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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>
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<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>
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<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>
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