<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>17(4)</volume><submitter>Sun JS</submitter><pubmed_abstract>Thioredoxin (Trx) is a small redox protein existing ubiquitously in all living organisms and plays an important role in multiple cellular processes, including transcriptional regulation and immune response. To date very few studies have been carried out to examine the function of piscine Trx. In this study, we identified and analyzed the function of a Trx homologue, CsTrx1, from half-smooth tongue sole (Cynoglossus semilaevis). The deduced amino acid sequence of CsTrx1 is composed of 107 residues and shares 54.1-60.8% overall identities with the Trx of other teleosts. CsTrx1 contains the highly conserved CXXC motif, which in mammals is known to be the active site, in the form of CQPC. Expression of CsTrx1 as determined by quantitative real-time reverse transcriptase PCR was highest in live</pubmed_abstract><journal>Cell stress &amp; chaperones</journal><pagination>445-55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3368026</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Cynoglossus semilaevis thioredoxin: a reductase and an antioxidant with immunostimulatory property.</pubmed_title><pmcid>PMC3368026</pmcid><pubmed_authors>Sun L</pubmed_authors><pubmed_authors>Sun JS</pubmed_authors><pubmed_authors>Li YX</pubmed_authors></additional><is_claimable>false</is_claimable><name>Cynoglossus semilaevis thioredoxin: a reductase and an antioxidant with immunostimulatory property.</name><description>Thioredoxin (Trx) is a small redox protein existing ubiquitously in all living organisms and plays an important role in multiple cellular processes, including transcriptional regulation and immune response. To date very few studies have been carried out to examine the function of piscine Trx. In this study, we identified and analyzed the function of a Trx homologue, CsTrx1, from half-smooth tongue sole (Cynoglossus semilaevis). The deduced amino acid sequence of CsTrx1 is composed of 107 residues and shares 54.1-60.8% overall identities with the Trx of other teleosts. CsTrx1 contains the highly conserved CXXC motif, which in mammals is known to be the active site, in the form of CQPC. Expression of CsTrx1 as determined by quantitative real-time reverse transcriptase PCR was highest in live</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Jul</publication><modification>2026-04-30T10:26:51.553Z</modification><creation>2026-04-07T15:58:48.791Z</creation></dates><accession>S-EPMC3368026</accession><cross_references><pubmed>22270611</pubmed><doi>10.1007/s12192-012-0322-x</doi></cross_references></HashMap>