Results 161 to 170 of about 97,251 (205)
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On the mechanism of guanosine triphosphate hydrolysis in ras p21 proteins

Biochemistry, 1992
The residue Gln61 is assumed to play a major role in the mechanism of ras p21, and mutations of this residue are often found in human tumors. Such mutations lead to a major reduction in the rate of GTP hydrolysis by the complex of ras p21 and the GTPase activating protein (GAP) and lock the protein in a growth-promoting state.
R, Langen, T, Schweins, A, Warshel
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Evidence for Guanosine Triphosphate—Binding Proteins in Trypanosoma cruzi

The American Journal of Tropical Medicine and Hygiene, 1994
The transformation of the parasite Trypanosoma cruzi from the blood-borne trypomastigote to the intracellular amastigote constitutes a key clinical feature in the pathophysiology of Chagas' disease. That this transition occurs without change in the integrity of the plasma membrane of the parasite suggests the presence of biochemical structures, i.e ...
H S, Oz   +5 more
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Direct photoaffinity labeling of tubulin with guanosine 5'-triphosphate

Biochemistry, 1985
Irradiation of tubulin in the presence of [3H]GTP or [3H]GDP at 254 nm led to the covalent incorporation of nucleotide into the protein. The specific nature of the labeling was shown in the following manner: with tubulin depleted of exchangeable nucleotide, the amount of labeling increased to a plateau value as the [3H]GTP concentration was increased ...
J P, Nath, G R, Eagle, R H, Himes
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The effect of guanosine 5′-triphosphate analogues on protein synthesis

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
Abstract Four GTP analogues, 6-mercaptoguanosine 5′-triphosphate (I), N2-methylguanosine 5′-triphosphate (II), N2-dimethylguanosine 5′-triphosphate (III) and 8-bromoguanosine 5′-triphosphate, (IV) were synthesized chemically and tested for their ability to replace GTP in the cell-free amino acid incorporation system of Escherichia coli.
H, Uno, S, Oyabu, E, Otsuka, M, Ikehara
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Acid-Cleavable Guanosine Triphosphate-Photoaffinity Probe for Global Profiling of Guanosine Triphosphate-Binding Proteins and Their Active Sites

Analytical Chemistry
Guanosine triphosphate (GTP)-binding proteins function as molecular switches in cell signaling, playing critical roles in various biological pathways. Their dysregulation is associated with the causes and progression of many diseases. Systematic analysis of GTP-binding proteins would facilitate studies of related signaling pathways and drugs ...
Can Gao   +8 more
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Structural and Functional Relationships of Guanosine Triphosphate Binding Proteins

1988
Information available at present documents the existence of three well-defined classes of guanine nucleotide binding proteins functioning as signal transducers: Gs and Gi which stimulate and inhibit adenylate cyclase, respectively, and transducin which transmits and amplifies the signal from light-activated rhodopsin to cGMP-dependent phosphodiesterase
T, Pfeuffer, E J, Helmreich
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[37] Guanosine triphosphate-8-formylhydrolase

1975
Publisher Summary This chapter discusses the assay and purification procedure of guanosine triphosphate-8-formylhydrolase. The assay method is based on two procedures. The first method involves the release of 14 C-labeled formic acid from carbon-8 of the imidazole ring of [8- 14 C]GTP. The formic acid is oxidized to carbon dioxide. The second method
E.F. Elstner, R.J. Suhadolnik
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Preparative method of obtaining guanosine 5′-triphosphate

Chemistry of Natural Compounds, 1965
1. The kinetics of the formation of guanosine 5′-triphosphate, 5′-diphosphate, and 5′-monophosphate in the reaction of the morpholide of guanosine 5′-monophosphate with bis-(tributylammonium) pyrophosphate in pyridine at 27° has been recorded. 2. In the reaction of the morpholide of guanosine 5′-monophosphate with bis-(tributylammonium) pyrophosphate ...
T. S. Lomakina, N. I. Grineva
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Guanosine-5?-triphosphate hydrolysis and tubulin polymerization

Molecular and Cellular Biochemistry, 1982
GTP hydrolysis associated with polymerization is a distinctive feature of microtubule assembly. This reaction may be fundamentally linked to the dynamic properties of microtubules in vivo. Kinetic analysis of the connection between microtubule assembly and associated GTP hydrolysis indicates that these two events are kinetically uncoupled, GTP ...
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Location of the Guanosine Triphosphate (GTP) Hydrolysis Site in Microtubulesa

Annals of the New York Academy of Sciences, 1986
The rate for GTP hydrolysis remains approximately constant during microtubule assembly from microtubular protein. This indicates that GTP hydrolysis does not accompany tubulin-GTP subunit addition to microtubule ends. We suggest that GTP, within tubulin-GTP subunits that are incorporated into microtubules, is hydrolyzed predominantly at one or both ...
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