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Localization of BiP to translating ribosomes increases soluble accumulation of secreted eukaryotic proteins in an E. coli cell-free system
The endoplasmic reticulum (ER) resident Hsp70 chaperone, BiP, docks to the Sec translocon and interacts co-translationally with polypeptides entering the ER to encourage proper folding. In order to recreate this interaction in E. coli cell-free protein synthesis (CFPS) reactions, a fusion protein wa...
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| Huvudupphovsmän: | , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
2011
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3120890/ https://ncbi.nlm.nih.gov/pubmed/21351069 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/bit.23111 |
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