PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15766710-3 2005 It used 3"-phosphoadenosine 5"-phosphosulfate regenerated from 3-phosphoadenosine 5"-phosphate by a recombinant phenol sulfotransferase (PST) using 4-methylumbelliferyl sulfate as the sulfuryl group donor. Phosphoadenosine Phosphosulfate 8-45 sulfotransferase family 1A member 1 Homo sapiens 112-135 2601684-9 1989 UV irradiation of partially purified human liver TS PST in the presence of [125 I]IAP and 3"-phosphoadenosine-5"-phosphosulfate, the sulfate donor for the reaction, resulted in the radioactive labeling of two proteins, with molecular weights of 32,000 and 34,000, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Phosphoadenosine Phosphosulfate 90-127 sulfotransferase family 1A member 1 Homo sapiens 49-55 3472524-13 1987 Km values of TS PST peak I for p-nitrophenol and for 3"-phosphoadenosine-5"-phosphosulfate were 0.91 and 0.86 microM, respectively, while the Km values of TS PST peak II for these two cosubstrates for the reaction were 0.43 and 0.64 microM, respectively. Phosphoadenosine Phosphosulfate 53-90 sulfotransferase family 1A member 1 Homo sapiens 13-19 3470439-0 1987 Inhibition of M and P phenol sulfotransferase by analogues of 3"-phosphoadenosine-5"-phosphosulfate. Phosphoadenosine Phosphosulfate 62-99 sulfotransferase family 1A member 1 Homo sapiens 22-45 3470439-1 1987 Structural analogues of the sulfate donor 3"-phosphoadenosine-5"-phosphosulfate (3",5"-PAPS) were examined for their ability to inhibit dopamine and phenol sulfation by the M and P forms of phenol sulfotransferase (PST), respectively. Phosphoadenosine Phosphosulfate 42-79 sulfotransferase family 1A member 1 Homo sapiens 190-213 3463246-5 1986 Kinetic analysis demonstrated that sulfation by P1-PST proceeds via a sequential ordered, bi-substrate reaction mechanism, where 3"-phosphoadenosine-5"-phosphosulfate (PAPS) is the leading substrate. Phosphoadenosine Phosphosulfate 129-166 sulfotransferase family 1A member 1 Homo sapiens 51-54 3463246-5 1986 Kinetic analysis demonstrated that sulfation by P1-PST proceeds via a sequential ordered, bi-substrate reaction mechanism, where 3"-phosphoadenosine-5"-phosphosulfate (PAPS) is the leading substrate. Phosphoadenosine Phosphosulfate 168-172 sulfotransferase family 1A member 1 Homo sapiens 51-54 30882918-2 2019 Human sulfotransferase 1A1 (SULT1A1) is involved in the sulfonation of xenobiotics with aid from the cofactor 3"-phosphoadenosine-5"-phosphosulfate that acts as a sulfonate donor. Phosphoadenosine Phosphosulfate 110-147 sulfotransferase family 1A member 1 Homo sapiens 6-26 30882918-2 2019 Human sulfotransferase 1A1 (SULT1A1) is involved in the sulfonation of xenobiotics with aid from the cofactor 3"-phosphoadenosine-5"-phosphosulfate that acts as a sulfonate donor. Phosphoadenosine Phosphosulfate 110-147 sulfotransferase family 1A member 1 Homo sapiens 28-35 22593037-7 2012 The K(d) for E2 binding to SULT1A1 changed from 2.3 +- 0.9 to 1.2 +- 0.56 muM in the presence of PAP. Phosphoadenosine Phosphosulfate 97-100 sulfotransferase family 1A member 1 Homo sapiens 27-34 22593037-8 2012 Docking studies with E2 indicate that E2 binds in a competent orientation in the resolved structure of SULT1A1 in the both presence and absence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS). Phosphoadenosine Phosphosulfate 147-184 sulfotransferase family 1A member 1 Homo sapiens 103-110 22593037-8 2012 Docking studies with E2 indicate that E2 binds in a competent orientation in the resolved structure of SULT1A1 in the both presence and absence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS). Phosphoadenosine Phosphosulfate 186-190 sulfotransferase family 1A member 1 Homo sapiens 103-110 20566371-2 2010 The methodology was based on the coupling of SULT1A1 to regenerate 3"-phosphoadenosine-5"-phosphosulfate (PAPS) using 4-methylumbelliferyl sulfate (MUS) as a sulfuryl group donor. Phosphoadenosine Phosphosulfate 67-104 sulfotransferase family 1A member 1 Homo sapiens 45-52 20566371-2 2010 The methodology was based on the coupling of SULT1A1 to regenerate 3"-phosphoadenosine-5"-phosphosulfate (PAPS) using 4-methylumbelliferyl sulfate (MUS) as a sulfuryl group donor. Phosphoadenosine Phosphosulfate 106-110 sulfotransferase family 1A member 1 Homo sapiens 45-52 22593037-0 2012 Potent inhibition of human sulfotransferase 1A1 by 17alpha-ethinylestradiol: role of 3"-phosphoadenosine 5"-phosphosulfate binding and structural rearrangements in regulating inhibition and activity. Phosphoadenosine Phosphosulfate 85-122 sulfotransferase family 1A member 1 Homo sapiens 27-47 15766710-3 2005 It used 3"-phosphoadenosine 5"-phosphosulfate regenerated from 3-phosphoadenosine 5"-phosphate by a recombinant phenol sulfotransferase (PST) using 4-methylumbelliferyl sulfate as the sulfuryl group donor. Phosphoadenosine Phosphosulfate 8-45 sulfotransferase family 1A member 1 Homo sapiens 137-140 10199779-9 1999 Of the latter, SULT1A1 clearly shows the highest affinity for both iodothyronines and PAPS, but it remains to be established whether it is the prominent isoenzyme for sulfation of thyroid hormone in human liver and kidney. Phosphoadenosine Phosphosulfate 86-90 sulfotransferase family 1A member 1 Homo sapiens 15-22 10853883-2 2000 METHODS: The activities of HL-PST and HL-CST were measured with 4 microM 4-nitrophenol and 60 microM dopamine (the sulfate acceptors) and 0.4 microM 3"-phosphoadenosine-5"-phosphosulfate [35S] (the sulfate donor). Phosphoadenosine Phosphosulfate 149-186 sulfotransferase family 1A member 1 Homo sapiens 30-33 10853883-2 2000 METHODS: The activities of HL-PST and HL-CST were measured with 4 microM 4-nitrophenol and 60 microM dopamine (the sulfate acceptors) and 0.4 microM 3"-phosphoadenosine-5"-phosphosulfate [35S] (the sulfate donor). Phosphoadenosine Phosphosulfate 188-191 sulfotransferase family 1A member 1 Homo sapiens 30-33