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@ARTICLE{Pazicky:476470,
author = {Pazicky, Samuel and Alder, Arne and Mertens, Haydyn and
Svergun, Dmitri and Gilberger, Tim and Loew, Christian},
title = {{N}-terminal phosphorylation regulates the activity of
glycogen synthase kinase 3 from {P}lasmodium falciparum},
journal = {The biochemical journal / Reviews},
volume = {479},
number = {3},
issn = {0264-6021},
address = {London [u.a.]},
publisher = {Portland Pr.},
reportid = {PUBDB-2022-01747},
pages = {337 - 356},
year = {2022},
note = {ISSN 1470-8728 not unique: **2 hits**.},
abstract = {As the decline of malaria cases stalled over the last five
years, novel targets in Plasmodium falciparum are necessary
for the development of new drugs. Glycogen Synthase Kinase
(PfGSK3) has been identified as a potential target, since
its selective inhibitors were shown to disrupt the
parasitès life cycle. In the uncanonical N-terminal region
of the parasite enzyme, we identified several
autophosphorylation sites and probed their role in activity
regulation of PfGSK3. By combining molecular modeling with
experimental small-angle X-ray scattering data, we show that
increased PfGSK3 activity is promoted by conformational
changes in the PfGSK3 N-terminus, triggered by N-terminal
phosphorylation. Our work provides novel insights into the
structure and regulation of the malarial PfGSK3.},
cin = {EMBL-User / EMBL / CSSB-EMBL / CSSB-EMBL-CL},
ddc = {540},
cid = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731 /
I:(DE-H253)CSSB-EMBL-20141216 /
I:(DE-H253)CSSB-EMBL-CL-20210806},
pnm = {6G3 - PETRA III (DESY) (POF4-6G3)},
pid = {G:(DE-HGF)POF4-6G3},
experiment = {EXP:(DE-H253)P-P12-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:35023554},
UT = {WOS:000753051700001},
doi = {10.1042/BCJ20210829},
url = {https://bib-pubdb1.desy.de/record/476470},
}