Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?
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Title
Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?
Authors
Keywords
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Journal
CLINICAL REVIEWS IN ALLERGY & IMMUNOLOGY
Volume -, Issue -, Pages -
Publisher
Springer Science and Business Media LLC
Online
2021-01-07
DOI
10.1007/s12016-020-08826-1
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- Changes in Allergenicity of Porcine Serum Albumin by Gamma Irradiation
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- Structural and immunologic characterization of bovine, horse, and rabbit serum albumins
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- Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound
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- Heat-Induced Structural Changes Affect OVA-Antigen Processing and Reduce Allergic Response in Mouse Model of Food Allergy
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- The Influence of the Presence of Wheat Flour on the Antigenic Activities of Egg White Proteins
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- Camel milk: An alternative for cow's milk allergy in children
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- Mammalian lipocalin allergens - insights into their enigmatic allergenicity
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- Nutritional Value and Technological Suitability of Milk from Various Animal Species Used for Dairy Production
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- Role of Sensitization to Mammalian Serum Albumin in Allergic Disease
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- Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests
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- Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon
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- Pathophysiology of Food Allergy
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- Current Understanding of Egg Allergy
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- Pulsed Ultraviolet Light Reduces Immunoglobulin E Binding to Atlantic White Shrimp (Litopenaeus setiferus) Extract
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- Clinical monosensitivity to salmonid fish linked to specific IgE-epitopes on salmon and trout beta-parvalbumins
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- Gut permeability and food allergies
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- Seafood workers and respiratory disease: an update
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- Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin
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- Visualization of clustered IgE epitopes on α-lactalbumin
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- Comparative study of in vitro digestibility of major allergen, tropomyosin and other proteins between Grass prawn (Penaeus monodon) and Pacific white shrimp (Litopenaeus vannamei)
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- Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry
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- Food allergy to chicken meat with IgE reactivity to muscle α-parvalbumin
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- Expression levels of parvalbumins determine allergenicity of fish species
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- Molecular aspects of milk allergens and their role in clinical events
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- Mammalian milk allergy: clinical suspicion, cross-reactivities and diagnosis
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- The role of protein digestibility and antacids on food allergy outcomes
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- Allergens are distributed into few protein families and possess a restricted number of biochemical functions
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