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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protein Folding in the Endoplasmic Reticulum</title><author><name sortKey="Braakman, Ineke" sort="Braakman, Ineke" uniqKey="Braakman I" first="Ineke" last="Braakman">Ineke Braakman</name><affiliation><nlm:aff id="af1">Cellular Protein Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Hebert, Daniel N" sort="Hebert, Daniel N" uniqKey="Hebert D" first="Daniel N." last="Hebert">Daniel N. Hebert</name><affiliation><nlm:aff id="af2">Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">23637286</idno><idno type="pmc">3632058</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3632058</idno><idno type="RBID">PMC:3632058</idno><idno type="doi">10.1101/cshperspect.a013201</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000C80</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000C80</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Protein Folding in the Endoplasmic Reticulum</title><author><name sortKey="Braakman, Ineke" sort="Braakman, Ineke" uniqKey="Braakman I" first="Ineke" last="Braakman">Ineke Braakman</name><affiliation><nlm:aff id="af1">Cellular Protein Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Hebert, Daniel N" sort="Hebert, Daniel N" uniqKey="Hebert D" first="Daniel N." last="Hebert">Daniel N. Hebert</name><affiliation><nlm:aff id="af2">Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003</nlm:aff></affiliation></author></analytic><series><title level="j">Cold Spring Harbor Perspectives in Biology</title><idno type="eISSN">1943-0264</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, <italic>N</italic>-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline <italic>cis</italic>–<italic>trans</italic> isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.</p></div></front></TEI><pmc article-type="review-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">Cold Spring Harb Perspect Biol</journal-id><journal-id journal-id-type="iso-abbrev">Cold Spring Harb Perspect Biol</journal-id><journal-id journal-id-type="publisher-id">cshperspect</journal-id><journal-id journal-id-type="hwp">cshperspect</journal-id><journal-title-group><journal-title>Cold Spring Harbor Perspectives in Biology</journal-title></journal-title-group><issn pub-type="epub">1943-0264</issn><publisher><publisher-name>Cold Spring Harbor Laboratory Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">23637286</article-id><article-id pub-id-type="pmc">3632058</article-id><article-id pub-id-type="doi">10.1101/cshperspect.a013201</article-id><article-id pub-id-type="publisher-id">a013201</article-id><article-categories><subj-group subj-group-type="hwp-journal-coll"><subject>014</subject></subj-group><subj-group subj-group-type="heading"><subject>Perspectives</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Protein Folding in the Endoplasmic Reticulum</article-title><alt-title alt-title-type="left-running">I. Braakman and D.N. Hebert</alt-title><alt-title alt-title-type="right-running">Protein Folding in the ER</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Braakman</surname><given-names>Ineke</given-names></name><xref ref-type="aff" rid="af1">1</xref></contrib><contrib contrib-type="author"><name><surname>Hebert</surname><given-names>Daniel N.</given-names></name><xref ref-type="aff" rid="af2">2</xref></contrib></contrib-group><aff id="af1"><label>1</label>Cellular Protein Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands</aff><aff id="af2"><label>2</label>Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003</aff><author-notes><corresp><italic>Correspondence:</italic><email>i.braakman@uu.nl</email>; <email>dhebert@biochem.umass.edu</email></corresp></author-notes><pub-date pub-type="ppub"><month>5</month><year>2013</year></pub-date><volume>5</volume><issue>5</issue><elocation-id>a013201</elocation-id><permissions><copyright-statement>Copyright © 2013 Cold Spring Harbor Laboratory Press; all rights reserved</copyright-statement><copyright-year>2013</copyright-year></permissions><self-uri content-type="pdf" xlink:type="simple" xlink:href="cshperspect-ERT-a013201.pdf"></self-uri><abstract><p>In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, <italic>N</italic>-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline <italic>cis</italic>–<italic>trans</italic> isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.</p></abstract><abstract abstract-type="precis"><p>A newly synthesized protein undergoes a series of modifications in the ER. Two major chaperone systems in the ER are the classical chaperones (e.g., Hsp70) and the carbohydrate-binding chaperone system.</p></abstract><counts><page-count count="17"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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