Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:1838987rdf:typepubmed:Citationlld:pubmed
pubmed-article:1838987lifeskim:mentionsumls-concept:C0010853lld:lifeskim
pubmed-article:1838987lifeskim:mentionsumls-concept:C0521390lld:lifeskim
pubmed-article:1838987lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:1838987lifeskim:mentionsumls-concept:C0679622lld:lifeskim
pubmed-article:1838987lifeskim:mentionsumls-concept:C1548696lld:lifeskim
pubmed-article:1838987lifeskim:mentionsumls-concept:C0205314lld:lifeskim
pubmed-article:1838987pubmed:issue4lld:pubmed
pubmed-article:1838987pubmed:dateCreated1992-4-6lld:pubmed
pubmed-article:1838987pubmed:abstractTextAssociated with the neuronal plasma membrane are cytoskeletal proteins which probably control the specialization of the membrane into axonal and dendritic domains. Specialized isoforms of the proteins spectrin and ankyrin are located in each region and provide molecular mechanisms for locating specific transmembrane proteins at required points. However, spectrin and ankyrin were defined by extensions of the model for the erythrocyte membrane, an analogy unlikely to provide a complete account of the neuronal membrane skeleton. We have defined two new proteins of the neuronal membrane skeleton, designated p103 and A60. p103 is enriched in post-synaptic densities and binds with high affinity to integral membrane proteins--we suggest that it may have a role in linking the cytoskeleton to synaptic glycoproteins. A60 is a 60 kDa axonal protein, which appears to form a lining to the axolemma. It is almost exclusively axonal, although some neurons (such as Purkinje cells) appear to contain it in the cell body and initial dendrite segment. A60 binds both ankyrin and neurofilaments, and may have a role in transmitting information critical to axonal morphology to the membrane.lld:pubmed
pubmed-article:1838987pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:languageenglld:pubmed
pubmed-article:1838987pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:citationSubsetIMlld:pubmed
pubmed-article:1838987pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1838987pubmed:statusMEDLINElld:pubmed
pubmed-article:1838987pubmed:monthNovlld:pubmed
pubmed-article:1838987pubmed:issn0300-5127lld:pubmed
pubmed-article:1838987pubmed:authorpubmed-author:WoodsAAlld:pubmed
pubmed-article:1838987pubmed:authorpubmed-author:BainesA JAJlld:pubmed
pubmed-article:1838987pubmed:authorpubmed-author:HayesN VNVlld:pubmed
pubmed-article:1838987pubmed:authorpubmed-author:RaynerD ADAlld:pubmed
pubmed-article:1838987pubmed:issnTypePrintlld:pubmed
pubmed-article:1838987pubmed:volume19lld:pubmed
pubmed-article:1838987pubmed:ownerNLMlld:pubmed
pubmed-article:1838987pubmed:authorsCompleteYlld:pubmed
pubmed-article:1838987pubmed:pagination1042-8lld:pubmed
pubmed-article:1838987pubmed:dateRevised2009-9-29lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:meshHeadingpubmed-meshheading:1838987-...lld:pubmed
pubmed-article:1838987pubmed:year1991lld:pubmed
pubmed-article:1838987pubmed:articleTitlep103 and A60: novel proteins of the neuronal membrane-associated cytoskeleton.lld:pubmed
pubmed-article:1838987pubmed:affiliationBiological Laboratory, University of Kent, Canterbury, U.K.lld:pubmed
pubmed-article:1838987pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1838987pubmed:publicationTypeReviewlld:pubmed
pubmed-article:1838987pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed