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Titlebook: Biology of Cellular Transducing Signals; Jack Y. Vanderhoek Book 1990 Plenum Press, New York 1990 Calcium.Colon.DNA.Nucleotide.cyclin.enzy

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https://doi.org/10.1007/978-3-322-89813-5ins bind guanine nucleotides with high affinity and specificity, and possess intrinsic GTPase activity that modulates interactions between the GTP-binding protein and other elements; 2) GTP-binding proteins serve as substrates for ADP-ribosylation by bacterial toxins; this covalent modification disrupts normal function.
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Antibodies as Probes of G-Protein Structure and Functionins bind guanine nucleotides with high affinity and specificity, and possess intrinsic GTPase activity that modulates interactions between the GTP-binding protein and other elements; 2) GTP-binding proteins serve as substrates for ADP-ribosylation by bacterial toxins; this covalent modification disrupts normal function.
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The Role of Covalent and Non-Covalent Mechanisms in Insulin Receptor Actiont the physiological and biochemical level for close to half a century, we are only beginning to obtain an in-depth understanding of the molecular mechanism of insulin signal transduction. A complete molecular analysis of this process will be necessary for a rational therapeutic approach to insulin-resistant disease states.
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https://doi.org/10.1007/978-1-4613-0559-0Calcium; Colon; DNA; Nucleotide; cyclin; enzymes; metabolism; proteins
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https://doi.org/10.1007/978-3-540-48592-6ide binding regulatory proteins (G-proteins). Activation of the G-protein by the agonist-occupied form of the receptor causes the release of GDP from the G-protein, allowing GTP to bind. The GTP-bound form of the G-protein is the active form, which dissociates from the receptor, leading to the activ
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