Results 311 to 320 of about 339,556 (339)
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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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Enzyme, 1979
The cytosolic form of phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) from rat liver was purified by a procedure involving affinity chromatography on agarose-hydrazide-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 agarose-hydrazide-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 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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GDP/GTP Exchange Proteins for Small GTP-Binding Proteins
1993There is a superfamily of small GTP-binding proteins in which more than forty members are included (Bourne et al. 1991; Hall 1990; Takai et al. 1992). They exhibit GDP/GTP-binding and GTPase activities and have two interconvertible forms: GDP-bound inactive and GTP-bound active forms (Fig. 1).
Y. Takai +3 more
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GTP-binding proteins in plants
Plant Molecular Biology, 1993Abstract Full length cDNAs of small GTP-binding proteins were inserted into PGEM1 under the control of the T7 promotor as described previously (Chavrier et al. 1990; Huber et al. 1993). GTP-binding proteins were then transiently expressed in BHK 21 cells with the T7 RNA polymeraserecombinant vaccinia virus system (Fuerst et al.
Terryn, N. +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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Expression cloning to identify monomeric GTP-binding proteins by GTP overlay
2001Publisher Summary More than 70 small Ras-related GTP-binding proteins have been identified and additional members of the family continue to be discovered. The majority of these proteins have been isolated by screening genomic or cDNA libraries at low stringency with oligonucleotide mixes corresponding to the conserved guanine nucleotide-binding ...
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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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The International Journal of Biochemistry & Cell Biology, 1997
RhoA, RhoB and RhoC are three closely related proteins, and are members of the Ras super-family of small GTP-binding proteins. They bind and hydrolyse GTP, and are active in the GTP-bound form. Their activity in cells is regulated by exchange factors, GTPase activating proteins and guanine nucleotide dissociation inhibitors.
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RhoA, RhoB and RhoC are three closely related proteins, and are members of the Ras super-family of small GTP-binding proteins. They bind and hydrolyse GTP, and are active in the GTP-bound form. Their activity in cells is regulated by exchange factors, GTPase activating proteins and guanine nucleotide dissociation inhibitors.
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