| pubmed-article:12239213 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0682701 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0042479 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0949653 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0060240 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0036451 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C0521116 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:12239213 | lifeskim:mentions | umls-concept:C1005220 | lld:lifeskim |
| pubmed-article:12239213 | pubmed:dateCreated | 2002-11-26 | lld:pubmed |
| pubmed-article:12239213 | pubmed:abstractText | The biophysical properties of small conductance Ca(2+)-activated K(+) (SK) channels are well suited to underlie afterhyperpolarizations (AHPs) shaping the firing patterns of a conspicuous number of central and peripheral neurons. We have identified a new scorpion toxin (tamapin) that binds to SK channels with high affinity and inhibits SK channel-mediated currents in pyramidal neurons of the hippocampus as well as in cell lines expressing distinct SK channel subunits. This toxin distinguished between the SK channels underlying the apamin-sensitive I(AHP) and the Ca(2+)-activated K(+) channels mediating the slow I(AHP) (sI(AHP)) in hippocampal neurons. Compared with related scorpion toxins, tamapin displayed a unique, remarkable selectivity for SK2 versus SK1 ( approximately 1750-fold) and SK3 ( approximately 70-fold) channels and is the most potent SK2 channel blocker characterized so far (IC(50) for SK2 channels = 24 pm). Tamapin will facilitate the characterization of the subunit composition of native SK channels and help determine their involvement in electrical and biochemical signaling. | lld:pubmed |
| pubmed-article:12239213 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12239213 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12239213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12239213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12239213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12239213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12239213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12239213 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:GadreS VSV | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:SapatnekarS... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:JosephJeremia... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:KiniR... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:StockerMartin... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:PedarzaniPaol... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:JeyaseelanKan... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:D'hoedtDieter... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:DoortyKevina... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:WadsworthJona... | lld:pubmed |
| pubmed-article:12239213 | pubmed:author | pubmed-author:StrongPeter... | lld:pubmed |
| pubmed-article:12239213 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12239213 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12239213 | pubmed:pagination | 46101-9 | lld:pubmed |
| pubmed-article:12239213 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12239213 | pubmed:articleTitle | Tamapin, a venom peptide from the Indian red scorpion (Mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and afterhyperpolarization currents in central neurons. | lld:pubmed |
| pubmed-article:12239213 | pubmed:affiliation | Department of Physiology, University College London, London WC1E 6BT, United Kingdom. | lld:pubmed |
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