S. Koppelman

发表

In vitro digestion and characterisation of 2S albumin and digestion‐resistant peptides in pecan

J. Nordlee, A. Knulst, J. Baumert, 2018 .

CTLA-4 Signaling Regulates the Intensity of Hypersensitivity Responses to Food Antigens, but is Not Decisive in the Induction of Sensitization

R. Pieters, L. Boon, S. Koppelman, 2005, The Journal of Immunology.

Allergenicity attributes of different peanut market types.

Steve L. Taylor, J. Nordlee, S. Maleki, 2016, Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association.

Detecting allergens in food.

S. Koppelman, S. Hefle, 2006 .

Appendix – Detecting tree nut and seed allergens in food

L. Harris, S. Koppelman, 2013 .

Measuring parvalbumin levels in fish muscle tissue: relevance of muscle locations and storage conditions.

J. Nordlee, J. Baumert, S. Koppelman, 2012, Food chemistry.

Evaluation and comparison of the species-specificity of 3 antiparvalbumin IgG antibodies.

J. Nordlee, J. Baumert, S. Koppelman, 2011, Journal of agricultural and food chemistry.

15 – Detecting soy, fish and crustaceans in food

S. Koppelman, 2006 .

12 – Detecting tree nuts and seeds in food

S. Koppelman, 2006 .

Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy.

R. Van Ree, S. Vieths, J. Akkerdaas, 2004, The Journal of allergy and clinical immunology.

Detection of peanut allergen in human blood after consumption of peanuts is skewed by endogenous immunoglobulins.

R. Witkamp, J. Baumert, J. Keijer, 2017, Journal of immunological methods.

The protein structure determines the sensitizing capacity of Brazil nut 2S albumin (Ber e1) in a rat food allergy model

J. V. van Bilsen, H. D. de Jongh, S. Koppelman, 2013, Clinical and Translational Allergy.

Digestibility and IgE-Binding of Glycosylated Codfish Parvalbumin

J. Nordlee, J. Baumert, H. D. de Jongh, 2013, BioMed research international.

Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing.

H. Gruppen, S. Koppelman, L. V. D. van den Broek, 2008, Food chemistry.

The effect of the food matrix on in vivo immune responses to purified peanut allergens.

R. Pieters, G. D. Jong, S. Koppelman, 2005, Toxicological sciences : an official journal of the Society of Toxicology.

Purification and immunoglobulin E‐binding properties of peanut allergen Ara h 6: evidence for cross‐reactivity with Ara h 2

E. Knol, A. Knulst, S. Koppelman, 2005, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Electrophoretic Behavior in Relation to the Structural Integrity of Codfish Parvalbumin upon Heat Treatment.

J. Baumert, H. D. de Jongh, S. Koppelman, 2015, Journal of agricultural and food chemistry.

Parvalbumin in fish skin-derived gelatin: is there a risk for fish allergic consumers?

J. Nordlee, S. Taylor, S. Koppelman, 2012, Food additives & contaminants. Part A, Chemistry, analysis, control, exposure & risk assessment.

Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world

E. Knol, C. Bruijnzeel‐Koomen, S. Koppelman, 2001, Allergy.

Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy?

E. Knol, C. Bruijnzeel‐Koomen, A. Knulst, 2007, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins.

R. Van Ree, J. Akkerdaas, R. Ree, 1997, The Journal of allergy and clinical immunology.

β(1,2)-Xylose and α(1,3)-Fucose Residues Have a Strong Contribution in IgE Binding to Plant Glycoallergens*

R. Van Ree, J. Milazzo, P. Lerouge, 2000, The Journal of Biological Chemistry.

Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins.

A. Knulst, H. D. de Jongh, H. Gruppen, 2002, Journal of agricultural and food chemistry.

Predicted number of peanut‐allergic patients needed to treat with epicutaneous immunotherapy (EPIT) to prevent one allergic reaction: A novel approach to assessing relevance

G. Roberts, B. Remington, G. Lack, 2021, Allergy.

Hidden hazelnut is a threat to allergic patients

A. Knulst, C. Bruijnzeel-Koomen, S. Koppelman, 2001, Allergy.

Risk of shared equipment in restaurants for consumers with peanut allergy: a simulation for preparing Asian foods: A simulation for preparing Asian foods.

