lysine has been researched along with 4-acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic acid in 18 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 7 (38.89) | 18.7374 |
1990's | 10 (55.56) | 18.2507 |
2000's | 1 (5.56) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
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Kaplan, JH; Kirley, TL; Pedemonte, CH; Treuheit, MJ | 1 |
Dierks, T; Krämer, R; Salentin, A; Stappen, R | 1 |
Müller, H; Passow, H; Sovak, M; Wood, PG | 1 |
Kay, MM; Lin, FB | 1 |
Begenisich, T; Spires, S | 1 |
Bartel, D; Kietz, D; Lepke, S; Passow, H | 1 |
Bartel, D; Hans, H; Passow, H | 1 |
Garcia, AM; Lodish, HF | 1 |
Anderson, MP; Jennings, ML; Monaghan, R | 1 |
Douglas, SM; Jennings, ML; Monaghan, R; Nicknish, JS | 1 |
Fasold, H; Gärtner, EM; Legrum, B; Passow, H; Ruffing, W; Zaki, L | 1 |
Gaarn, A; Ramjeesingh, M; Rothstein, A | 1 |
Jennings, ML | 1 |
Michelangeli, F | 1 |
Knauf, PA; Liu, SQ | 1 |
Johnson, RM; Tang, K | 1 |
Alper, SL; Shmukler, BE; Zolotarev, AS | 1 |
Giangregorio, N; Indiveri, C; Palmieri, F; Tonazzi, A | 1 |
1 review(s) available for lysine and 4-acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic acid
Article | Year |
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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 |
17 other study(ies) available for lysine and 4-acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic acid
Article | Year |
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Inactivation of the Na,K-ATPase by modification of Lys-501 with 4-acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic acid (SITS).
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Animals; Dogs; Kidney; Kinetics; Lysine; Molecular Sequence Data; Peptide Mapping; Potassium Chloride; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Structure-Activity Relationship | 1992 |
Probing the active site of the reconstituted aspartate/glutamate carrier from bovine heart mitochondria: carbodiimide-catalyzed acylation of a functional lysine residue.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; Acylation; Amino Acid Transport Systems, Acidic; Animals; Antiporters; Aspartic Acid; Binding Sites; Biological Transport; Carrier Proteins; Catalysis; Cattle; Diethyl Pyrocarbonate; Electrophoresis, Polyacrylamide Gel; Ethyldimethylaminopropyl Carbodiimide; Glutamates; Glutamic Acid; Kinetics; Lysine; Mitochondria, Heart; Proteolipids; Pyridoxal Phosphate | 1992 |
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 |
Molecular mapping of the active site of an aging antigen: senescent cell antigen requires lysine(s) for antigenicity and is located on an anion-binding segment of band 3 membrane transport protein.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Sequence; Anion Exchange Protein 1, Erythrocyte; Anions; Antigens, Surface; Binding Sites; Epitopes; Erythrocyte Aging; Humans; Lysine; Molecular Sequence Data; Peptide Mapping | 1990 |
Modification of potassium channel kinetics by amino group reagents.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; Acetic Anhydrides; Animals; Axons; Decapodiformes; Hydrogen-Ion Concentration; Imidoesters; Ion Channel Gating; Lysine; Potassium; Potassium Channels; Succinic Anhydrides; Trinitrobenzenesulfonic Acid | 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 |
Lysine 539 of human band 3 is not essential for ion transport or inhibition by stilbene disulfonates.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Anion Exchange Protein 1, Erythrocyte; Base Sequence; Chlorides; Dipyridamole; Erythrocytes; Female; Humans; Kinetics; Lysine; Molecular Sequence Data; Mutation; Oligonucleotide Probes; Oocytes; Protein Binding; Stilbenes; Xenopus laevis | 1989 |
Monoclonal antibodies against human erythrocyte band 3 protein. Localization of proteolytic cleavage sites and stilbenedisulfonate-binding lysine residues.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Anion Exchange Protein 1, Erythrocyte; Antibodies, Monoclonal; Erythrocyte Membrane; Humans; Hybridomas; Lysine; Mice; Mice, Inbred BALB C; Molecular Weight; Peptide Fragments; Protein Binding; Stilbenes; Trypsin | 1986 |
Functions of extracellular lysine residues in the human erythrocyte anion transport protein.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Carrier Proteins; Chemical Phenomena; Chemistry; Cross-Linking Reagents; Erythrocyte Membrane; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Lysine; Membrane Proteins; Peptide Fragments; Succinimides | 1985 |
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 |
The effects of amino acid-reactive reagents on the functioning of the inositol 1,4,5-trisphosphate-sensitive calcium channel from rat cerebellum.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Adenosine Triphosphate; Animals; Arginine; Binding Sites; Biological Transport, Active; Calcimycin; Calcium; Calcium Channels; Cerebellum; Cysteine; Inositol 1,4,5-Trisphosphate; Lysine; Microsomes; Phenylglyoxal; Rats; Ruthenium Red; Signal Transduction; Silver Nitrate; Vanadates | 1993 |
Lys-430, site of irreversible inhibition of band 3 Cl- flux by eosin-5-maleimide, is not at the transport site.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Sequence; Anion Exchange Protein 1, Erythrocyte; Binding Sites; Chlorides; Eosine Yellowish-(YS); Erythrocyte Membrane; Humans; Kinetics; Lysine; Mathematics; Models, Biological; Protein Conformation | 1993 |
DIDS inhibition of deformation-induced cation flux in human erythrocytes.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Cations; Cell Membrane Permeability; Cell Size; Chlorides; Chymotrypsin; Erythrocytes; Humans; Lysine; Potassium; Sodium | 1993 |
AE2 anion exchanger polypeptide is a homooligomer in pig gastric membranes: a chemical cross-linking study.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Sequence; Animals; Anion Transport Proteins; Antiporters; Cell Membrane; Cross-Linking Reagents; Dimerization; DNA, Complementary; Gastric Mucosa; Lysine; Membrane Proteins; Molecular Sequence Data; Peptide Fragments; Peptides; SLC4A Proteins; Swine | 1999 |
Relationships of Cysteine and Lysine residues with the substrate binding site of the mitochondrial ornithine/citrulline carrier: an inhibition kinetic approach combined with the analysis of the homology structural model.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Amino Acid Transport Systems, Basic; Animals; Binding Sites; Biological Transport; Citrulline; Cysteine; Lysine; Mutation; Ornithine; Protein Conformation; Pyridoxal Phosphate; Rats; Structural Homology, Protein; Sulfhydryl Reagents | 2005 |