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

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

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (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
Evans, RJ; Roberts, JA	1

Other Studies

2 other study(ies) available for proline 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
Mutagenesis studies of conserved proline residues of human P2X receptors for ATP indicate that proline 272 contributes to channel function. Journal of neurochemistry, 2005, Volume: 92, Issue:5 Topics: Adenosine Triphosphate; Animals; Conserved Sequence; Dose-Response Relationship, Drug; Drug Interactions; Extracellular Space; Gene Expression Regulation; Humans; Membrane Potentials; Mutagenesis; Oocytes; Patch-Clamp Techniques; Proline; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Sequence Alignment; Xenopus laevis	2005

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

Mutagenesis studies of conserved proline residues of human P2X receptors for ATP indicate that proline 272 contributes to channel function.

Journal of neurochemistry, 2005, Volume: 92, Issue:5

Topics: Adenosine Triphosphate; Animals; Conserved Sequence; Dose-Response Relationship, Drug; Drug Interactions; Extracellular Space; Gene Expression Regulation; Humans; Membrane Potentials; Mutagenesis; Oocytes; Patch-Clamp Techniques; Proline; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Sequence Alignment; Xenopus laevis

2005