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• W2912300448 abstract "Abstract EGFR is an oncogene that encodes for a trans-membrane tyrosine kinase receptor. Its mis-regulation is associated to several human cancers that, consistently, can be treated by selective tyrosine kinase inhibitors. The proximal promoter of EGFR contains a G-rich domain located at 272 bases upstream the transcription start site. We previously proved it folds into two main interchanging G-quadruplex structures, one of parallel and one of hybrid topology. Here we present the first evidences supporting the ability of the complementary C-rich strand (EGFR-272_C) to assume an intramolecular i-Motif (iM) structure that, according to the experimental conditions (pH, presence of co-solvent and salts), can coexist with a different arrangement we referred to as a hairpin. The herein identified iM efficiently competes with the canonical pairing of the two complementary strands, indicating it as a potential novel target for anticancer therapies. A preliminary screening for potential binders identified some phenanthroline derivatives as able to target EGFR-272_C at multiple binding sites when it is folded into an iM." @default.
• W2912300448 created "2019-02-21" @default.
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• W2912300448 date "2019-02-04" @default.
• W2912300448 modified "2023-10-17" @default.
• W2912300448 title "pH-driven conformational switch between non-canonical DNA structures in a C-rich domain of EGFR promoter" @default.
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• W2912300448 doi "https://doi.org/10.1038/s41598-018-37968-8" @default.
• W2912300448 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6362134" @default.
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