| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-139 |
Sentence |
denotes |
The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. |
| T2 |
140-316 |
Sentence |
denotes |
The initiation step of mucin-type O-glycosylation is controlled by a large family of homologous UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). |
| T3 |
317-498 |
Sentence |
denotes |
Differences in kinetic properties, substrate specificities, and expression patterns of these isoenzymes provide for differential regulation of O-glycan attachment sites and density. |
| T4 |
499-706 |
Sentence |
denotes |
Recently, it has emerged that some GalNAc-transferase isoforms in vitro selectively function with partially GalNAc O-glycosylated acceptor peptides rather than with the corresponding unglycosylated peptides. |
| T5 |
707-871 |
Sentence |
denotes |
O-Glycan attachment to selected sites, most notably two sites in the MUC1 tandem repeat, is entirely dependent on the glycosylation-dependent function of GalNAc-T4. |
| T6 |
872-1030 |
Sentence |
denotes |
Here we present data that a putative lectin domain found in the C terminus of GalNAc-T4 functions as a GalNAc lectin and confers its glycopeptide specificity. |
| T7 |
1031-1244 |
Sentence |
denotes |
A single amino acid substitution in the lectin domain of a secreted form of GalNAc-T4 selectively blocked GalNAc-glycopeptide activity, while the general activity to peptides exerted by this enzyme was unaffected. |
| T8 |
1245-1413 |
Sentence |
denotes |
Furthermore, the GalNAc-glycopeptide activity of wild-type secreted GalNAc-T4 was selectively inhibited by free GalNAc, while the activity with peptides was unaffected. |
