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@ARTICLE{Yu:827731,
author = {Yu, Kun and Yang, Ge and Labahn, Jörg},
title = {{H}igh-efficient production and biophysical
characterisation of nicastrin, and ist interaction with
{APPC}100},
journal = {Scientific reports},
volume = {7},
issn = {2045-2322},
address = {London},
publisher = {Nature Publishing Group},
reportid = {FZJ-2017-01837},
pages = {44297},
year = {2017},
abstract = {Nicastrin, 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.},
cin = {ICS-6},
ddc = {000},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000395977600001},
doi = {10.1038/srep44297},
url = {https://juser.fz-juelich.de/record/827731},
}