Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-126 |
Sentence |
denotes |
A Cyclin D2-derived peptide acts on specific cell cycle phases by activating ERK1/2 to cause the death of breast cancer cells. |
T2 |
127-209 |
Sentence |
denotes |
Protein degradation by the proteasome generates functional intracellular peptides. |
T3 |
210-350 |
Sentence |
denotes |
Pep5, a peptide derived from Cyclin D2, induces cell death in tumor cell lines and reduces the volume of rat C6 glioblastoma tumors in vivo. |
T4 |
351-501 |
Sentence |
denotes |
Here, we chose the human MDA-MB-231 breast cancer cells to evaluate the mechanism of cell death induced by pep5 in different phases of the cell cycle. |
T5 |
502-669 |
Sentence |
denotes |
Fluorescently labeled pep5, monitored by real time confocal microscopy, entered the MDA-MB-231 cells 3min after application and localized to the nucleus and cytoplasm. |
T6 |
670-825 |
Sentence |
denotes |
Pep5-induced cell death was increased when the MDA-MB-231 cell population was arrested at the G1/S transition or in S phase compared to asynchronous cells. |
T7 |
826-964 |
Sentence |
denotes |
Pep5 induced permanent extracellular signal-regulated kinase (ERK1/2) phosphorylation in MDA-MB-231 cells synchronized in G1/S or S phase. |
T8 |
965-1154 |
Sentence |
denotes |
Affinity chromatography followed by mass spectrometry identified CLIC1 and Plectin as the only two proteins that interacted with pep5 in both asynchronous and synchronized MDA-MB-231 cells. |
T9 |
1155-1357 |
Sentence |
denotes |
These interactions could explain the long-lasting ERK1/2 phosphorylation and the cytoskeleton perturbations in the MDA-MB-231 cells, in which the stress fibers' integrity is affected by pep5 treatments. |
T1 |
0-126 |
Sentence |
denotes |
A Cyclin D2-derived peptide acts on specific cell cycle phases by activating ERK1/2 to cause the death of breast cancer cells. |
T2 |
127-209 |
Sentence |
denotes |
Protein degradation by the proteasome generates functional intracellular peptides. |
T3 |
210-350 |
Sentence |
denotes |
Pep5, a peptide derived from Cyclin D2, induces cell death in tumor cell lines and reduces the volume of rat C6 glioblastoma tumors in vivo. |
T4 |
351-501 |
Sentence |
denotes |
Here, we chose the human MDA-MB-231 breast cancer cells to evaluate the mechanism of cell death induced by pep5 in different phases of the cell cycle. |
T5 |
502-669 |
Sentence |
denotes |
Fluorescently labeled pep5, monitored by real time confocal microscopy, entered the MDA-MB-231 cells 3min after application and localized to the nucleus and cytoplasm. |
T6 |
670-825 |
Sentence |
denotes |
Pep5-induced cell death was increased when the MDA-MB-231 cell population was arrested at the G1/S transition or in S phase compared to asynchronous cells. |
T7 |
826-964 |
Sentence |
denotes |
Pep5 induced permanent extracellular signal-regulated kinase (ERK1/2) phosphorylation in MDA-MB-231 cells synchronized in G1/S or S phase. |
T8 |
965-1154 |
Sentence |
denotes |
Affinity chromatography followed by mass spectrometry identified CLIC1 and Plectin as the only two proteins that interacted with pep5 in both asynchronous and synchronized MDA-MB-231 cells. |
T9 |
1155-1357 |
Sentence |
denotes |
These interactions could explain the long-lasting ERK1/2 phosphorylation and the cytoskeleton perturbations in the MDA-MB-231 cells, in which the stress fibers' integrity is affected by pep5 treatments. |