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Host protein arginine methyltransferases (PRMTs) methylates SARS-CoV-2 N protein at residues R95 and R177 within RGG/RG motifs.Type I PRMT inhibitor (MS023) or substitution of R95 or R177 with lysine inhibits interaction of N protein with the 5-UTR of SARS-CoV-2 genomic RNA, a property required for viral packaging. | Type I PRMT inhibitors (MS023), cancer drug canditates, have found to reduce SARS-CoV-2 production by inhibiting the methylation of arginine in the N protein of SARS-CoV-2 and hence are promising antivirals. ✍ | 34029587
(J Biol Chem)
| PMID | 34029587 Date of Publishing: 2021 May 23 | | Title | Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication | | Author(s) name | Cai T, Yu Z et al. | | Journal | J Biol Chem | | Impact factor | 3.96 Citation count: 11 | | Date of Entry | 2021 Jul 28 |
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| NLM format |
| Cai T, Yu Z, Wang Z, Liang C, Richard S. Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication. J Biol Chem. 2021 May 23;297(1):100821. PMID:34029587 |
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| | Nsp13-1 stabilizes SARS-CoV-2 replication and transcription (RTC) complex by contacting with nsp13-2, which anchors the 5'-extension of RNA template, and interacting with nsp7-nsp8-nsp12-RNA. Different orientations of nsp13-1 results in different interactions with the two forms of mini RTC. | Mini RTC with an nsp12R365A mutation has greater helicase activity compared to individual apsnsp13. Nsp13-1T216A mutation has a decreased helicase activity. ✍ | 33208736
(Nat Commun)
| PMID | 33208736 Date of Publishing: 2020 Nov 18 | | Title | Architecture of a SARS-CoV-2 mini replication and transcription complex | | Author(s) name | Yan L, Zhang Y et al. | | Journal | Nat Commun | | Impact factor | 11.8 Citation count: 61 |
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| Yan L, Zhang Y, Ge J, Zheng L, Gao Y, Wang T, Jia Z, Wang H, Huang Y, Li M, Wang Q, Rao Z, Lou Z. Architecture of a SARS-CoV-2 mini replication and transcription complex. Nat Commun. 2020 Nov 18;11(1):5874. PMID:33208736 |
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| | The complex cryo-electron microscopy structure of SARS-CoV-2 RdRp with a 50-base template-primer RNA and remdesivir, shows the partial double-stranded RNA template is present in the central channel of RdRp where remdesivir is covalently attached as the first replicated base pair and results in the termination of chain elongation. |
The conserved protein-RNA interactions and the catalytic active site residues, in the diverse RNA viruses, makes it possible to develop broad spectrum antiviral inhibitors. ✍ | 32358203
(Science)
| PMID | 32358203 Date of Publishing: 2020 Jun 26 | | Title | Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir | | Author(s) name | Yin W, Mao C et al. | | Journal | Science | | Impact factor | 20.57 Citation count: 459 |
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| Yin W, Mao C, Luan X, Shen DD, Shen Q, Su H, Wang X, Zhou F, Zhao W, Gao M, Chang S, Xie YC, Tian G, Jiang HW, Tao SC, Shen J, Jiang Y, Jiang H, Xu Y, Zhang S, Zhang Y, Xu HE. Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir. Science. 2020 Jun 26;368(6498):1499-1504. PMID:32358203 |
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