Structural basis for the dual recognition of IL-12 and IL-23 by ustekinumab.

By Jinquan Luo, Sheng-Jiun Wu, E. Lacy, Yevgeniya I. Orlovsky, Audrey E. Baker, A. Teplyakov, G. Obmolova, G. Heavner, H. Richter, J. Benson. 2010

111 citations recorded by the source corpus.

Subfields: Immunology, Oncology, Radiology, Nuclear Medicine and Imaging

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1. Y. Bloch
2. L. Bouchareychas
3. R. Merceron
4. K. Składanowska
5. L. Van den Bossche
6. S. Detry
7. S. Govindarajan
8. J. Benson

Citations in the corpus

• Structural activation of pro-inflammatory human cytokine IL-23 by cognate IL-23 receptor enables recruitment of the shared receptor IL-12Rβ1 (2017, background): “…and 37D5 (Saunders et al., 2009), which bind to sizeable albeit non-overlapping sites on IL-23, the therapeutic monoclonal antibody ustekinumab (Benson et al., 2011) binding to the D1–D2 junction of IL-12p40 (Luo et al., 2010), and the monoclonal antibody briakinumab (ABT-874) (Reich et al., 2011).”
• Therapeutic targeting of the IL-12/23 pathways: generation and characterization of ustekinumab (2011, background): “Ustekinumab was shown to bind IL-12p40 with the expected 2:1 cytokine/antibody stoichiometr”