Extracellular protons in the range of 10−9 to 10−5 M effectively suppressed Na+ current (K 1/2=10... more Extracellular protons in the range of 10−9 to 10−5 M effectively suppressed Na+ current (K 1/2=10−6.1) through the bovine retinal guanosine 3′,5′‐cyclic mononucleotide‐gated ion channel expressed in Xenopus oocytes. The reduction of channel current was mediated by a single glutamate residue (Glu363) within the pore‐forming region of the channel, also involved in extracellular divalent cation binding. Increasing the concentration of extracellular proton decreased the binding affinity of the extracellular divalent cation (e.g. Sr2+) and the large difference of binding affinity previously observed between the wild‐type and E363D mutant channel disappeared. These results indicate that the permeation characteristics of cyclic nucleotide‐gated ion channel can be altered by extracellular pH through a single acidic residue in the channel conduction pathway.
Summary: The Heart and Calcium functional Network (HCNet) database is a collection of functional ... more Summary: The Heart and Calcium functional Network (HCNet) database is a collection of functional gene modules calculated from the microarray data compendium available from the GEO database. It is a specialized database designed to assist experimentalists for cardiac calcium signaling research by providing the pre-calculated gene clusters and their potential correlation network in heart. In the current release of HCNet, 57 functional modules from 786 target genes obtained by a bi-clustering analysis of 381 microarray datasets are available. Detailed information of the clusters such as expression profiles, network diagrams is provided in two categories, heart-specific genes and heart-specific genes along with calcium toolkit genes. Overrepresented gene ontological categories and transcription factors in each cluster are also provided to infer the biological implications of the detected functional modules. Availability: HCNet is available at Contact: dhkim@gist.ac.kr
Extracellular protons in the range of 10−9 to 10−5 M effectively suppressed Na+ current (K 1/2=10... more Extracellular protons in the range of 10−9 to 10−5 M effectively suppressed Na+ current (K 1/2=10−6.1) through the bovine retinal guanosine 3′,5′‐cyclic mononucleotide‐gated ion channel expressed in Xenopus oocytes. The reduction of channel current was mediated by a single glutamate residue (Glu363) within the pore‐forming region of the channel, also involved in extracellular divalent cation binding. Increasing the concentration of extracellular proton decreased the binding affinity of the extracellular divalent cation (e.g. Sr2+) and the large difference of binding affinity previously observed between the wild‐type and E363D mutant channel disappeared. These results indicate that the permeation characteristics of cyclic nucleotide‐gated ion channel can be altered by extracellular pH through a single acidic residue in the channel conduction pathway.
Summary: The Heart and Calcium functional Network (HCNet) database is a collection of functional ... more Summary: The Heart and Calcium functional Network (HCNet) database is a collection of functional gene modules calculated from the microarray data compendium available from the GEO database. It is a specialized database designed to assist experimentalists for cardiac calcium signaling research by providing the pre-calculated gene clusters and their potential correlation network in heart. In the current release of HCNet, 57 functional modules from 786 target genes obtained by a bi-clustering analysis of 381 microarray datasets are available. Detailed information of the clusters such as expression profiles, network diagrams is provided in two categories, heart-specific genes and heart-specific genes along with calcium toolkit genes. Overrepresented gene ontological categories and transcription factors in each cluster are also provided to infer the biological implications of the detected functional modules. Availability: HCNet is available at Contact: dhkim@gist.ac.kr
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