id stringlengths 13 16 | sentence stringlengths 46 809 | label stringclasses 6
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23019138.T26.T13 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the <P>vanilloid receptor type I</P> antagonist <C>capsazepine</C>, nor were... | CPR:6 |
23019138.T13.T27 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist <C>capsazepine</C>, nor were the ef... | 0 |
23019138.T25.T14 | In further studies, the diuretic effects of the <P>CB1</P> agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist capsazepine, nor were the ef... | 0 |
23019138.T26.T14 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the <P>vanilloid receptor type I</P> antagonist capsazepine, nor were the ef... | 0 |
23019138.T14.T27 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist capsazepine, nor were the effects o... | CPR:5 |
23019138.T25.T15 | In further studies, the diuretic effects of the <P>CB1</P> agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist capsazepine, nor were the ef... | 0 |
23019138.T26.T15 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the <P>vanilloid receptor type I</P> antagonist capsazepine, nor were the ef... | 0 |
23019138.T27.T15 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist capsazepine, nor were the effects o... | CPR:6 |
23019138.T25.T16 | In further studies, the diuretic effects of the <P>CB1</P> agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist capsazepine, nor were the ef... | 0 |
23019138.T26.T16 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the <P>vanilloid receptor type I</P> antagonist capsazepine, nor were the ef... | 0 |
23019138.T27.T16 | In further studies, the diuretic effects of the CB1 agonist AM4054 were similar in male and female rats, displayed a relatively rapid onset to action, and were dose-dependently antagonized by 30 minutes pretreatment with rimonabant, but not by the vanilloid receptor type I antagonist capsazepine, nor were the effects o... | CPR:6 |
12065695.T12.T24 | <C>N-[2-(cyclohexyloxyl)-4-nitrophenyl]-methanesulfonamide</C> (NS-398), a selective <P>cyclooxygenase-2</P> inhibitor, also inhibited cell proliferation, whereas it did not cause apoptosis. | CPR:4 |
12065695.T13.T24 | N-[2-(cyclohexyloxyl)-4-nitrophenyl]-methanesulfonamide (<C>NS-398</C>), a selective <P>cyclooxygenase-2</P> inhibitor, also inhibited cell proliferation, whereas it did not cause apoptosis. | CPR:4 |
12065695.T14.T1 | Rheumatoid synovial cells expressed <P>PPARgamma</P> mRNA, and the PPARgamma ligands <C>15-deoxy-Delta(12,14)-prostaglandin J(2)</C> and troglitazone reduced the proliferation and induced apoptosis in synovial cells. | 0 |
12065695.T15.T1 | Rheumatoid synovial cells expressed PPARgamma mRNA, and the <P>PPARgamma</P> ligands <C>15-deoxy-Delta(12,14)-prostaglandin J(2)</C> and troglitazone reduced the proliferation and induced apoptosis in synovial cells. | 0 |
12065695.T14.T2 | Rheumatoid synovial cells expressed <P>PPARgamma</P> mRNA, and the PPARgamma ligands 15-deoxy-Delta(12,14)-prostaglandin J(2) and <C>troglitazone</C> reduced the proliferation and induced apoptosis in synovial cells. | 0 |
12065695.T15.T2 | Rheumatoid synovial cells expressed PPARgamma mRNA, and the <P>PPARgamma</P> ligands 15-deoxy-Delta(12,14)-prostaglandin J(2) and <C>troglitazone</C> reduced the proliferation and induced apoptosis in synovial cells. | 0 |
16840830.T12.T1 | The Turkish patient and her affected relatives all had a heterozygous <P>A to G transition at codon 557</P> (AAG-->GAG) of exon 10 of MEN1 that results in a replacement of <C>lysine</C> by glutamic acid. | 0 |
16840830.T13.T1 | The Turkish patient and her affected relatives all had a heterozygous A to G transition at codon 557 (<P>AAG-->GAG</P>) of exon 10 of MEN1 that results in a replacement of <C>lysine</C> by glutamic acid. | 0 |
16840830.T14.T1 | The Turkish patient and her affected relatives all had a heterozygous A to G transition at codon 557 (AAG-->GAG) of exon 10 of <P>MEN1</P> that results in a replacement of <C>lysine</C> by glutamic acid. | 0 |
16840830.T12.T2 | The Turkish patient and her affected relatives all had a heterozygous <P>A to G transition at codon 557</P> (AAG-->GAG) of exon 10 of MEN1 that results in a replacement of lysine by <C>glutamic acid</C>. | 0 |
16840830.T13.T2 | The Turkish patient and her affected relatives all had a heterozygous A to G transition at codon 557 (<P>AAG-->GAG</P>) of exon 10 of MEN1 that results in a replacement of lysine by <C>glutamic acid</C>. | 0 |
16840830.T14.T2 | The Turkish patient and her affected relatives all had a heterozygous A to G transition at codon 557 (AAG-->GAG) of exon 10 of <P>MEN1</P> that results in a replacement of lysine by <C>glutamic acid</C>. | 0 |
