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1 UDP-Gal(f) was detected in wild-type animals while absen
2 UDP-Gal:betaGlcNAc beta1,3-galactosyltransferase (Gal-T-
3 ormation (apo-enzyme), its Mn(2+) and Mn(2+)-UDP-Gal-bound complexes, and of a pentenary complex of b
4 Klebsiella pneumoniae sonicate could add 3H-UDP-Gal to human RBCs in the alpha configuration at 37 d
6 owever, in the absence of a glycan acceptor, UDP-Gal is slowly converted to UDP and two other product
7 a long flexible loop, which upon Mn(2+) and UDP-Gal binding changes from an open to a closed conform
9 calculated kcat/Km values for UDP-GalNAc and UDP-Gal are approximately 2-4 times higher than those fo
12 ulated abnormally high levels of Gal-1-P and UDP-Gal and abnormally low levels of UDP-Glc and UDP-Glc
15 in the form of UDP-GlcNAc, and galactose, as UDP-Gal, are delivered into the Golgi apparatus by SLC35
16 e developed a nonradioactive method to assay UDP-Gal:beta-d-GlcNAcbeta1,4-galactosyltransferase (beta
18 on, (ii) growth on galactose, and (iii) both UDP-Gal and UDP-GalNAc 4-epimerase activities in cell ex
22 -T1), upon the binding of Mn(2+) followed by UDP-Gal, two flexible loops, a long and a short loop, ch
23 ing functional GalE1 but not GalE2 contained UDP-Gal 4-epimerase but not UDP-GalNAc 4-epimerase activ
25 90 is critical in the binding of sugar donor UDP-Gal, whereas 174DYD176 may participate in the bindin
26 A resolution in complex with natural donors UDP-Gal, UDP-Glc and, in an attempt to overcome one of t
27 tures of M344H-Gal-T1 in complex with either UDP-Gal.Mn(2+) or UDP-Gal.Mg(2+), determined at 2.3 A re
30 is remarkably stable, has an apparent Km for UDP-Gal of 630 microm and an apparent Vmax of 206 microm
31 increase in steady-state levels of mRNA for UDP-Gal:beta-D-Gal alpha1,3-galactosyltransferase (alpha
33 nsfers in the presence of manganese Gal from UDP-Gal to an acceptor sugar (xylose) that is attached t
34 on, an activity that could transfer Gal from UDP-Gal to both a Fuc-terminated glycoform of Skp1 and s
35 1 is synthesized by the transfer of Gal from UDP-Gal to GalNAcalpha1-R by core 1 beta3-galactosyltran
36 ltransferase (T-synthase) transfers Gal from UDP-Gal to GalNAcalpha1-Ser/Thr (Tn antigen) to form the
37 I (beta4Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion (Gal-T a
41 se 1 (Gal-T1) transfers galactose (Gal) from UDP-Gal to N-acetylglucosamine (GlcNAc), which constitut
42 lT5 catalyzes the transfer of galactose from UDP-Gal to a broad spectrum of glycan acceptors with an
43 l-T activity that transferred galactose from UDP-Gal to GalNAcalpha1-O-phenyl, and a synthetic glycop
47 alpha3GT catalyzes galactose transfer from UDP-Gal to beta-linked galactosides, such as lactose, an
48 ique uridine-5'-diphospho-alpha-d-galactose (UDP-Gal) derivative, each functionalized with either a f
49 ose (Gal), and uridyl diphosphate galactose (UDP-Gal) confirms type I, II, and III galactosemia disea
50 ansferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protei
51 or the native donor substrate UDP-galactose (UDP-Gal) and several glycan acceptors at different react
52 higher UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal) and UDP-Glucuronic levels, lower ATP, GTP and U
53 phosphate (gal-1-P) is bound, UDP-galactose (UDP-Gal) is released, and the free enzyme is recycled.
