glutamic acid has been researched along with n-ethyl-5-phenylisoxazolium-3'-sulfonate in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (14.29) | 18.7374 |
| 1990's | 2 (28.57) | 18.2507 |
| 2000's | 4 (57.14) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Jennings, ML; Smith, JS | 1 |
| Anderson, MP; Jennings, ML | 1 |
| Dekker, EE; Johnson, AR | 1 |
| Chen, G; Falany, CN; Rabjohn, PA; Radominska-Pandya, A; Wooldridge, C; York, JL; Zhang, D | 1 |
| Cordes, KS; Salhany, JM; Sloan, RL | 1 |
| Banerjee, S; Ray, M; Ray, S; SinhaRoy, S | 1 |
| Alper, SL; Barry, PN; Chernova, MN; Jennings, ML; Stewart, AK | 1 |
7 other study(ies) available for glutamic acid and n-ethyl-5-phenylisoxazolium-3'-sulfonate
| Article | Year |
|---|---|
Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.
Topics: Amino Acid Sequence; Animals; Anion Exchange Protein 1, Erythrocyte; Anions; Carboxypeptidases; Chlorides; Erythrocytes; Glutamates; Glutamic Acid; Humans; Isoxazoles; Molecular Sequence Data; Peptide Fragments; Protons; Sequence Homology, Nucleic Acid; Sulfates | 1992 |
Chemical modification and labeling of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Anion Exchange Protein 1, Erythrocyte; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Chymotrypsin; Glutamates; Glutamic Acid; Humans; Isoxazoles; Membrane Proteins; Methylation; Molecular Weight; Stilbenes | 1987 |
Woodward's reagent K inactivation of Escherichia coli L-threonine dehydrogenase: increased absorbance at 340-350 nm is due to modification of cysteine and histidine residues, not aspartate or glutamate carboxyl groups.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Aspartic Acid; Bacterial Proteins; Cysteine; Enzyme Inhibitors; Escherichia coli; Glutamic Acid; Histidine; Isoxazoles; Kinetics; Models, Chemical; Molecular Sequence Data; Solvents; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds | 1996 |
Carboxyl residues in the active site of human phenol sulfotransferase (SULT1A1).
Topics: Amino Acid Sequence; Arylsulfotransferase; Aspartic Acid; Binding Sites; Computer Simulation; Dose-Response Relationship, Drug; Enzyme Activation; Glutamic Acid; Humans; Hydrogen-Ion Concentration; Indicators and Reagents; Isoxazoles; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphoadenosine Phosphosulfate; Substrate Specificity | 2000 |
The carboxyl side chain of glutamate 681 interacts with a chloride binding modifier site that allosterically modulates the dimeric conformational state of band 3 (AE1). Implications for the mechanism of anion/proton cotransport.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Allosteric Regulation; Allosteric Site; Anion Exchange Protein 1, Erythrocyte; Borohydrides; Chlorides; Dimerization; Erythrocyte Membrane; Glutamic Acid; Humans; Indicators and Reagents; Ion Transport; Isoxazoles; Kinetics; Models, Chemical; Peptide Fragments; Protein Binding; Protein Conformation; Protein Subunits; Protons; Spectrometry, Fluorescence | 2003 |
Possible involvement of glutamic and/or aspartic acid residue(s) and requirement of mitochondrial integrity for the protective effect of creatine against inhibition of cardiac mitochondrial respiration by methylglyoxal.
Topics: Alamethicin; Animals; Aspartic Acid; Binding Sites; Cell Respiration; Creatine; Electron Transport Complex I; Glutamic Acid; Goats; Intracellular Membranes; Isoxazoles; Mitochondria, Heart; NAD; NADH Dehydrogenase; Oxygen Consumption; Permeability; Protective Agents; Pyruvaldehyde; Submitochondrial Particles | 2005 |
Mouse Ae1 E699Q mediates SO42-i/anion-o exchange with [SO42-]i-dependent reversal of wild-type pHo sensitivity.
Topics: Amino Acid Substitution; Animals; Anion Exchange Protein 1, Erythrocyte; Anions; Borohydrides; Chlorides; Female; Glutamic Acid; Humans; Hydrogen-Ion Concentration; Isoxazoles; Kinetics; Mesylates; Mice; Oocytes; Sulfates; Sulfonic Acids; Xenopus laevis | 2008 |