Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:20868680rdf:typepubmed:Citationlld:pubmed
pubmed-article:20868680lifeskim:mentionsumls-concept:C0019360lld:lifeskim
pubmed-article:20868680lifeskim:mentionsumls-concept:C0020792lld:lifeskim
pubmed-article:20868680lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:20868680lifeskim:mentionsumls-concept:C0332281lld:lifeskim
pubmed-article:20868680lifeskim:mentionsumls-concept:C1423674lld:lifeskim
pubmed-article:20868680lifeskim:mentionsumls-concept:C0679622lld:lifeskim
pubmed-article:20868680lifeskim:mentionsumls-concept:C0205314lld:lifeskim
pubmed-article:20868680pubmed:issue19lld:pubmed
pubmed-article:20868680pubmed:dateCreated2010-10-25lld:pubmed
pubmed-article:20868680pubmed:abstractTextWith the aim of discovering new molecular interactions of the tight junction protein ZO-2, a two-hybrid screen was performed on a human kidney cDNA library using as bait the middle segment of ZO-2. Through this assay we identified a 24-kDa novel protein herein named ZASP for ZO-2 associated speckle protein. ZO-2/ZASP interaction further confirmed by pull down and immunoprecipitation experiments, requires the presence of the intact PDZ binding motif SQV of ZASP and the third PDZ domain of ZO-2. ZASP mRNA and protein are present in the kidney and in several epithelial cell lines. Endogenous ZASP is expressed primarily in nuclear speckles in co-localization with splicing factor SC-35. Nocodazole treatment and wash out reveals that ZASP disappears from the nucleus during mitosis in accordance with speckle disassembly during metaphase. ZASP amino acid sequence exhibits a canonical nuclear exportation signal and in agreement the protein exits the nucleus through a process mediated by exportin/CRM1. ZASP over-expression blocks the inhibitory activity of ZO-2 on cyclin D1 gene transcription and protein expression. The identification of ZASP helps to unfold the complex nuclear molecular arrays that form on ZO-2 scaffolds.lld:pubmed
pubmed-article:20868680pubmed:languageenglld:pubmed
pubmed-article:20868680pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:citationSubsetIMlld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:20868680pubmed:statusMEDLINElld:pubmed
pubmed-article:20868680pubmed:monthNovlld:pubmed
pubmed-article:20868680pubmed:issn1090-2422lld:pubmed
pubmed-article:20868680pubmed:authorpubmed-author:González-Mari...lld:pubmed
pubmed-article:20868680pubmed:authorpubmed-author:HuertaMiriamMlld:pubmed
pubmed-article:20868680pubmed:authorpubmed-author:Lopez-Bayghen...lld:pubmed
pubmed-article:20868680pubmed:authorpubmed-author:AlarcónLourde...lld:pubmed
pubmed-article:20868680pubmed:authorpubmed-author:LechugaSusana...lld:pubmed
pubmed-article:20868680pubmed:authorpubmed-author:SolanoJesúsJlld:pubmed
pubmed-article:20868680pubmed:copyrightInfoCopyright © 2010 Elsevier Inc. All rights reserved.lld:pubmed
pubmed-article:20868680pubmed:issnTypeElectroniclld:pubmed
pubmed-article:20868680pubmed:day15lld:pubmed
pubmed-article:20868680pubmed:volume316lld:pubmed
pubmed-article:20868680pubmed:ownerNLMlld:pubmed
pubmed-article:20868680pubmed:authorsCompleteYlld:pubmed
pubmed-article:20868680pubmed:pagination3124-39lld:pubmed
pubmed-article:20868680pubmed:dateRevised2011-11-17lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:meshHeadingpubmed-meshheading:20868680...lld:pubmed
pubmed-article:20868680pubmed:year2010lld:pubmed
pubmed-article:20868680pubmed:articleTitleIdentification of ZASP, a novel protein associated to Zona occludens-2.lld:pubmed
pubmed-article:20868680pubmed:affiliationDepartment of Physiology, Biophysics and Neuroscience, Center for Research and Advanced Studies (Cinvestav), México, DF 07360, Mexico.lld:pubmed
pubmed-article:20868680pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20868680pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:9414entrezgene:pubmedpubmed-article:20868680lld:entrezgene
entrez-gene:403854entrezgene:pubmedpubmed-article:20868680lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:20868680lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:20868680lld:entrezgene