Pub. Date : 2010 Oct
PMID : 20457661
32 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogues of ADP and ATP. | arsenic acid | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 2 | Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogues of ADP and ATP. | arsenite | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 3 | Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogues of ADP and ATP. | Adenosine Diphosphate | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 4 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | Poly A | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 5 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | Poly A | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 6 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | Poly A | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 7 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | Poly A | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 8 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | amp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 9 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | amp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 10 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | adp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 11 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | adp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 12 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | asunaprevir | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 13 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | asunaprevir | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 14 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | asiii | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 15 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | asiii | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 16 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | Sulfhydryl Compounds | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 17 | To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols. | Sulfhydryl Compounds | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 18 | Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH. | asiii | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 19 | Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH. | Poly A | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 20 | Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH. | asunaprevir | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 21 | Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH. | Glutathione | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 22 | PNPase-mediated AsV reduction depended on arsenolysis of poly-A and presence of a thiol. | Poly A | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 23 | PNPase-mediated AsV reduction depended on arsenolysis of poly-A and presence of a thiol. | Sulfhydryl Compounds | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 24 | PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP). | amp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 25 | PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP). | Adenosine Diphosphate | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 26 | PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP). | asunaprevir | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 27 | PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP). | Adenosine Diphosphate | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 28 | Although various thiols did not influence the arsenolytic yield of AMP-AsV, they differentially promoted the PNPase-mediated reduction of AsV, with GSH being the most effective. | Sulfhydryl Compounds | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 29 | Although various thiols did not influence the arsenolytic yield of AMP-AsV, they differentially promoted the PNPase-mediated reduction of AsV, with GSH being the most effective. | Glutathione | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 30 | Circumstantial evidence indicated that AMP-AsV formed by PNPase is more reducible to AsIII by GSH than inorganic AsV. | amp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 31 | Circumstantial evidence indicated that AMP-AsV formed by PNPase is more reducible to AsIII by GSH than inorganic AsV. | Glutathione | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |
| 32 | Thus, whereas PNPase promotes reduction of AsV by incorporating it into AMP-AsV, the mitochondrial ATP synthase facilitates AsV reduction by forming ADP-AsV; then GSH can easily reduce these arsenylated nucleotides to AsIII. | amp-asv | polyribonucleotide nucleotidyltransferase 1 | Homo sapiens |