| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-169 |
Sentence |
denotes |
Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite surface protein 1 expressed in mammalian cells. |
| T1 |
0-169 |
Sentence |
denotes |
Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite surface protein 1 expressed in mammalian cells. |
| T1 |
0-169 |
Sentence |
denotes |
Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite surface protein 1 expressed in mammalian cells. |
| TextSentencer_T2 |
170-484 |
Sentence |
denotes |
The cDNAs that encode the 70 kDa C-terminal portion of Plasmodium falciparum merozoite surface protein 1 (MSP-1), with or without an N-terminal signal peptide sequence and C-terminal glycosylphosphatidylinositol (GPI) signal sequence of MSP-1, were expressed in mammalian cell lines via recombinant vaccinia virus. |
| T2 |
170-484 |
Sentence |
denotes |
The cDNAs that encode the 70 kDa C-terminal portion of Plasmodium falciparum merozoite surface protein 1 (MSP-1), with or without an N-terminal signal peptide sequence and C-terminal glycosylphosphatidylinositol (GPI) signal sequence of MSP-1, were expressed in mammalian cell lines via recombinant vaccinia virus. |
| T2 |
170-484 |
Sentence |
denotes |
The cDNAs that encode the 70 kDa C-terminal portion of Plasmodium falciparum merozoite surface protein 1 (MSP-1), with or without an N-terminal signal peptide sequence and C-terminal glycosylphosphatidylinositol (GPI) signal sequence of MSP-1, were expressed in mammalian cell lines via recombinant vaccinia virus. |
| TextSentencer_T3 |
485-601 |
Sentence |
denotes |
The polypeptides were studied with respect to the nature of glycosylation, localization, and proteolytic processing. |
| T3 |
485-601 |
Sentence |
denotes |
The polypeptides were studied with respect to the nature of glycosylation, localization, and proteolytic processing. |
| T3 |
485-601 |
Sentence |
denotes |
The polypeptides were studied with respect to the nature of glycosylation, localization, and proteolytic processing. |
| TextSentencer_T4 |
602-884 |
Sentence |
denotes |
The polypeptides derived from the cDNAs that contained the N-terminal signal peptide were modified with N -linked high mannose type structures and low levels of O -linked oligosaccharides, whereas the polypeptides from the cDNAs that lacked the signal peptide were not glycosylated. |
| T4 |
602-884 |
Sentence |
denotes |
The polypeptides derived from the cDNAs that contained the N-terminal signal peptide were modified with N -linked high mannose type structures and low levels of O -linked oligosaccharides, whereas the polypeptides from the cDNAs that lacked the signal peptide were not glycosylated. |
| T4 |
602-884 |
Sentence |
denotes |
The polypeptides derived from the cDNAs that contained the N-terminal signal peptide were modified with N -linked high mannose type structures and low levels of O -linked oligosaccharides, whereas the polypeptides from the cDNAs that lacked the signal peptide were not glycosylated. |
| TextSentencer_T5 |
885-1062 |
Sentence |
denotes |
The GPI anchor moiety is either absent or present at a very low level in the polypeptide expressed from the cDNA that contained both the signal peptide and GPI signal sequences. |
| T5 |
885-1062 |
Sentence |
denotes |
The GPI anchor moiety is either absent or present at a very low level in the polypeptide expressed from the cDNA that contained both the signal peptide and GPI signal sequences. |
| T5 |
885-1062 |
Sentence |
denotes |
The GPI anchor moiety is either absent or present at a very low level in the polypeptide expressed from the cDNA that contained both the signal peptide and GPI signal sequences. |
| TextSentencer_T6 |
1063-1236 |
Sentence |
denotes |
Together, these data establish that whereas the signal peptide of MSP-1 is functional, the GPI anchor signal is either nonfunctional or poorly functional in mammalian cells. |
| T6 |
1063-1236 |
Sentence |
denotes |
