Abstract
Justin Stebbing, Aleksandra Filipović and Georgios Giamas 1 Department of Oncology and Surgery, Imperial College, Hammersmith Campus, London Received: June 8, 2011; Accepted: June 9, 2011; Published: June 16, 2011; Correspondence: Justin Stebbing, email: // // Abstract
Highlights
While presumably all proteins must have been positively selected for their biochemical functions at some time in the past, only a very few show protein-coding sequence evidence of such adaptive evolution; we thought it notable that LMTK3 fell into this category
An excess of nonsynonymous over synonymous codon mutations was used to identify sites of positive selection and clarified that only LMTK3 amongst all the molecules we studied had adaptively evolved
We decided to focus our attention on LMTK3; in doing so, we attempted to explain in part the unique susceptibility of humans to estrogen receptor-α (ERα) positive breast cancers
Summary
Estrogen receptor positive breast cancer remains the commonest form of metastatic incurable disease. As kinases are some of the most common drug targets [1], we sought to identify previously uncharacterized molecules that regulate the estrogen receptor-α (ERα) [2,3].
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