| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-67 |
Sentence |
denotes |
Factors influencing glycosylation of Trichoderma reesei cellulases. |
| T1 |
0-67 |
Sentence |
denotes |
Factors influencing glycosylation of Trichoderma reesei cellulases. |
| T1 |
0-67 |
Sentence |
denotes |
Factors influencing glycosylation of Trichoderma reesei cellulases. |
| TextSentencer_T2 |
68-142 |
Sentence |
denotes |
II: N-glycosylation of Cel7A core protein isolated from different strains. |
| T2 |
68-142 |
Sentence |
denotes |
II: N-glycosylation of Cel7A core protein isolated from different strains. |
| T2 |
68-142 |
Sentence |
denotes |
II: N-glycosylation of Cel7A core protein isolated from different strains. |
| TextSentencer_T3 |
143-338 |
Sentence |
denotes |
A systematic analysis of the N-glycosylation of the catalytic domain of cellobiohydrolase I (Cel7A or CBH I) isolated from several Trichoderma reesei strains grown in minimal media was performed. |
| T3 |
143-338 |
Sentence |
denotes |
A systematic analysis of the N-glycosylation of the catalytic domain of cellobiohydrolase I (Cel7A or CBH I) isolated from several Trichoderma reesei strains grown in minimal media was performed. |
| T3 |
143-338 |
Sentence |
denotes |
A systematic analysis of the N-glycosylation of the catalytic domain of cellobiohydrolase I (Cel7A or CBH I) isolated from several Trichoderma reesei strains grown in minimal media was performed. |
| TextSentencer_T4 |
339-621 |
Sentence |
denotes |
Using a combination of chromatographic, electrophoretic, and mass spectrometric methods, the presence of glucosylated and phosphorylated oligosaccharides on the three N-glycosylation sites of Cel7A core protein (from T. reesei strains Rut-C30 and RL-P37) confirms previous findings. |
| T4 |
339-621 |
Sentence |
denotes |
Using a combination of chromatographic, electrophoretic, and mass spectrometric methods, the presence of glucosylated and phosphorylated oligosaccharides on the three N-glycosylation sites of Cel7A core protein (from T. reesei strains Rut-C30 and RL-P37) confirms previous findings. |
| T4 |
339-621 |
Sentence |
denotes |
Using a combination of chromatographic, electrophoretic, and mass spectrometric methods, the presence of glucosylated and phosphorylated oligosaccharides on the three N-glycosylation sites of Cel7A core protein (from T. reesei strains Rut-C30 and RL-P37) confirms previous findings. |
| TextSentencer_T5 |
622-707 |
Sentence |
denotes |
With N-glycans isolated from other strains, no end-capping glucose could be detected. |
| T5 |
622-707 |
Sentence |
denotes |
With N-glycans isolated from other strains, no end-capping glucose could be detected. |
| T5 |
622-707 |
Sentence |
denotes |
With N-glycans isolated from other strains, no end-capping glucose could be detected. |
| TextSentencer_T6 |
708-891 |
Sentence |
denotes |
Phosphodiester linkages were however found in proteins from each strain and these probably occur on both the alpha1-3 and the alpha1-6 branch of the high-mannose oligosaccharide tree. |
| T6 |
708-891 |
Sentence |
denotes |
Phosphodiester linkages were however found in proteins from each strain and these probably occur on both the alpha1-3 and the alpha1-6 branch of the high-mannose oligosaccharide tree. |
| T6 |
708-891 |
Sentence |
denotes |
Phosphodiester linkages were however found in proteins from each strain and these probably occur on both the alpha1-3 and the alpha1-6 branch of the high-mannose oligosaccharide tree. |
| TextSentencer_T7 |
892-989 |
Sentence |
denotes |
Evidence is also presented for the occurrence of mannobiosyl units on the phosphodiester linkage. |
| T7 |
892-989 |
Sentence |
denotes |
Evidence is also presented for the occurrence of mannobiosyl units on the phosphodiester linkage. |
| T7 |
892-989 |
Sentence |
denotes |
Evidence is also presented for the occurrence of mannobiosyl units on the phosphodiester linkage. |
| TextSentencer_T8 |
990-1227 |
Sentence |
denotes |
Therefore the predominant N-glycans on Cel7A can be represented as (ManP)(0-1)GlcMan(7-8)GlcNAc2 for the hyperproducing Rut-C30 and RL-P37 mutants and as (Man(1-2)P)(0-1-2)Man(5-6-7)GlcNAc2 for the wild-type strain and the other mutants. |
| T8 |
990-1227 |
Sentence |
denotes |
Therefore the predominant N-glycans on Cel7A can be represented as (ManP)(0-1)GlcMan(7-8)GlcNAc2 for the hyperproducing Rut-C30 and RL-P37 mutants and as (Man(1-2)P)(0-1-2)Man(5-6-7)GlcNAc2 for the wild-type strain and the other mutants. |
| T8 |
990-1227 |
Sentence |
denotes |
Therefore the predominant N-glycans on Cel7A can be represented as (ManP)(0-1)GlcMan(7-8)GlcNAc2 for the hyperproducing Rut-C30 and RL-P37 mutants and as (Man(1-2)P)(0-1-2)Man(5-6-7)GlcNAc2 for the wild-type strain and the other mutants. |
| TextSentencer_T9 |
1228-1394 |
Sentence |
denotes |
As shown by ESI-MS, random substitution of these structures on the N-glycosylation sites explains the heterogeneous glycoform population of the isolated core domains. |
| T9 |
1228-1394 |
Sentence |
denotes |
As shown by ESI-MS, random substitution of these structures on the N-glycosylation sites explains the heterogeneous glycoform population of the isolated core domains. |
| T9 |
1228-1394 |
Sentence |
denotes |
As shown by ESI-MS, random substitution of these structures on the N-glycosylation sites explains the heterogeneous glycoform population of the isolated core domains. |
| TextSentencer_T10 |
1395-1555 |
Sentence |
denotes |
PAG-IEF separates up to five isoforms, resulting from posttranslational modification of Cel7A with mannosyl phosphodiester residues at the three distinct sites. |
| T10 |
1395-1555 |
Sentence |
denotes |
PAG-IEF separates up to five isoforms, resulting from posttranslational modification of Cel7A with mannosyl phosphodiester residues at the three distinct sites. |
| T10 |
1395-1555 |
Sentence |
denotes |
PAG-IEF separates up to five isoforms, resulting from posttranslational modification of Cel7A with mannosyl phosphodiester residues at the three distinct sites. |
| TextSentencer_T11 |
1556-1851 |
Sentence |
denotes |
This study clearly shows that posttranslational phosphorylation of glycoproteins is not atypical for Trichoderma sp. and that, in the case of the Rut-C30 and RL-P37 strains, the presence of an end-capped glucose residue at the alpha1-3 branch apparently hinders a second mannophoshoryl transfer. |
| T11 |
1556-1851 |
Sentence |
denotes |
This study clearly shows that posttranslational phosphorylation of glycoproteins is not atypical for Trichoderma sp. and that, in the case of the Rut-C30 and RL-P37 strains, the presence of an end-capped glucose residue at the alpha1-3 branch apparently hinders a second mannophoshoryl transfer. |
| T11 |
1556-1851 |
Sentence |
denotes |
This study clearly shows that posttranslational phosphorylation of glycoproteins is not atypical for Trichoderma sp. and that, in the case of the Rut-C30 and RL-P37 strains, the presence of an end-capped glucose residue at the alpha1-3 branch apparently hinders a second mannophoshoryl transfer. |