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000057477 0247_ $$2DOI$$a10.1038/sj.embor.7401025
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000057477 084__ $$2WoS$$aBiochemistry & Molecular Biology
000057477 084__ $$2WoS$$aCell Biology
000057477 1001_ $$0P:(DE-Juel1)VDB69395$$aCukkemane, A.$$b0$$uFZJ
000057477 245__ $$aSubunits act independently in a cyclic nucleotide-activated K+ channel
000057477 260__ $$aLondon [u.a.]$$bNature Publishing Group$$c2007
000057477 300__ $$a749 - 755
000057477 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000057477 440_0 $$012322$$aEMBO Reports$$v8$$x1469-221X$$y8
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000057477 520__ $$aIon channels gated by cyclic nucleotides have crucial roles in neuronal excitability and signal transduction of sensory neurons. Here, we studied ligand binding of a cyclic nucleotide-activated K(+) channel from Mesorhizobium loti and its isolated cyclic nucleotide-binding domain. The channel and the binding domain alone bind cyclic AMP with similar affinity in a non-cooperative manner. The cAMP sensitivities of binding and activation coincide. Thus, each subunit in the tetrameric channel acts independently of the others. The binding and gating properties of the bacterial channel are distinctively different from those of eukaryotic cyclic nucleotide-gated channels.
000057477 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000057477 588__ $$aDataset connected to Web of Science, Pubmed
000057477 650_2 $$2MeSH$$aAlphaproteobacteria: metabolism
000057477 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000057477 650_2 $$2MeSH$$aBacterial Proteins: genetics
000057477 650_2 $$2MeSH$$aCyclic AMP: chemistry
000057477 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: chemistry
000057477 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: genetics
000057477 650_2 $$2MeSH$$aLigands
000057477 650_2 $$2MeSH$$aPotassium Channels: chemistry
000057477 650_2 $$2MeSH$$aPotassium Channels: genetics
000057477 650_2 $$2MeSH$$aProtein Structure, Tertiary
000057477 650_2 $$2MeSH$$aProtein Subunits: chemistry
000057477 650_2 $$2MeSH$$aSpectrometry, Fluorescence
000057477 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000057477 650_7 $$00$$2NLM Chemicals$$aCyclic Nucleotide-Gated Cation Channels
000057477 650_7 $$00$$2NLM Chemicals$$aLigands
000057477 650_7 $$00$$2NLM Chemicals$$aPotassium Channels
000057477 650_7 $$00$$2NLM Chemicals$$aProtein Subunits
000057477 650_7 $$060-92-4$$2NLM Chemicals$$aCyclic AMP
000057477 650_7 $$2WoSType$$aJ
000057477 65320 $$2Author$$acyclic nucleotides
000057477 65320 $$2Author$$afluorescence assay
000057477 65320 $$2Author$$aion channels
000057477 65320 $$2Author$$aITC
000057477 65320 $$2Author$$asignalling
000057477 7001_ $$0P:(DE-Juel1)VDB64412$$aGrüter, B.$$b1$$uFZJ
000057477 7001_ $$0P:(DE-Juel1)VDB15802$$aNovak, K.$$b2$$uFZJ
000057477 7001_ $$0P:(DE-Juel1)131924$$aGensch, T.$$b3$$uFZJ
000057477 7001_ $$0P:(DE-Juel1)VDB22199$$aBönigk, W.$$b4$$uFZJ
000057477 7001_ $$0P:(DE-Juel1)VDB2886$$aGerharz, T.$$b5$$uFZJ
000057477 7001_ $$0P:(DE-Juel1)VDB728$$aKaupp, U. B.$$b6$$uFZJ
000057477 7001_ $$0P:(DE-Juel1)VDB1505$$aSeifert, R.$$b7$$uFZJ
000057477 773__ $$0PERI:(DE-600)2025376-X$$a10.1038/sj.embor.7401025$$gVol. 8, p. 749 - 755$$p749 - 755$$q8<749 - 755$$tEMBO reports$$v8$$x1469-221X$$y2007
000057477 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1978089
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000057477 9141_ $$y2007
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000057477 9201_ $$0I:(DE-Juel1)VDB804$$d31.12.2008$$gINB$$kINB-1$$lZelluläre Biophysik$$x0
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