PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10715121-4 2000 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 0-5 solute carrier family 2 member 1 Homo sapiens 190-195 10715121-4 2000 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 78-83 solute carrier family 2 member 1 Homo sapiens 190-195 10715121-4 2000 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 143-148 solute carrier family 2 member 1 Homo sapiens 190-195 10715121-5 2000 Kinetic analysis of net sugar fluxes indicates that GluT1 sugar binding sites are cytoplasmic. Sugars 24-29 solute carrier family 2 member 1 Homo sapiens 52-57 10715121-5 2000 Kinetic analysis of net sugar fluxes indicates that GluT1 sugar binding sites are cytoplasmic. Sugars 58-63 solute carrier family 2 member 1 Homo sapiens 52-57 10715121-6 2000 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 34-39 solute carrier family 2 member 1 Homo sapiens 28-33 10715121-6 2000 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 34-39 solute carrier family 2 member 1 Homo sapiens 98-103 10715121-6 2000 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 138-143 solute carrier family 2 member 1 Homo sapiens 28-33 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 16-21 solute carrier family 2 member 1 Homo sapiens 38-43 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 16-21 solute carrier family 2 member 1 Homo sapiens 125-130 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 68-73 solute carrier family 2 member 1 Homo sapiens 38-43 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 68-73 solute carrier family 2 member 1 Homo sapiens 125-130