serine has been researched along with 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 5 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cho, YK; Kim, JJ; Miziorko, HM; Ríos, SE | 1 |
Amler, E; Ettrich, R; Hofbauerová, K; Kopecký, V; Krumscheid, R; Kubala, M; Plásek, J; Schoner, W; Teisinger, J | 1 |
Amler, E; Ettrich, R; Kubala, M; Kutý, M; Lánský, Z; Plásek, J; Schoner, W; Teisinger, J | 1 |
Krepkiy, DV; Miziorko, HM | 1 |
Broomhead, HE; Cao, L; Fountain, SJ; North, RA; Young, MT | 1 |
5 other study(ies) available for serine and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
Article | Year |
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Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate binding motif and a site implicated in human inherited disease.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Amino Acid Substitution; Animals; Arabidopsis; Bacteria; Binding Sites; Fluorescent Dyes; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphotransferases; Phosphotransferases (Alcohol Group Acceptor); Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Serine; Spectrometry, Fluorescence; Threonine | 2001 |
Phe(475) and Glu(446) but not Ser(445) participate in ATP-binding to the alpha-subunit of Na(+)/K(+)-ATPase.
Topics: Adenosine Triphosphate; Animals; Binding Sites; Fluorescent Dyes; Glutamic Acid; Mice; Models, Molecular; Phenylalanine; Protein Conformation; Protein Subunits; Recombinant Fusion Proteins; Serine; Sodium-Potassium-Exchanging ATPase | 2002 |
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.
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 |
Investigation of the functional contributions of invariant serine residues in yeast mevalonate diphosphate decarboxylase.
Topics: Adenosine Triphosphate; Alanine; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Carboxy-Lyases; Enzyme Stability; Fluorescent Dyes; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphotransferases; Protein Folding; Protein Subunits; Saccharomyces cerevisiae Proteins; Serine; Spectrometry, Fluorescence; Substrate Specificity | 2005 |
Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; Binding Sites; Cell Line; Cell Membrane; Humans; Ion Channel Gating; Lysine; Mutagenesis; Protein Binding; Protein Structure, Tertiary; Purinergic P2 Receptor Antagonists; Rats; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Serine; Suramin; Threonine | 2007 |