16840830.T5.T3 | The Chinese index patient and one of her siblings had a heterozygous mutation at codon 418 of exon 9 (<P>GAC-->TAT</P>) that results in a substitution of <C>aspartic acid</C> by tyrosine. | 0 |
16840830.T5.T4 | The Chinese index patient and one of her siblings had a heterozygous mutation at codon 418 of exon 9 (<P>GAC-->TAT</P>) that results in a substitution of aspartic acid by <C>tyrosine</C>. | 0 |
15736931.T36.T56 | Mutation of <C>arginine</C> 228 to lysine enhances the <P>glucosyltransferase</P> activity of bovine beta-1,4-galactosyltransferase I. | 0 |
15736931.T36.T57 | Mutation of <C>arginine</C> 228 to lysine enhances the glucosyltransferase activity of <P>bovine beta-1,4-galactosyltransferase I</P>. | 0 |
15736931.T37.T56 | Mutation of arginine 228 to <C>lysine</C> enhances the <P>glucosyltransferase</P> activity of bovine beta-1,4-galactosyltransferase I. | CPR:3 |
15736931.T37.T57 | Mutation of arginine 228 to <C>lysine</C> enhances the glucosyltransferase activity of <P>bovine beta-1,4-galactosyltransferase I</P>. | 0 |
15736931.T38.T3 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of <C>Mn(2+)</C> ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T3.T43 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of <C>Mn(2+)</C> ion (<P>Gal-T</P> activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T3.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of <C>Mn(2+)</C> ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T3 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to GlcNAc in the presence of <C>Mn(2+)</C> ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T6 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<C>Gal</C>-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T6.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<C>Gal</C>-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T6 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<C>Gal</C>-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T13 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers <C>Glc</C> from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T43.T13 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers <C>Glc</C> from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T13.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers <C>Glc</C> from UDP-Glc to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T13 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers <C>Glc</C> from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T15 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from <C>UDP-Glc</C> to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T43.T15 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers Glc from <C>UDP-Glc</C> to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T15.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from <C>UDP-Glc</C> to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | CPR:9 |
15736931.T49.T15 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from <C>UDP-Glc</C> to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T16 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to <C>GlcNAc</C> (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T43.T16 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers Glc from UDP-Glc to <C>GlcNAc</C> (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T16.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to <C>GlcNAc</C> (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T16 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to <C>GlcNAc</C> (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T17 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<C>Glc</C>-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T43.T17 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers Glc from UDP-Glc to GlcNAc (<C>Glc</C>-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T17 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<C>Glc</C>-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T28 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers <C>Gal</C> from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T28.T43 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers <C>Gal</C> from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T28.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers <C>Gal</C> from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T28 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers <C>Gal</C> from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T38.T30 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from <C>UDP-Gal</C> to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | CPR:9 |
15736931.T30.T43 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from <C>UDP-Gal</C> to GlcNAc in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | CPR:9 |
