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Interaction between Bax and Bcl-XL proteins confirmed by partial acceptor photobleaching-based FRET imaging 被引量:1
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作者 Fangfang Yang Mengyan Du +1 位作者 Xiaoping Wang Tongsheng Chen 《Journal of Innovative Optical Health Sciences》 SCIE EI CAS 2020年第3期81-91,共11页
Exact interaction mechanism between Bax and Bcl-XL,two key Bcl-2 family proteins,is an interesting and controversial issue.Partial acceptor photobleaching-based quantitative fluores-cence resonance energy transfer(FRE... Exact interaction mechanism between Bax and Bcl-XL,two key Bcl-2 family proteins,is an interesting and controversial issue.Partial acceptor photobleaching-based quantitative fluores-cence resonance energy transfer(FRET)measurement,PbFRET,is a widely used FRET quantification method in living cells.In this report,we implemented pixel-to-pixel PbFRET imaging on a wide-field microscope to map the FRET efficiency(E)images of single living HepG2 cells co-expressing CFP-Bax and YFP-Bcl-XL.The E value between CFP-Bax and YFP-Bcl-XL was 4.59%in cytosol and 11.31%on mitochondria,conclusively indicating the direct interaction of the two proteins,and the interaction of the two proteins was strong on mitochondria and modest in cytosol. 展开更多
关键词 BAX BCL-XL protein-protein interaction fret imaging living cells
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