Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-117 |
Sentence |
denotes |
Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia. |
T1 |
0-117 |
Sentence |
denotes |
Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia. |
T1 |
0-117 |
Sentence |
denotes |
Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia. |
TextSentencer_T2 |
118-378 |
Sentence |
denotes |
Untreated classic galactosemia (galactose-1-phosphate uridyltransferase [GALT] deficiency) is known as a secondary congenital disorders of glycosylation (CDG) characterized by galactose deficiency of glycoproteins and glycolipids (processing defect or CDG-II). |
T2 |
118-378 |
Sentence |
denotes |
Untreated classic galactosemia (galactose-1-phosphate uridyltransferase [GALT] deficiency) is known as a secondary congenital disorders of glycosylation (CDG) characterized by galactose deficiency of glycoproteins and glycolipids (processing defect or CDG-II). |
T2 |
118-378 |
Sentence |
denotes |
Untreated classic galactosemia (galactose-1-phosphate uridyltransferase [GALT] deficiency) is known as a secondary congenital disorders of glycosylation (CDG) characterized by galactose deficiency of glycoproteins and glycolipids (processing defect or CDG-II). |
TextSentencer_T3 |
379-447 |
Sentence |
denotes |
The mechanism of this undergalactosylation has not been established. |
T3 |
379-447 |
Sentence |
denotes |
The mechanism of this undergalactosylation has not been established. |
T3 |
379-447 |
Sentence |
denotes |
The mechanism of this undergalactosylation has not been established. |
TextSentencer_T4 |
448-677 |
Sentence |
denotes |
Here we show that in untreated galactosemia, there is also a partial deficiency of whole glycans of serum transferrin associated with increased fucosylation and branching as seen in genetic glycosylation assembly defects (CDG-I). |
T4 |
448-677 |
Sentence |
denotes |
Here we show that in untreated galactosemia, there is also a partial deficiency of whole glycans of serum transferrin associated with increased fucosylation and branching as seen in genetic glycosylation assembly defects (CDG-I). |
T4 |
448-677 |
Sentence |
denotes |
Here we show that in untreated galactosemia, there is also a partial deficiency of whole glycans of serum transferrin associated with increased fucosylation and branching as seen in genetic glycosylation assembly defects (CDG-I). |
TextSentencer_T5 |
678-798 |
Sentence |
denotes |
Thus galactosemia seems to be a secondary "dual" CDG causing a processing as well as an assembly N-glycosylation defect. |
T5 |
678-798 |
Sentence |
denotes |
Thus galactosemia seems to be a secondary "dual" CDG causing a processing as well as an assembly N-glycosylation defect. |
T5 |
678-798 |
Sentence |
denotes |
Thus galactosemia seems to be a secondary "dual" CDG causing a processing as well as an assembly N-glycosylation defect. |
TextSentencer_T6 |
799-920 |
Sentence |
denotes |
We also demonstrated that in galactosemia patients, transferrin N-glycan biosynthesis is restored upon dietary treatment. |
T6 |
799-920 |
Sentence |
denotes |
We also demonstrated that in galactosemia patients, transferrin N-glycan biosynthesis is restored upon dietary treatment. |
T6 |
799-920 |
Sentence |
denotes |
We also demonstrated that in galactosemia patients, transferrin N-glycan biosynthesis is restored upon dietary treatment. |