Your browser doesn't support javascript.
loading
Three-dimensional structure of the wheat ß-amylase Tri a 17, a clinically relevant food allergen.
Hofer, Gerhard; Wieser, Sandra; Bogdos, Michael K; Gattinger, Pia; Nakamura, Ryosuke; Ebisawa, Motohiro; Mäkelä, Mika; Papadopoulos, Nikolaos; Valenta, Rudolf; Keller, Walter.
Afiliación
  • Hofer G; Institute of Molecular Biosciences, BioTechMed Graz, University of Graz, Graz, Austria.
  • Wieser S; Division of Immunopathology, Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.
  • Bogdos MK; Institute of Molecular Biosciences, BioTechMed Graz, University of Graz, Graz, Austria.
  • Gattinger P; Division of Immunopathology, Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.
  • Nakamura R; Division of Medicinal Safety Science, National Institute of Health Sciences, Kanagawa, Japan.
  • Ebisawa M; Clinical Research Center for Allergology and Rheumatology, National Hospital Organization, Sagamihara National Hospital, Kanagawa, Japan.
  • Mäkelä M; Department of Allergology, Skin and Allergy Hospital, Helsinki University Central Hospital, Helsinki, Finland.
  • Papadopoulos N; Allergy Department, 2nd Pediatric Clinic, University of Athens, Athens, Greece.
  • Valenta R; Division of Immunopathology, Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.
  • Keller W; NRC Institute of Immunology FMBA of Russia, Moscow, Russia.
Allergy ; 74(5): 1009-1013, 2019 05.
Article en En | MEDLINE | ID: mdl-30515829
Asunto(s)
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Plantas / Conformación Proteica / Triticum / Beta-Amilasa / Alérgenos / Modelos Moleculares Idioma: En Revista: Allergy Año: 2019 Tipo del documento: Article País de afiliación: Austria
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Plantas / Conformación Proteica / Triticum / Beta-Amilasa / Alérgenos / Modelos Moleculares Idioma: En Revista: Allergy Año: 2019 Tipo del documento: Article País de afiliación: Austria