aspartic acid has been researched along with vanadates in 23 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (4.35) | 18.7374 |
| 1990's | 10 (43.48) | 18.2507 |
| 2000's | 11 (47.83) | 29.6817 |
| 2010's | 1 (4.35) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kyriakidis, DA; Triantafillou, DJ; Tsavdaridis, IK | 1 |
| Fürst, P; Solioz, M | 1 |
| Salter, MW; Wang, YT | 1 |
| Driessen, AJ; Jacobs, MH; Konings, WN | 1 |
| Anderson, SA; Jiang, S; Mukkada, AJ | 1 |
| Denu, JM; Dixon, JE; Lohse, DL; Saper, MA; Vijayalakshmi, J | 1 |
| Driessen, AJ; Jacobs, MH; Konings, WN; van der Heide, T | 1 |
| Evans, GJ; Pocock, JM | 1 |
| Fujimoto, S; Fujisawa, Y; Kanamori, K; Nagaoka, T; Sakurai, H; Taniyama, J; Tawa, R; Uchida, K | 1 |
| Chen, W; Frasch, WD; Hu, CY | 1 |
| Cheng, PW; Germann, UA; Gottesman, MM; Hrycyna, CA; Pastan, I; Ramachandra, M | 1 |
| Chen, W; Crampton, DJ; Frasch, WD; Hu, CY | 1 |
| Buch-Pedersen, MJ; Palmgren, MG; Serrano, R; Venema, K | 1 |
| Chang, XB; Cui, L; Hou, YX; Riordan, JR | 1 |
| Cole, SP; Deeley, RG; Gao, M; Payen, LF; Westlake, CJ | 1 |
| Andersen, HS; Guo, XL; Iversen, LF; Kastrup, JS; Mortensen, SB; Møller, KB; Møller, NP; Pedersen, AK; Peters, GH; Zhang, ZY | 1 |
| Cole, SP; Conseil, G; Deeley, RG; Haimeur, A; Situ, D; Sparks, KE; Zhang, D | 1 |
| Bartholomew, LA; Gimi, K; Senior, AE; Tombline, G; Tyndall, GA; Urbatsch, IL | 1 |
| Blanchetot, C; Chagnon, M; Dubé, N; Hallé, M; Tremblay, ML | 1 |
| Chan, FH; Hegde, RS; Kattamuri, C; Rayapureddi, JP | 1 |
| Altendorf, K; Bramkamp, M | 1 |
| Brecker, L; Goedl, C; Mueller, M; Nidetzky, B; Schwarz, A | 1 |
| Barry, R; Champeil, P; Hennrich, H; Holthuis, J; Jacquot, A; Jaxel, C; le Maire, M; Lenoir, G; Montigny, C | 1 |
1 review(s) available for aspartic acid and vanadates
| Article | Year |
|---|---|
Mechanistic differences among retaining disaccharide phosphorylases: insights from kinetic analysis of active site mutants of sucrose phosphorylase and alpha,alpha-trehalose phosphorylase.
Topics: Agaricales; Amino Acid Sequence; Aspartic Acid; Binding Sites; Fructose; Glucosyltransferases; Glutamic Acid; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Leuconostoc; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Phosphates; Vanadates | 2008 |
22 other study(ies) available for aspartic acid and vanadates
| Article | Year |
|---|---|
Transport of L-asparagine in Tetrahymena pyriformis ecto-L-asparaginase is not related to L-asparagine-protein transport system.
Topics: Animals; Asparaginase; Asparagine; Aspartic Acid; Biological Transport, Active; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Ouabain; Potassium; Tetrahymena pyriformis; Vanadates | 1991 |
Formation of a beta-aspartyl phosphate intermediate by the vanadate-sensitive ATPase of Streptococcus faecalis.
Topics: Adenosine Triphosphatases; Amino Acids; Aspartic Acid; Enterococcus faecalis; Phosphorylation; Vanadates; Vanadium | 1985 |
Regulation of NMDA receptors by tyrosine kinases and phosphatases.
Topics: Animals; Aspartic Acid; Cells, Cultured; Genistein; Humans; Isoflavones; Magnesium; Membrane Potentials; Mice; Neurons; Phenols; Protein Tyrosine Phosphatases; Protein-Tyrosine Kinases; Proto-Oncogene Proteins pp60(c-src); Rats; Rats, Wistar; Receptors, N-Methyl-D-Aspartate; Vanadates | 1994 |
Characterization of a binding protein-dependent glutamate transport system of Rhodobacter sphaeroides.
