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      <dc:title>Improved stability of multivalent antibodies containing the human collagen XV trimerization domain</dc:title>
      <dc:creator>Cuesta Martínez, Ángel</dc:creator>
      <dc:creator>Sánchez-Martín, David</dc:creator>
      <dc:creator>Blanco-Toribio, Ana</dc:creator>
      <dc:creator>Villate, Maider</dc:creator>
      <dc:creator>Enciso-Álvarez, Kelly</dc:creator>
      <dc:creator>Álvarez-Cienfuegos, Ana</dc:creator>
      <dc:creator>Sainz-Pastor, Noelia</dc:creator>
      <dc:creator>Sanz, Laura</dc:creator>
      <dc:creator>Blanco, Francisco J.</dc:creator>
      <dc:creator>Álvarez-Vallina, Luis</dc:creator>
      <dc:description>We recently described the in vitro and in vivo properties of an engineered homotrimeric antibody made by fusing the N-terminal trimerization region of collagen XVIII NC1 domain to the C-terminus of a scFv fragment [trimerbody (scFv-NC1) 3; 110 kDa]. Here, we demonstrated the utility of the N-terminal trimerization region of collagen XV NC1 domain in the engineering of trivalent antibodies. We constructed several scFv-based trimerbodies containing the human type XV trimerization domain and demonstrated that all the purified trimerbodies were trimeric in solution and exhibited excellent antigen binding capacity. Importantly, type XV trimerbodies demonstrated substantially greater thermal and serum stability and resistance to protease digestion than type XVIII trimerbodies. In summary, the small size, high expression level, solubility and stability of the trimerization domain of type XV collagen make it the ideal choice for engineering homotrimeric antibodies for cancer detection and therapy.</dc:description>
      <dc:date>2025-01-22T11:16:09Z</dc:date>
      <dc:date>2025-01-22T11:16:09Z</dc:date>
      <dc:date>2012-03</dc:date>
      <dc:type>journal article</dc:type>
      <dc:identifier>Cuesta ÁM, Sánchez-Martín D, Blanco-Toribio A, Villate M, Enciso-Álvarez K, Álvarez-Cienfuegos A, et al. Improved stability of multivalent antibodies containing the human collagen XV trimerization domain. mAbs [Internet]. marzo de 2012 [citado 22 de enero de 2025];4(2):226-32. Disponible en: http://www.tandfonline.com/doi/abs/10.4161/mabs.4.2.19140</dc:identifier>
      <dc:identifier>1942-0862</dc:identifier>
      <dc:identifier>1942-0870</dc:identifier>
      <dc:identifier>10.4161/mabs.4.2.19140</dc:identifier>
      <dc:identifier>https://hdl.handle.net/20.500.14352/115540</dc:identifier>
      <dc:identifier>https://doi.org/10.4161/mabs.4.2.19140</dc:identifier>
      <dc:language>eng</dc:language>
      <dc:relation>IMMUNONET-SOE1/P1/E014</dc:relation>
      <dc:relation>info:eu-repo/grantAgreement/MICINN//BIO2008-03233/ES/DESARROLLO DE UN MODELO HUMANIZADO DE METASTASIS EN RATON PARA SU MONITORIZACION IN VIVO EN TIEMPO REAL/</dc:relation>
      <dc:relation>S-BIO-0236-2006</dc:relation>
      <dc:relation>info:eu-repo/grantAgreement/MICINN//CTQ2011-28680/ES/RECONOCIMIENTO MOLECULAR DE MODIFICACIONES POSTRADUCCIONALES DE HISTONAS POR LAS PROTEINAS SUPRESORAS DE TUMORES ING4 E ING5/</dc:relation>
      <dc:relation>info:eu-repo/grantAgreement/MICINN//PS09%2F00227/ES/PAPEL DE LAS MOLECULAS DE GUIA AXONAL EN ANGIOGENESIS: POTENCIALES DIANAS PARA LA INTERVENCION TERAPEUTICA/</dc:relation>
      <dc:relation>FPI-000531</dc:relation>
      <dc:relation>CA08/00087</dc:relation>
      <dc:rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</dc:rights>
      <dc:rights>open access</dc:rights>
      <dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 International</dc:rights>
      <dc:publisher>Taylor &amp; Francis</dc:publisher>
   </ow:Publication>
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