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The channel domain of colicin A is inhibited by its immunity protein through direct interaction in the Escherichia coli inner membrane.
A bacterial signal sequence was fused to the colicin A pore-forming domain: the exported pore-forming domain was highly cytotoxic. We thus introduced a cysteine-residue pair in the fusion protein which has been shown to form a disulfide bond in the natural colicin A pore-forming domain between alpha...
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| Veröffentlicht in: | EMBO J |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Nature Publishing Group
1996
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC450165/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8665842/ |
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