Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
By C. Pargellis, L. Tong, L. Churchill, P. Cirillo, T. Gilmore, A. G. Graham, P. Grob, E. Hickey, N. Moss, S. Pav and 1 more. Nature Structural Biology, 2002
793 citations recorded by the source corpus.
Subfields: Cancer Research, Molecular Biology, Organic Chemistry
View Paper: https://www.semanticscholar.org/paper/9d5befeee5feb4f038e275371e5bca599a7db909
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
In Organic Chemistry
Citations in the corpus
- Molecular Interaction Studies Using Microscale Thermophoresis (2011, background): “The dissociation constant is determined to be 6 – 2 nM in good agreement with literature values.(33) Also, the evaluation of the MST T-Jump response is shown in Figure 3, which in case of p38 BIRB-796 interaction yields a binding curve with a KD of 11 – 6 nM, in good agreement with the corresponding”
- Is allostery an intrinsic property of all dynamic proteins? (2004, methodology): “That allostery can involve monomeric proteins was also observed in the human p38 MAP kinase, where a new allosteric binding site was reported.(36) The NMR study by Volkman et al.”
- p38 MAP-kinases pathway regulation, function and role in human diseases. (2007, background): “Moreover, the diaryl urea compound BIRB796 [80] is not only a potent inhibitor of p38α and p38β, but also inhibits p38γ and p38δ at higher concentrations in cell-based assays providing a new tool for identifying physiological roles of these two p38 MAPK isoforms by using varying concentrations of th”
- Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. (2004, background): “(Figure 5B) (Nagar et al., 2002; Schindler et al., 2000), and it also shares significant similarities with the p38Overall Structure and B-RAF MAP kinase-BIRB 796 complex (Pargellis et al., 2002).”