Allergen sequence databases.

A number of specialized databases have been developed to facilitate studies of human allergens. These include molecular databases focused on protein sequences and structures, informational databases focused on clinical, biochemical and epidemiological data related to protein allergens, a database on allergen nomenclature, and other knowledge bases or informational websites that are peripherally-related to research on allergens. Examples of each type of databases are listed and described briefly in this review. Database construction and maintenance and their impact on database quality and usefulness are also discussed.

[1]  A. Silvanovich,et al.  Bioinformatic Methods for Allergenicity Assessment Using a Comprehensive Allergen Database , 2002, International Archives of Allergy and Immunology.

[2]  Marie-Paule Lefranc,et al.  IMGT, the international ImMunoGeneTics database , 2001, Nucleic Acids Res..

[3]  E. Herman,et al.  Mutational analysis of the IgE-binding epitopes of P34/Gly m Bd 30K. , 2000, The Journal of allergy and clinical immunology.

[4]  Adriano Mari,et al.  The allergome web site - a database of allergenic molecules. Aim, structure, and data of a web-based resource , 2004 .

[5]  M. Chapman Allergen nomenclature. , 2020, Clinical allergy and immunology.

[6]  Roeland C. H. J. van Ham,et al.  Allermatch™, a webtool for the prediction of potential allergenicity according to current FAO/WHO Codex alimentarius guidelines , 2004, BMC Bioinformatics.

[7]  R. Helm,et al.  A Soybean G2 Glycinin Allergen , 2000, International Archives of Allergy and Immunology.

[8]  G. Sarath,et al.  Soybean Glycinin G1 Acidic Chain Shares IgE Epitopes with Peanut Allergen Ara h 3 , 2000, International Archives of Allergy and Immunology.

[9]  A. van Amerongen,et al.  The major peanut allergen Ara h 1 and its cleaved-off N-terminal peptide; possible implications for peanut allergen detection. , 2004, Journal of agricultural and food chemistry.

[10]  R. S. Dwivedi,et al.  A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation. , 1992, The Journal of biological chemistry.

[11]  Werner Braun,et al.  SDAP: database and computational tools for allergenic proteins , 2003, Nucleic Acids Res..

[12]  E. Herman,et al.  Cellular and Molecular Characterization of a Major Soybean Allergen , 1998, International Archives of Allergy and Immunology.

[13]  G. Sarath,et al.  Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins. , 2002, Archives of biochemistry and biophysics.

[14]  Karin Hoffmann-Sommergruber,et al.  Cross‐reactive N‐glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients , 2003, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[15]  F. Schoentgen,et al.  Molecular characterization of a cytokinin-inducible periwinkle protein showing sequence homology with pathogenesis-related proteins and the Bet v 1 allergen family , 1998, Plant Molecular Biology.

[16]  V Brusic,et al.  Allergen databases , 2003, Allergy.

[17]  S M Gendel,et al.  Sequence databases for assessing the potential allergenicity of proteins used in transgenic foods. , 1998, Advances in food and nutrition research.

[18]  R. Van Ree,et al.  Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. , 2004, The Journal of allergy and clinical immunology.

[19]  R. Helm,et al.  A Soybean G2 Glycinin Allergen , 2000, International Archives of Allergy and Immunology.

[20]  R. Helm,et al.  Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. , 1997, European journal of biochemistry.