54 ion transfers galactose from UDP-galactose (UDP-Gal) to N-acetylglucosamine (GlcNAc) that is either
55 mono-functional, synthesising UDP-galactose (UDP-Gal), or bi-functional, synthesising UDP-Gal and UDP
56 ted by UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal), UDP-N-acetylglucosamine (UDP-GlcNAc), and UDP-
58 crease of specific UDP-derivatives (UDP-Glc, UDP-Gal and UDP-Glucuronic), also potentially explaining
63 e cells showed concentrations of UDP-GlcNAc, UDP-Gal, UDP-Glc, GDP-Fuc, and GDP-Man equal to or highe
64 tant by heterologous expression of the human UDP-Gal transporter, and heterologous expression of LPG5
65 Both of these cell lines are defective in UDP-Gal 4-epimerase and cannot synthesize GM3 unless cul
66 inese hamster ovary ldl-D cells defective in UDP-Gal/UDP-GalNAc 4-epimerase in which N- and O-linked
70 action in CHS, rs686237, strongly influenced UDP-Gal:betaGlcNAc beta-1,4-galactosyltransferase, polyp
71 n from the precursor GalNAc-alpha-Ser/Thr is UDP-Gal:GalNAc-alpha-Ser/Thr beta3-galactosyltransferase
72 ucleotides (CMP-Neu5Ac, CMP-Neu5Gc, CMP-KDN, UDP-Gal, UDP-Glc, UDP-GalNAc, UDP-GlcNAc, GDP-Fuc, GDP-M
73 structure of R228K-Gal-T1 complexed with LA, UDP-Gal, and Mn(2+) determined at 1.9 A resolution shows
74 ransferase C1GalT1 with isotopically labeled UDP-Gal((13)C(6)), to tag and convert Tn to Gal((13)C(6)
75 Chinese hamster ovary (CHO) cells that lack UDP-Gal transporter activity and express GlcNAc-terminat
78 letion mutant showed loss of GDP-Man but not UDP-Gal uptake, which was restored by introduction of th
79 8 cells was active using UDP-GalNAc, but not UDP-Gal, as a donor toward a variety of acceptor substra
82 nding to Gal-T1 is similar to the binding of UDP-Gal to Gal-T1, except for an additional hydrogen bon
84 ssay is based on the enzymatic conversion of UDP-Gal to UDP, using 1-4-beta-galactosyltransferase.
86 DP-Gal, probably causing the dissociation of UDP-Gal and the reduced k(cat) of the Gal-T reaction.
87 4-epimerase catalyzes the interconversion of UDP-Gal and UDP-Glc during normal galactose metabolism.
89 act with the 2-OH of the galactose moiety of UDP-Gal, is a key residue in the stringent donor substra
90 o the O4 hydroxyl group of the Gal moiety of UDP-Gal, probably causing the dissociation of UDP-Gal an
92 (bGalE) catalyzes epimerization reactions of UDP-Gal into UDP-Glc and UDP-GalNAc into UDP-GlcNAc with
94 various cell types, and increased release of UDP-Gal was observed in 1321N1 human astrocytoma cells s
97 -T1 in complex with either UDP-Gal.Mn(2+) or UDP-Gal.Mg(2+), determined at 2.3 A resolution, show tha
98 ctures shows that, upon manganese and UDP or UDP-Gal binding, the enzyme undergoes conformational cha
99 can be glycosylated by UDP-Glc, UDP-Xyl, or UDP-Gal, and isolated a cDNA encoding it, apparently der
100 stal structure reported earlier, the present UDP-Gal bound structure exhibits a large conformational
101 tion to its role in glycosylation reactions, UDP-Gal is an important extracellular signaling molecule
106 found that levels of Gg4 and of mRNA for the UDP-Gal:beta1-3galactosyltransferase-4 (beta3GalT4) gene
107 ns were able to convert UDP-glucose (Glc) to UDP-Gal, but only the BAS5304-encoded protein could conv
108 a loss of epimerase activity with regard to UDP-Gal by almost 5-fold, it resulted in a gain of activ
110 h the binding of UDP-Glc is quite similar to UDP-Gal, there are few significant differences observed
115 Although these galactosyltransferases use UDP-Gal as the galactose donor, a third pathway involves
116 The MIC activity did not correlate with UDP-Gal mutase inhibition, suggesting an alternative pri
117 syltransferase (Gal-T1) co-crystallized with UDP-Gal and MnCl(2) has been solved at 2.8 A resolution.
118 hough either Mn(2+) or Mg(2+), together with UDP-Gal, binds and changes the conformation of the M344H