| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-127 |
Sentence |
denotes |
Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment. |
| T1 |
0-127 |
Sentence |
denotes |
Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment. |
| TextSentencer_T2 |
128-369 |
Sentence |
denotes |
Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides. |
| T2 |
128-369 |
Sentence |
denotes |
Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides. |
| TextSentencer_T3 |
370-670 |
Sentence |
denotes |
Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment. |
| T3 |
370-670 |
Sentence |
denotes |
Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment. |
| TextSentencer_T4 |
671-995 |
Sentence |
denotes |
By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer. |
| T4 |
671-995 |
Sentence |
denotes |
By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer. |
| TextSentencer_T5 |
996-1206 |
Sentence |
denotes |
In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides. |
| T5 |
996-1206 |
Sentence |
denotes |
In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides. |
| TextSentencer_T6 |
1207-1420 |
Sentence |
denotes |
Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway. |
| T6 |
1207-1420 |
Sentence |
denotes |
Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway. |
| TextSentencer_T7 |
1421-1655 |
Sentence |
denotes |
Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides. |
| T7 |
1421-1655 |
Sentence |
denotes |
Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides. |
