Arachis

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  Subject Areas on Research

  • A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses. 
  • A voluntary registry for peanut and tree nut allergy: characteristics of the first 5149 registrants. 
  • Adverse reactions during peanut oral immunotherapy home dosing. 
  • Allergenicity of peanut and soybean extracts altered by chemical or thermal denaturation in patients with atopic dermatitis and positive food challenges. 
  • Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein. 
  • Clinical efficacy and immune regulation with peanut oral immunotherapy. 
  • Clinical features of acute allergic reactions to peanut and tree nuts in children. 
  • Comparison of commercial peanut skin test extracts. 
  • Competitive inhibition ELISA for quantification of Ara h 1 and Ara h 2, the major allergens of peanuts. 
  • Contribution of Ara h 2 to peanut-specific, immunoglobulin E-mediated, cell activation. 
  • Early peanut consumption: postpone or promote? 
  • Effects of cooking methods on peanut allergenicity. 
  • Engineered recombinant peanut protein and heat-killed Listeria monocytogenes coadministration protects against peanut-induced anaphylaxis in a murine model. 
  • Engineering, characterization and in vitro efficacy of the major peanut allergens for use in immunotherapy. 
  • Epitope specificity and immunoaffinity purification of the major peanut allergen, Ara h I. 
  • Epitope specificity of the major peanut allergen, Ara h II. 
  • Evaluating pH-induced gastrointestinal aggregation of Arachis hypogaea 1 fragments as potential components of peanut allergy. 
  • Evidence for emulation in chimpanzees in social settings using the floating peanut task. 
  • Hypoallergenic legume crops and food allergy: factors affecting feasibility and risk. 
  • Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. 
  • Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2. 
  • Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. 
  • Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. 
  • Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies. 
  • Immunologic features of infants with milk or egg allergy enrolled in an observational study (Consortium of Food Allergy Research) of food allergy. 
  • Immunology in the Clinic Review Series; focus on allergies: immunotherapy for food allergy. 
  • Impairing oral tolerance promotes allergy and anaphylaxis: a new murine food allergy model. 
  • In vivo and T cell cross-reactivity between walnut, cashew and peanut. 
  • Increased peanut-specific IgA levels in saliva correlate with food challenge outcomes after peanut sublingual immunotherapy. 
  • Isolation, identification, and characterization of clones encoding antigens responsible for peanut hypersensitivity. 
  • Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. 
  • Modification of a major peanut allergen leads to loss of IgE binding. 
  • Molecular cloning and epitope analysis of the peanut allergen Ara h 3. 
  • Monitoring peanut allergen in food products by measuring Ara h 1. 
  • Nasal peanut+ CpG immunotherapy enhances peanut-specific IFN-γ in Th2 cells and IL-10 in non-Th2 cells in mice. 
  • Oral administration of IL-12 suppresses anaphylactic reactions in a murine model of peanut hypersensitivity. 
  • Oral gene delivery with chitosan--DNA nanoparticles generates immunologic protection in a murine model of peanut allergy. 
  • Peanut allergenicity. 
  • Peanut allergy: recurrence and its management. 
  • Peanut and soy allergy: a clinical and therapeutic dilemma. 
  • Peanut hypersensitivity. IgE binding characteristics of a recombinant Ara h I protein. 
  • Peanut protein allergens: the effect of roasting on solubility and allergenicity. 
  • Peanut protein as a major cause of adverse food reactions in patients with atopic dermatitis. 
  • Plant proteins in the amelioration of protein deficiency states. 
  • Predictive value of skin prick tests using recombinant allergens for diagnosis of peanut allergy. 
  • Preparation and Analysis of Peanut Flour Used in Oral Immunotherapy Clinical Trials. 
  • Prevalence of peanut and tree nut allergy in the US determined by a random digit dial telephone survey. 
  • Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. 
  • Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. 
  • STUDIES ON A VEGETABLE PROTEIN MIXTURE BASED ON PEANUT AND SOYA FLOURS. 
  • Safety of a peanut oral immunotherapy protocol in children with peanut allergy. 
  • Sensitization and allergic response and intervention therapy in animal models. 
  • Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. 
  • Sublingual versus oral immunotherapy for peanut-allergic children: a retrospective comparison. 
  • Sustained unresponsiveness to peanut in subjects who have completed peanut oral immunotherapy. 
  • THE USE OF INFANT FOOD FORMULATIONS BASED ON FULL-FAT SOYA FLOUR AND PEANUT PROTEIN ISOLATE IN THE TREATMENT OF PROTEIN MALNUTRITION (KWASHIORKOR). 
  • Tertiary structure and biophysical properties of a major peanut allergen, implications for the production of a hypoallergenic protein. 
  • The effect of supplements of groundnut flour or groundnut protein isolate fortified with calcium salts and vitamins or of skim-milk powder on the digestibility coefficient, biological value and net utilization of the proteins of poor Indian diets given to undernourished children. 
  • The major glycoprotein allergen from Arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. 
  • The metabolism of nitrogen, calcium and phosphorus in undernourished children. 2. The effect of supplementary groundnut-milk curds on the metabolism of nitrogen, calcium and phosphorus. 
  • The natural progression of peanut allergy: Resolution and the possibility of recurrence. 
  • The production of interferon-gamma in response to a major peanut allergy, Ara h II correlates with serum levels of IgE anti-Ara h II. 
  • The supplementary value of certain processed protein foods based on blends of groundnut, soya-bean, sesame, chick-pea (Cicer arietinum) flours and skim-milk powder to a maize--tapioca diet. 
  • Type B CpG oligodeoxynucleotides induce Th1 responses to peanut antigens: modulation of sensitization and utility in a truncated immunotherapy regimen in mice. 
  • USE OF AN INFANT FOOD FORMULA BASED ON GROUNDNUT PROTEIN ISOLATE AND SKIM MILK POWDER IN FEEDING INFANTS. 
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  Keywords of People

  • Zhong, Xiaoping, Professor of Pediatrics, Immunology