Crystal Structure of the Major Celery Allergen Api g 1: Molecular Analysis of Cross-reactivity
- 2 September 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 351 (5), 1101-1109
- https://doi.org/10.1016/j.jmb.2005.06.054
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structureBiochemical Journal, 2003
- Bet v 1, the major birch pollen allergen, initiates sensitization to Api g 1, the major allergen in celery: evidence at the T cell levelEuropean Journal of Immunology, 2003
- Crystal Structures of Two Homologous Pathogenesis-related Proteins from Yellow LupineJournal of Molecular Biology, 2002
- The Major Birch Allergen, Bet v 1, Shows Affinity for a Broad Spectrum of Physiological LigandsJournal of Biological Chemistry, 2002
- 413 Amin oacid positions involved in the formation of IgE-binding epitopes of Api g 1 and Mal d 1 allergensJournal of Allergy and Clinical Immunology, 2000
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- X-ray and NMR structure of Bet v 1, the origin of birch pollen allergyNature Structural & Molecular Biology, 1996
- Type I allergic reactions to plant-derived food: A consequence of primary sensitization to pollen allergens*Journal of Allergy and Clinical Immunology, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Molecular recognitionJournal of Molecular Biology, 1991