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Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase
Methylation of flavivirus RNA is vital for its stability and translation in the infected host cell. This methylation is mediated by the flavivirus methyltransferase (MTase), which methylates the N7 and 2′-O positions of the viral RNA cap by using S-adenosyl-l-methionine (SAM) as a methyl donor. In t...
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| Gepubliceerd in: | Protein Sci |
|---|---|
| Hoofdauteurs: | , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Blackwell Publishing Ltd
2015
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4282417/ https://ncbi.nlm.nih.gov/pubmed/25352331 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2594 |
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