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TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain
The lectin chaperone calreticulin (CRT) assists the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum (ER). It interacts with ERp57, a thiol-disulfide oxidoreductase that promotes the formation of disulfide bonds in glycoproteins bound by CRT. Here, we inves...
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| Autors principals: | , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
The National Academy of Sciences
2002
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC122301/ https://ncbi.nlm.nih.gov/pubmed/11842220 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.042699099 |
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