PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 32975211-3 2020 The steady-state level of SO2 (Cysteine sulfinic acid, Cys-SO2H) form for peroxiredoxin 3 (PRX3) was measured by a western blot. cys-so2h 55-63 peroxiredoxin 3 Homo sapiens 74-89 16565085-1 2006 Among many proteins with cysteine sulfinic acid (Cys-SO2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfiredoxin (Srx) in the presence of ATP. cys-so2h 49-57 peroxiredoxin 1 Homo sapiens 99-113 16565085-1 2006 Among many proteins with cysteine sulfinic acid (Cys-SO2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfiredoxin (Srx) in the presence of ATP. cys-so2h 49-57 sulfiredoxin 1 Homo sapiens 148-160 16565085-1 2006 Among many proteins with cysteine sulfinic acid (Cys-SO2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfiredoxin (Srx) in the presence of ATP. cys-so2h 49-57 sulfiredoxin 1 Homo sapiens 162-165 15590625-1 2005 Cysteine residues of certain peroxiredoxins (Prxs) undergo reversible oxidation to sulfinic acid (Cys-SO2H) and the reduction reaction is catalyzed by sulfiredoxin (Srx). cys-so2h 98-106 peroxiredoxin 1 Homo sapiens 29-43 15590625-7 2005 These results suggest that reduction of Cys-SO2H by Srx is specific to 2-Cys Prx isoforms. cys-so2h 40-48 sulfiredoxin 1 Homo sapiens 52-55 15590625-7 2005 These results suggest that reduction of Cys-SO2H by Srx is specific to 2-Cys Prx isoforms. cys-so2h 40-48 periaxin Homo sapiens 77-80 9278398-10 1997 Electrospray ionization mass spectrometry demonstrated that the mass of PTP1B increased by 34 +/- 2 units after the enzyme was inactivated with alendronate/calcium, due to the oxidization of the catalytic cysteine to sulfinic acid (Cys-SO2H). cys-so2h 232-240 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 72-77 15448164-2 2004 The cysteine residue in the active site of certain eukaryotic Prx enzymes undergoes reversible oxidation to sulfinic acid (Cys-SO2H) during catalysis, and sulfiredoxin (Srx) has been identified as responsible for reversal of the resulting enzyme inactivation in yeast. cys-so2h 123-131 periaxin Homo sapiens 62-65 15448164-2 2004 The cysteine residue in the active site of certain eukaryotic Prx enzymes undergoes reversible oxidation to sulfinic acid (Cys-SO2H) during catalysis, and sulfiredoxin (Srx) has been identified as responsible for reversal of the resulting enzyme inactivation in yeast. cys-so2h 123-131 sulfiredoxin Saccharomyces cerevisiae S288C 155-167 15448164-2 2004 The cysteine residue in the active site of certain eukaryotic Prx enzymes undergoes reversible oxidation to sulfinic acid (Cys-SO2H) during catalysis, and sulfiredoxin (Srx) has been identified as responsible for reversal of the resulting enzyme inactivation in yeast. cys-so2h 123-131 sulfiredoxin Saccharomyces cerevisiae S288C 169-172 15448164-8 2004 Finally, depletion of human Srx by RNA interference suggested that Srx is largely responsible for reduction of the Cys-SO2H of Prx in A549 human cells. cys-so2h 115-123 sulfiredoxin 1 Homo sapiens 28-31 15448164-8 2004 Finally, depletion of human Srx by RNA interference suggested that Srx is largely responsible for reduction of the Cys-SO2H of Prx in A549 human cells. cys-so2h 115-123 sulfiredoxin 1 Homo sapiens 67-70 15448164-8 2004 Finally, depletion of human Srx by RNA interference suggested that Srx is largely responsible for reduction of the Cys-SO2H of Prx in A549 human cells. cys-so2h 115-123 periaxin Homo sapiens 127-130 32975211-3 2020 The steady-state level of SO2 (Cysteine sulfinic acid, Cys-SO2H) form for peroxiredoxin 3 (PRX3) was measured by a western blot. cys-so2h 55-63 peroxiredoxin 3 Homo sapiens 91-95