B. Remington, S. Koppelman, W. Blom, 2020 .

Risk of shared equipment in restaurants for peanut-allergic consumers: a simulation for preparing Asian foods.

B. Remington, S. Koppelman, W. Blom, 2020, Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology.

Quantitative risk reduction through peanut immunotherapy: Safety benefits of an increased threshold in Europe

B. Remington, T. Krone, S. Koppelman, 2018, Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology.

Effect of chemical modifications on allergenic potency of peanut proteins.

A. Nowak‐Wegrzyn, S. Koppelman, R. Bencharitiwong, 2015, Allergy and asthma proceedings.

The importance of reducing risk in peanut allergy: Current and future therapies.

B. Remington, J. Baumert, W. Shreffler, 2017, Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology.

Proteolytic processing of the peanut allergen Ara h 3.

M. Gaspari, S. Piersma, S. Koppelman, 2005, Molecular nutrition & food research.

Glutaraldehyde-Modified Recombinant Fel d 1: A Hypoallergen With Negligible Biological Activity But Retained Immunogenicity

R. Van Ree, S. Koppelman, E. D. de Jong, 2011, The World Allergy Organization journal.

Development of a Sandwich Enzyme-Linked Immunosorbent Assay for Detection and Quantification of Clam Residues in Food Products

J. Baumert, S. Koppelman, Steve L Taylor, 2021, BioMed research international.

Comparison of recovery and immunochemical detection of peanut proteins from differentially roasted peanut flour using ELISA.

J. Baumert, Balunkeswar Nayak, S. Koppelman, 2019, Food chemistry.

Detection of soy proteins in processed foods: literature overview and new experimental work.

C. Lakemond, S. Koppelman, S. Hefle, 2004, Journal of AOAC International.

FAST: towards safe and effective subcutaneous immunotherapy of persistent life-threatening food allergies

N. Rigby, R. Van Ree, C. Mills, 2012, Clinical and Translational Allergy.

Children with peanut allergy recognize predominantly Ara h2 and Ara h6, which remains stable over time

A. Knulst, E. Knol, C. Bruijnzeel‐Koomen, 2007, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Controlling the aggregation propensity and thereby digestibility of allergens by Maillardation as illustrated for cod fish parvalbumin.

H. D. de Jongh, S. Koppelman, Steve L Taylor, 2011, Journal of bioscience and bioengineering.

A perspective on pea allergy and pea allergens

Philip E. Johnson, Steve L. Taylor, J. Marsh, 2021 .

Effect of heat treatment on the conformational stability of intact and cleaved forms ofthe peanut allergen Ara h 6 in relation to its IgE-binding potency.

J. Baumert, H. D. de Jongh, S. Koppelman, 2020, Food chemistry.

Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6; characterization of intermediate- and end products.

T. Velickovic, S. Koppelman, D. Stanić-Vučinić, 2013, Biochimica et biophysica acta.

Purification of parvalbumin from carp: a protocol that avoids heat-treatment.

R. Romijn, J. Nordlee, H. D. de Jongh, 2010, Journal of food science.

Chemical modification of peanut conglutin reduces IgE reactivity but not T cell reactivity in peanut‐allergic patients

A. Knulst, D. Opstelten, E. Knol, 2014, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

T-cell reactivity for a peanut-derived epitope in the skin of a young infant with atopic dermatitis.

C. Bruijnzeel-Koomen, S. Koppelman, A. Felius, 1998, The Journal of allergy and clinical immunology.

Comparison of antibody responses to hen's egg and cow's milk proteins in orally sensitized rats and food‐allergic patients

S. Koppelman, G. Houben, A. Felius, 2000, Allergy.

Endurance Exercise Increases Intestinal Uptake of the Peanut Allergen Ara h 6 after Peanut Consumption in Humans

R. Witkamp, J. Keijer, K. Lenaerts, 2017, Nutrients.

Transglutaminase Catalyzed Reactions: Impact on Food Applications

G. D. Jong, S. Koppelman, G.A.H. de Jong, 2002 .

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Joseph L. Baumert, J. Nordlee, J. Baumert, 2016, Scientific Reports.

