PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1959168-4 1991 In the 6 putative metabolites of PQ, 5-OH PQ and 5,6-OH PQ were the most potent hemolytic toxidants which could produce similar level of methemoglobin formation at concentrations several orders of magnitude less than that of PQ, while the hemolytic toxicity of 6-OH PQ, AQD and AQL was also higher than that of PQ itself. Primaquine 33-35 hemoglobin subunit gamma 2 Homo sapiens 137-150 1959168-4 1991 In the 6 putative metabolites of PQ, 5-OH PQ and 5,6-OH PQ were the most potent hemolytic toxidants which could produce similar level of methemoglobin formation at concentrations several orders of magnitude less than that of PQ, while the hemolytic toxicity of 6-OH PQ, AQD and AQL was also higher than that of PQ itself. Primaquine 42-44 hemoglobin subunit gamma 2 Homo sapiens 137-150 1959168-4 1991 In the 6 putative metabolites of PQ, 5-OH PQ and 5,6-OH PQ were the most potent hemolytic toxidants which could produce similar level of methemoglobin formation at concentrations several orders of magnitude less than that of PQ, while the hemolytic toxicity of 6-OH PQ, AQD and AQL was also higher than that of PQ itself. Primaquine 42-44 hemoglobin subunit gamma 2 Homo sapiens 137-150 28440745-3 2017 There is evidence that metabolites of primaquine formed by the cytochrome pathway are responsible for methemoglobin formation; a genetic polymorphism of cytochrome isoforms; and a potential influence of gender in the activities of these enzymes requiring the establishment of dose x response curves profiles in different population groups. Primaquine 38-48 hemoglobin subunit gamma 2 Homo sapiens 102-115 7126253-5 1982 Stimulation of the hexose monophosphate shunt by primaquine does not primarily involve H2O2 accumulation since stimulation of the pathway by primaquine was also observed in red cells containing methemoglobin, a red cell preparation in which no H2O2 accumulates. Primaquine 141-151 hemoglobin subunit gamma 2 Homo sapiens 194-207 7126253-6 1982 Methemoglobin prevented the formation and/or accumulation of H2O2 in intact red cells incubated with primaquine as well as in a non-cellular system containing primaquine plus Fe2+-EDTA as an H2O2 source. Primaquine 101-111 hemoglobin subunit gamma 2 Homo sapiens 0-13 7126253-6 1982 Methemoglobin prevented the formation and/or accumulation of H2O2 in intact red cells incubated with primaquine as well as in a non-cellular system containing primaquine plus Fe2+-EDTA as an H2O2 source. Primaquine 159-169 hemoglobin subunit gamma 2 Homo sapiens 0-13 7126253-8 1982 In the red cell, primaquine stimulated glucose-dependent conversion of methemoglobin to oxyhemoglobin. Primaquine 17-27 hemoglobin subunit gamma 2 Homo sapiens 71-84 3202898-3 1988 The results show that a 1.5 mM concentration of (-)PQ produced a significantly greater increase in Met Hb content and decrease in reduced glutathione (GSH) level than did (+)PQ. Primaquine 48-53 hemoglobin subunit gamma 2 Homo sapiens 99-105 6699888-0 1984 Synthesis of certain hydroxy analogues of the antimalarial drug primaquine and their in vitro methemoglobin-producing and glutathione-depleting activity in human erythrocytes. Primaquine 64-74 hemoglobin subunit gamma 2 Homo sapiens 94-107 27223244-1 2016 The administration of primaquine (PQ), an essential drug for the treatment and radical cure of malaria, can lead to methemoglobin formation and life-threatening hemolysis for glucose-6-phosphate dehydrogenase deficient patients. Primaquine 22-32 hemoglobin subunit gamma 2 Homo sapiens 116-129 27223244-6 2016 Several literature and proposed 8-AQ analogues were studied to evaluate substituent effects on their potential to generate methemoglobin, with the finding that hydroxylations at N1" and C5 contribute the most to the potential hemotoxicity of PQ-based antimalarials, whereas hydroxylation at C7 has little effect. Primaquine 242-244 hemoglobin subunit gamma 2 Homo sapiens 123-136 27223244-1 2016 The administration of primaquine (PQ), an essential drug for the treatment and radical cure of malaria, can lead to methemoglobin formation and life-threatening hemolysis for glucose-6-phosphate dehydrogenase deficient patients. Primaquine 34-36 hemoglobin subunit gamma 2 Homo sapiens 116-129 27223244-2 2016 The ionization potential (IP, a quantitative measure of the ability to lose