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Disulfide Bonds of Thyroid Peroxidase Are Critical Elements for Subcellular Localization, Proteasome-Dependent Degradation, and Enzyme Activity.

Thyroid : official journal of the American Thyroid Association - 1 May 2024

Iwasaki Hajime, Suwanai Hirotsugu, Yakou Fumiyoshi, Sakai Hiroyuki, Ishii Keitaro, Hara Natsuko, Buckle Ashley M, Kanekura Kohsuke, Miyagi Tamami, Narumi Satoshi, Suzuki Ryo

Abstract excerpt

Background: Congenital hypothyroidism (CH) is caused by mutations in cysteine residues, including Cys655 and Cys825 that form disulfide bonds in thyroid peroxidase (TPO). It is highly likely that these disulfide bonds could play an important role in TPO activity. However, to date, no study has comprehensively analyzed cysteine mutations that form disulfide bonds in TPO. In this study, we induced mutations in...

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PMID: 38482822
DOI: 10.1089/thy.2023.0514

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