Pub. Date : 2000 Mar 21
PMID : 10715121
12 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Sugar binding assays using cells and membrane protein fractions indicate that sugar binding to erythrocytes is quantitatively accounted for by sugar binding to the hexose transport protein, GluT1. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 2 | Sugar binding assays using cells and membrane protein fractions indicate that sugar binding to erythrocytes is quantitatively accounted for by sugar binding to the hexose transport protein, GluT1. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 3 | Sugar binding assays using cells and membrane protein fractions indicate that sugar binding to erythrocytes is quantitatively accounted for by sugar binding to the hexose transport protein, GluT1. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 4 | Kinetic analysis of net sugar fluxes indicates that GluT1 sugar binding sites are cytoplasmic. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 5 | Kinetic analysis of net sugar fluxes indicates that GluT1 sugar binding sites are cytoplasmic. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 6 | Intracellular ATP increases GluT1 sugar binding capacity from 1 to 2 mol of 3-O-methylglucose/mol GluT1 and inhibits the release of bound sugar into cytosol. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 7 | Intracellular ATP increases GluT1 sugar binding capacity from 1 to 2 mol of 3-O-methylglucose/mol GluT1 and inhibits the release of bound sugar into cytosol. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 8 | Intracellular ATP increases GluT1 sugar binding capacity from 1 to 2 mol of 3-O-methylglucose/mol GluT1 and inhibits the release of bound sugar into cytosol. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 9 | We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 10 | We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 11 | We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. | Sugars | solute carrier family 2 member 1 | Homo sapiens |
| 12 | We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. | Sugars | solute carrier family 2 member 1 | Homo sapiens |