Legumin allergens from peanuts and soybeans: effects of denaturation and aggregation on allergenicity.

H. Gruppen, S. Koppelman, L. V. D. van den Broek, 2008, Molecular nutrition & food research.

Transglutaminase inhibitor from milk

G. Wijngaards, G. D. Jong, S. Koppelman, 2003 .

Chemically modified peanut extract shows increased safety while maintaining immunogenicity

R. Pieters, R. Van Ree, A. Knulst, 2019, Allergy.

Comparison of different immunochemical methods for the detection and quantification of hazelnut proteins in food products.

A. Knulst, S. Koppelman, I. Pigmans, 1999, Journal of immunological methods.

The range of minimum provoking doses in hazelnut‐allergic patients as determined by double‐blind, placebo‐controlled food challenges

R. Van Ree, A. Knulst, R. Ree, 2002, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Relevance of Ara h1, Ara h2 and Ara h3 in peanut‐allergic patients, as determined by immunoglobulin E Western blotting, basophil–histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen

A. Knulst, E. Knol, A. Knulst, 2004, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Release of Major Peanut Allergens from Their Matrix under Various pH and Simulated Saliva Conditions—Ara h2 and Ara h6 Are Readily Bio-Accessible

R. Pieters, R. Witkamp, J. Baumert, 2018, Nutrients.

Comparison of six commercial ELISA kits for their specificity and sensitivity in detecting different major peanut allergens.

R. Pieters, J. Nordlee, J. Baumert, 2015, Journal of agricultural and food chemistry.

The distribution of individual threshold doses eliciting allergic reactions in a population with peanut allergy.

A. Knulst, C. Bruijnzeel-Koomen, S. Koppelman, 2002, The Journal of allergy and clinical immunology.

Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin.

M. Gaspari, H. D. de Jongh, E. Knol, 2005, Journal of agricultural and food chemistry.

Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1).

A. Knulst, S. Piersma, E. Knol, 2003, The Journal of allergy and clinical immunology.

Clinical relevance of sensitization to lupine in peanut‐sensitized adults

S. Taylor, A. Knulst, C. Bruijnzeel‐Koomen, 2009, Allergy.

Anaphylaxis from passive transfer of peanut allergen in a blood product.

J. Baumert, E. V. van Pampus, I. Joosten, 2011, The New England journal of medicine.

Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistant peptides.

S. Koppelman, S. Hefle, G. D. de Jong, 2010, Molecular nutrition & food research.

Distribution of Intact Peanut Protein and Digestion-Resistant Ara h 2 Peptide in Human Serum and Saliva

J. Nordlee, R. Bush, J. Baumert, 2009 .

Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut.

R. Van Ree, S. Wünschmann, M. Chapman, 2014, Journal of agricultural and food chemistry.

Peanut Cross-contamination in Randomly Selected Baked Goods.

J. Baumert, S. Koppelman, J. Bird, 2022, Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology.

The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts and sesame seeds.

Surendra S. Negi, C. Schein, W. Braun, 2020, The Journal of allergy and clinical immunology.

Quantitative Assessment of the Safety Benefits Associated with Increasing Clinical Peanut Thresholds Through Immunotherapy.

Steve L. Taylor, J. Baumert, S. Koppelman, 2016, The journal of allergy and clinical immunology. In practice.

Anaphylaxis caused by the unexpected presence of casein in salmon

A. Knulst, G. D. Jong, S. Koppelman, 1999, The Lancet.

Mixed antibody and T cell responses to peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in an oral sensitization model

R. Pieters, S. Koppelman, F. van Wijk, 2004, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization

S. Piersma, H. Gruppen, E. Knol, 2003, Allergy.

Heat-induced Conformational Changes of Ara h 1, a Major Peanut Allergen, Do Not Affect Its Allergenic Properties*

H. D. de Jongh, C. Bruijnzeel-Koomen, S. Koppelman, 1999, The Journal of Biological Chemistry.

RIDASCREEN® FAST PEANUT, a rapid and safe tool to determine peanut contamination in food

U. Immer, S. Koppelman, B. Reck, 2004 .

Relevance of ara h1, ara h2, and ara h3 in peanut allergic patients, as determined by IgE-western-blotting, basophil histamine release, and intracultaneous testing: Ara h2 is the most important peanut allergen

A. Knulst, E. Knol, S. Koppelman, 2003 .

Development of an enzyme-linked immunosorbent assay method to detect mustard protein in mustard seed oil.

