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Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
Before secretion, newly synthesized thyroglobulin (Tg) folds via a series of intermediates: disulfide-linked aggregates and unfolded monomers-->folded monomers-->dimers. Immediately after synthesis, very little Tg associated with calnexin (a membrane-bound molecular chaperone in the ER), while...
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| フォーマット: | Artigo |
|---|---|
| 言語: | Inglês |
| 出版事項: |
The Rockefeller University Press
1995
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2120331/ https://ncbi.nlm.nih.gov/pubmed/7822419 |
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