| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-112 |
Sentence |
denotes |
Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity. |
| T1 |
0-112 |
Sentence |
denotes |
Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity. |
| TextSentencer_T2 |
113-252 |
Sentence |
denotes |
Late infantile neuronal ceroid lipofuscinosis (LINCL) is caused by the deficiency of the lysosomal tripeptidyl peptidase-I encoded by CLN2. |
| T2 |
113-252 |
Sentence |
denotes |
Late infantile neuronal ceroid lipofuscinosis (LINCL) is caused by the deficiency of the lysosomal tripeptidyl peptidase-I encoded by CLN2. |
| TextSentencer_T3 |
253-389 |
Sentence |
denotes |
We previously detected in two LINCL patients a homozygous missense mutation, p.Asn286Ser, that affects a potential N-glycosylation site. |
| T3 |
253-389 |
Sentence |
denotes |
We previously detected in two LINCL patients a homozygous missense mutation, p.Asn286Ser, that affects a potential N-glycosylation site. |
| TextSentencer_T4 |
390-616 |
Sentence |
denotes |
We introduced the p.Asn286Ser mutation into the wild-type CLN2 cDNA and performed transient expression analysis to determine the effect on the catalytic activity, intracellular targeting, and glycosylation of the CLN2 protein. |
| T4 |
390-616 |
Sentence |
denotes |
We introduced the p.Asn286Ser mutation into the wild-type CLN2 cDNA and performed transient expression analysis to determine the effect on the catalytic activity, intracellular targeting, and glycosylation of the CLN2 protein. |
| TextSentencer_T5 |
617-723 |
Sentence |
denotes |
Expression of mutant p.Asn286Ser CLN2 in HEK293 cells revealed that the mutant was enzymatically inactive. |
| T5 |
617-723 |
Sentence |
denotes |
Expression of mutant p.Asn286Ser CLN2 in HEK293 cells revealed that the mutant was enzymatically inactive. |
| TextSentencer_T6 |
724-876 |
Sentence |
denotes |
Western blot analysis demonstrated that at steady state the amounts of expressed p.Asn286Ser CLN2 were reduced compared with wild-type expressing cells. |
| T6 |
724-876 |
Sentence |
denotes |
Western blot analysis demonstrated that at steady state the amounts of expressed p.Asn286Ser CLN2 were reduced compared with wild-type expressing cells. |
| TextSentencer_T7 |
877-1024 |
Sentence |
denotes |
The rate of synthesis and the sorting of the newly synthesized p.Asn286Ser CLN2 in the Golgi was not affected compared with wild-type CLN2 protein. |
| T7 |
877-1024 |
Sentence |
denotes |
The rate of synthesis and the sorting of the newly synthesized p.Asn286Ser CLN2 in the Golgi was not affected compared with wild-type CLN2 protein. |
| TextSentencer_T8 |
1025-1271 |
Sentence |
denotes |
The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size. |
| T8 |
1025-1271 |
Sentence |
denotes |
The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size. |
| TextSentencer_T9 |
1272-1386 |
Sentence |
denotes |
The data suggest that mutant p.Asn286Ser CLN2 lacks one oligosaccharide chain resulting in enzymatic inactivation. |
| T9 |
1272-1386 |
Sentence |
denotes |
The data suggest that mutant p.Asn286Ser CLN2 lacks one oligosaccharide chain resulting in enzymatic inactivation. |