<?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>2026-06-28T10:28:24Z</responseDate><request verb="GetRecord" identifier="oai:docta.ucm.es:20.500.14352/94131" metadataPrefix="marc">https://docta.ucm.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:docta.ucm.es:20.500.14352/94131</identifier><datestamp>2024-04-15T14:36:57Z</datestamp><setSpec>com_20.500.14352_14</setSpec><setSpec>col_20.500.14352_15</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
   <leader>00925njm 22002777a 4500</leader>
   <datafield ind2=" " ind1=" " tag="042">
      <subfield code="a">dc</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Sánchez-Jaut, Sandra </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Pérez-Benavente, Susana </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Abad, Paloma </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Méndez Cuadro, Darío </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Puyet Catalina, Antonio</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Díez Martín, Amalia</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Galicia Poblet, Gonzalo </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Gómez Domínguez, Elena </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Moran Jiménez, María J. </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Bautista Santa Cruz, José Manuel</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Azcárate, Isabel G. </subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="260">
      <subfield code="c">2023-02-02</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="520">
      <subfield code="a">Iron overload caused by hereditary hemochromatosis (HH) increases free reactive oxygen species that, in turn, induce lipid peroxidation. Its 4-hydroxynonenal (HNE) by-product is a wellestablished marker of lipid peroxidation since it reacts with accessible proteins with deleterious consequences. Indeed, elevated levels of HNE are often detected in a wide variety of human diseases related to oxidative stress. Here, we evaluated HNE-modified proteins in the membrane of erythrocytes from HH patients and in organs of Hfe−/− male and female mice, a mouse model of HH. For this purpose, we used one- and two-dimensional gel electrophoresis, immunoblotting and MALDI-TOF/TOF analysis. We identified cytoskeletal membrane proteins and membrane receptors of erythrocytes bound to HNE exclusively in HH patients. Furthermore, kidney and brain of Hfe−/−mice contained more HNE-adducted protein than healthy controls. Our results identified main HNE-modified proteins suggesting that HH favours preferred protein targets for oxidation by HNE.</subfield>
   </datafield>
   <datafield ind1="8" ind2=" " tag="024">
      <subfield code="a">Sánchez-Jaut, S.; Pérez-Benavente, S.; Abad, P.; Méndez-Cuadro, D.; Puyet, A.; Diez, A.; Galicia-Poblet, G.; Gómez-Domínguez, E.; Moran-Jiménez, M.J.; Bautista, J.M.; et al. Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis. Int. J. Mol. Sci. 2023, 24, 2922. https:// doi.org/10.3390/ijms24032922</subfield>
   </datafield>
   <datafield ind1="8" ind2=" " tag="024">
      <subfield code="a">1422-0067</subfield>
   </datafield>
   <datafield ind1="8" ind2=" " tag="024">
      <subfield code="a">10.3390/ijms24032922</subfield>
   </datafield>
   <datafield ind1="8" ind2=" " tag="024">
      <subfield code="a">https://hdl.handle.net/20.500.14352/94131</subfield>
   </datafield>
   <datafield ind1="8" ind2=" " tag="024">
      <subfield code="a">https://www.mdpi.com/1422-0067/24/3/2922</subfield>
   </datafield>
   <datafield ind2="0" ind1="0" tag="245">
      <subfield code="a">Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis</subfield>
   </datafield>
</record></metadata></record></GetRecord></OAI-PMH>