<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>Kelley WL</dc:creator>
  <dc:creator>Georgopoulos C</dc:creator>
  <dc:date>1992</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Chaperones are centrally involved in the control of protein structure, function, localization and transport. A flurry of scientific activity continues to examine the molecular nature of chaperone-substrate recognition and the role of auxiliary chaperones (cohort proteins) and small molecules that expedite these processes. Chaperones have been implicated in processes as diverse as protein secretion, nuclear transport, thermotolerance, the steroid receptor signal transduction pathway, T-cell receptor and major histocompatibility complex class I and II multimeric assembly and bacterial virulence.</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/127603</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/0955-0674(92)90130-5</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/1336670</dc:relation>
  <dc:source>Current opinion in cell biology. - 1992</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Amino Acid Isomerases</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Heat-Shock Proteins</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Immunity</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Protein Conformation</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Proteins</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Receptors, Cell Surface</dc:subject>
  <dc:title xmlns:ns8="xml" ns8:lang="en">Chaperones and protein folding.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
