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Signal Transduction by Guanine Nucleotide-Binding Proteins
1988Publisher Summary The protein Gs is now known to be a member of a larger and growing family of heterotrimeric GTP-binding proteins (G-proteins) involved in signal transduction across cell membranes. For some G-proteins, correlation between the amino acid sequence of purified protein, predicted amino acid sequence of the cloned cDNA, and function of ...
ALLEN Spiegel +10 more
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Biochemistry, 1997
The Rac GTPases are currently being subjected to intensive study due to their involvement in a wide array of cellular phenomena. Many studies of Rac function have relied upon the use of relatively uncharacterized Rac dominant active, dominant negative, and effector domain mutants on the basis of the analogy to Ras structure.
David C. Barry +4 more
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The Rac GTPases are currently being subjected to intensive study due to their involvement in a wide array of cellular phenomena. Many studies of Rac function have relied upon the use of relatively uncharacterized Rac dominant active, dominant negative, and effector domain mutants on the basis of the analogy to Ras structure.
David C. Barry +4 more
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Neuroscience, 1992
Based on the ability of guanine nucleotides to inhibit the binding of vasoactive intestinal peptide to its receptors, a guanosine 5'-triphosphate analog, guanylyl-imidodiphosphate, was used to differentiate two subtypes (or different functional states of a single subtype) of vasoactive intestinal peptide receptor in brain with in vitro autoradiography.
D.I. Hilton-Clarke +2 more
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Based on the ability of guanine nucleotides to inhibit the binding of vasoactive intestinal peptide to its receptors, a guanosine 5'-triphosphate analog, guanylyl-imidodiphosphate, was used to differentiate two subtypes (or different functional states of a single subtype) of vasoactive intestinal peptide receptor in brain with in vitro autoradiography.
D.I. Hilton-Clarke +2 more
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Dbl family guanine nucleotide exchange factors
Trends in Biochemical Sciences, 2001The Dbl family of guanine nucleotide exchange factors are multifunctional molecules that transduce diverse intracellular signals leading to the activation of Rho GTPases. The tandem Dbl-homology and pleckstrin-homology domains shared by all members of this family represent the structural module responsible for catalyzing the GDP-GTP exchange reaction ...
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Signal transduction by guanine nucleotide binding proteins
Molecular and Cellular Endocrinology, 1987High affinity binding of guanine nucleotides and the ability to hydrolyze bound GTP to GDP are characteristics of an extended family of intracellular proteins. Subsets of this family include cytosolic initiation and elongation factors involved in protein synthesis, and cytoskeletal proteins such as tubulin (Hughes, S.M. (1983) FEBS Lett. 164, 1-8).
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Guanine Nucleotide Binding Proteins and Signal Transduction
1988Publisher Summary This chapter discusses the general aspects and functions of guanine nucleotide binding proteins and signal transduction. The function of several identified G-proteins such as G o and the multiple forms of “G i ” are also defined. The function of ras and ras -related gene products likewise are also elucidated in the chapter.
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Prebiotic Syntheses of Noncanonical Nucleosides and Nucleotides
Chemical Reviews, 2020Nicholas V Hud, Tyler P Roche
exaly
Cofactor‐Driven Cascade Reactions Enable the Efficient Preparation of Sugar Nucleotides
Angewandte Chemie - International Edition, 2022Liuqing Wen
exaly
The Guanine — Nucleotide Binding Proteins
1989B. Kraal, Andrea Parmeggiani, L. Bosch
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