Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-85 |
Sentence |
denotes |
The multiple roles of epidermal growth factor repeat O-glycans in animal development. |
T1 |
0-85 |
Sentence |
denotes |
The multiple roles of epidermal growth factor repeat O-glycans in animal development. |
T1 |
0-85 |
Sentence |
denotes |
The multiple roles of epidermal growth factor repeat O-glycans in animal development. |
TextSentencer_T2 |
86-258 |
Sentence |
denotes |
The epidermal growth factor (EGF)-like repeat is a common, evolutionarily conserved motif found in secreted proteins and the extracellular domain of transmembrane proteins. |
T2 |
86-258 |
Sentence |
denotes |
The epidermal growth factor (EGF)-like repeat is a common, evolutionarily conserved motif found in secreted proteins and the extracellular domain of transmembrane proteins. |
T2 |
86-258 |
Sentence |
denotes |
The epidermal growth factor (EGF)-like repeat is a common, evolutionarily conserved motif found in secreted proteins and the extracellular domain of transmembrane proteins. |
TextSentencer_T3 |
259-401 |
Sentence |
denotes |
EGF repeats harbor six cysteine residues which form three disulfide bonds and help generate the three-dimensional structure of the EGF repeat. |
T3 |
259-401 |
Sentence |
denotes |
EGF repeats harbor six cysteine residues which form three disulfide bonds and help generate the three-dimensional structure of the EGF repeat. |
T3 |
259-401 |
Sentence |
denotes |
EGF repeats harbor six cysteine residues which form three disulfide bonds and help generate the three-dimensional structure of the EGF repeat. |
TextSentencer_T4 |
402-573 |
Sentence |
denotes |
A subset of EGF repeats harbor consensus sequences for the addition of one or more specific O-glycans, which are initiated by O-glucose, O-fucose or O-N-acetylglucosamine. |
T4 |
402-573 |
Sentence |
denotes |
A subset of EGF repeats harbor consensus sequences for the addition of one or more specific O-glycans, which are initiated by O-glucose, O-fucose or O-N-acetylglucosamine. |
T4 |
402-573 |
Sentence |
denotes |
A subset of EGF repeats harbor consensus sequences for the addition of one or more specific O-glycans, which are initiated by O-glucose, O-fucose or O-N-acetylglucosamine. |
TextSentencer_T5 |
574-641 |
Sentence |
denotes |
These glycans are relatively rare compared to mucin-type O-glycans. |
T5 |
574-641 |
Sentence |
denotes |
These glycans are relatively rare compared to mucin-type O-glycans. |
T5 |
574-641 |
Sentence |
denotes |
These glycans are relatively rare compared to mucin-type O-glycans. |
TextSentencer_T6 |
642-864 |
Sentence |
denotes |
However, genetic experiments in model organisms and cell-based assays indicate that at least some of the glycosyltransferases involved in the addition of O-glycans to EGF repeats play important roles in animal development. |
T6 |
642-864 |
Sentence |
denotes |
However, genetic experiments in model organisms and cell-based assays indicate that at least some of the glycosyltransferases involved in the addition of O-glycans to EGF repeats play important roles in animal development. |
T6 |
642-864 |
Sentence |
denotes |
However, genetic experiments in model organisms and cell-based assays indicate that at least some of the glycosyltransferases involved in the addition of O-glycans to EGF repeats play important roles in animal development. |
TextSentencer_T7 |
865-1086 |
Sentence |
denotes |
These studies, combined with state-of-the-art biochemical and structural biology experiments have started to provide an in-depth picture of how these glycans regulate the function of the proteins to which they are linked. |
T7 |
865-1086 |
Sentence |
denotes |
These studies, combined with state-of-the-art biochemical and structural biology experiments have started to provide an in-depth picture of how these glycans regulate the function of the proteins to which they are linked. |
T7 |
865-1086 |
Sentence |
denotes |
These studies, combined with state-of-the-art biochemical and structural biology experiments have started to provide an in-depth picture of how these glycans regulate the function of the proteins to which they are linked. |
TextSentencer_T8 |
1087-1216 |
Sentence |
denotes |
In this review, we will discuss the biological roles assigned to EGF repeat O-glycans and the corresponding glycosyltransferases. |
T8 |
1087-1216 |
Sentence |
denotes |
In this review, we will discuss the biological roles assigned to EGF repeat O-glycans and the corresponding glycosyltransferases. |
T8 |
1087-1216 |
Sentence |
denotes |
In this review, we will discuss the biological roles assigned to EGF repeat O-glycans and the corresponding glycosyltransferases. |
TextSentencer_T9 |
1217-1445 |
Sentence |
denotes |
Since Notch receptors are the best studied proteins with biologically-relevant O-glycans on EGF repeats, a significant part of this review is devoted to the role of these glycans in the regulation of the Notch signaling pathway. |
T9 |
1217-1445 |
Sentence |
denotes |
Since Notch receptors are the best studied proteins with biologically-relevant O-glycans on EGF repeats, a significant part of this review is devoted to the role of these glycans in the regulation of the Notch signaling pathway. |
T9 |
1217-1445 |
Sentence |
denotes |
Since Notch receptors are the best studied proteins with biologically-relevant O-glycans on EGF repeats, a significant part of this review is devoted to the role of these glycans in the regulation of the Notch signaling pathway. |
TextSentencer_T10 |
1446-1564 |
Sentence |
denotes |
We also discuss recently identified proteins other than Notch which depend on EGF repeat glycans to function properly. |
T10 |
1446-1564 |
Sentence |
denotes |
We also discuss recently identified proteins other than Notch which depend on EGF repeat glycans to function properly. |
T10 |
1446-1564 |
Sentence |
denotes |
We also discuss recently identified proteins other than Notch which depend on EGF repeat glycans to function properly. |
TextSentencer_T11 |
1565-1691 |
Sentence |
denotes |
Several glycosyltransferases involved in the addition or elongation of O-glycans on EGF repeats are mutated in human diseases. |
T11 |
1565-1691 |
Sentence |
denotes |
Several glycosyltransferases involved in the addition or elongation of O-glycans on EGF repeats are mutated in human diseases. |
T11 |
1565-1691 |
Sentence |
denotes |
Several glycosyltransferases involved in the addition or elongation of O-glycans on EGF repeats are mutated in human diseases. |
TextSentencer_T12 |
1692-1859 |
Sentence |
denotes |
Therefore, mechanistic understanding of the functional roles of these carbohydrate modifications is of interest from both basic science and translational perspectives. |
T12 |
1692-1859 |
Sentence |
denotes |
Therefore, mechanistic understanding of the functional roles of these carbohydrate modifications is of interest from both basic science and translational perspectives. |
T12 |
1692-1859 |
Sentence |
denotes |
Therefore, mechanistic understanding of the functional roles of these carbohydrate modifications is of interest from both basic science and translational perspectives. |