| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-105 |
Sentence |
denotes |
Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation. |
| T1 |
0-105 |
Sentence |
denotes |
Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation. |
| T1 |
0-105 |
Sentence |
denotes |
Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation. |
| TextSentencer_T2 |
106-241 |
Sentence |
denotes |
N-Glycosylation is an important post-translational modification that occurs in many secreted and membrane proteins in eukaryotic cells. |
| T2 |
106-241 |
Sentence |
denotes |
N-Glycosylation is an important post-translational modification that occurs in many secreted and membrane proteins in eukaryotic cells. |
| T2 |
106-241 |
Sentence |
denotes |
N-Glycosylation is an important post-translational modification that occurs in many secreted and membrane proteins in eukaryotic cells. |
| TextSentencer_T3 |
242-385 |
Sentence |
denotes |
Golgi alpha-mannosidase I hydrolases (MANI) are key enzymes that play a role in the early N-glycan modification pathway in the Golgi apparatus. |
| T3 |
242-385 |
Sentence |
denotes |
Golgi alpha-mannosidase I hydrolases (MANI) are key enzymes that play a role in the early N-glycan modification pathway in the Golgi apparatus. |
| T3 |
242-385 |
Sentence |
denotes |
Golgi alpha-mannosidase I hydrolases (MANI) are key enzymes that play a role in the early N-glycan modification pathway in the Golgi apparatus. |
| TextSentencer_T4 |
386-497 |
Sentence |
denotes |
In Arabidopsis thaliana, two putative MANI genes, AtMANIa (At3g21160) and AtMANIb (At1g51590), were identified. |
| T4 |
386-497 |
Sentence |
denotes |
In Arabidopsis thaliana, two putative MANI genes, AtMANIa (At3g21160) and AtMANIb (At1g51590), were identified. |
| T4 |
386-497 |
Sentence |
denotes |
In Arabidopsis thaliana, two putative MANI genes, AtMANIa (At3g21160) and AtMANIb (At1g51590), were identified. |
| TextSentencer_T5 |
498-751 |
Sentence |
denotes |
Biochemical analysis using bacterially produced recombinant AtMANI isoforms revealed that both AtMANI isoforms encode 1-deoxymannojirimycin-sensitive alpha-mannosidase I and act on Man(8)GlcNAc(2) and Man(9)GlcNAc(2) structures to yield Man(5)GlcNAc(2). |
| T5 |
498-751 |
Sentence |
denotes |
Biochemical analysis using bacterially produced recombinant AtMANI isoforms revealed that both AtMANI isoforms encode 1-deoxymannojirimycin-sensitive alpha-mannosidase I and act on Man(8)GlcNAc(2) and Man(9)GlcNAc(2) structures to yield Man(5)GlcNAc(2). |
| T5 |
498-751 |
Sentence |
denotes |
Biochemical analysis using bacterially produced recombinant AtMANI isoforms revealed that both AtMANI isoforms encode 1-deoxymannojirimycin-sensitive alpha-mannosidase I and act on Man(8)GlcNAc(2) and Man(9)GlcNAc(2) structures to yield Man(5)GlcNAc(2). |
| TextSentencer_T6 |
752-915 |
Sentence |
denotes |
Structures of hydrolytic intermediates accumulated in the AtMANI reactions indicate that AtMANIs employ hydrolytic pathways distinct from those of mammalian MANIs. |
| T6 |
752-915 |
Sentence |
denotes |
Structures of hydrolytic intermediates accumulated in the AtMANI reactions indicate that AtMANIs employ hydrolytic pathways distinct from those of mammalian MANIs. |
| T6 |
752-915 |
Sentence |
denotes |
Structures of hydrolytic intermediates accumulated in the AtMANI reactions indicate that AtMANIs employ hydrolytic pathways distinct from those of mammalian MANIs. |
| TextSentencer_T7 |
916-994 |
Sentence |
denotes |
In planta, AtMANI-GFP/DsRed fusion proteins were detected in the Golgi stacks. |
| T7 |
916-994 |
Sentence |
denotes |
In planta, AtMANI-GFP/DsRed fusion proteins were detected in the Golgi stacks. |
| T7 |
916-994 |
Sentence |
denotes |
In planta, AtMANI-GFP/DsRed fusion proteins were detected in the Golgi stacks. |
| TextSentencer_T8 |
995-1113 |
Sentence |
denotes |
Arabidopsis mutant lines manIa-1, manIa-2, manIb-1, and manIb-2 showed N-glycan profiles similar to that of wild type. |
| T8 |
995-1113 |
Sentence |
denotes |
Arabidopsis mutant lines manIa-1, manIa-2, manIb-1, and manIb-2 showed N-glycan profiles similar to that of wild type. |
| T8 |
995-1113 |
Sentence |
denotes |
Arabidopsis mutant lines manIa-1, manIa-2, manIb-1, and manIb-2 showed N-glycan profiles similar to that of wild type. |
| TextSentencer_T9 |
1114-1277 |
Sentence |
denotes |
On the other hand, the manIa manIb double mutant lines produced Man(8)GlcNAc(2) as the predominant N-glycan and lacked plant-specific complex and hybrid N-glycans. |
| T9 |
1114-1277 |
Sentence |
denotes |
On the other hand, the manIa manIb double mutant lines produced Man(8)GlcNAc(2) as the predominant N-glycan and lacked plant-specific complex and hybrid N-glycans. |
| T9 |
1114-1277 |
Sentence |
denotes |
On the other hand, the manIa manIb double mutant lines produced Man(8)GlcNAc(2) as the predominant N-glycan and lacked plant-specific complex and hybrid N-glycans. |
| TextSentencer_T10 |
1278-1469 |
Sentence |
denotes |
These data indicate that either AtMANIa or AtMANIb can function as the Golgi alpha-mannosidase I that produces the Man(5)GlcNAc(2) N-glycan structure necessary for complex N-glycan synthesis. |
| T10 |
1278-1469 |
Sentence |
denotes |
These data indicate that either AtMANIa or AtMANIb can function as the Golgi alpha-mannosidase I that produces the Man(5)GlcNAc(2) N-glycan structure necessary for complex N-glycan synthesis. |
| T10 |
1278-1469 |
Sentence |
denotes |
These data indicate that either AtMANIa or AtMANIb can function as the Golgi alpha-mannosidase I that produces the Man(5)GlcNAc(2) N-glycan structure necessary for complex N-glycan synthesis. |