Pub. Date : 2002 Oct 22
PMID : 12379105
12 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Intracellular ATP inhibits human erythrocyte net sugar transport by binding cooperatively to the glucose transport protein (GluT1). | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 2 | ATP binding produces altered transporter affinity for substrate and promotes substrate occlusion within a post-translocation vestibule formed by GluT1 cytosolic domains. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 3 | (2002) Biochemistry 41, 12639-12651) demonstrates that reduced intracellular pH promotes high-affinity ATP binding to GluT1 but inhibits ATP-modulation of GluT1-mediated sugar transport. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 4 | (2002) Biochemistry 41, 12639-12651) demonstrates that reduced intracellular pH promotes high-affinity ATP binding to GluT1 but inhibits ATP-modulation of GluT1-mediated sugar transport. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 5 | The present study explores the role of GluT1 residues 326-343 (a proposed GluT1 ATP-binding site subdomain) in GluT1 ATP binding by using alanine scanning mutagenesis. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 6 | The present study explores the role of GluT1 residues 326-343 (a proposed GluT1 ATP-binding site subdomain) in GluT1 ATP binding by using alanine scanning mutagenesis. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 7 | The present study explores the role of GluT1 residues 326-343 (a proposed GluT1 ATP-binding site subdomain) in GluT1 ATP binding by using alanine scanning mutagenesis. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 8 | The present study explores the role of GluT1 residues 326-343 (a proposed GluT1 ATP-binding site subdomain) in GluT1 ATP binding by using alanine scanning mutagenesis. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 9 | The present study explores the role of GluT1 residues 326-343 (a proposed GluT1 ATP-binding site subdomain) in GluT1 ATP binding by using alanine scanning mutagenesis. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 10 | The present study explores the role of GluT1 residues 326-343 (a proposed GluT1 ATP-binding site subdomain) in GluT1 ATP binding by using alanine scanning mutagenesis. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 11 | Isolated, detergent-solubilized GluT1.HA.H6 is photolabeled by [gamma-32P]-azidoATP in an ATP-protectable manner. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |
| 12 | These actions resemble those of reduced pH on ATP binding to and modulation of red cell GluT1. | Adenosine Triphosphate | solute carrier family 2 member 1 | Homo sapiens |