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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 over 400 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. Methods in Enzymology is now available online at ScienceDirect - full-text online of volumes 1 onw

Guanosine triphosphatase. --- Enzymology. --- GTP phosphohydrolase --- GTPase --- Guanosine triphosphate phosphohydrolase --- Guanosinetriphosphatase --- Biochemistry --- Enzymes --- Phosphatases

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The Ras superfamily (>150 human members) encompasses Ras GTPases involved in cell proliferation, Rho GTPases involved in regulating the cytoskeleton, Rab GTPases involved in membrane targeting/fusion and a group of GTPases including Sar1, Arf, Arl and dynamin involved in vesicle budding/fission. These GTPases act as molecular switches and their activities are controlled by a large number of regulatory molecules that affect either GTP loading (guanine nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase activating proteins or GAPs). In their active state, they interact with a continua

GTP Phosphohydrolases. --- GTP-Phosphohydrolases. --- Guanosine triphosphatase. --- Physiology. --- ras GTPase-Activating Proteins. --- ras Proteins. --- Ras proteins. --- GTP phosphohydrolase --- GTPase --- Guanosine triphosphate phosphohydrolase --- Guanosinetriphosphatase --- G proteins --- Guanosine triphosphatase --- Phosphatases

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Since 1982, Ras proteins have been the subject of intense research investigation by the biomedical research community. The wide interest in Ras has been stimulated for three key reasons. First, their frequent mutational activation in human cancers establishes Ras proteins as important mediators of oncogenesis and targets for anti-cancer drug discovery. Second, Ras proteins act as signalling nodes activated by diverse extracellular stimuli, and activated Ras in turn regulates a diversity of cytoplasmic signalling networks. Third, Ras proteins are founding members of a large superfamily of Ras-related small GTPases. Over 150 Ras-related small GTPases are found in the human genome, with orthologs found in all vertebrate species and invertebrates. This book features chapters by leading investigators in the field that highlight the current state-of-the art in Ras biochemistry, structure and biology. This book is an excellent reference for students in the biomedical sciences and for investigators in the field.

GTPase-activating protein. --- Guanosine triphosphatase genes. --- Guanosine triphosphatase. --- Ras oncogenes. --- Ras proteins. --- G proteins --- Guanosine triphosphatase --- GAP (Protein) --- Proteins --- Ras genes --- Guanosine triphosphatase genes --- Oncogenes --- GTP phosphohydrolase --- GTPase --- Guanosine triphosphate phosphohydrolase --- Guanosinetriphosphatase --- Phosphatases --- Genes

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For the first time experts in the area of signalling research with a focus on the ARF family have contributed to the production of a title devoted to ARF biology. A comprehensive phylogenetic analysis of the ARF family, tables of the ARF GEFs and ARF GAPs, and more than a dozen chapters describing them in detail are provided. The impact of the ARF proteins on widely diverse aspects of cell biology and cell signalling can be clearly seen from the activities described; including membrane traffic, lipid metabolism, receptor desensitization, mouse development, microtubule dynamics, and bacterial pathogenesis. Anyone interested in understanding the complexities of cell signalling and the integration of signalling networks will benefit from this volume.

Guanosine triphosphatase. --- GTPase-activating protein. --- ADP-ribosylation. --- Biochemistry. --- Evolution (Biology). --- Biochemistry, general. --- Evolutionary Biology. --- Evolutionary biology. --- Animal evolution --- Animals --- Biological evolution --- Darwinism --- Evolutionary biology --- Evolutionary science --- Origin of species --- Biology --- Evolution --- Biological fitness --- Homoplasy --- Natural selection --- Phylogeny --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Composition --- Cellular signal transduction --- GAP (Protein) --- Proteins --- GTP phosphohydrolase --- GTPase --- Guanosine triphosphate phosphohydrolase --- Guanosinetriphosphatase --- Phosphatases

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Acid Anhydride Hydrolases --- Cellular Structures --- Cells --- Hydrolases --- Enzymes --- Anatomy --- Enzymes and Coenzymes --- Chemicals and Drugs --- Cell Membrane --- GTP Phosphohydrolases --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- GTP Phosphohydrolase --- GTPase --- GTPases --- Guanosine Triphosphate Phosphohydrolases --- Guanosinetriphosphatases --- Phosphohydrolase, GTP --- Phosphohydrolases, GTP --- Phosphohydrolases, Guanosine Triphosphate --- Triphosphate Phosphohydrolases, Guanosine --- Cytoplasmic Membrane --- Plasma Membrane --- Cell Membranes --- Cytoplasmic Membranes --- Membrane, Cell --- Membrane, Cytoplasmic --- Membrane, Plasma --- Membranes, Cell --- Membranes, Cytoplasmic --- Membranes, Plasma --- Plasma Membranes --- Coenzymes and Enzymes --- Anatomies --- Biocatalysts --- Cell --- Cell Components --- Cell Component --- Cellular Structure --- Component, Cell --- Components, Cell --- Structure, Cellular --- Structures, Cellular --- Anhydride Hydrolases, Acid --- Hydrolases, Acid Anhydride