Pub. Date : 2020 Jan
PMID : 31746080
17 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Gamabufotalin induces a negative feedback loop connecting ATP1A3 expression and the AQP4 pathway to promote temozolomide sensitivity in glioblastoma cells by targeting the amino acid Thr794. | gamabufotalin | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 2 | RESULTS: Mechanistic research revealed a negative feedback loop between ATP1A3 and AQP4 through which CS-6 inhibited GBM growth and mediated the synergistic treatment effect of CS-6 and TMZ. | 1-hexene | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 3 | RESULTS: Mechanistic research revealed a negative feedback loop between ATP1A3 and AQP4 through which CS-6 inhibited GBM growth and mediated the synergistic treatment effect of CS-6 and TMZ. | 1-hexene | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 4 | RESULTS: Mechanistic research revealed a negative feedback loop between ATP1A3 and AQP4 through which CS-6 inhibited GBM growth and mediated the synergistic treatment effect of CS-6 and TMZ. | Temozolomide | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 5 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 6 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 7 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Hydrogen | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 8 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Hydrogen | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 9 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 10 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 11 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 12 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 13 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Temozolomide | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 14 | In addition, by mutating potential amino acid residues of ATP1A3, which were predicted by modelling and docking to interact with CS-6, we demonstrated that abrogating hydrogen bonding of the amino acid Thr794 interferes with the activation of ATP1A3 by CS-6 and that the Thr794Ala mutation directly affects the synergistic treatment efficacy of CS-6 and TMZ. | Temozolomide | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 15 | CONCLUSIONS: As the main potential target of CS-6, ATP1A3 activation critically depends on the hydrogen bonding of Thr794 with CS-6. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 16 | CONCLUSIONS: As the main potential target of CS-6, ATP1A3 activation critically depends on the hydrogen bonding of Thr794 with CS-6. | Hydrogen | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |
| 17 | CONCLUSIONS: As the main potential target of CS-6, ATP1A3 activation critically depends on the hydrogen bonding of Thr794 with CS-6. | Cesium | ATPase Na+/K+ transporting subunit alpha 3 | Homo sapiens |