Pub. Date : 2019 Apr 23
PMID : 30900874
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | In this report, biochemical analysis with various divalent cations was used to demonstrate that NNRTIs and divalent cation-dNTP complexes are mutually exclusive, inhibiting each other"s binding to RT/primer/template (RT-P/T) complexes. | Parathion | MORN repeat containing 4 | Homo sapiens |
2 | The binding of catalytically competent divalent cation-dNTP complexes to RT-P/T was measured with Mg2+, Mn2+, Zn2+, Co2+, and Ni2+ using Ca2+, a noncatalytic cation, for displacement. | Parathion | MORN repeat containing 4 | Homo sapiens |
3 | Filtration assays demonstrated that divalent cation-dNTP complexes inhibited the binding of 14C-labeled EFV to RT-P/T with stronger binding complexes formed with Mn2+ inhibiting more potently than those with Mg2+. | Parathion | MORN repeat containing 4 | Homo sapiens |
4 | Conversely, filter binding assays demonstrated that EFV inhibited 3H-labeled dNTP binding to RT-P/T complexes with displacement of Mn2+-dNTP complexes requiring much greater concentrations of EFV than the more weakly bound Mg2+-dNTP complexes. | Parathion | MORN repeat containing 4 | Homo sapiens |
5 | Conversely, filter binding assays demonstrated that EFV inhibited 3H-labeled dNTP binding to RT-P/T complexes with displacement of Mn2+-dNTP complexes requiring much greater concentrations of EFV than the more weakly bound Mg2+-dNTP complexes. | Parathion | MORN repeat containing 4 | Homo sapiens |
6 | Conversely, filter binding assays demonstrated that EFV inhibited 3H-labeled dNTP binding to RT-P/T complexes with displacement of Mn2+-dNTP complexes requiring much greater concentrations of EFV than the more weakly bound Mg2+-dNTP complexes. | Parathion | MORN repeat containing 4 | Homo sapiens |