EC Number   |
Application |
Reference |
|---|
   3.4.22.B79 | analysis |
assay for quantitative measurement of Nsp2 protease activity based on a substrate fusion protein consisting of eGFP and Gaussia luciferase linked together by a small peptide containing a Nsp2 protease cleavage sequence. The expression of the substrate protein in cells along with recombinant Nsp2 protease results in cleavage of the substrate protein resulting in extracellular release of free Gaussia luciferase |
-, 755648 |
| 3.4.22.B79 | analysis |
nsP2 protease-based cell free high throughput screening assay |
755486 |
| 3.4.22.B79 | drug development |
alphavirus nsp2pro proteases are not very useful tools for the removal of affinity tags from recombinant proteins although they do remain promising therapeutic targets for the treatment of a variety of diseases |
701065 |
| 3.4.22.B79 | medicine |
minimal linear Nsp2 B cell epitopes, 188ELSDDSNRPV197, 42HLKRYSPPAE51, and 54CGWHCISA61, are identified by the monoclonal antibodies 4A12, 4G8, and 8H11, respectively. 42HLKRYSPPAE51 and 188ELSDDSNRPV197 are located separately in hypervariable region 1 and hypervariable region 2 of Nsp2. 54CGWHCISA61 is located in the PL2 region, which is highly conserved in all arteriviruses. 54CGWHCISA61 is located in the inner region of the expected 3D structure of Nsp2 |
752573 |
| 3.4.22.B79 | medicine |
plays an essential role in virus propagation |
679819 |
| 3.4.22.B79 | medicine |
SINV nsP2 is an important factor in viral RNA replication and modification of cell biology |
699903 |
| 3.4.22.B79 | medicine |
the nsp2pro N-terminal domain is a novel cysteine protease fold. the C-terminal domain displays structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases. This structure will significantly aid drug discovery and development efforts to combat Venezuelan equine encephalitis alphavirus and related viruses |
682878 |
| 3.4.22.B79 | medicine |
ubiquitin-like protein ISG15 overexpression inhibits porcine reproductive and respiratory syndrome virus replication in cell culture and the antiviral activity of interferon is reduced by inhibition of ISG15 conjugation. Nonstructural protein nsp2 is a key factor in counteracting the antiviral function of ISG15 |
732411 |
| 3.4.22.B79 | more |
nsP2/GFP is capable of efficient functioning in Sindbis virus replication complexes that can synthesize RNA and, ultimately, produce virus at a level comparable to that of wild-type Sindbis virus. GFP inserted into nsP2 is accessible to specific antibodies and capable of functioning as an efficient tag for the isolation of protein complexes formed during Sindbis virus replication |
681688 |
