Transient Covalent Interactions of Newly Synthesized Thyroglobulin with Oxidoreductases of the Endoplasmic Reticulum

Newly synthesized thyroglobulin (Tg), the thyroid prohormone, forms detectable high molecular weight mixed disulfide adducts: until now, only Tg “adduct B” was identified as primarily engaging the endoplasmic reticulum oxidoreductases ERp57 and protein disulfide isomerase. Here, we demonstrate that...

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Bibliografiset tiedot
Päätekijät: Di Jeso, Bruno, Morishita, Yoshiaki, Treglia, Antonella S., Lofrumento, Dario D., Nicolardi, Giuseppe, Beguinot, Francesco, Kellogg, Aaron P., Arvan, Peter
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Biochemistry and Molecular Biology 2014
Aiheet:
Protein Structure and Folding
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC4036284/
https://ncbi.nlm.nih.gov/pubmed/24599957
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.520767
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