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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
Can Gao   +8 more
semanticscholar   +1 more source

Water-soluble luminescent copper nanoclusters reduced and protected by histidine for sensing of guanosine 5′-triphosphate

, 2014
A one step synthesis of water-soluble luminescent copper nanoclusters (CuNCs) reduced and protected by histidine is reported. When excited at 350 nm, the as-synthesized CuNCs exhibit luminescence centered at 456 nm with a quantum yield of 1.6%, which is ...
X. Zhao, C. Huang
semanticscholar   +1 more source

Repetitive recycling of guanosine triphosphate cyclohydrolase I for synthesis of dihydroneopterin triphosphate

Analytical Biochemistry, 1989
A procedure for enzymatic production of dihydroneopterin triphosphate is described that allows GTP cyclohydrolase I to be reused repetitively. The reaction takes place in an ultrafiltration cell, and the product is collected in the filtrate, whereas the enzyme remains in the cell to be reused with additional substrate. This is repeated until the enzyme
Edwin W. Naylor   +2 more
openaire   +3 more sources

Selective detection of guanosine-5'-triphosphate and iodide by fluorescent benzimidazolium-based cyclophanes.

Organic and biomolecular chemistry, 2013
New fluorescent benzimidazolium-based receptors selectively display the effective fluorescence quenching effect for biologically important anions, GTP and I(-), in aqueous solution of physiological pH 7.4. These affinities can be attributed to the strong
Nisar Ahmed   +4 more
semanticscholar   +1 more source

Controlling Supramolecular Fiber Formation of Nucleopeptide by Guanosine Triphosphate

Biomacromolecules, 2023
Cells use dynamic self-assembly to construct functional structures for maintaining cellular homeostasis. However, using a natural biological small molecule to mimic this phenomenon remains challenging. This work reports the dynamic microfiber formation of nucleopeptide driven by guanosine triphosphate, the small molecule that controls microtubule ...
Hongyue Zhang   +7 more
openaire   +2 more sources

Structural and guanosine triphosphate/diphosphate requirements for transit peptide recognition by the cytosolic domain of the chloroplast outer envelope receptor, Toc34.

Biochemistry, 2002
Toc34 is a transmembrane protein located in the outer envelope membrane of chloroplasts and involved in transit peptide recognition. The cytosolic region of Toc34 reveals 34% alpha-helical and 26% beta-strand structure and is stabilized by intramolecular
Enrico Schleiff   +7 more
semanticscholar   +1 more source

Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of beta-tubulin.

Science, 1994
Microtubule dynamic instability underlies many cellular functions, including spindle morphogenesis and chromosome movement. The role of guanosine triphosphate (GTP) hydrolysis in dynamic instability was investigated by introduction of four mutations into
Ashley S. Davis   +3 more
semanticscholar   +1 more source

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 ...
Richard H. Himes   +2 more
openaire   +3 more sources

[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
R.J. Suhadolnik, E.F. Elstner
openaire   +2 more sources

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.
Ralf Langen   +2 more
openaire   +3 more sources

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