| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T111 |
0-154 |
Sentence |
denotes |
Recent studies have also demonstrated the interaction of SARS-CoV-2 proteins with multiple host cell NAS signaling molecules and downstream IFN signaling. |
| T112 |
155-279 |
Sentence |
denotes |
An extensive proteomic study by Gordon et al. (2020), showed multiple SARS-CoV-2 protein and host cell protein interactions. |
| T113 |
280-378 |
Sentence |
denotes |
A proteome map of 26 SARS-CoV-2 proteins predicted 332 viral proteins interacting with host cells. |
| T114 |
379-522 |
Sentence |
denotes |
Among these, Nsp9, Nsp13, Nsp15, ORF3a, ORF9b, and ORF9c interacted with proteins in downstream NAS signaling, IFN response, and NF-κB pathway. |
| T115 |
523-738 |
Sentence |
denotes |
Similarly, Nsp5 interacted with HDAC2, which may be thus involved in limiting the IFN signaling and inflammatory response, but the specific functional role of these proteins was not determined (Gordon et al., 2020). |
| T116 |
739-833 |
Sentence |
denotes |
In two recent studies, the functional relevance of some of these proteins was tested in vitro. |
| T117 |
834-1024 |
Sentence |
denotes |
In the first study, Li J.Y. et al. (2020) tested the effects of ORF6, ORF8 and N protein on the antiviral response in HEK293 cells and found these proteins inhibit IFN-β and NF-κB signaling. |
| T118 |
1025-1192 |
Sentence |
denotes |
Similarly, Yuen et al. (2020) showed that IFN antagonizing effect of ORF6 was due to its association with the interferon-inducible nuclear export complex (NUP98–RAE1). |
| T119 |
1193-1338 |
Sentence |
denotes |
The study further showed that Nsp13, Nsp14, and Nsp15 could also antagonize IFN response, but the mechanism was not explored (Yuen et al., 2020). |