an electron) of the metabolites generated by antimalarial 8-aminoquinoline (8-AQ) drugs like PQ has been believed to be correlated in part to this methemoglobinemia hemotoxicity: the lower the IP of an 8-AQ derivative, the higher the concentration of methemoglobin generated. Primaquine 169-171 hemoglobin subunit gamma 2 Homo sapiens 223-236 25222923-0 2015 Computational Study on the Effect of Exocyclic Substituents on the Ionization Potential of Primaquine: Insights into the Design of Primaquine-Based Antimalarial Drugs with Less Methemoglobin Generation. Primaquine 91-101 hemoglobin subunit gamma 2 Homo sapiens 177-190 25222923-0 2015 Computational Study on the Effect of Exocyclic Substituents on the Ionization Potential of Primaquine: Insights into the Design of Primaquine-Based Antimalarial Drugs with Less Methemoglobin Generation. Primaquine 131-141 hemoglobin subunit gamma 2 Homo sapiens 177-190 24224488-0 2013 Methemoglobin generation by 8-aminoquinolines: effect of substitution at 5-position of primaquine. Primaquine 87-97 hemoglobin subunit gamma 2 Homo sapiens 0-13 19616568-11 2009 Primaquine caused similar methemoglobin formation in G6PD(-) and normal human erythrocytes. Primaquine 0-10 hemoglobin subunit gamma 2 Homo sapiens 26-39 23412873-0 2013 Methemoglobin incites primaquine toxicity through single-electron oxidation and modification. Primaquine 22-32 hemoglobin subunit gamma 2 Homo sapiens 0-13 23412873-2 2013 METHODS: Methemoglobin (MetHb)-Pq molecular modeling was used to identify the Pq binding pocket. Primaquine 31-33 hemoglobin subunit gamma 2 Homo sapiens 9-22 23412873-2 2013 METHODS: Methemoglobin (MetHb)-Pq molecular modeling was used to identify the Pq binding pocket. Primaquine 31-33 hemoglobin subunit gamma 2 Homo sapiens 24-29 23412873-5 2013 RESULTS: MetHb binded Pq at the heme site with KD =6.4 muM as evidenced by a difference spectroscopy study. Primaquine 22-24 hemoglobin subunit gamma 2 Homo sapiens 9-14 23412873-6 2013 MetHb oxidized Pq through a single e-transfer mechanism to form Pqox. Primaquine 15-17 hemoglobin subunit gamma 2 Homo sapiens 0-5 23412873-7 2013 The analysis of Pq from MetHb-H2O2 peroxidase reaction mixture gave peaks at m/z 300.53 and m/z 243.42, corresponding to the hydroxyl and desamino derivative of Pq, respectively. Primaquine 16-18 hemoglobin subunit gamma 2 Homo sapiens 24-29 23412873-7 2013 The analysis of Pq from MetHb-H2O2 peroxidase reaction mixture gave peaks at m/z 300.53 and m/z 243.42, corresponding to the hydroxyl and desamino derivative of Pq, respectively. Primaquine 161-163 hemoglobin subunit gamma 2 Homo sapiens 24-29 23412873-12 2013 MetHb-H2O2-mediated Pq hemolytic potentiation that is sensitive to spin trap indicates the role of Pq* radical or other single e-species in the process. Primaquine 20-22 hemoglobin subunit gamma 2 Homo sapiens 0-5 22330256-2 2012 Recent investigations at our lab have shown that the metabolites generated through cytochrome P(450)-dependent metabolic reactions are responsible for hemotoxic effects of primaquine, which could be monitored with accumulation of methemoglobin and increased oxidative stress. Primaquine 172-182 hemoglobin subunit gamma 2 Homo sapiens 230-243 22330256-5 2012 Primaquine, presumably through redox active hemotoxic metabolites generated in situ in human liver microsomal metabolism-linked assay, induced a dose-dependent methemoglobin accumulation and oxidative stress, which were almost similar in normal and G6PD-deficient erythrocytes. Primaquine 0-10 hemoglobin subunit gamma 2 Homo sapiens 160-173 19190211-5 2009 MetHB levels were detected at > or = 4% in 46-50% 1 day after PQ treatment in all three groups and 4-9% of subjects had MetHB levels > or = 4% 15 days after treatment. Primaquine 65-67 hemoglobin subunit gamma 2 Homo sapiens 0-5 7947943-3 1994 PQ caused RBC lysis and facilitated the oxidation of oxyhemoglobin (oxyHb) to methemoglobin (MetHb). Primaquine 0-2 hemoglobin subunit gamma 2 Homo sapiens 78-91 7947943-3 1994 PQ caused RBC lysis and facilitated the oxidation of oxyhemoglobin (oxyHb) to methemoglobin (MetHb). Primaquine 0-2 hemoglobin subunit gamma 2 Homo sapiens 93-98 8757424-4 1996 The initial methemoglobin level ranged from 15.3% in the patient whose methemoglobinemia was caused by primaquine alone to 33.1%. Primaquine 103-113 hemoglobin subunit gamma 2 Homo sapiens 12-25