S. Koppelman, P. H. van der Schaft, R. Vlooswijk, 2007, Journal of food protection.

Estimated Risk Reduction to Packaged Food Reactions by Epicutaneous Immunotherapy (EPIT) for Peanut Allergy.

B. Remington, G. Lack, D. Fleischer, 2019, Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology.

Detecting peanut allergens : the development of an immunochemical assay for peanut proteins

S. Koppelman, M. Hessing, G. V. Duijn, 1999 .

Sandwich Enzyme-Linked Immunosorbent Assay for Detecting Sesame Seed in Foods

J. Baumert, S. Koppelman, Steve L Taylor, 2015, BioMed research international.

Peanut allergy: sensitization by peanut oil-containing local therapeutics seems unlikely.

A. Knulst, C. Bruijnzeel-Koomen, S. Koppelman, 2004, The Journal of allergy and clinical immunology.

Characterization of IgG and IgE Binding to Parvalbumin Derived from Commercially Important Fish Species

J. Nordlee, J. Baumert, S. Koppelman, 2011 .

Dose and route of administration determine the efficacy of prophylactic immunotherapy for peanut allergy in a Brown Norway rat model

J. Marsh, N. Rigby, A. Sancho, 2023, Frontiers in Immunology.

Determination of Allergen Levels, Isoforms, and Their Hydroxyproline Modifications Among Peanut Genotypes by Mass Spectrometry

J. Marsh, S. Koppelman, P. Johnson, 2022, Frontiers in Allergy.

Purification and Initial Characterization of Ara h 7, a Peanut Allergen from the 2S Albumin Protein Family.

J. Marsh, J. Baumert, H. D. de Jongh, 2021, Journal of agricultural and food chemistry.

Epicutaneous immunotherapy for peanut allergy modifies IgG4 responses to major peanut allergens.

H. Sampson, S. Koppelman, W. Agbotounou, 2019, The Journal of allergy and clinical immunology.

Purification and Characterization of Naturally Occurring Post-Translationally Cleaved Ara h 6, an Allergen That Contributes Substantially to the Allergenic Potency of Peanut.

J. Marsh, J. Nordlee, J. Baumert, 2018, Journal of agricultural and food chemistry.

Basophil response to peanut allergens in Mediterranean peanut-allergic patients.

M. Blanca, S. Koppelman, A. Díaz‐Perales, 2014, Allergy.

Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer.

H. Gruppen, S. Koppelman, L. V. D. van den Broek, 2006, Journal of agricultural and food chemistry.

Peanut allergen Ara h 1 interacts with proanthocyanidins into higher molecular weight complexes.

J. Vincken, H. Gruppen, S. Koppelman, 2007, Journal of agricultural and food chemistry.

Detection of Digestion-Resistant Ara h 2 Peptide in Breast Milk of Lactating Mothers

J. Baumert, S. Koppelman, S. Hefle, 2008 .

Determination of pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated peanut allergen Ara h 1.

H. Gruppen, S. Koppelman, L. V. D. van den Broek, 2008, Journal of agricultural and food chemistry.

Identification and partial characterization of multiple major allergens in peanut proteins

S. Koppelman, Koppelman, Penninks, 1998, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Physicochemical characterization of allergens: quantity, identity, purity, aggregation and conformation.

H. D. de Jongh, S. Koppelman, D. Luykx, 2009, Arbeiten aus dem Paul-Ehrlich-Institut (Bundesinstitut fur Impfstoffe und biomedizinische Arzneimittel) Langen/Hessen.

Smartphone Instrument for Portable Enzyme- Linked Immunosorbent Assays

Hojeong Yu, Kenneth D Long, Brian T Cunningham, 2022 .