rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
2005-8-26
|
pubmed:abstractText |
The coxsackievirus and adenovirus receptor (CAR) is a cell surface protein that is proposed to be involved in cell-cell adhesion. Based on a yeast two-hybrid screen, co-immunoprecipitation and binding experiments, the intracellular tail of CAR was found to interact both in vivo and in vitro with the Ligand-of-Numb Protein-X2 (LNX2). The interacting domains between the two proteins were identified by truncation analyses and affinity chromatography. CAR and LNX2 protein expression in embryonic mouse tissues was analyzed by immunohistochemistry. The results suggest that CAR is a partner in a protein complex organized at specific subcellular sites by LNX2.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0014-4827
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
309
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
110-20
|
pubmed:dateRevised |
2011-7-1
|
pubmed:meshHeading |
pubmed-meshheading:15979067-Adenoviridae,
pubmed-meshheading:15979067-Amino Acid Sequence,
pubmed-meshheading:15979067-Animals,
pubmed-meshheading:15979067-Binding Sites,
pubmed-meshheading:15979067-Carrier Proteins,
pubmed-meshheading:15979067-Embryo, Mammalian,
pubmed-meshheading:15979067-Enterovirus,
pubmed-meshheading:15979067-Gene Expression Regulation, Developmental,
pubmed-meshheading:15979067-Humans,
pubmed-meshheading:15979067-Immunohistochemistry,
pubmed-meshheading:15979067-Membrane Proteins,
pubmed-meshheading:15979067-Mice,
pubmed-meshheading:15979067-Molecular Sequence Data,
pubmed-meshheading:15979067-Protein Binding,
pubmed-meshheading:15979067-Protein Structure, Tertiary,
pubmed-meshheading:15979067-Receptors, Virus,
pubmed-meshheading:15979067-Tight Junctions
|
pubmed:year |
2005
|
pubmed:articleTitle |
The cell surface protein coxsackie- and adenovirus receptor (CAR) directly associates with the Ligand-of-Numb Protein-X2 (LNX2).
|
pubmed:affiliation |
Ludwig Institute for Cancer Research, Stockholm Branch, Karolinska Intitutet, Box 240, SE-17177 Stockholm, Sweden.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|