<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>Abriel H</dc:creator>
  <dc:creator>Staub O</dc:creator>
  <dc:date>2005</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Ubiquitylation (i.e., covalent attachment of ubiquitin moieties to proteins) of ion channels allows regulation of their activity and fate. Nedd4/Nedd4-like ubiquitin-protein ligases bind to, ubiquitylate, and modulate the internalization of several channels bearing PY motifs, whereas endoplasmic reticulum-associated degradation (involving ubiquitylation) plays an important role in the biogenesis of normal and defective channels.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/78329</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1152/physiol.00033.2005</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/16287989</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Physiology (Bethesda, Md.). - 2005</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Amino Acid Motifs</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Endoplasmic Reticulum</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Ion Channels</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Mutation</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Protein Folding</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Ubiquitin</dc:subject>
  <dc:title xmlns:ns9="xml" ns9:lang="en">Ubiquitylation of ion channels.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>