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báo cáo khoa học: "Sweet fruit from a poisonous kiss"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài:Sweet fruit from a poisonous kiss | Liu Journal of Hematology Oncology 2010 3 19 http www.jhoonline.Org content 3 1 19 JOURNAL OF HEMATOLOGY ONCOLOGY EDITORIAL Open Access Sweet fruit from a poisonous kiss Delong Liu Editorial Acute promyelocytic leukemia APL once a rapidly fatal disease has become most curable of all leukemias thanks to the two Chinese wonder drugs all-trans retinoid acid and arsenic trioxide AT . PML-RXARa fusion protein is the hallmark and driving force of APL. In the April 9th issue of the journal Science Zhang et al. provided new and convincing evidence on how AT an ancient poisonous medicine plays the tricks on the oncoprotein PML-RARa and sheds lights on how a poisonous kiss leads to the sweet fruit 1 . A comprehensive approach and an epic story of science Zhang et al. have indeed done a tremendous amount of work in this study. Several cell lines and transfectants were used and or established including HEK 293T NB4 and HeLa cells to name a few. Numerous mutants of PML as well as EGFP-fusion proteins were generated to pinpoint the kissing spot of AT. To be even more convincing two additional organic arsenicals PAPAO and ReAsH were also employed. With collaborations from the leading institutions of biotechnology and physics in China MALDI-TOF mass spectrometry EXAFS XANE S spectroscopy and circular dichroism were orchestrated marvelously into the study. As the stu dy evolves it reads like an epic story of science. Solid evidences-with no stones left unturned The scientific team has provided strong and convincing evidence step by step and proved to the world that AT poisons the PML-RARa protein by kissing the cysteine residues in the zinc fingers within the RBCC domain of PML. They first demonstrated that AT binds to PML- not the RARa - portion of the fusion oncoprotein. Using EGFP-fusion mutants of PML protein they showed colocalization of arsenicals with various PML mutants and pinpointed that AT binds to the RING domain of PML. With the help of NMR and a variety of .