<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Guevara-Flores A</submitter><funding>Dirección General de Asuntos del Personal Académico (DGAPA) at Universidad Nacional Autónoma de México (UNAM)</funding><funding>Dirección General de Asuntos del Personal Académico (DGAPA) at Universidad Nacional Autónoma de México (UNAM).</funding><pagination>444</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11047392</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(4)</volume><pubmed_abstract>Peroxiredoxins (Prxs) and glutathione peroxidases (GPxs) are the main enzymes of the thiol-dependent antioxidant systems responsible for reducing the H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub> produced via aerobic metabolism or parasitic organisms by the host organism. These antioxidant systems maintain a proper redox state in cells. The cysticerci of &lt;i>Taenia crassiceps&lt;/i> tolerate millimolar concentrations of this oxidant. To understand the role played by Prxs in this cestode, two genes for Prxs, identified in the genome of &lt;i>Taenia solium&lt;/i> (&lt;i>Ts&lt;/i>Prx1 and &lt;i>Ts&lt;/i>Prx3), were cloned. The sequence of the proteins suggests that both isoforms belong to the class of typical Prxs 2-Cys. In addition, &lt;i>Ts&lt;/i>Prx3 harbors a mitochondrial localization signal peptide and two motifs (-GGLG- and -YP-) a</pubmed_abstract><journal>Antioxidants (Basel, Switzerland)</journal><pubmed_title>A Physiological Approach to Explore How Thioredoxin-Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub> in Cysticerci of &lt;i>Taenia&lt;/i>.</pubmed_title><pmcid>PMC11047392</pmcid><funding_grant_id>IN215223</funding_grant_id><pubmed_authors>Guevara-Flores A</pubmed_authors><pubmed_authors>Nava-Balderas G</pubmed_authors><pubmed_authors>Rendon JL</pubmed_authors><pubmed_authors>Vasquez-Lima C</pubmed_authors><pubmed_authors>de Jesus Martinez-Gonzalez J</pubmed_authors><pubmed_authors>Del Arenal Mena IP</pubmed_authors></additional><is_claimable>false</is_claimable><name>A Physiological Approach to Explore How Thioredoxin-Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub> in Cysticerci of &lt;i>Taenia&lt;/i>.</name><description>Peroxiredoxins (Prxs) and glutathione peroxidases (GPxs) are the main enzymes of the thiol-dependent antioxidant systems responsible for reducing the H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub> produced via aerobic metabolism or parasitic organisms by the host organism. These antioxidant systems maintain a proper redox state in cells. The cysticerci of &lt;i>Taenia crassiceps&lt;/i> tolerate millimolar concentrations of this oxidant. To understand the role played by Prxs in this cestode, two genes for Prxs, identified in the genome of &lt;i>Taenia solium&lt;/i> (&lt;i>Ts&lt;/i>Prx1 and &lt;i>Ts&lt;/i>Prx3), were cloned. The sequence of the proteins suggests that both isoforms belong to the class of typical Prxs 2-Cys. In addition, &lt;i>Ts&lt;/i>Prx3 harbors a mitochondrial localization signal peptide and two motifs (-GGLG- and -YP-) a</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Apr</publication><modification>2026-04-24T03:16:48.56Z</modification><creation>2026-04-24T03:09:46.093Z</creation></dates><accession>S-EPMC11047392</accession><cross_references><pubmed>38671892</pubmed><doi>10.3390/antiox13040444</doi></cross_references></HashMap>