Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active-site sequence of thiol-disulfide exchange enzymes.
Previous studies have indicated that the surface (SU) and transmembrane (TM) subunits of the envelope protein (Env) of murine leukemia viruses (MuLVs) are joined by a labile disulfide bond that can be stabilized by treatment of virions with thiol-specific reagents. In the present study this observat...
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| Gepubliceerd in: | J Virol |
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| Hoofdauteurs: | , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
1997
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC192174/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9311907/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.71.10.8073-8077.1997 |
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