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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Getting the better of ER stress</title><author><name sortKey="Mollereau, Bertrand" sort="Mollereau, Bertrand" uniqKey="Mollereau B" first="Bertrand" last="Mollereau">Bertrand Mollereau</name><affiliation><nlm:aff id="Aff1">Laboratory of Molecular Biology of the Cell, UMR5239 CNRS/Ecole Normale Supérieure de Lyon, UMS 3444 Biosciences Lyon Gerland, University of Lyon, Lyon, France</nlm:aff></affiliation></author><author><name sortKey="Manie, Serge" sort="Manie, Serge" uniqKey="Manie S" first="Serge" last="Manié">Serge Manié</name><affiliation><nlm:aff id="Aff2">UMR CNRS 5286, INSERM 1052, University of Lyon, Cancer Research Center of Lyon, 69000 Lyon, France</nlm:aff></affiliation></author><author><name sortKey="Napoletano, Francesco" sort="Napoletano, Francesco" uniqKey="Napoletano F" first="Francesco" last="Napoletano">Francesco Napoletano</name><affiliation><nlm:aff id="Aff1">Laboratory of Molecular Biology of the Cell, UMR5239 CNRS/Ecole Normale Supérieure de Lyon, UMS 3444 Biosciences Lyon Gerland, University of Lyon, Lyon, France</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25354560</idno><idno type="pmc">4390799</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390799</idno><idno type="RBID">PMC:4390799</idno><idno type="doi">10.1007/s12079-014-0251-9</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000205</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000205</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Getting the better of ER stress</title><author><name sortKey="Mollereau, Bertrand" sort="Mollereau, Bertrand" uniqKey="Mollereau B" first="Bertrand" last="Mollereau">Bertrand Mollereau</name><affiliation><nlm:aff id="Aff1">Laboratory of Molecular Biology of the Cell, UMR5239 CNRS/Ecole Normale Supérieure de Lyon, UMS 3444 Biosciences Lyon Gerland, University of Lyon, Lyon, France</nlm:aff></affiliation></author><author><name sortKey="Manie, Serge" sort="Manie, Serge" uniqKey="Manie S" first="Serge" last="Manié">Serge Manié</name><affiliation><nlm:aff id="Aff2">UMR CNRS 5286, INSERM 1052, University of Lyon, Cancer Research Center of Lyon, 69000 Lyon, France</nlm:aff></affiliation></author><author><name sortKey="Napoletano, Francesco" sort="Napoletano, Francesco" uniqKey="Napoletano F" first="Francesco" last="Napoletano">Francesco Napoletano</name><affiliation><nlm:aff id="Aff1">Laboratory of Molecular Biology of the Cell, UMR5239 CNRS/Ecole Normale Supérieure de Lyon, UMS 3444 Biosciences Lyon Gerland, University of Lyon, Lyon, France</nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Cell Communication and Signaling</title><idno type="ISSN">1873-9601</idno><idno type="eISSN">1873-961X</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Research over the past few years has highlighted the ability of the unfolded protein response (UPR) to minimize the deleterious effects of accumulated misfolded proteins under both physiological and pathological conditions. The endoplasmic reticulum (ER) adapts to endogenous and exogenous stressors by expanding its protein-folding capacity and by stimulating protective processes such as autophagy and antioxidant responses. Although it is clear that severe ER stress can elicit cell death, several recent studies have shown that low levels of ER stress may actually be beneficial to cells by eliciting an adaptive UPR that ‘preconditions’ the cell to a subsequent lethal insult; this process is called ER hormesis. The findings have important implications for the treatment of a wide variety of diseases associated with defective proteostasis, including neurodegenerative diseases, diabetes, and cancer. Here, we review the physiological and pathological functions of the ER, with a particular focus on the molecular mechanisms that lead to ER hormesis and cellular protection, and discuss the implications for disease treatment.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Cell Commun Signal</journal-id><journal-id journal-id-type="iso-abbrev">J Cell Commun Signal</journal-id><journal-title-group><journal-title>Journal of Cell Communication and Signaling</journal-title></journal-title-group><issn pub-type="ppub">1873-9601</issn><issn pub-type="epub">1873-961X</issn><publisher><publisher-name>Springer Netherlands</publisher-name><publisher-loc>Dordrecht</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25354560</article-id><article-id pub-id-type="pmc">4390799</article-id><article-id pub-id-type="publisher-id">251</article-id><article-id pub-id-type="doi">10.1007/s12079-014-0251-9</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Getting the better of ER stress</article-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Mollereau</surname><given-names>Bertrand</given-names></name><address><phone>33 4 72 72 81 63</phone><email>bertrand.mollereau@ens-lyon.fr</email></address><xref ref-type="aff" rid="Aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Manié</surname><given-names>Serge</given-names></name><xref ref-type="aff" rid="Aff2"></xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Napoletano</surname><given-names>Francesco</given-names></name><address><phone>33 4 72 72 81 63</phone><email>francesco.napoletano@ens-lyon.fr</email></address><xref ref-type="aff" rid="Aff1"></xref></contrib><aff id="Aff1"><label></label>Laboratory of Molecular Biology of the Cell, UMR5239 CNRS/Ecole Normale Supérieure de Lyon, UMS 3444 Biosciences Lyon Gerland, University of Lyon, Lyon, France</aff><aff id="Aff2"><label></label>UMR CNRS 5286, INSERM 1052, University of Lyon, Cancer Research Center of Lyon, 69000 Lyon, France</aff></contrib-group><pub-date pub-type="epub"><day>30</day><month>10</month><year>2014</year></pub-date><pub-date pub-type="ppub"><month>12</month><year>2014</year></pub-date><volume>8</volume><issue>4</issue><fpage>311</fpage><lpage>321</lpage><history><date date-type="received"><day>19</day><month>9</month><year>2014</year></date><date date-type="accepted"><day>15</day><month>10</month><year>2014</year></date></history><permissions><copyright-statement>© The International CCN Society 2014</copyright-statement></permissions><abstract id="Abs1"><p>Research over the past few years has highlighted the ability of the unfolded protein response (UPR) to minimize the deleterious effects of accumulated misfolded proteins under both physiological and pathological conditions. The endoplasmic reticulum (ER) adapts to endogenous and exogenous stressors by expanding its protein-folding capacity and by stimulating protective processes such as autophagy and antioxidant responses. Although it is clear that severe ER stress can elicit cell death, several recent studies have shown that low levels of ER stress may actually be beneficial to cells by eliciting an adaptive UPR that ‘preconditions’ the cell to a subsequent lethal insult; this process is called ER hormesis. The findings have important implications for the treatment of a wide variety of diseases associated with defective proteostasis, including neurodegenerative diseases, diabetes, and cancer. Here, we review the physiological and pathological functions of the ER, with a particular focus on the molecular mechanisms that lead to ER hormesis and cellular protection, and discuss the implications for disease treatment.</p></abstract><kwd-group xml:lang="en"><title>Keywords</title><kwd>Endoplasmic reticulum</kwd><kwd>Mitochondria</kwd><kwd>Unfolded protein response</kwd><kwd>Neurodegenerative diseases</kwd><kwd>Cancer</kwd><kwd>Diabetes</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© The International CCN Society 2014</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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