Topics: Adenosine Triphosphate; Aspartic Acid; Biological Transport; Carrier Proteins; Glutamic Acid; Hydrogen-Ion Concentration; Rhodobacter sphaeroides; Substrate Specificity; Vanadates | 1995 |
The beta-aspartyl phosphate intermediate in a Leishmania donovani promastigote plasma membrane P-type ATPase.
Topics: Adenosine Triphosphatases; Animals; Aspartic Acid; Cell Membrane; Ethylmaleimide; Fluorescein-5-isothiocyanate; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Leishmania donovani; Phosphoproteins; Phosphorylation; Vanadates | 1994 |
Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Tyrosine Phosphatases; Rats; Structure-Activity Relationship; Vanadates; Yersinia | 1996 |
Glutamate transport in Rhodobacter sphaeroides is mediated by a novel binding protein-dependent secondary transport system.
Topics: Aspartic Acid; Binding, Competitive; Biological Transport; Cell Membrane; Glutamic Acid; Glutamine; Ionophores; Kinetics; Mutation; Nigericin; Rhodobacter sphaeroides; Sodium; Valinomycin; Vanadates | 1996 |
Modulation of neurotransmitter release by dihydropyridine-sensitive calcium channels involves tyrosine phosphorylation.
Topics: Adenosine Triphosphate; Animals; Aspartic Acid; Calcium; Calcium Channel Blockers; Calcium Channels; Calcium Channels, L-Type; Cell Adhesion Molecules; Cerebellum; Dihydropyridines; Electrophysiology; Focal Adhesion Kinase 1; Focal Adhesion Protein-Tyrosine Kinases; Membrane Potentials; Nerve Tissue Proteins; Nifedipine; omega-Conotoxins; Peptides; Phosphorylation; Potassium; Protein Tyrosine Phosphatases; Protein-Tyrosine Kinases; Rats; Rats, Wistar; Time Factors; Tritium; Tyrosine; Vanadates; Vinculin | 1999 |
A new insulin-mimetic vanadyl complex, (N-pyridylmethylaspartate)oxovanadium(IV) with VO(N2O2) coordination mode, and evaluation of its effect on uptake of D-glucose by Ehrlich ascites tumour cells.
Topics: Animals; Aspartic Acid; Carcinoma, Ehrlich Tumor; Deoxyglucose; Dose-Response Relationship, Drug; Drug Evaluation; Glucose; Hypoglycemic Agents; Insulin; Male; Mice; Picolinic Acids; Rats; Rats, Wistar; Time Factors; Tritium; Vanadates; Vanadium Compounds | 1999 |
Metal ligation by Walker homology B aspartate betaD262 at site 3 of the latent but not activated form of the chloroplast F(1)-ATPase from Chlamydomonas reinhardtii.
Topics: Animals; Aspartic Acid; Binding Sites; Chlamydomonas reinhardtii; Chloroplasts; Electron Spin Resonance Spectroscopy; Hydrogen Bonding; Ligands; Mutagenesis, Site-Directed; Photophosphorylation; Proton-Translocating ATPases; Recombinant Proteins; Thylakoids; Vanadates | 1999 |
Both ATP sites of human P-glycoprotein are essential but not symmetric.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Substitution; Antibodies, Monoclonal; Asparagine; Aspartic Acid; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; Biological Transport; Body Temperature; Cell Membrane; Consensus Sequence; Enzyme Activation; Freezing; HeLa Cells; Humans; Peptide Fragments; Phosphorus Radioisotopes; Photoaffinity Labels; Point Mutation; Prazosin; Protein Conformation; Recombinant Fusion Proteins; Vanadates; Verapamil | 1999 |
Characterization of the metal binding environment of catalytic site 1 of chloroplast F1-ATPase from Chlamydomonas.
Topics: Adenosine Diphosphate; Animals; Aspartic Acid; Binding Sites; Catalysis; Chlamydomonas reinhardtii; Chloroplasts; Electron Spin Resonance Spectroscopy; Glutamic Acid; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Spin Labels; Vanadates | 2000 |
Abolishment of proton pumping and accumulation in the E1P conformational state of a plant plasma membrane H+-ATPase by substitution of a conserved aspartyl residue in transmembrane segment 6.
