Catalysis leads to post-translational inactivation of the Type 1 deiodinase and alters its conformation

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 of r...

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Bibliografische gegevens
Hoofdauteurs: 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
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2012
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3612969/
https://ncbi.nlm.nih.gov/pubmed/22544951
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1530/JOE-11-0459
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