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000202103 1001_ $$0P:(DE-Juel1)132020$$aSchünke, Sven$$b0
000202103 245__ $$aStructural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
000202103 260__ $$aBerlin [u.a.]$$bde Gruyter$$c2013
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000202103 520__ $$aCyclic 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.
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000202103 650_7 $$2NLM Chemicals$$aCalcium Channels
000202103 650_7 $$2NLM Chemicals$$aCyclic Nucleotide-Gated Cation Channels
000202103 650_7 $$2NLM Chemicals$$aLigands
000202103 650_7 $$2NLM Chemicals$$aPotassium Channels, Voltage-Gated
000202103 650_7 $$2NLM Chemicals$$aSodium Channels
000202103 650_7 $$0E0399OZS9N$$2NLM Chemicals$$aCyclic AMP
000202103 7001_ $$0P:(DE-Juel1)132023$$aStoldt, Matthias$$b1$$eCorresponding Author$$ufzj
000202103 773__ $$0PERI:(DE-600)1466062-3$$a10.1515/hsz-2013-0228$$gVol. 394, no. 11$$n11$$p1439–1451$$tBiological chemistry$$v394$$x1437-4315$$y2013
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