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Conformationally constrained peptides target the allosteric kinase dimer interface and inhibit EGFR activation
Although EGFR is a highly sought-after drug target, inhibitor resistance remains a challenge. As an alternative strategy for kinase inhibition, we sought to explore whether allosteric activation mechanisms could effectively be disrupted. The kinase domain of EGFR forms an atypical asymmetric dimer v...
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| Pubblicato in: | Bioorg Med Chem |
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| Autori principali: | , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2017
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5837902/ https://ncbi.nlm.nih.gov/pubmed/28911855 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bmc.2017.08.051 |
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