1 Ocak 2004 Dergi makalesi Açık Erişim

Avilov, SV; Aleksandrova, NA; Demchenko, AP

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/93943</identifier>
  <creators>
    <creator>
      <creatorName>Avilov, SV</creatorName>
      <givenName>SV</givenName>
      <familyName>Avilov</familyName>
    </creator>
    <creator>
      <creatorName>Aleksandrova, NA</creatorName>
      <givenName>NA</givenName>
      <familyName>Aleksandrova</familyName>
    </creator>
    <creator>
      <creatorName>Demchenko, AP</creatorName>
      <givenName>AP</givenName>
      <familyName>Demchenko</familyName>
    </creator>
  </creators>
  <titles>
    <title>Quaternary Structure Of Alpha-Crystallin Is Necessary For The Binding Of Unfolded Proteins: A Surface Plasmon Resonance Study</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2004</publicationYear>
  <dates>
    <date dateType="Issued">2004-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/93943</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsVersionOf">10.81043/aperta.93942</relatedIdentifier>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.81043/aperta.93943</relatedIdentifier>
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  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
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  <descriptions>
    <description descriptionType="Abstract">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.</description>
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