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Birgit A. Helm

Researcher at University of Sheffield

Publications -  39
Citations -  855

Birgit A. Helm is an academic researcher from University of Sheffield. The author has contributed to research in topics: Immunoglobulin E & Mast cell. The author has an hindex of 15, co-authored 39 publications receiving 828 citations. Previous affiliations of Birgit A. Helm include Laboratory of Molecular Biology.

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Potential allergens stimulate the release of mediators of the allergic response from cells of mast cell lineage in the absence of sensitization with antigen-specific IgE

TL;DR: The study indicates that non‐immunological degranulation by prototypic allergens, such as bee venom phos‐pholipase A2 or proteases associated with house dust mite emanations, is critically dependent on enzymatic activity and has potentially important implications for vaccine design in allergic and parasitic disease.
Journal Article

A link between catalytic activity, IgE-independent mast cell activation, and allergenicity of bee venom phospholipase A2.

TL;DR: It is found that mast cells might be a source of IL-4 at the onset of specific immunity against sources of allergens such as bee venom that contain PLA2 and support the concept that the biologic action of an Ag on cells of the innate immune system can play a role in determining adaptive immune responses.
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Blocking of passive sensitization of human mast cells and basophil granulocytes with IgE antibodies by a recombinant human epsilon-chain fragment of 76 amino acids

TL;DR: The recombinant peptide corresponding to residues 301-376 at the junction of constant regions 2 and 3 of the human IgE epsilon chain blocked the in vivo passive sensitization of human skin mast cells and in vitro sensitized human basophil granulocytes with human Ig E antibodies.
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Solid-Phase Synthesis of an A-B Loop Mimetic of the CE3 Domain of Human IgE: Macrocyclization by Sonogashira Coupling

TL;DR: The solid-phase synthesis of a cyclic peptide containing the 21-residue epitope found in the A-B loop of the Cepsilon3 domain of human immunoglobulin E has been carried out.
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Identification of the high affinity receptor binding region in human immunoglobulin E.

TL;DR: In this paper, the capacity of N-and C-terminally truncated and chimeric human (h) IgE-derived peptides to inhibit the binding of I-labeled hIgE, and to engage cell lines expressing high and low affinity receptors (FcRI/II) was investigated.