Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody

Autor: Chen, Jiun-Bo, Ramadani, Faruk, Pang, Marie O. Y., Beavil, Rebecca L., Holdom, Mary D., Mitropoulou, Alkistis N., Beavil, Andrew J., Gould, Hannah J., Chang, Tse Wen, Sutton, Brian J., McDonnell, James M., Davies, Anna M.

Publikováno v: Chen, J-B, Ramadani, F, Pang, M O Y, Beavil, R L, Holdom, M D, Mitropoulou, A N, Beavil, A J, Gould, H J, Chang, T W, Sutton, B J, McDonnell, J M & Davies, A M 2018, ' Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody ', Scientific Reports, vol. 8, no. 1, 11548 . https://doi.org/10.1038/s41598-018-29664-4
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Scientific Reports

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https://kclpure.kcl.ac.uk/en/publications/9f48eecf-6631-4720-9e1c-34478ed33a1b

Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.

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Synthesis and Incorporation into Cyclic Peptides of Tolan Amino Acids and Their Hydrogenated Congeners: Construction of an Array of A--B-loop Mimetics of the Cε3 Domain of Human IgE.

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Expression of the Cu,Zn superoxide dismutase of Aspergillus fumigatus as determined by immunochemistry and immunoelectron microscopy.

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