triphosphoric acid and adenylyl imidodiphosphate

triphosphoric acid has been researched along with adenylyl imidodiphosphate in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Gelfand, VI; Kuznetsov, SA	1
Markham, GD; Reczkowski, RS	1

Other Studies

2 other study(ies) available for triphosphoric acid and adenylyl imidodiphosphate

Article	Year
Bovine brain kinesin is a microtubule-activated ATPase. Proceedings of the National Academy of Sciences of the United States of America, 1986, Volume: 83, Issue:22 Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Brain Chemistry; Cattle; Enzyme Activation; Hydrolysis; Kinesins; Kinetics; Microtubule Proteins; Microtubules; Nerve Tissue Proteins; Polyphosphates	1986
Slow binding inhibition of S-adenosylmethionine synthetase by imidophosphate analogues of an intermediate and product. Biochemistry, 1999, Jul-13, Volume: 38, Issue:28 Topics: Acid Anhydride Hydrolases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Amino Acid Substitution; Arginine; Binding, Competitive; Diphosphates; Diphosphonates; Enzyme Inhibitors; Hydrolysis; Leucine; Methionine Adenosyltransferase; Mutagenesis, Site-Directed; Polyphosphates	1999

Article

Year

Bovine brain kinesin is a microtubule-activated ATPase.

Proceedings of the National Academy of Sciences of the United States of America, 1986, Volume: 83, Issue:22

Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Brain Chemistry; Cattle; Enzyme Activation; Hydrolysis; Kinesins; Kinetics; Microtubule Proteins; Microtubules; Nerve Tissue Proteins; Polyphosphates

1986

Slow binding inhibition of S-adenosylmethionine synthetase by imidophosphate analogues of an intermediate and product.

Biochemistry, 1999, Jul-13, Volume: 38, Issue:28

Topics: Acid Anhydride Hydrolases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Amino Acid Substitution; Arginine; Binding, Competitive; Diphosphates; Diphosphonates; Enzyme Inhibitors; Hydrolysis; Leucine; Methionine Adenosyltransferase; Mutagenesis, Site-Directed; Polyphosphates

1999