Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-124 |
Sentence |
denotes |
Arginine-rich anti-vascular endothelial growth factor peptides inhibit tumor growth and metastasis by blocking angiogenesis. |
T1 |
0-124 |
Sentence |
denotes |
Arginine-rich anti-vascular endothelial growth factor peptides inhibit tumor growth and metastasis by blocking angiogenesis. |
TextSentencer_T2 |
125-209 |
Sentence |
denotes |
Tumor angiogenesis is a critical step for the growth and metastasis of solid tumors. |
T2 |
125-209 |
Sentence |
denotes |
Tumor angiogenesis is a critical step for the growth and metastasis of solid tumors. |
TextSentencer_T3 |
210-378 |
Sentence |
denotes |
Vascular endothelial growth factor (VEGF) is a specific and potent angiogenic factor and contributes to the development of solid tumors by promoting tumor angiogenesis. |
T3 |
210-378 |
Sentence |
denotes |
Vascular endothelial growth factor (VEGF) is a specific and potent angiogenic factor and contributes to the development of solid tumors by promoting tumor angiogenesis. |
TextSentencer_T4 |
379-482 |
Sentence |
denotes |
Therefore, it is a prime therapeutic target for the development of antagonists for treatment of cancer. |
T4 |
379-482 |
Sentence |
denotes |
Therefore, it is a prime therapeutic target for the development of antagonists for treatment of cancer. |
TextSentencer_T5 |
483-634 |
Sentence |
denotes |
We identified from peptide libraries arginine-rich hexapeptides that inhibit the interaction of VEGF(165) with VEGF receptor (IC(50) = 2-4 micrometer). |
T5 |
483-634 |
Sentence |
denotes |
We identified from peptide libraries arginine-rich hexapeptides that inhibit the interaction of VEGF(165) with VEGF receptor (IC(50) = 2-4 micrometer). |
TextSentencer_T6 |
635-721 |
Sentence |
denotes |
They have no effect on binding of basic fibroblast growth factor to cellular receptor. |
T6 |
635-721 |
Sentence |
denotes |
They have no effect on binding of basic fibroblast growth factor to cellular receptor. |
TextSentencer_T7 |
722-845 |
Sentence |
denotes |
The hexapeptides inhibit the proliferation of human umbilical vein endothelial cells induced by VEGF(165) without toxicity. |
T7 |
722-845 |
Sentence |
denotes |
The hexapeptides inhibit the proliferation of human umbilical vein endothelial cells induced by VEGF(165) without toxicity. |
TextSentencer_T8 |
846-1053 |
Sentence |
denotes |
The peptides bind to VEGF and inhibit binding of both VEGF(165) and VEGF(121), suggesting that the peptides interact with the main body of VEGF but not the heparin-binding domain that is absent in VEGF(121). |
T8 |
846-1053 |
Sentence |
denotes |
The peptides bind to VEGF and inhibit binding of both VEGF(165) and VEGF(121), suggesting that the peptides interact with the main body of VEGF but not the heparin-binding domain that is absent in VEGF(121). |
TextSentencer_T9 |
1054-1190 |
Sentence |
denotes |
The identified peptides block the angiogenesis induced by VEGF(165) in vivo in the chick chorioallantoic membrane and the rabbit cornea. |
T9 |
1054-1190 |
Sentence |
denotes |
The identified peptides block the angiogenesis induced by VEGF(165) in vivo in the chick chorioallantoic membrane and the rabbit cornea. |
TextSentencer_T10 |
1191-1333 |
Sentence |
denotes |
Furthermore, one of the hexapeptides, RRKRRR, blocks the growth and metastasis of VEGF-secreting HM7 human colon carcinoma cells in nude mice. |
T10 |
1191-1333 |
Sentence |
denotes |
Furthermore, one of the hexapeptides, RRKRRR, blocks the growth and metastasis of VEGF-secreting HM7 human colon carcinoma cells in nude mice. |
TextSentencer_T11 |
1334-1597 |
Sentence |
denotes |
Based on our results, the arginine-rich hexapeptides may be effective for the treatment of various human tumors and other angiogenesis-dependent diseases that are related to the action of VEGF and could also serve as leads for development of more effective drugs. |
T11 |
1334-1597 |
Sentence |
denotes |
Based on our results, the arginine-rich hexapeptides may be effective for the treatment of various human tumors and other angiogenesis-dependent diseases that are related to the action of VEGF and could also serve as leads for development of more effective drugs. |