGS Protein, Sst2, from Saccharomyces cerevisiae and Escherichia coli</p> <p>[45]: RGS Domain: Production and Uses of Recombinant Protein</p> <p>[46]: Screening for Interacting Partners for Gα<SUB>i3</SUB> and RGS–GAIP Using the Two-Hybrid System</p> <p>[47]: Assay of RGS Protein Activity in Vitro Using Purified Components</p> <p>[48]: Measuring RGS Protein Interactions with G<SUB>q</SUB>α</p> <p>[49]: Assays of Complex Formation between RGS Protein Gγ Subunit-like Domains and Gβ Subunits</p> <p>[50]: RGS Function in Visual Signal Transduction</p> <p>[51]: Molecular Cloning of Regulators of G-Protein Signaling Family Members and Characterization of Binding Specificity of RGS 12 PDZ Domain</p> <p>Author index</p> <p>Subject Index</p>