Together, these data establish that whereas the signal peptide of MSP-1 is functional, the GPI anchor signal is either nonfunctional or poorly functional in mammalian cells. |
| T6 |
1063-1236 |
Sentence |
denotes |
Together, these data establish that whereas the signal peptide of MSP-1 is functional, the GPI anchor signal is either nonfunctional or poorly functional in mammalian cells. |
| TextSentencer_T7 |
1237-1458 |
Sentence |
denotes |
The polypeptides expressed from the cDNAs that contained the signal peptide were proteolytically cleaved at their C-termini, whereas the polypeptides expressed from the cDNAs that lacked the signal peptide were uncleaved. |
| T7 |
1237-1458 |
Sentence |
denotes |
The polypeptides expressed from the cDNAs that contained the signal peptide were proteolytically cleaved at their C-termini, whereas the polypeptides expressed from the cDNAs that lacked the signal peptide were uncleaved. |
| T7 |
1237-1458 |
Sentence |
denotes |
The polypeptides expressed from the cDNAs that contained the signal peptide were proteolytically cleaved at their C-termini, whereas the polypeptides expressed from the cDNAs that lacked the signal peptide were uncleaved. |
| TextSentencer_T8 |
1459-1756 |
Sentence |
denotes |
While the polypeptide expressed from the cDNA containing both the signal peptide and GPI anchor signal was truncated by approximately 14 kDa at the C-terminus, the polypeptide derived from the cDNA with only the signal peptide was processed to remove approximately 6 kDa, also from the C-terminus. |
| T8 |
1459-1756 |
Sentence |
denotes |
While the polypeptide expressed from the cDNA containing both the signal peptide and GPI anchor signal was truncated by approximately 14 kDa at the C-terminus, the polypeptide derived from the cDNA with only the signal peptide was processed to remove approximately 6 kDa, also from the C-terminus. |
| T8 |
1459-1756 |
Sentence |
denotes |
While the polypeptide expressed from the cDNA containing both the signal peptide and GPI anchor signal was truncated by approximately 14 kDa at the C-terminus, the polypeptide derived from the cDNA with only the signal peptide was processed to remove approximately 6 kDa, also from the C-terminus. |
| TextSentencer_T9 |
1757-2099 |
Sentence |
denotes |
Furthermore, the polypeptides derived from cDNAs that lacked the signal peptide were exclusively localized intra-cellularly, the polypeptides from cDNAs that contained the signal peptide were predominantly intracellular, with low levels on the cell surface; none of the polypeptides was secreted into the culture medium to a detectable level. |
| T9 |
1757-2099 |
Sentence |
denotes |
Furthermore, the polypeptides derived from cDNAs that lacked the signal peptide were exclusively localized intra-cellularly, the polypeptides from cDNAs that contained the signal peptide were predominantly intracellular, with low levels on the cell surface; none of the polypeptides was secreted into the culture medium to a detectable level. |
| T9 |
1757-2099 |
Sentence |
denotes |
Furthermore, the polypeptides derived from cDNAs that lacked the signal peptide were exclusively localized intra-cellularly, the polypeptides from cDNAs that contained the signal peptide were predominantly intracellular, with low levels on the cell surface; none of the polypeptides was secreted into the culture medium to a detectable level. |
| TextSentencer_T10 |
2100-2297 |
Sentence |
denotes |
These results suggest that N -glycosylation alone is not sufficient for the efficient extracellular transport of the recombinant MSP-1 polypeptides through the secretory pathway in mammalian cells. |
| T10 |
2100-2297 |
Sentence |
denotes |
These results suggest that N -glycosylation alone is not sufficient for the efficient extracellular transport of the recombinant MSP-1 polypeptides through the secretory pathway in mammalian cells. |
| T10 |
2100-2297 |
Sentence |
denotes |
These results suggest that N -glycosylation alone is not sufficient for the efficient extracellular transport of the recombinant MSP-1 polypeptides through the secretory pathway in mammalian cells. |