Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition
By J. Ohren, Huifen Chen, A. Pavlovsky, C. Whitehead, E. Zhang, Peter Kuffa, Chunhong Yan, P. McConnell, Cindy Spessard, C. Banotai and 12 more. Nature Structural &Molecular Biology, 2004
603 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5e68fe7fae34cf44e890d09ba11ab5f17b3a2bd8
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In Molecular Biology
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Citations in the corpus
- Features of selective kinase inhibitors. (2005, background): “Moreover, the low degree of sequence conservation in this region of the kinase explains the high selectivity of these compounds [94].”
- MEK1 mutations confer resistance to MEK and B-RAF inhibition (2009, background): “Arylamine MEK inhibitors function by locking the kinase into a ‘‘closed’’ inactive conformation, in which the activation loop causes helix C to become externally rotated and displaced (27).”
- The MEK/ERK cascade: from signaling specificity to diverse functions. (2007, background): “X-ray analysis of truncated human MEK1 and MEK2 revealed that they are indeed similar in structure to other protein kinases [22].”
- BRafV600E cooperates with Pten silencing to elicit metastatic melanoma (2009, methodology): “To do so, we used specific and selective inhibitors of MEK1/2 (PD325901) or mTorc1 (rapamycin), which are downstream of BRaf V600E or PI3′-kinase, respectivel”
- A quantitative analysis of kinase inhibitor selectivity (2008, background): “and not designed to identify allosteric interactions, yet binding of at least some non-ATP competitive compounds, such as the MEK inhibitor CI-1040 (ref”