| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-188 |
Sentence |
denotes |
Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans. |
| T2 |
189-470 |
Sentence |
denotes |
The core 3 structure of the O-glycan, GlcNAcbeta1-3GalNAcalpha1-serine/threonine, an important precursor in the biosynthesis of mucin-type glycoproteins, is synthesized by UDP-N-acetylglucosamine:GalNAc-peptide beta1,3-N- acetylglucosaminyltransferase (beta3Gn-T; core 3 synthase). |
| T3 |
471-604 |
Sentence |
denotes |
The core 3 structure is restricted in its occurrence to mucins from specific tissues such as the stomach, small intestine, and colon. |
| T4 |
605-713 |
Sentence |
denotes |
A partial sequence encoding a novel member of the human beta3Gn-T family was found in one of the data bases. |
| T5 |
714-781 |
Sentence |
denotes |
We cloned a complementary DNA of this gene and named it beta3Gn-T6. |
| T6 |
782-922 |
Sentence |
denotes |
The putative amino acid sequence of beta3Gn-T6 retains the beta3Gn-T motifs and is predicted to comprise a typical type II membrane protein. |
| T7 |
923-1073 |
Sentence |
denotes |
The soluble form of beta3Gn-T6 expressed in insect cells showed beta3Gn-T activity toward GalNAcalpha-p-nitrophenyl and GalNAcalpha1-serine/threonine. |
| T8 |
1074-1355 |
Sentence |
denotes |
The beta1,3-linkage between GlcNAc and GalNAc of the enzyme reaction product was confirmed by high performance liquid chromatography and NMR analyses. beta3Gn-T6 effectively transferred a GlcNAc to the GalNAc residue on MUC1 mucin, resulting in the synthesis of a core 3 structure. |
| T9 |
1356-1505 |
Sentence |
denotes |
Real time PCR analysis revealed that the beta3Gn-T6 transcript was restricted in its distribution, mainly to the stomach, colon, and small intestine. |
| T10 |
1506-1681 |
Sentence |
denotes |
We concluded that beta3Gn-T6 is the most logical candidate for the core 3 synthase, which plays an important role in the synthesis of mucin-type O-glycans in digestive organs. |