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Article

Catalysis leads to posttranslational inactivation of the type 1 deiodinase and alters its conformation.

The Journal of endocrinology - 1 Jul 2012

Zhu Bo, Shrivastava Ashutosh, Luongo Cristina, Chen Ting, Harney John W, Marsili Alessandro, Tran Thuy-Van, Bhadouria Anulika, Mopala Radhika, Steen Amanda I, Larsen P Reed, Zavacki Ann Marie

Abstract excerpt

Previously, it was shown that the type 1 deiodinase (D1) is subject to substrate-dependent inactivation that is blocked by pretreatment with the inhibitor of D1 catalysis, propylthiouracil (PTU). Using HepG2 cells with endogenous D1 activity, we found that while considerable D1-mediated catalysis...

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Identifiers

PMID: 22544951
DOI: 10.1530/JOE-11-0459
PMCID: PMC3612969

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22544951-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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