| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-62 |
Sentence |
denotes |
Minimal catalytic domain of N-acetylglucosaminyltransferase V. |
| T1 |
0-62 |
Sentence |
denotes |
Minimal catalytic domain of N-acetylglucosaminyltransferase V. |
| T1 |
0-62 |
Sentence |
denotes |
Minimal catalytic domain of N-acetylglucosaminyltransferase V. |
| TextSentencer_T2 |
63-74 |
Sentence |
denotes |
UDP-GlcNAc: |
| T2 |
63-74 |
Sentence |
denotes |
UDP-GlcNAc: |
| T2 |
63-74 |
Sentence |
denotes |
UDP-GlcNAc: |
| TextSentencer_T3 |
75-282 |
Sentence |
denotes |
Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. |
| T3 |
75-282 |
Sentence |
denotes |
Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. |
| T3 |
75-282 |
Sentence |
denotes |
Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. |
| TextSentencer_T4 |
283-427 |
Sentence |
denotes |
GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. |
| T4 |
283-427 |
Sentence |
denotes |
GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. |
| T4 |
283-427 |
Sentence |
denotes |
GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. |
| TextSentencer_T5 |
428-626 |
Sentence |
denotes |
Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. |
| T5 |
428-626 |
Sentence |
denotes |
Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. |
| T5 |
428-626 |
Sentence |
denotes |
Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. |
| TextSentencer_T6 |
627-732 |
Sentence |
denotes |
In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. |
| T6 |
627-732 |
Sentence |
denotes |
In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. |
| T6 |
627-732 |
Sentence |
denotes |
In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. |
| TextSentencer_T7 |
733-879 |
Sentence |
denotes |
Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. |
| T7 |
733-879 |
Sentence |
denotes |
Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. |
| T7 |
733-879 |
Sentence |
denotes |
Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. |
| TextSentencer_T8 |
880-998 |
Sentence |
denotes |
The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. |
| T8 |
880-998 |
Sentence |
denotes |
The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. |
| T8 |
880-998 |
Sentence |
denotes |
The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. |
| TextSentencer_T9 |
999-1243 |
Sentence |
denotes |
The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. |
| T9 |
999-1243 |
Sentence |
denotes |
The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. |
| T9 |
999-1243 |
Sentence |
denotes |
The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. |
| TextSentencer_T10 |
1244-1342 |
Sentence |
denotes |
Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. |
| T10 |
1244-1342 |
Sentence |
denotes |
Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. |
| T10 |
1244-1342 |
Sentence |
denotes |
Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. |
| TextSentencer_T11 |
1343-1522 |
Sentence |
denotes |
Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. |
| T11 |
1343-1522 |
Sentence |
denotes |
Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. |
| T11 |
1343-1522 |
Sentence |
denotes |
Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. |
| TextSentencer_T12 |
1523-1628 |
Sentence |
denotes |
Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. |
| T12 |
1523-1628 |
Sentence |
denotes |
Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. |
| T12 |
1523-1628 |
Sentence |
denotes |
Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. |
| TextSentencer_T13 |
1629-1790 |
Sentence |
denotes |
Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain. |
| T13 |
1629-1790 |
Sentence |
denotes |
Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain. |
| T13 |
1629-1790 |
Sentence |
denotes |
Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain. |