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A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo
Escherichia coli thioredoxin is normally a cytoplasmic protein involved in the reduction of disulfide bonds. However, thioredoxin can be translocated to the periplasm when it is attached to a cotranslational signal sequence. When exported to the periplasm, it can partially replace the activity of Ds...
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| Main Authors: | , , , , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
National Academy of Sciences
2005
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1323206/ https://ncbi.nlm.nih.gov/pubmed/16357193 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0509583102 |
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