Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-64 |
Sentence |
denotes |
O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa. |
T1 |
0-64 |
Sentence |
denotes |
O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa. |
T1 |
0-64 |
Sentence |
denotes |
O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa. |
TextSentencer_T2 |
65-282 |
Sentence |
denotes |
We describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. |
T2 |
65-282 |
Sentence |
denotes |
We describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. |
T2 |
65-282 |
Sentence |
denotes |
We describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. |
TextSentencer_T3 |
283-435 |
Sentence |
denotes |
CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. |
T3 |
283-435 |
Sentence |
denotes |
CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. |
T3 |
283-435 |
Sentence |
denotes |
CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. |
TextSentencer_T4 |
436-629 |
Sentence |
denotes |
In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. |
T4 |
436-629 |
Sentence |
denotes |
In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. |
T4 |
436-629 |
Sentence |
denotes |
In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. |
TextSentencer_T5 |
630-883 |
Sentence |
denotes |
Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering. |
T5 |
630-883 |
Sentence |
denotes |
Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering. |
T5 |
630-883 |
Sentence |
denotes |
Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering. |