Disulfide Bonds of Thyroid Peroxidase Are Critical Elements for Subcellular Localization, Proteasome-Dependent Degradation, and Enzyme Activity-Reference-Cited by-同舟云学术

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

Published:2024-05-01 Issue:5 Volume:34 Page:659-667
ISSN:1050-7256
Container-title:Thyroid®
language:en
Short-container-title:Thyroid®

Author:

Iwasaki Hajime¹,Suwanai Hirotsugu¹^ORCID,Yakou Fumiyoshi¹,Sakai Hiroyuki¹,Ishii Keitaro¹,Hara Natsuko¹,Buckle Ashley M.²,Kanekura Kohsuke³,Miyagi Tamami³,Narumi Satoshi⁴,Suzuki Ryo¹

Affiliation:

1. Department of Diabetes, Metabolism, and Endocrinology, Tokyo Medical University, Tokyo, Japan.

2. Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.

3. Department of Pharmacology, Tokyo Medical University, Tokyo, Japan.

4. Department of Pediatrics, Keio University School of Medicine, Tokyo, Japan.

Publisher

Mary Ann Liebert Inc

Link

https://www.liebertpub.com/doi/pdf/10.1089/thy.2023.0514

Reference35 articles.

1. Purification and characterization of a large, tryptic fragment of human thyroid peroxidase with high catalytic activity

2. Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs.

3. Novel genetic variants in theTPOgene cause congenital hypothyroidism

4. A common thyroid peroxidase gene mutation (G319R) in Turkish patients with congenital hypothyroidism could be due to a founder effect

5. Mutation screening of theTPOgene in a cohort of 192 Chinese patients with congenital hypothyroidism

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