hydrogen and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate

hydrogen has been researched along with 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Amler, E; Ettrich, R; Kubala, M; Kutý, M; Lánský, Z; Plásek, J; Schoner, W; Teisinger, J	1

Other Studies

1 other study(ies) available for hydrogen and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate

Article	Year
The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase. Biochemistry, 2004, Jul-06, Volume: 43, Issue:26 Topics: Adenosine; Adenosine Triphosphate; Amino Acid Sequence; Amino Acids; Animals; Arginine; Aspartic Acid; Binding Sites; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescent Dyes; Genetic Vectors; Glutamic Acid; Glutathione Transferase; Hydrogen; Hydrogen Bonding; Hydrolysis; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular Sequence Data; Mutation; Nucleotides; Point Mutation; Proline; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Serine; Sodium-Potassium-Exchanging ATPase; Software; Spectrophotometry; Temperature	2004

Article

Year

The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.

Biochemistry, 2004, Jul-06, Volume: 43, Issue:26

Topics: Adenosine; Adenosine Triphosphate; Amino Acid Sequence; Amino Acids; Animals; Arginine; Aspartic Acid; Binding Sites; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescent Dyes; Genetic Vectors; Glutamic Acid; Glutathione Transferase; Hydrogen; Hydrogen Bonding; Hydrolysis; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular Sequence Data; Mutation; Nucleotides; Point Mutation; Proline; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Serine; Sodium-Potassium-Exchanging ATPase; Software; Spectrophotometry; Temperature

2004