pubmed-article:10624965 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:10624965 | lifeskim:mentions | umls-concept:C2752518 | lld:lifeskim |
pubmed-article:10624965 | lifeskim:mentions | umls-concept:C0682682 | lld:lifeskim |
pubmed-article:10624965 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:10624965 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
pubmed-article:10624965 | lifeskim:mentions | umls-concept:C0392752 | lld:lifeskim |
pubmed-article:10624965 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
pubmed-article:10624965 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:10624965 | pubmed:dateCreated | 2000-1-27 | lld:pubmed |
pubmed-article:10624965 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10624965 | pubmed:abstractText | Rapid conduction in myelinated axons depends on the generation of specialized subcellular domains to which different sets of ion channels are localized. Here, we describe the identification of Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), and show that this neurexin-like protein and the closely related molecule Caspr/Paranodin demarcate distinct subdomains in myelinated axons. While contactin-associated protein (Caspr) is present at the paranodal junctions, Caspr2 is precisely colocalized with Shaker-like K+ channels in the juxtaparanodal region. We further show that Caspr2 specifically associates with Kv1.1, Kv1.2, and their Kvbeta2 subunit. This association involves the C-terminal sequence of Caspr2, which contains a putative PDZ binding site. These results suggest a role for Caspr family members in the local differentiation of the axon into distinct functional subdomains. | lld:pubmed |
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pubmed-article:10624965 | pubmed:language | eng | lld:pubmed |
pubmed-article:10624965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10624965 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10624965 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10624965 | pubmed:month | Dec | lld:pubmed |
pubmed-article:10624965 | pubmed:issn | 0896-6273 | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:ShragerPP | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:MartinezRR | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:PoliakSS | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:PelesEE | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:SalzerJ LJL | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:TrimmerJ SJS | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:EinheberSS | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:GollanLL | lld:pubmed |
pubmed-article:10624965 | pubmed:author | pubmed-author:CusterAA | lld:pubmed |
pubmed-article:10624965 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10624965 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:10624965 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10624965 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10624965 | pubmed:pagination | 1037-47 | lld:pubmed |
pubmed-article:10624965 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:10624965 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10624965 | pubmed:articleTitle | Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels. | lld:pubmed |
pubmed-article:10624965 | pubmed:affiliation | Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot, Israel. | lld:pubmed |
pubmed-article:10624965 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10624965 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10624965 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:10624965 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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