<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Noack, Julia</dc:creator>
  <dc:creator>Brambilla Pisoni, Giorgia</dc:creator>
  <dc:creator>Molinari, Maurizio</dc:creator>
  <dc:date>2014-08-21</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and  maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells  proteome. The capacity to produce correctly folded polypeptides and to transport them to their  correct intra- or extracellular destinations relies on proteostasis networks that regulate and  balance the activity of protein folding, quality control, transport and degradation machineries.  Nutrient and environmental changes, pathogen infection aging and, more relevant for the topics  discussed in this review, mutations that impair attainment of the correct 3D structure of nascent  polypeptide chains may compromise the activity of the proteostasis networks with devastating  consequences on cells, organs and organisms’ homeostasis. Here we present a review of  mechanisms regulating folding and quality control of proteins expressed in the ER, and we  describe the protein degradation and the ER stress pathways activated by the expression of  misfolded proteins in the ER lumen. Finally, we highlight select examples of proteopathies (also  known as conformational disorders or protein misfolding diseases) caused by protein misfolding in  the ER and/or affecting cellular proteostasis and therapeutic interventions that might alleviate or  cure the disease symptoms.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/319028</dc:identifier>
  <dc:identifier>https://n2t.net/ark:/12658/srd1319028</dc:identifier>
  <dc:identifier>https://sonar.ch/documents/319028/files/Noack_SMW_2014.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.4414/smw.2014.14001</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/ark/12658/srd1319028</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>CC BY-NC-SA</dc:rights>
  <dc:source>Swiss medical weekly. - 2014, vol. 144, p. w14001</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Endoplasmic reticulum (ER)</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Chemical chaperones</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Pharmacologic chaperones</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Protein folding</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Protein quality control</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Proteopathies</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Conformational diseases</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Proteostasis network</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">ER associated degradation (ERAD)</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Unfolded protein response (UPR)</dc:subject>
  <dc:subject>info:eu-repo/classification/udc/54</dc:subject>
  <dc:title xmlns:ns11="xml" ns11:lang="en">Proteostasis : bad news and good news from the endoplasmic reticulum</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>