Results 251 to 260 of about 222,027 (284)
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Regulation of GTP biosynthesis
Advances in Enzyme Regulation, 1992In the regulation of GTP biosynthesis, complex interactions are observed. A major factor is the behavior of the activity of IMPDH, the rate-limiting enzyme of de novo GTP biosynthesis, and the activity of GPRT, the salvage enzyme of guanylate production. The activities of GMP synthase, GMP kinase and nucleoside-diphosphate kinase are also relevant.
G, Weber +4 more
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Physiological Reviews, 2001
Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and Ran families.
Y, Takai, T, Sasaki, T, Matozaki
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Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and Ran families.
Y, Takai, T, Sasaki, T, Matozaki
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Stabilization of microtubules by GTP analogues
Biochemical and Biophysical Research Communications, 1990We recently demonstrated that the nonhydrolyzable analogues of GTP (GMPPCP and GMPPNP) and ATP support the elongation phase of tubulin assembly and are incorporated into the E-site of polymerized tubulin. In this report we studied the stability of microtubules containing GTP analogues by examining length redistributions after shearing at polymer steady
M R, Mejillano, J S, Barton, R H, Himes
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GTP-binding proteins in plants
Cellular and Molecular Life Sciences CMLS, 1999GTP-binding proteins are found in all organisms. They are important switches that cycle between an active and an inactive state, ensuring vectorial flow of information on the expense of guanosine triphosphate (GTP). In this review, we discuss current progress in the molecular characterization and functional analysis of plant genes encoding ...
F, Bischoff +3 more
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Inhibition of erythrocyte transglutaminase by GTP
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987The guanine nucleotides GTP, GDP and GMP inhibit the activity of erythrocyte transglutaminase (protein-glutamine:amine gamma-glutamyltransferase, EC 2.3.2.13) in a decreasing order of effectiveness. The inhibition is more apparent at low than at saturating levels of calcium ions and is not due to the chelation of Ca2+, but to an interference with the ...
C M, Bergamini +2 more
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Determination of GTP loading on Rho
2000Publisher Summary This chapter discusses the determination of guanosine 5'-triphosphate (GTP) loading on Rho. Rho is a member of the Ras superfamily of low molecular weight GTPase that is implicated in the regulation of actin cytoskeleton organization.
X D, Ren, M A, Schwartz
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The effect of GTP on benzodiazepine receptors
European Journal of Pharmacology, 1982GTP decreases the specific binding of [3H]flunitrazepam to cerebral cortical membrane sites. Scatchard analysis data show that GTP does not alter the maximum binding sites (Bmax), but increases the dissociation constant (KD) for [3H]flunitrazepam. GTP also inhibits the specific binding of the benzodiazepine antagonist [3H]CGS-8216. The specific binding
J C, Fong, K, Okada, M, Goldstein
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Enzyme, 2017
The cytosolic form of phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) from rat liver was purified by a procedure involving affinity chromatography on agarosehydrazide- GTP. Phosphoenolpyruvate carboxykinase is retained quantitatively by the affinity medium in the presence of manganese and can be specifically eluted by a pulse of GTP.
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The cytosolic form of phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) from rat liver was purified by a procedure involving affinity chromatography on agarosehydrazide- GTP. Phosphoenolpyruvate carboxykinase is retained quantitatively by the affinity medium in the presence of manganese and can be specifically eluted by a pulse of GTP.
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Annual Review of Cell and Developmental Biology, 2013
Shape changes and topological remodeling of membranes are essential for the identity of organelles and membrane trafficking. Although all cellular membranes have common features, membranes of different organelles create unique environments that support specialized biological functions.
James A, McNew +4 more
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Shape changes and topological remodeling of membranes are essential for the identity of organelles and membrane trafficking. Although all cellular membranes have common features, membranes of different organelles create unique environments that support specialized biological functions.
James A, McNew +4 more
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GTP binding and growth control
Current Opinion in Cell Biology, 1990Guanosine triphosphate (GTP)-binding proteins are involved, directly or indirectly, in virtually every aspect of cellular growth control and metabolism. At least three major classes of GTP-binding protein have been identified. The first includes elongation factors and initiation factors that are part of the machinery of protein synthesis, and also part
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