dihydro-dids has been researched along with lysine in 10 studies
| Studies (dihydro-dids) | Trials (dihydro-dids) | Recent Studies (post-2010) (dihydro-dids) | Studies (lysine) | Trials (lysine) | Recent Studies (post-2010) (lysine) |
|---|---|---|---|---|---|
| 127 | 0 | 5 | 37,449 | 622 | 11,213 |
| Protein | Taxonomy | dihydro-dids (IC50) | lysine (IC50) |
|---|---|---|---|
| Cationic amino acid transporter 3 | Homo sapiens (human) | 158 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (40.00) | 18.7374 |
| 1990's | 6 (60.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Müller, H; Passow, H; Sovak, M; Wood, PG | 1 |
| Bartel, D; Kietz, D; Lepke, S; Passow, H | 1 |
| Bartel, D; Hans, H; Passow, H | 1 |
| Fasold, H; Gärtner, EM; Legrum, B; Passow, H; Ruffing, W; Zaki, L | 1 |
| Gaarn, A; Ramjeesingh, M; Rothstein, A | 1 |
| Jennings, ML | 1 |
| Appelhans, H; Karbach, D; König, J; Lepke, S; Müller-Berger, S; Passow, H; Wood, PG | 1 |
| Hoshino, F; Makino, S; Moriyama, R; Tomida, M | 1 |
| Hamasaki, N; Jennings, ML; Kang, D; Okubo, K | 1 |
| Gärtner, EM; Legrum, B; Lepke, S; Passow, H; Ruffing, W | 1 |
1 review(s) available for dihydro-dids and lysine
| Article | Year |
|---|---|
Anion transport across the red blood cell membrane and the conformation of the protein in Band 3.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Anion Exchange Protein 1, Erythrocyte; Anions; Benzothiazoles; Binding Sites; Biological Transport, Active; Blood Proteins; Chemical Phenomena; Chemistry; Erythrocyte Membrane; Erythrocytes; Humans; Lysine; Membrane Proteins; Models, Biological; Protein Conformation; Structure-Activity Relationship; Thiazoles | 1980 |
9 other study(ies) available for dihydro-dids and lysine
| Article | Year |
|---|---|
Role of Lys 558 and Lys 869 in substrate and inhibitor binding to the murine band 3 protein: a study of the effects of site-directed mutagenesis of the band 3 protein expressed in the oocytes of Xenopus laevis.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Sequence; Animals; Anion Exchange Protein 1, Erythrocyte; Binding Sites; Biological Transport; Chlorides; Lysine; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Protein Binding; Pyridoxal Phosphate; Stilbenes; Xenopus laevis | 1992 |
pH-dependence of inhibition by H2DIDS of mouse erythroid band 3-mediated Cl- transport in Xenopus oocytes. The effect of oligonucleotide-directed replacement of Lys-558 by an Asn residue.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Anion Exchange Protein 1, Erythrocyte; Asparagine; Chlorides; Erythrocyte Membrane; Hydrogen-Ion Concentration; Kinetics; Lysine; Mice; Mutagenesis, Site-Directed; Oligonucleotide Probes; Oocytes; Temperature; Xenopus | 1991 |
Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Anion Exchange Protein 1, Erythrocyte; Anions; Autoradiography; Biological Transport; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Lysine; Mice; Mutation; Oocytes; Stilbenes; Substrate Specificity; Xenopus | 1989 |
The amino acid conjugate formed by the interaction of the anion transport inhibitor 4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid (DIDS) with band 3 protein from human red blood cell membranes.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Anion Exchange Protein 1, Erythrocyte; Arginine; Biological Transport; Blood Proteins; Chemical Phenomena; Chemistry; Chromatography, Thin Layer; Erythrocyte Membrane; Erythrocytes; Humans; Hydrolysis; Lysine; Membrane Proteins; Stilbenes | 1981 |
Reductive methylation of the two 4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonate-binding lysine residues of band 3, the human erythrocyte anion transport protein.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Anion Exchange Protein 1, Erythrocyte; Binding Sites; Blood Proteins; Electrophoresis, Polyacrylamide Gel; Humans; Lysine; Methylation; Peptide Fragments; Protein Binding; Stilbenes | 1982 |
Inhibition of mouse erythroid band 3-mediated chloride transport by site-directed mutagenesis of histidine residues and its reversal by second site mutation of Lys 558, the locus of covalent H2DIDS binding.
Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Sequence; Animals; Anion Exchange Protein 1, Erythrocyte; Biological Transport; Cell Membrane; Chlorides; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Erythrocytes; Female; Histidine; Lysine; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Point Mutation; Protein Biosynthesis; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Reticulocytes; Xenopus laevis | 1995 |
Local structural difference between human and bovine band 3 in the anion transport inhibitor-binding region.
Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Anion Exchange Protein 1, Erythrocyte; Cattle; Cell Membrane Permeability; Chromatography; Chymotrypsin; Circular Dichroism; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Erythrocytes; Humans; Lysine; Peptide Fragments; Pyridoxal Phosphate; Serine Endopeptidases | 1995 |
Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonic acid) molecule.
Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Sequence; Anion Exchange Protein 1, Erythrocyte; Binding Sites; Blotting, Western; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Endopeptidases; Erythrocyte Membrane; Humans; Hydrogen-Ion Concentration; Lysine; Models, Molecular; Models, Structural; Molecular Sequence Data; Molecular Structure; Peptide Fragments | 1994 |
Transport-related conformational states of the band 3 protein: probing with 1-fluoro-2,4-dinitrobenzene.
Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Anion Exchange Protein 1, Erythrocyte; Chlorides; Dinitrofluorobenzene; Humans; Hydrogen-Ion Concentration; Ion Transport; Kinetics; Lysine; Mice; Mutation; Protein Conformation; Sulfates; Xenopus | 1996 |