1 Ocak 2004 Dergi makalesi Açık Erişim

Avilov, SV; Aleksandrova, NA; Demchenko, AP

Dublin Core

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  <dc:creator>Avilov, SV</dc:creator>
  <dc:creator>Aleksandrova, NA</dc:creator>
  <dc:creator>Demchenko, AP</dc:creator>
  <dc:date>2004-01-01</dc:date>
  <dc:description>The interactions between an oligomeric heat-shock protein, alpha-crystallin, and its individual subunits with unfolded proteins were monitored by surface plasmon resonance. Immobilization at the sensor chip allowed us for the first time to study isolated alpha-crystallin subunits under physiological conditions. We observe that these subunits, in contrast to alpha-crystallin oligomers, do not bind unfolded protein. Our data indicate that quaternary structure of alpha-crystallin is necessary for its chaperone-like activity.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/93943</dc:identifier>
  <dc:identifier>oai:zenodo.org:93943</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>PROTEIN AND PEPTIDE LETTERS 11(1) 41-48</dc:source>
  <dc:title>Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
</oai_dc:dc>