Allosteric inhibition of IgE–FcεRI interactions by simultaneous targeting of IgE F(ab’)2 epitopes
Abstract Immunoglobulin E (IgE) plays pivotal roles in allergic diseases through interaction with a high-affinity receptor (FcεRI). We established that Fab fragments of anti-IgE antibodies (HMK-12 Fab) rapidly dissociate preformed IgE-FcεRI complexes in a temperature-dependent manner and inhibit IgE...
Váldodahkkit: | Takao Hirano, Akemi Koyanagi, Hideo Ago, Masaki Yamamoto, Jiro Kitaura, Masataka Kasai, Ko Okumura |
---|---|
Materiálatiipa: | Artihkal |
Giella: | English |
Almmustuhtton: |
Nature Portfolio
2024-08-01
|
Ráidu: | Communications Biology |
Liŋkkat: | https://doi.org/10.1038/s42003-024-06633-4 |
Geahča maid
-
Tuning IgE: IgE-Associating Molecules and Their Effects on IgE-Dependent Mast Cell Reactions
Dahkki: Tomoaki Ando, et al.
Almmustuhtton: (2021-07-01) -
Identification of contact residues in the IgE binding site of human FcεRIα
Dahkki: Cook, J, et al.
Almmustuhtton: (1997) -
Effects of Omalizumab on FcεRI and IgE Expression in Lesional Skin of Bullous Pemphigoid
Dahkki: S. Morteza Seyed Jafari, et al.
Almmustuhtton: (2019-08-01) -
Structural basis of the IgE-Fc epsilon RI interaction.
Dahkki: Beavil, A, et al.
Almmustuhtton: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
Dahkki: Beavil, A, et al.
Almmustuhtton: (1993)