| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-141 |
Sentence |
denotes |
Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. |
| T1 |
0-141 |
Sentence |
denotes |
Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. |
| TextSentencer_T2 |
142-306 |
Sentence |
denotes |
We report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. |
| T2 |
142-306 |
Sentence |
denotes |
We report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. |
| TextSentencer_T3 |
307-397 |
Sentence |
denotes |
The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. |
| T3 |
307-397 |
Sentence |
denotes |
The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. |
| TextSentencer_T4 |
398-607 |
Sentence |
denotes |
The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. |
| T4 |
398-607 |
Sentence |
denotes |
The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. |
| TextSentencer_T5 |
608-735 |
Sentence |
denotes |
Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. |
| T5 |
608-735 |
Sentence |
denotes |
Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. |
| TextSentencer_T6 |
736-1054 |
Sentence |
denotes |
The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. |
| T6 |
736-1054 |
Sentence |
denotes |
The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. |
| TextSentencer_T7 |
1055-1163 |
Sentence |
denotes |
Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. |
| T7 |
1055-1163 |
Sentence |
denotes |
Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. |
| TextSentencer_T8 |
1164-1430 |
Sentence |
denotes |
This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation. |
| T8 |
1164-1430 |
Sentence |
denotes |
This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation. |