The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12.

By P. Lupardus, K. Garcia. 2008

148 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine–Nanobody Complex (2017, background): “The p40 protein is formed of three domains, each composed of a 7 β-stranded β-sandwich (2, 21, 24, 25).”
The molecular details of cytokine signaling via the JAK/STAT pathway (2018, methodology): “IFNαR1 has a large extracellular domain that consists of two CHRs while IFNαR2, similar to all other Class II cytokine receptors has only a single CHR. IFNαR2 is the high affinity chain, interacting with ligand with sub-nanomolar affinity whilst IFNαR1 binds with an affinity approximately two orders”
Non-Canonical Interleukin 23 Receptor Complex Assembly (2014, background): “Unfortunately, only the structure of IL-23, highlighting site I of p19 (13) but not of the IL-23 IL23R IL-12R 1 complex is available.”
Structural activation of pro-inflammatory human cytokine IL-23 by cognate IL-23 receptor enables recruitment of the shared receptor IL-12Rβ1 (2017, background): “This is because the functional role of this particular position had been postulated based on structural considerations of the receptor-free cytokine (Lupardus and Garcia, 2008), and has only recently been probed via reporter cellular assays in vitro (Schroder et al., 2015).”