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The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes.
Sevcnikar, Benjamin; Schaffner, Irene; Chuang, Christine Y; Gamon, Luke; Paumann-Page, Martina; Hofbauer, Stefan; Davies, Michael J; Furtmüller, Paul G; Obinger, Christian.
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  • Sevcnikar B; Department of Chemistry, Institute of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
  • Schaffner I; Department of Chemistry, Institute of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
  • Chuang CY; Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
  • Gamon L; Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
  • Paumann-Page M; Department of Pathology and Biomedical Science, University of Otago, Christchurch, New Zealand.
  • Hofbauer S; Department of Chemistry, Institute of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
  • Davies MJ; Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
  • Furtmüller PG; Department of Chemistry, Institute of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria. Electronic address: paul.furtmueller@boku.ac.at.
  • Obinger C; Department of Chemistry, Institute of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria. Electronic address: christian.obinger@boku.ac.at.
Arch Biochem Biophys ; 689: 108443, 2020 08 15.
Article en En | MEDLINE | ID: mdl-32485152
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Peroxidasas / Membrana Basal / Laminina Límite: Animals / Humans Idioma: En Revista: Arch Biochem Biophys Año: 2020 Tipo del documento: Article País de afiliación: Austria
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Peroxidasas / Membrana Basal / Laminina Límite: Animals / Humans Idioma: En Revista: Arch Biochem Biophys Año: 2020 Tipo del documento: Article País de afiliación: Austria