1 Ocak 2004 Dergi makalesi Açık Erişim

Avilov, SV; Aleksandrova, NA; Demchenko, AP

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{
  "@context": "https://schema.org/", 
  "@id": 93943, 
  "@type": "ScholarlyArticle", 
  "creator": [
    {
      "@type": "Person", 
      "name": "Avilov, SV"
    }, 
    {
      "@type": "Person", 
      "name": "Aleksandrova, NA"
    }, 
    {
      "@type": "Person", 
      "name": "Demchenko, AP"
    }
  ], 
  "datePublished": "2004-01-01", 
  "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.", 
  "headline": "Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study", 
  "identifier": 93943, 
  "image": "https://aperta.ulakbim.gov.tr/static/img/logo/aperta_logo_with_icon.svg", 
  "license": "http://www.opendefinition.org/licenses/cc-by", 
  "name": "Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study", 
  "url": "https://aperta.ulakbim.gov.tr/record/93943"
}