Expression, Purification, and Posttranslational Modification: A.J. Self and A. Hall, Purification of Recombinant Rho/Rac/G25K fromEscherichia coli. R.A.Cerione, D. Leonard, and Y. Zheng, Purification of Baculovirus-Expressed Cdc42Hs. T. Mizuno, H. Nakanishi, and Y. Takai, Purification and Properties of Rac2 from Human Leukemia Cells. U.G. Knaus and G.M. Bokoch, Purification of Rac2 from Human Neutrophils. A. Abo, Purification of Rac(GDI Dissociation Inhibitor Complex from Phagocyte Cytosol. K. Tanaka, T. Sasaki, and Y. Takai, Purification and Properties of Recombinant Rho(GDP Dissociation Inhibitor. M.R. Philips and M.H. Pillinger, Prenylcysteine-Directed Carboxyl Methyltransferase Activity in Human Neutrophil Membranes. Guanine Nucleotide Exchange and Hydrolysis: A.J. Self and A. Hall, Measurement of Intrinsic Nucleotide Exchange and GTP Hydrolysis Rates. Y. Zheng, M.J. Hart, and R.A. Cerione, Guanine Nucleotide Exchange Catalyzed by dbl Oncogene Product. E. Porfiri and J.F. Hancock, Stimulation of Nucleotide Exchange on Ras- and Rho-Related Proteins by Small GTP-Binding Protein GDP Dissociation Stimulator. T. Miki, Interaction of Ect2 and Dblwith Rho-related GTPases. D.A. Leonard and R.A. Cerione, Solubilization of Cdc42Hs from Membranes by Rho(GDP Dissociation Inhibitor. J. Settleman and R. Foster, Purification and GTPase-Activating Protein Activity of Baculovirus Expressed p190. S. Ahmed, R. Kozma, C. Hall, and L. Lim, GTPase-Activating Protein Activity of n(alpha1)-Chimaerin and Effect of Lipids. D.E.H. Afar and O.N. Witte, Characterization of Breakdown Cluster Region Kinase and SH2-Binding Activities. E. Manser, T. Leung, and L. Lim, Identification of GTPase-Activating Proteins by Nitrocellulose Overlay Assay. P. Cicchetti and D. Baltimore, Identification of 3BP-1 in cDNA Expression Library by SH3 Domain Screening. Cell Expression and in Vitro Analysis: P. Fort and S. Vincent, Serum Induction of RhoG Expression. H. Paterson, P. Adamson, and D. Robertson, Microinjection of Epitope-Tagged Rho Family cDNAs and Analysis by Immunolabeling. S.T. Dillon and L.A.Feig, Purification and Assay of Recombinant C3 Transferase. K. Aktories and I. Just, In Vitro ADP-Ribosylation of Rho by Bacterial ADP-Ribosyltransferases. N. Morii and S. Narumiya, Preparation of Native and Recombinant Clostridium botulinum C3 ADP-Ribosyltransferase and Identification of Rho Proteins by ADP-Ribosylation. D. Diekmann and A. Hall, In Vitro Binding Assay for Interactions of Rho and Rac with GTPase-Activating Proteins and Effectors. E. Manser, T. Leung, and L. Lim, Purification and Assay of Kinases That Interact with Rac/Cdc42. P. Aspenstrim and M.F. Olson, Yeast Two-Hybrid System to Detect Protein(Protein Interactions with Rho GTPases. S.E. Rittenhouse, Assay for Rho-Dependent Phosphoinositide 3-Kinase Activity in Platelet Cytosol. E.P. Bowman, D.J. Uhlinger, and J.D. Lambeth, Neutrophil Phospholipase D: Inhibition by Rho(GDP Dissociation Inhibitor and Stimulation by Small GTPase GDP Dissociation Stimulator. M.T. Quinn and G.M. Bokoch, Measurement of Rac Translocation from Cytosol to Membranes in Activated Neutrophils. A. Abo and A.W. Segal, Reconstitution of Cell-Free NADPH Oxidase Activity by Purified Components. Biological Activity: J. Posada, P.J. Miller, J. McCullough, M. Ziman, and D.I. Johnson, Genetic and Biochemical Analysis of Cdc42p Function in Saccharomyces cerevisiae and Schizosaccharomyces pombe. T. Tominaga and S. Narumiya, Lymphocyte Aggregation Assay and Inhibition by Clostridium botulinum C3 ADP-Ribosyltransferase. P. Boquet, M.R. Popoff, M. Giry, E. Lemichez, and P. Bergez-Aullo, Inhibition of p21 Rho in Intact Cells by C3 Diphtheria Toxin Chimera Proteins. A.J. Ridley, Growth Factor-Induced Actin Reorganization in Swiss 3T3 Cells. A.J. Ridley, Microinjection of Rho and Rac into Quiescent Swiss 3T3 Cells. P. Lang and J. Bertoglio, Inhibition of Lymphocyte-Mediated Cytotoxicity by Clostridium botulinum C3 Transferase. M.-J. Stasia and P.V. Vignais, Neutrophil Chemotaxis Assay and Inhibition by C3 ADP-Ribosyltransferase. K. Takaishi, T. Sasaki, and Y. Takai, Cell Motility Assay and Inhibition by Rho(GDP Dissociation Inhibitor. D. Zangrilli and A. Eva, Cell Transformation by dbl Oncogene. O. Dorseuil, G. Leca, A. Vazquez, and G. Gacon, Inhibition of Rac Function Using Antisense Oligonucleotides. Author Index. Subject Index.
General Description of the Volume: Small GTPases play a key role in many aspects of contemporary cell biology: control of cell growth and differentiation; regulation of cell adhesion and cell movement; the organization of the actin cytoskeleton; and the regulation of intracellular vesicular transport. This volume plus its companion Volumes 255 and 257 cover all biochemical and biological assays currently in use for analyzing the role of small GTPases in these aspects of cell biology at the molecular level. It is the first compendium of practical techniques for working with small GTPases of the Rho group. General Description of the Series: The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
Researchers in biochemistry, molecular biology, cell biology, pharmacology, neurophysiology, and neurochemistry.
- No. of pages:
- © Academic Press 1995
- 15th August 1995
- Academic Press
- eBook ISBN:
@from:Praise for the Volume @qu:"This book makes a unique contribution...it is...the first place to turn when thinking about how to measure, analyze, and interpret the thermodynamics of conformational change and interactions of proteins and nucleic acids. It would make a fine textbook for a graduate course...Instructors who teach courses in less depth will find it an important background reference. For researchers, it belongs not just in the library, but on the personal bookshelf of anyone who is serious about research in molecular biophysics.." @source:--Victor A. Bloomfield, University of Minnesota, in BIOPHYSICAL JOURNAL @qu:"These books are a most useful and valuable resource to everyone involved in the field of protein research. They will certainly serve as guidance books and many of the techniques described might remain central to the field of signal transduction in the future." @source:--Tilat A. Rizvi, University of Cincinnati Medical Center, in TINS @from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
The Scripps Research Institute, La Jolla, CA, USA
Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, USA
University College of London, U.K.
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