15736931.T30.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from <C>UDP-Gal</C> to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T30 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from <C>UDP-Gal</C> to GlcNAc in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | CPR:9 |
15736931.T38.T34 | <P>Beta-1,4-galactosyltransferase I</P> (beta4Gal-T1) normally transfers Gal from UDP-Gal to <C>GlcNAc</C> in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T34.T43 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to <C>GlcNAc</C> in the presence of Mn(2+) ion (<P>Gal-T</P> activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T34.T45 | Beta-1,4-galactosyltransferase I (beta4Gal-T1) normally transfers Gal from UDP-Gal to <C>GlcNAc</C> in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (<P>Glc-T</P> activity), albeit at only 0.3% efficiency. | 0 |
15736931.T49.T34 | Beta-1,4-galactosyltransferase I (<P>beta4Gal-T1</P>) normally transfers Gal from UDP-Gal to <C>GlcNAc</C> in the presence of Mn(2+) ion (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3% efficiency. | 0 |
15736931.T46.T18 | In addition, <P>alpha-lactalbumin</P> (LA) enhances this <C>Glc</C>-T activity more than 25 times. | 0 |
15736931.T47.T18 | In addition, alpha-lactalbumin (<P>LA</P>) enhances this <C>Glc</C>-T activity more than 25 times. | 0 |
15736931.T19.T50 | Comparison of the crystal structures of <C>UDP-Gal</C>- and UDP-Glc-bound <P>beta4Gal-T1</P> reveals that the O4 hydroxyl group in both Gal and Glc moieties forms a hydrogen bond with the side chain carboxylate group of Glu317. | 0 |
15736931.T20.T50 | Comparison of the crystal structures of UDP-Gal- and <C>UDP-Glc</C>-bound <P>beta4Gal-T1</P> reveals that the O4 hydroxyl group in both Gal and Glc moieties forms a hydrogen bond with the side chain carboxylate group of Glu317. | 0 |
15736931.T50.T21 | Comparison of the crystal structures of UDP-Gal- and UDP-Glc-bound <P>beta4Gal-T1</P> reveals that the <C>O4 hydroxyl</C> group in both Gal and Glc moieties forms a hydrogen bond with the side chain carboxylate group of Glu317. | 0 |
15736931.T50.T22 | Comparison of the crystal structures of UDP-Gal- and UDP-Glc-bound <P>beta4Gal-T1</P> reveals that the O4 hydroxyl group in both <C>Gal</C> and Glc moieties forms a hydrogen bond with the side chain carboxylate group of Glu317. | 0 |
15736931.T50.T23 | Comparison of the crystal structures of UDP-Gal- and UDP-Glc-bound <P>beta4Gal-T1</P> reveals that the O4 hydroxyl group in both Gal and <C>Glc</C> moieties forms a hydrogen bond with the side chain carboxylate group of Glu317. | 0 |
15736931.T50.T24 | Comparison of the crystal structures of UDP-Gal- and UDP-Glc-bound <P>beta4Gal-T1</P> reveals that the O4 hydroxyl group in both Gal and Glc moieties forms a <C>hydrogen</C> bond with the side chain carboxylate group of Glu317. | 0 |
15736931.T50.T25 | Comparison of the crystal structures of UDP-Gal- and UDP-Glc-bound <P>beta4Gal-T1</P> reveals that the O4 hydroxyl group in both Gal and Glc moieties forms a hydrogen bond with the side chain <C>carboxylate</C> group of Glu317. | 0 |
15736931.T26.T51 | The orientation of the <C>O4 hydroxyl of glucose</C> causes a steric hindrance to the side chain carboxylate group of Glu317, accounting for the enzyme's low <P>Glc-T</P> activity. | 0 |
15736931.T27.T51 | The orientation of the O4 hydroxyl of glucose causes a steric hindrance to the side chain <C>carboxylate</C> group of Glu317, accounting for the enzyme's low <P>Glc-T</P> activity. | 0 |
15736931.T31.T52 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to <C>lysine</C> (<P>R228K</P>-Gal-T1) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T31.T53 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to <C>lysine</C> (R228K-<P>Gal-T1</P>) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T31.T54 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to <C>lysine</C> (R228K-Gal-T1) results in a 15-fold higher <P>Glc-T</P> activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T31.T55 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to <C>lysine</C> (R228K-Gal-T1) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the <P>Gal-T</P> activity of the wild type. | 0 |
15736931.T52.T32 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (<P>R228K</P>-<C>Gal</C>-T1) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T32.T54 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (R228K-<C>Gal</C>-T1) results in a 15-fold higher <P>Glc-T</P> activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T32.T55 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (R228K-<C>Gal</C>-T1) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the <P>Gal-T</P> activity of the wild type. | 0 |
