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000827731 1001_ $$0P:(DE-HGF)0$$aYu, Kun$$b0
000827731 245__ $$aHigh-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100
000827731 260__ $$aLondon$$bNature Publishing Group$$c2017
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000827731 520__ $$aNicastrin, the largest member among the four components of the γ-secretase complex, has been identified to be the substrate recognizer for the proteolytic activity of the complex. Here we report that full-length human nicastrin (hNCT) can be obtained by heterologous expression in E. coli. Milligram quantities of the target protein are purified in a two-step purification protocol using affinity chromatography followed by SEC. The FOS-choline 14 purified tetrameric hNCT exhibits a proper folding with 31% α-helix and 23% β-sheet content. Thermal stability studies reveal stable secondary and tertiary structure of the detergent purified hNCT. A physical interaction between nicastrin and the γ-secretase substrate APPC100 confirmed the functionality of hNCT as a substrate recognizer.
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000827731 7001_ $$0P:(DE-Juel1)131989$$aYang, Ge$$b1$$ufzj
000827731 7001_ $$0P:(DE-Juel1)131973$$aLabahn, Jörg$$b2$$eCorresponding author$$ufzj
000827731 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/srep44297$$gVol. 7, p. 44297 -$$p44297$$tScientific reports$$v7$$x2045-2322$$y2017
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