aspartic acid has been researched along with 4-nitrophenylphosphate in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (33.33) | 18.2507 |
| 2000's | 3 (50.00) | 29.6817 |
| 2010's | 1 (16.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Denu, JM; Dixon, JE; Guo, Y; Zhou, G | 1 |
| Kantrowitz, ER; Xu, X | 1 |
| Denu, JM; Hengge, AC; Hoff, RH; Rice, AE; Rigas, JD | 1 |
| Hausmann, S; Shuman, S | 1 |
| Andersen, HS; Guo, XL; Iversen, LF; Kastrup, JS; Mortensen, SB; Møller, KB; Møller, NP; Pedersen, AK; Peters, GH; Zhang, ZY | 1 |
| Dixon, JE; Gill, GN; Kim, Y; Liu, J; Noel, JP; Pfaff, SL; Zhang, M; Zhang, Y | 1 |
6 other study(ies) available for aspartic acid and 4-nitrophenylphosphate
| Article | Year |
|---|---|
The catalytic role of aspartic acid-92 in a human dual-specific protein-tyrosine-phosphatase.
Topics: Amino Acid Sequence; Aspartic Acid; Base Sequence; Catalysis; Conserved Sequence; DNA; Dual Specificity Phosphatase 3; Humans; Hydrogen-Ion Concentration; Iodoacetates; Iodoacetic Acid; Kinetics; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Organophosphorus Compounds; Protein Tyrosine Phosphatases; Sequence Homology, Amino Acid; Substrate Specificity | 1995 |
Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism.
Topics: Alanine; Alkaline Phosphatase; Amino Acid Sequence; Aspartic Acid; Binding Sites; Escherichia coli; Glutamates; Glutamic Acid; Kinetics; Magnesium; Mutagenesis, Site-Directed; Nitrophenols; Organophosphorus Compounds; Protein Conformation; Recombinant Proteins; Zinc | 1993 |
Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase.
Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Dual Specificity Phosphatase 3; Dual Specificity Phosphatase 6; Enzyme Activation; Hydrogen-Ion Concentration; Kinetics; Mitogen-Activated Protein Kinases; Mutagenesis, Site-Directed; Nitrogen; Nitrogen Isotopes; Nitrophenols; Organophosphorus Compounds; Oxygen Isotopes; Phosphorylation; Protein Tyrosine Phosphatases; Substrate Specificity | 2001 |
Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1.
Topics: Alanine; Amino Acid Sequence; Amino Acids; Arginine; Aspartic Acid; Binding Sites; Catalytic Domain; DNA Mutational Analysis; Dose-Response Relationship, Drug; Gene Deletion; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Organophosphorus Compounds; Phosphoprotein Phosphatases; Protein Structure, Tertiary; Schizosaccharomyces; Sequence Homology, Amino Acid | 2003 |
Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis.
Topics: Amino Acid Sequence; Amino Acids; Aspartic Acid; Catalysis; Enzyme Inhibitors; Histidine; Humans; Hydrolysis; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenols; Organophosphorus Compounds; Peptides; Phenylalanine; Phosphotyrosine; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Protein Tyrosine Phosphatase, Non-Receptor Type 3; Protein Tyrosine Phosphatases; Sequence Alignment; Vanadates | 2004 |
Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1.
Topics: Aspartic Acid; Catalytic Domain; Escherichia coli; Humans; Hydrolases; Kinetics; Models, Molecular; Mutation; Nitrophenols; Nuclear Proteins; Organophosphorus Compounds; Phosphoprotein Phosphatases; Phosphorylation; Protein Conformation; Protein Structure, Tertiary; Recombinant Proteins; Sequence Alignment; Structural Homology, Protein; Structure-Activity Relationship | 2010 |