| pubmed-article:11856755 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11856755 | lifeskim:mentions | umls-concept:C0205341 | lld:lifeskim |
| pubmed-article:11856755 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:11856755 | lifeskim:mentions | umls-concept:C1511997 | lld:lifeskim |
| pubmed-article:11856755 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:11856755 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:11856755 | pubmed:dateCreated | 2002-4-29 | lld:pubmed |
| pubmed-article:11856755 | pubmed:abstractText | Cadherin is a cell adhesion molecule crucial for epithelial and endothelial cell monolayer integrity. The previously solved x-ray crystallographic structure of the E-CAD12 cis-dimer displayed an unpaired Cys(9), which protruded away from the Cys(9) on the other protomer. To investigate the possible biological function of Cys(9) within the first repeat (the E-cadherin-derived N-terminal repeat), E-CAD1 was overexpressed and secreted into the periplasmic space of Escherichia coli cells. Recombinant E-CAD1 produced a mixed monomer and dimer in an equilibrium fashion. The dimer was linked by a disulfide through Cys(9) pairing. Analysis by high pressure liquid chromatography and electron microscopy suggested the existence of oligomeric complexes. Mutation at Trp(2) appears to indicate that these oligomeric complexes trans-dimerize. Interestingly, mutation of Cys(9) affected not only the cis-dimerization, but also the trans-oligomerization of E-CAD1. Accordingly, it is plausible that, under oxidative stress, the homophilic interactions of E-cadherin through E-CAD1 may be promoted and stabilized by this disulfide bond. | lld:pubmed |
| pubmed-article:11856755 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11856755 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11856755 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11856755 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11856755 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11856755 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11856755 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11856755 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11856755 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11856755 | pubmed:month | May | lld:pubmed |
| pubmed-article:11856755 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:SiahaanTeruna... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:UrbauerJeffre... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:KuczeraKrzysz... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:MakagiansarIr... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:NguyenPhuong... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:IkesueAtsutos... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:DentlerWillia... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:GalevaNadezhd... | lld:pubmed |
| pubmed-article:11856755 | pubmed:author | pubmed-author:AltermanMicha... | lld:pubmed |
| pubmed-article:11856755 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11856755 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:11856755 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11856755 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11856755 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11856755 | pubmed:pagination | 16002-10 | lld:pubmed |
| pubmed-article:11856755 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
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| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
| pubmed-article:11856755 | pubmed:meshHeading | pubmed-meshheading:11856755... | lld:pubmed |
| pubmed-article:11856755 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11856755 | pubmed:articleTitle | Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat. | lld:pubmed |
| pubmed-article:11856755 | pubmed:affiliation | Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047, USA. | lld:pubmed |
| pubmed-article:11856755 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11856755 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11856755 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:999 | entrezgene:pubmed | pubmed-article:11856755 | lld:entrezgene |
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