| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-90 |
Sentence |
denotes |
Functional expression of the Fc-fused extracellular domains of group II membrane proteins. |
| TextSentencer_T2 |
91-257 |
Sentence |
denotes |
The complicated delivery mechanism of group II membrane proteins makes it difficult to decide the fusion pattern of their extracellular domains (ECDs) with Fc moiety. |
| TextSentencer_T3 |
258-405 |
Sentence |
denotes |
In this study, we compared the expression of ECDs of three group II membrane proteins including CLEC-2, Dectin-1, and LOX-1 by fusion of Fc moiety. |
| TextSentencer_T4 |
406-648 |
Sentence |
denotes |
We found that the pattern of ECD-Fc fusion order produced the functionally active recombinant proteins while the pattern of Fc-ECD fusion order led to the altered glycosylation which abolished the binding of these proteins with their ligands. |
| TextSentencer_T5 |
649-877 |
Sentence |
denotes |
Meanwhile, our results indicated that the secretion of mouse Fc (mFc)-fused ECD of CLEC-2 was more efficient than that of rabbit Fc (rFc)-fused protein, while rFc moiety was more sensitive for detection compared with mFc moiety. |
| TextSentencer_T6 |
878-990 |
Sentence |
denotes |
Altogether, we provide a favorable fusion pattern of Fc moiety with the ECDs of group II transmembrane proteins. |
| T1 |
0-90 |
Sentence |
denotes |
Functional expression of the Fc-fused extracellular domains of group II membrane proteins. |
| T2 |
91-257 |
Sentence |
denotes |
The complicated delivery mechanism of group II membrane proteins makes it difficult to decide the fusion pattern of their extracellular domains (ECDs) with Fc moiety. |
| T3 |
258-405 |
Sentence |
denotes |
In this study, we compared the expression of ECDs of three group II membrane proteins including CLEC-2, Dectin-1, and LOX-1 by fusion of Fc moiety. |
| T4 |
406-648 |
Sentence |
denotes |
We found that the pattern of ECD-Fc fusion order produced the functionally active recombinant proteins while the pattern of Fc-ECD fusion order led to the altered glycosylation which abolished the binding of these proteins with their ligands. |
| T5 |
649-877 |
Sentence |
denotes |
Meanwhile, our results indicated that the secretion of mouse Fc (mFc)-fused ECD of CLEC-2 was more efficient than that of rabbit Fc (rFc)-fused protein, while rFc moiety was more sensitive for detection compared with mFc moiety. |
| T6 |
878-990 |
Sentence |
denotes |
Altogether, we provide a favorable fusion pattern of Fc moiety with the ECDs of group II transmembrane proteins. |