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• W2893444880 abstract "ABSTRACT Expression of the enzyme human asparagine synthetase (ASNS) promotes metastatic progression in breast cancer, which affects L-asparagine levels and tumor cell invasiveness. Human ASNS has therefore emerged as a bona fide drug target for cancer therapy. We have reported a slow-onset, tight binding ASNS inhibitor with nanomolar affinity, but our compound exhibits poor cell permeability. On the other hand, we show here that this inhibitor exhibits remarkable selectivity for the human ASNS in HCT-116 cell lysates. By determining the first high-resolution (1.85 Å) X-ray crystal structure for human ASNS, we have built a computational model of the enzyme complexed to our inhibitor, which provides the first insights into the intermolecular interactions mediating specificity. These findings should facilitate the development of a second generation of ASNS inhibitors, leading to the discovery of drugs to prevent metastasis." @default.
• W2893444880 created "2018-10-05" @default.
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• W2893444880 date "2018-09-29" @default.
• W2893444880 modified "2023-09-27" @default.
• W2893444880 title "Molecular basis of human asparagine synthetase inhibitor specificity" @default.
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• W2893444880 doi "https://doi.org/10.1101/428508" @default.
• W2893444880 hasPublicationYear "2018" @default.
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