% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Yang:837812,
author = {Yang, Ge and Yu, Kun and Kubicek, Jan and Labahn, Jörg},
title = {{E}xpression, purification, and preliminary
characterization of human presenilin-2},
journal = {Process biochemistry},
volume = {64},
issn = {1359-5113},
address = {Amsterdam [u.a.]},
publisher = {Elsevier Science},
reportid = {FZJ-2017-06601},
pages = {63-73},
year = {2018},
abstract = {Presenilins (PS1 and PS2) exhibit similar
γ-secretase-dependent and −independent functions with
subtle variations. In this study, we established a
cost-effective process to overexpress and purify full-length
human PS2 in sufficient quantities and quality for
structural studies. Upon optimization, milligram quantities
of homogeneous trimeric hisPS2 were purified, which enabled
the preliminary characterization of human hisPS2 zymogen.
Far-UV and near-UV CD as well as fluorescence spectroscopy
revealed that purified hisPS2 contained the expected
secondary structure and was folded into a defined tertiary
structure. Thermal stability analysis revealed a Tm value of
∼55 °C for secondary structure while cholesterol
significantly increased the stability. The low melting
temperature of ∼34 °C for the tertiary structure was able
to explain the purity and aggregation problems observed
during purification. Additionally, the occurrence of calcium
ions induced structural changes to different extents for
PS2WT and PS2-D263A/D366A was observed, which is consistent
with previous studies.},
cin = {ICS-6},
ddc = {530},
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:000423003200008},
doi = {10.1016/j.procbio.2017.09.012},
url = {https://juser.fz-juelich.de/record/837812},
}