Access the full text.
Sign up today, get DeepDyve free for 14 days.
G. Paesen, P. Adams, K. Harlos, P. Nuttall, D. Stuart (1999)
Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure.Molecular cell, 3 5
Boaz Shaanan, H. Lis, Nathan Sharon (1991)
Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose.Science, 254 5033
Proceedings ICACI 2000 , Sydney . Allergen : the trigger
H. Koistinen, R. Koistinen, M. Seppälä, T. Burova, Y. Choiset, T. Haertlé (1999)
Glycodelin and β‐lactoglobulin, lipocalins with a high structural similarity, differ in ligand binding propertiesFEBS Letters, 450
S. Do, K. Lee, H. Kim (2000)
Novel induction of alpha-lactalbumin-mediated lacdiNAc-R expression in vivo.The Biochemical journal, 348 Pt 1
M. Kämäräinen, M. Halttunen, R. Koistinen, K. Boguslawsky, K. Smitten, L. Andersson, M. Seppälä (1999)
Expression of glycodelin in human breast and breast cancerInternational Journal of Cancer, 83
T. Virtanen, T. Zeiler, R. Mäntyjärvi (1999)
Important Animal Allergens Are Lipocalin Proteins: Why Are They Allergenic?International Archives of Allergy and Immunology, 120
C. Beuckmann, Masaaki Aoyagi, I. Okazaki, T. Hiroike, Hiroyuki Toh, O. Hayaishi, Y. Urade (1999)
Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase.Biochemistry, 38 25
(2000)
Sydney. Allergen: the trigger
W. Hof, M. Blankenvoorde, E. Veerman, A. Amerongen (1997)
The Salivary Lipocalin Von Ebner's Gland Protein Is a Cysteine Proteinase Inhibitor*The Journal of Biological Chemistry, 272
(1995)
Alpha-lactalbumin induces bovine milk beta 1,4-galactosyltransferase to utilize UDP-GalNAc
M. Ganfornina, Gabriel Gutiérrez, Michael Bastiani, Diego Sánchez (2000)
A phylogenetic analysis of the lipocalin protein family.Molecular biology and evolution, 17 1
S. Spitzauer (1999)
Allergy to Mammalian Proteins: At the Borderline between Foreign and Self?International Archives of Allergy and Immunology, 120
(1989)
Crossreactivity of IgE antibodies to caddisfly with arthtropoda and mollusca
(1997)
The salivary lipocalin von Ebner’s Structure of food allergens 13 gland protein is a cysteine proteinase inhibitor
ISSN 0905-6157 Structure of food allergens in relation to allergenicity Aalberse RC, Stapel SO. Structure of food allergens in relation to allergenicity. Pediatr Allergy Immunol 2001: 12(suppl 14): 10â14. # Munksgaard 2001. Rob C. Aalberse, Steven O. Stapel Department of Immunopathology, CLB and Laboratory for Experimental and Clinical Immunology, Academic Medical Centre, University of Amsterdam, the Netherlands Key words: cow milk; cross-reactive carbohydrate determinant; cross-reactivity; food allergens; IgE Rob C. Aalberse, CLB and Laboratory for Experimental and Clinical Immunology, Academic Medical Centre, University of Amsterdam, the Netherlands Introduction The three-dimensional structure of a substantial number of allergens has been solved or can be predicted based on sequence homology with proteins of known structure. These structures can often be classiï¬ed into a few structural families with common folds (1. . Examples of four ) of the structural families that are particularly relevant from the point of view of food allergy are: 1. alpha-helical proteins: napins (52S albumins from seeds) and non-speciï¬c lipid transfer proteins (LTPs); 2. largely beta-sheet proteins with a prominent helix in close contact: lipocalins, proï¬lins and Bet v 1-related proteins; 3. (alpha+beta)-structures, in which the alphaand beta-structural elements are not intimately associated: lactalbumin; and 4. serpins:
Pediatric Allergy and Immunology – Wiley
Published: May 1, 2001
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.