Bet v 1 and other birch allergens are more resistant to proteolysis and more abundant than other birch pollen proteins
Author:
Affiliation:
1. Department of Chemistry Duke University Durham North Carolina USA
2. Genome Integrity and Structural Biology Laboratory National Institute of Environmental Health Sciences Durham North Carolina USA
Funder
National Institute of Environmental Health Sciences
Publisher
Wiley
Subject
Immunology,Immunology and Allergy
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/all.15209
Reference11 articles.
1. Are dust mite allergens more abundant and/or more stable than other Dermatophagoides pteronyssinus proteins?
2. Are allergens more abundant and/or more stable than other proteins in pollens and dust?
3. Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen
4. Energetics-Based Discovery of Protein–Ligand Interactions on a Proteomic Scale
5. Global analysis of protein structural changes in complex proteomes
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