pubmed-article:20584905 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20584905 | lifeskim:mentions | umls-concept:C0032824 | lld:lifeskim |
pubmed-article:20584905 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:20584905 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:20584905 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:20584905 | lifeskim:mentions | umls-concept:C1882151 | lld:lifeskim |
pubmed-article:20584905 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
pubmed-article:20584905 | pubmed:issue | 36 | lld:pubmed |
pubmed-article:20584905 | pubmed:dateCreated | 2010-8-30 | lld:pubmed |
pubmed-article:20584905 | pubmed:abstractText | Kv7 channels, especially Kv7.2 (KCNQ2) and Kv7.3 (KCNQ3), are key determinants for membrane excitability in the brain. Some chemical modulators of KCNQ channels are in development for use as anti-epileptic drugs, such as retigabine (D-23129, N-(2-amino-4-(4-fluorobenzylamino)-phenyl)), which was recently approved for clinical use. In addition, several other compounds were also reported to potentiate activity of the Kv7 channels. It is therefore of interest to investigate compound-channel interactions, so that more insights may be gained to aid future development of therapeutics. We have conducted a screen of 20,000 compounds for KCNQ2 potentiators using rubidium flux combined with atomic absorption spectrometry. Here, we report the characterization of a series of new structures that display isoform specificity and induce a marked reduction of deactivation distinct from that of retigabine. Furthermore, KCNQ2(W236L), a previously reported mutation that abolishes sensitivity to retigabine, remains fully sensitive to these compounds. This result, together with mutagenesis and other studies, suggests that the reported compounds confer a unique mode of action and involve new molecular determinants on the channel protein, consistent with the idea of recognizing a new site on channel protein. | lld:pubmed |
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pubmed-article:20584905 | pubmed:language | eng | lld:pubmed |
pubmed-article:20584905 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20584905 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20584905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20584905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20584905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20584905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20584905 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20584905 | pubmed:month | Sep | lld:pubmed |
pubmed-article:20584905 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:VighB JBJ | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:KoçLL | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:WuMengM | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:SunHaiyanH | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:XiongQiaojieQ | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:ZuLiansuoL | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:ZhangYinanY | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:GaoZhaobingZ | lld:pubmed |
pubmed-article:20584905 | pubmed:author | pubmed-author:ZhangTangzhiT | lld:pubmed |
pubmed-article:20584905 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20584905 | pubmed:day | 3 | lld:pubmed |
pubmed-article:20584905 | pubmed:volume | 285 | lld:pubmed |
pubmed-article:20584905 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20584905 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20584905 | pubmed:pagination | 28322-32 | lld:pubmed |
pubmed-article:20584905 | pubmed:dateRevised | 2011-9-13 | lld:pubmed |
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pubmed-article:20584905 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20584905 | pubmed:articleTitle | Isoform-specific prolongation of Kv7 (KCNQ) potassium channel opening mediated by new molecular determinants for drug-channel interactions. | lld:pubmed |
pubmed-article:20584905 | pubmed:affiliation | Department of Neuroscience, High Throughput Biology Center, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, USA. | lld:pubmed |
pubmed-article:20584905 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20584905 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:20584905 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20584905 | lld:pubmed |