Compounds > p(1),p(5)-di(adenosine-5'-)pentaphosphate
Page last updated: 2024-09-03

p(1),p(5)-di(adenosine-5'-)pentaphosphate and guanosine triphosphate

p(1),p(5)-di(adenosine-5'-)pentaphosphate has been researched along with guanosine triphosphate in 3 studies

Compound Research Comparison

Studies
(p(1),p(5)-di(adenosine-5'-)pentaphosphate)		Trials
(p(1),p(5)-di(adenosine-5'-)pentaphosphate)		Recent Studies (post-2010)
(p(1),p(5)-di(adenosine-5'-)pentaphosphate)		Studies
(guanosine triphosphate)		Trials
(guanosine triphosphate)		Recent Studies (post-2010) (guanosine triphosphate)
21522614,728252,115

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's1 (33.33)18.2507
2000's0 (0.00)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Shimizu, T1
Assfalg-Machleidt, I; Auerswald, EA; Eckerskorn, C; Machleidt, W; Neth, P; Randak, C1
Kimura, Y; Oka, M; Takegawa, K1

Other Studies

3 other study(ies) available for p(1),p(5)-di(adenosine-5'-)pentaphosphate and guanosine triphosphate

ArticleYear
The substrate specificity of dynein from Tetrahymena cilia.
    Journal of biochemistry, 1987, Volume: 102, Issue:5

    Topics: Adenine Nucleotides; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Binding, Competitive; Dinucleoside Phosphates; Diphosphates; Dyneins; Guanosine Triphosphate; Hydrolysis; Inosine Triphosphate; Kinetics; Substrate Specificity; Tetrahymena

1987
A recombinant polypeptide model of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator functions as an active ATPase, GTPase and adenylate kinase.
    FEBS letters, 1997, Jun-30, Volume: 410, Issue:2-3

    Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Adenylate Kinase; Cystic Fibrosis Transmembrane Conductance Regulator; Dinucleoside Phosphates; Enzyme Inhibitors; GTP Phosphohydrolases; Guanosine Triphosphate; Peptides; Recombinant Fusion Proteins

1997
Lysyl-tRNA synthetase from Myxococcus xanthus catalyzes the formation of diadenosine penta- and hexaphosphates from adenosine tetraphosphate.
    Archives of biochemistry and biophysics, 2016, 08-15, Volume: 604

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Bacterial Proteins; Catalysis; Dinucleoside Phosphates; DNA Mutational Analysis; Guanosine Triphosphate; Hydrolysis; Kinetics; Lysine-tRNA Ligase; Manganese; Myxococcus xanthus; Phosphates; Pyrophosphatases; Ribonucleotides

2016