ck2-mediated hyperphosphorylation of topoisomerase i targets serine 506, enhances topoisomerase i–dna binding, and increases cellular camptothecin sensitivityck2-mediated hyperphosphorylation拓扑异构酶的丝氨酸506目标,提高拓扑异构酶i-dna绑定,并增加细胞的喜树碱的敏感性.pdfVIP

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ck2-mediated hyperphosphorylation of topoisomerase i targets serine 506, enhances topoisomerase i–dna binding, and increases cellular camptothecin sensitivityck2-mediated hyperphosphorylation拓扑异构酶的丝氨酸506目标,提高拓扑异构酶i-dna绑定,并增加细胞的喜树碱的敏感性.pdf

ck2-mediated hyperphosphorylation of topoisomerase i targets serine 506, enhances topoisomerase i–dna binding, and increases cellular camptothecin sensitivityck2-mediated hyperphosphorylation拓扑异构酶的丝氨酸506目标,提高拓扑异构酶i-dna绑定,并增加细胞的喜树碱的敏感性

CK2-Mediated Hyperphosphorylation of Topoisomerase I Targets Serine 506, Enhances Topoisomerase I–DNA Binding, and Increases Cellular Camptothecin Sensitivity Keya Bandyopadhyay, Pingchuan Li, Ruth A. Gjerset* Torrey Pines Institute for Molecular Studies, San Diego, California, United States of America Abstract Topoisomerase I is the target for a potent class of chemotherapeutic drugs derived from the plant alkaloid camptothecin that includes irinotecan and topotecan. In this study we have identified a novel site of CK2-mediated topoisomerase I (topo I) phosphoryla

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