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The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
ERp57 is an oxidoreductase that, in conjunction with calnexin and calreticulin, assists disulfide bond formation in folding glycoproteins. ERp57 also forms a mixed disulfide with the MHC class I-specific chaperone tapasin, and this dimeric conjugate edits the peptide repertoire bound by MHC class I...
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| 主要な著者: | , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2008
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2483232/ https://ncbi.nlm.nih.gov/pubmed/18650385 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0805044105 |
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