English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

From studies with their cDNAs, the types 1 and 3 deiodinases (D1 and D3) have been shown unequivocally to be selenoproteins. Studies with recently cloned cDNAs for the mammalian type 2 deiodinase (D2) indicate that they also code for selenoproteins. However, these D2 cDNAs are not full length and they do not contain an essential selenocysteine insertion sequence (SECIS) in their 3'UTR; a heterologous SECIS had to be ligated to the coding region before expression of the D2 could be achieved. Thus their role as cDNAs for the native D2 is open to question. We now report the cloning of a 5.8 kb cDNA for the mouse D2. This cDNA contains a SECIS in its 3'UTR located more than 4.5 kb from the coding region. When the mRNA transcribed in vitro from this cDNA is injected into X. laevis oocytes, a deiodinase with characteristics of D2 is expressed.

Cloning of a 5.8 kb cDNA for a Mouse Type 2 Deiodinase