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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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Sonraí Bibleagrafaíochta
Formáid: Artigo
Teanga:Inglês
Foilsithe: The Rockefeller University Press 1995
Ábhair:
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2120331/
https://ncbi.nlm.nih.gov/pubmed/7822419
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