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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-38 Sentence denotes The Golgi CMP-sialic acid transporter:
T1 0-38 Sentence denotes The Golgi CMP-sialic acid transporter:
T1 0-85 Sentence denotes The Golgi CMP-sialic acid transporter: A new CHO mutant provides functional insights.
TextSentencer_T2 39-85 Sentence denotes A new CHO mutant provides functional insights.
T2 39-85 Sentence denotes A new CHO mutant provides functional insights.
TextSentencer_T3 86-187 Sentence denotes A CHO mutant line, MAR-11, was isolated using a cytotoxic lectin, Maackia amurensis agglutinin (MAA).
T2 86-187 Sentence denotes A CHO mutant line, MAR-11, was isolated using a cytotoxic lectin, Maackia amurensis agglutinin (MAA).
T3 86-187 Sentence denotes A CHO mutant line, MAR-11, was isolated using a cytotoxic lectin, Maackia amurensis agglutinin (MAA).
TextSentencer_T4 188-309 Sentence denotes This mutant has decreased levels of cell surface sialic acid relative to both wild-type CHO-K1 and Lec2 mutant CHO cells.
T3 188-309 Sentence denotes This mutant has decreased levels of cell surface sialic acid relative to both wild-type CHO-K1 and Lec2 mutant CHO cells.
T4 188-309 Sentence denotes This mutant has decreased levels of cell surface sialic acid relative to both wild-type CHO-K1 and Lec2 mutant CHO cells.
TextSentencer_T5 310-441 Sentence denotes The CMP-sialic acid transporter (CMP-SAT) gene in the MAR-11 mutant cell has a C-T mutation that results in a premature stop codon.
T4 310-441 Sentence denotes The CMP-sialic acid transporter (CMP-SAT) gene in the MAR-11 mutant cell has a C-T mutation that results in a premature stop codon.
T5 310-441 Sentence denotes The CMP-sialic acid transporter (CMP-SAT) gene in the MAR-11 mutant cell has a C-T mutation that results in a premature stop codon.
TextSentencer_T6 442-605 Sentence denotes As a result, MAR-11 cells express a truncated version of CMP-SAT which contains only 100 amino acids rather than the normal CMP-SAT which contains 336 amino acids.
T5 442-605 Sentence denotes As a result, MAR-11 cells express a truncated version of CMP-SAT which contains only 100 amino acids rather than the normal CMP-SAT which contains 336 amino acids.
T6 442-605 Sentence denotes As a result, MAR-11 cells express a truncated version of CMP-SAT which contains only 100 amino acids rather than the normal CMP-SAT which contains 336 amino acids.
TextSentencer_T7 606-728 Sentence denotes Biochemical analyses indicate that recombinant interferon-gamma (IFN-gamma) produced by the mutant cells lack sialic acid.
T6 606-728 Sentence denotes Biochemical analyses indicate that recombinant interferon-gamma (IFN-gamma) produced by the mutant cells lack sialic acid.
T7 606-728 Sentence denotes Biochemical analyses indicate that recombinant interferon-gamma (IFN-gamma) produced by the mutant cells lack sialic acid.
TextSentencer_T8 729-832 Sentence denotes Using MAR-11 as host cells, an EPO/IEF assay for the structure-function study of CMP-SAT was developed.
T7 729-832 Sentence denotes Using MAR-11 as host cells, an EPO/IEF assay for the structure-function study of CMP-SAT was developed.
T8 729-832 Sentence denotes Using MAR-11 as host cells, an EPO/IEF assay for the structure-function study of CMP-SAT was developed.
TextSentencer_T9 833-938 Sentence denotes This assay seems more sensitive than previous assays that were used to analyze sialylation in Lec2 cells.
T8 833-938 Sentence denotes This assay seems more sensitive than previous assays that were used to analyze sialylation in Lec2 cells.
T9 833-938 Sentence denotes This assay seems more sensitive than previous assays that were used to analyze sialylation in Lec2 cells.
TextSentencer_T10 939-1136 Sentence denotes Cotransfection of constructs that express CMP-SAT into MAR-11 cells completely converted the recombinant EPO to a sialylation pattern that is similar to the EPO produced by the wild-type CHO cells.
T9 939-1136 Sentence denotes Cotransfection of constructs that express CMP-SAT into MAR-11 cells completely converted the recombinant EPO to a sialylation pattern that is similar to the EPO produced by the wild-type CHO cells.
T10 939-1136 Sentence denotes Cotransfection of constructs that express CMP-SAT into MAR-11 cells completely converted the recombinant EPO to a sialylation pattern that is similar to the EPO produced by the wild-type CHO cells.
TextSentencer_T11 1137-1285 Sentence denotes Using this assay, we showed that CMP-SAT lacking C-terminal 18 amino acids from the cytosolic tail was able to allow high levels of EPO sialylation.
T10 1137-1285 Sentence denotes Using this assay, we showed that CMP-SAT lacking C-terminal 18 amino acids from the cytosolic tail was able to allow high levels of EPO sialylation.
T11 1137-1285 Sentence denotes Using this assay, we showed that CMP-SAT lacking C-terminal 18 amino acids from the cytosolic tail was able to allow high levels of EPO sialylation.
TextSentencer_T12 1286-1437 Sentence denotes Substitution of the Gly residues with Ile in three different transmembrane domains of CMP-SAT resulted in dramatic decreases in transporter's activity.
T11 1286-1437 Sentence denotes Substitution of the Gly residues with Ile in three different transmembrane domains of CMP-SAT resulted in dramatic decreases in transporter's activity.
T12 1286-1437 Sentence denotes Substitution of the Gly residues with Ile in three different transmembrane domains of CMP-SAT resulted in dramatic decreases in transporter's activity.
TextSentencer_T13 1438-1649 Sentence denotes The CMP-SAT only lost partial activity if the same Gly residues were substituted with Ala, suggesting that the lack of side chain in Gly residues in the transmembrane domains is essential for transport activity.
T12 1438-1649 Sentence denotes The CMP-SAT only lost partial activity if the same Gly residues were substituted with Ala, suggesting that the lack of side chain in Gly residues in the transmembrane domains is essential for transport activity.
T13 1438-1649 Sentence denotes The CMP-SAT only lost partial activity if the same Gly residues were substituted with Ala, suggesting that the lack of side chain in Gly residues in the transmembrane domains is essential for transport activity.