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@ARTICLE{Schnke:202103,
author = {Schünke, Sven and Stoldt, Matthias},
title = {{S}tructural snapshot of cyclic nucleotide binding domains
from cyclic nucleotide-sensitive ion channels.},
journal = {Biological chemistry},
volume = {394},
number = {11},
issn = {1437-4315},
address = {Berlin [u.a.]},
publisher = {de Gruyter},
reportid = {FZJ-2015-04392},
pages = {1439–1451},
year = {2013},
abstract = {Cyclic nucleotide-binding domains (CNBDs) that are present
in various channel proteins play crucial roles in signal
amplification cascades. Although atomic resolution
structures of some of those CNBDs are available, the
detailed mechanism by which they confer cyclic
nucleotide-binding to the ion channel pore remains poorly
understood. In this review, we describe structural insights
about cyclic nucleotide-binding-induced conformational
changes in CNBDs and their potential coupling with channel
gating.},
keywords = {Calcium Channels (NLM Chemicals) / Cyclic Nucleotide-Gated
Cation Channels (NLM Chemicals) / Ligands (NLM Chemicals) /
Potassium Channels, Voltage-Gated (NLM Chemicals) / Sodium
Channels (NLM Chemicals) / Cyclic AMP (NLM Chemicals)},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)36 / PUB:(DE-HGF)16},
pubmed = {pmid:24021595},
UT = {WOS:000325717100008},
doi = {10.1515/hsz-2013-0228},
url = {https://juser.fz-juelich.de/record/202103},
}