15736931.T52.T33 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (<P>R228K</P>-Gal-T1) results in a 15-fold higher <C>Glc</C>-T activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T53.T33 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (R228K-<P>Gal-T1</P>) results in a 15-fold higher <C>Glc</C>-T activity, which is further enhanced by LA to nearly 25% of the Gal-T activity of the wild type. | 0 |
15736931.T33.T55 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (R228K-Gal-T1) results in a 15-fold higher <C>Glc</C>-T activity, which is further enhanced by LA to nearly 25% of the <P>Gal-T</P> activity of the wild type. | 0 |
15736931.T52.T35 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (<P>R228K</P>-Gal-T1) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the <C>Gal</C>-T activity of the wild type. | 0 |
15736931.T53.T35 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (R228K-<P>Gal-T1</P>) results in a 15-fold higher Glc-T activity, which is further enhanced by LA to nearly 25% of the <C>Gal</C>-T activity of the wild type. | 0 |
15736931.T54.T35 | In this study, we show that mutation of Arg228, a residue in the vicinity of Glu317, to lysine (R228K-Gal-T1) results in a 15-fold higher <P>Glc-T</P> activity, which is further enhanced by LA to nearly 25% of the <C>Gal</C>-T activity of the wild type. | 0 |
15736931.T1.T39 | The kinetic parameters indicate that the main effect of the mutation of Arg228 to <C>lysine</C> is on the k(cat) of <P>Glc-T</P>, which increases 3-4-fold, both in the absence and in the presence of LA; simultaneously, the k(cat) for the Gal-T reaction is reduced 30-fold. | 0 |
15736931.T1.T40 | The kinetic parameters indicate that the main effect of the mutation of Arg228 to <C>lysine</C> is on the k(cat) of Glc-T, which increases 3-4-fold, both in the absence and in the presence of LA; simultaneously, the k(cat) for the <P>Gal-T</P> reaction is reduced 30-fold. | 0 |
15736931.T2.T40 | The kinetic parameters indicate that the main effect of the mutation of Arg228 to lysine is on the k(cat) of <C>Glc</C>-T, which increases 3-4-fold, both in the absence and in the presence of LA; simultaneously, the k(cat) for the <P>Gal-T</P> reaction is reduced 30-fold. | 0 |
15736931.T39.T4 | The kinetic parameters indicate that the main effect of the mutation of Arg228 to lysine is on the k(cat) of <P>Glc-T</P>, which increases 3-4-fold, both in the absence and in the presence of LA; simultaneously, the k(cat) for the <C>Gal</C>-T reaction is reduced 30-fold. | 0 |
15736931.T41.T5 | The crystal structure of <P>R228K</P>-<C>Gal</C>-T1 complexed with LA, UDP-Gal, and Mn(2+) determined at 1.9 A resolution shows that the Asp318 side chain exhibits a minor alternate conformation, compared to that in the wild type. | 0 |
15736931.T41.T7 | The crystal structure of <P>R228K</P>-Gal-T1 complexed with LA, <C>UDP-Gal</C>, and Mn(2+) determined at 1.9 A resolution shows that the Asp318 side chain exhibits a minor alternate conformation, compared to that in the wild type. | 0 |
15736931.T42.T7 | The crystal structure of R228K-<P>Gal-T1</P> complexed with LA, <C>UDP-Gal</C>, and Mn(2+) determined at 1.9 A resolution shows that the Asp318 side chain exhibits a minor alternate conformation, compared to that in the wild type. | 0 |
15736931.T41.T8 | The crystal structure of <P>R228K</P>-Gal-T1 complexed with LA, UDP-Gal, and <C>Mn(2+)</C> determined at 1.9 A resolution shows that the Asp318 side chain exhibits a minor alternate conformation, compared to that in the wild type. | 0 |
15736931.T42.T8 | The crystal structure of R228K-<P>Gal-T1</P> complexed with LA, UDP-Gal, and <C>Mn(2+)</C> determined at 1.9 A resolution shows that the Asp318 side chain exhibits a minor alternate conformation, compared to that in the wild type. | 0 |
15736931.T9.T44 | This alternate conformation now causes a steric hindrance to the <C>O4 hydroxyl</C> group of the Gal moiety of UDP-Gal, probably causing the dissociation of UDP-Gal and the reduced k(cat) of the <P>Gal-T</P> reaction. | 0 |
15736931.T10.T44 | This alternate conformation now causes a steric hindrance to the O4 hydroxyl group of the <C>Gal</C> moiety of UDP-Gal, probably causing the dissociation of UDP-Gal and the reduced k(cat) of the <P>Gal-T</P> reaction. | 0 |
15736931.T11.T44 | This alternate conformation now causes a steric hindrance to the O4 hydroxyl group of the Gal moiety of <C>UDP-Gal</C>, probably causing the dissociation of UDP-Gal and the reduced k(cat) of the <P>Gal-T</P> reaction. | 0 |
15736931.T12.T44 | This alternate conformation now causes a steric hindrance to the O4 hydroxyl group of the Gal moiety of UDP-Gal, probably causing the dissociation of <C>UDP-Gal</C> and the reduced k(cat) of the <P>Gal-T</P> reaction. | 0 |
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