<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-14T02:04:18Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/19690" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/19690</identifier><datestamp>2024-11-28T16:48:48Z</datestamp><setSpec>com_20.500.12105_15322</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>com_20.500.12105_2052</setSpec><setSpec>col_20.500.12105_16958</setSpec><setSpec>col_20.500.12105_19617</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Jiménez-Hidalgo, María</subfield>
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      <subfield code="a">Kurz, Cyril Léopold</subfield>
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      <subfield code="a">Pedrajas, José Rafael</subfield>
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      <subfield code="a">Naranjo-Galindo, Francisco José</subfield>
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      <subfield code="a">González-Barrios, María</subfield>
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      <subfield code="a">Cabello, Juan</subfield>
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      <subfield code="a">Saez, Alberto G</subfield>
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      <subfield code="a">Lozano, Encarnacion</subfield>
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      <subfield code="a">Button, Emma L</subfield>
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      <subfield code="a">Veal, Elizabeth A</subfield>
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      <subfield code="a">Fierro-González, Juan Carlos</subfield>
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      <subfield code="a">Swoboda, Peter</subfield>
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      <subfield code="a">Miranda-Vizuete, Antonio</subfield>
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      <subfield code="c">2014-03</subfield>
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      <subfield code="a">Thioredoxins are a class of evolutionarily conserved proteins that have been demonstrated to play a key role in many cellular processes involving redox reactions. We report here the genetic and biochemical characterization of Caenorhabditis elegans TRX-3, the first metazoan thioredoxin with an intestine-specific expression pattern. By using green fluorescent protein reporters we have found that TRX-3 is expressed in both the cytoplasm and the nucleus of intestinal cells, with a prominent localization at the apical membrane. Although intestinal function, reproductive capacity, longevity, and resistance of trx-3 loss-of-function mutants to many stresses are indistinguishable from those of wild-type animals, we have observed a slight reduction in size and a minor reduction in the defecation cycle timing of trx-3 mutants. Interestingly, trx-3 is induced upon infection by Photorhabdus luminescens and Candida albicans, and TRX-3 overexpression provides a modest protection against these pathogens. Together, our data indicate that TRX-3 function in the intestine is dispensable for C. elegans development but may be important to fight specific bacterial and fungal infections.</subfield>
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      <subfield code="a">Free Radic Biol Med. 2014 Mar;68(100):205-19.</subfield>
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      <subfield code="a">10.1016/j.freeradbiomed.2013.11.023</subfield>
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      <subfield code="a">Free radical biology &amp; medicine</subfield>
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      <subfield code="a">24316195</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.12105/19690</subfield>
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      <subfield code="a">Caenorhabditis elegans</subfield>
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      <subfield code="a">Thioredoxin</subfield>
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      <subfield code="a">Intestine</subfield>
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      <subfield code="a">Stress</subfield>
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      <subfield code="a">Pathogen infection</subfield>
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      <subfield code="a">Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin</subfield>
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