glutamine and inosine diphosphate

glutamine has been researched along with inosine diphosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Allison, WS; Di Pietro, A; Divita, G; Jault, JM	1
Nadanaciva, S; Senior, AE; Weber, J	1

Other Studies

2 other study(ies) available for glutamine and inosine diphosphate

Article	Year
Glutamine 170 to tyrosine substitution in yeast mitochondrial F1 beta-subunit increases catalytic site interaction with GDP and IDP and produces negative cooperativity of GTP and ITP hydrolysis. The Journal of biological chemistry, 1993, Oct-05, Volume: 268, Issue:28 Topics: Azides; Bicarbonates; Catalysis; Enzyme Activation; Glutamine; GTP Phosphohydrolases; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Hydrogen-Ion Concentration; Hydrolysis; Inosine Diphosphate; Inosine Nucleotides; Inosine Triphosphatase; Inosine Triphosphate; Mitochondria; Proton-Translocating ATPases; Pyrophosphatases; Schizosaccharomyces; Tyrosine	1993
New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously. Biochemistry, 2000, Aug-08, Volume: 39, Issue:31 Topics: Adenosine Diphosphate; Arginine; Binding Sites; Catalysis; Drug Synergism; Enzyme Activation; Enzyme Inhibitors; Escherichia coli; Glutamine; Inosine Diphosphate; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Scandium; Spectrometry, Fluorescence; Titrimetry; Tryptophan; Tyrosine	2000

Article

Year

Glutamine 170 to tyrosine substitution in yeast mitochondrial F1 beta-subunit increases catalytic site interaction with GDP and IDP and produces negative cooperativity of GTP and ITP hydrolysis.

The Journal of biological chemistry, 1993, Oct-05, Volume: 268, Issue:28

Topics: Azides; Bicarbonates; Catalysis; Enzyme Activation; Glutamine; GTP Phosphohydrolases; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Hydrogen-Ion Concentration; Hydrolysis; Inosine Diphosphate; Inosine Nucleotides; Inosine Triphosphatase; Inosine Triphosphate; Mitochondria; Proton-Translocating ATPases; Pyrophosphatases; Schizosaccharomyces; Tyrosine

1993

New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously.

Biochemistry, 2000, Aug-08, Volume: 39, Issue:31

Topics: Adenosine Diphosphate; Arginine; Binding Sites; Catalysis; Drug Synergism; Enzyme Activation; Enzyme Inhibitors; Escherichia coli; Glutamine; Inosine Diphosphate; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Scandium; Spectrometry, Fluorescence; Titrimetry; Tryptophan; Tyrosine

2000