ArticleComputational and structural biotechnology journal2026
Deciphering the Structural Basis of Allosteric Inhibition of Mutant Epidermal Growth Factor Receptor and Identification of Novel Inhibitors.
Article in Computational and structural biotechnology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The non-small cell lung cancer-associated epidermal growth factor receptor (EGFR) mutant L858R/T790M confers resistance to first- and second-generation tyrosine kinase inhibitors (TKIs). Allosteric inhibitors have emerged as alternative therapeutic agents. Unlike orthosteric inhibitors, they preferentially stabilize EGFR in an inactive conformation. Hence, understanding the mechanistic basis of this inhibition is essential for designing potent allosteric inhibitors. In this study, we performed microsecond-scale molecular dynamics (MD) simulations on the inactive conformations of apo-EGFR
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