Topics: Adenosine Triphosphatases; Arabidopsis; Asparagine; Aspartic Acid; Blotting, Western; Catalysis; Cell Membrane; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Ligands; Mutagenesis, Site-Directed; Phosphorylation; Plant Proteins; Protein Conformation; Proton-Translocating ATPases; Protons; Saccharomyces cerevisiae; Time Factors; Trypsin; Vanadates | 2000 |
ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Allosteric Site; Amino Acid Motifs; Animals; Anions; Aspartic Acid; Blotting, Western; Catalysis; Cell Membrane; Cricetinae; DNA-Binding Proteins; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Hydrolysis; Immunoblotting; Light; Lysine; Mice; Multidrug Resistance-Associated Proteins; Mutation; MutS Homolog 3 Protein; Protein Binding; Protein Structure, Tertiary; Temperature; Vanadates | 2002 |
Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1).
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Sequence; Animals; Aspartic Acid; Biological Transport; Carboxylic Acids; Catalysis; Cell Line; Cell Membrane; DNA, Complementary; Drug Resistance, Multiple; Electrophoresis, Polyacrylamide Gel; Glutamic Acid; Humans; Hydrolysis; Insecta; Leukotriene C4; Light; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutation; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Time Factors; Vanadates | 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 |
Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Anions; Arginine; Aspartic Acid; Biological Transport; Catalysis; Cell Line, Transformed; Cytoplasm; DNA Mutational Analysis; DNA, Complementary; Glutamic Acid; Humans; Ions; Leukotriene C4; Models, Molecular; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutagenesis, Site-Directed; Mutation; Organic Anion Transporters; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Time Factors; Transfection; Vanadates | 2004 |
Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Alanine; Animals; Aspartic Acid; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding, Competitive; Carboxylic Acids; Catalysis; Dimerization; Dithiothreitol; Dose-Response Relationship, Drug; Glutamic Acid; Hydrolysis; Kinetics; Lipid Metabolism; Lysine; Mice; Models, Chemical; Mutation; Pichia; Protein Conformation; Protein Structure, Tertiary; Time Factors; Vanadates | 2004 |
Substrate-trapping techniques in the identification of cellular PTP targets.
Topics: Alanine; Aspartic Acid; Catalytic Domain; Cysteine; Glutathione; Mutation; Protein Tyrosine Phosphatases; Recombinant Fusion Proteins; Serine; Substrate Specificity; Vanadates | 2005 |
Characterization of a plant, tyrosine-specific phosphatase of the aspartyl class.
Topics: Animals; Arabidopsis; Arabidopsis Proteins; Aspartic Acid; Binding Sites; Catalysis; DNA Mutational Analysis; Drosophila Proteins; Enzyme Inhibitors; Eye Proteins; Hydrogen-Ion Concentration; Metals, Heavy; Peptide Fragments; Peptides; Phosphorylation; Phosphotyrosine; Protein Tyrosine Phosphatases; Structural Homology, Protein; Substrate Specificity; Tungsten Compounds; Vanadates | 2005 |
Single amino acid substitution in the putative transmembrane helix V in KdpB of the KdpFABC complex of Escherichia coli uncouples ATPase activity and ion transport.
Topics: Adenosine Triphosphatases; Alanine; Amino Acid Substitution; Aspartic Acid; Biological Transport, Active; Cation Transport Proteins; Cations, Monovalent; Enzyme Activation; Escherichia coli Proteins; Genetic Complementation Test; Glutamic Acid; Hydrolysis; Ion Channel Gating; Lysine; Membrane Proteins; Mutagenesis, Site-Directed; Potassium; Protein Structure, Secondary; Protein Subunits; Proteolipids; Vanadates | 2005 |
Phosphatidylserine stimulation of Drs2p·Cdc50p lipid translocase dephosphorylation is controlled by phosphatidylinositol-4-phosphate.
Topics: Adenosine Triphosphate; Aspartic Acid; Calcium-Transporting ATPases; Detergents; Fluorides; Phosphatidylinositol Phosphates; Phosphatidylserines; Phosphorus Radioisotopes; Phosphorylation; Plasmids; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solubility; Vanadates | 2012 |