pubmed-article:2444603 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C0282587 | lld:lifeskim |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C0129439 | lld:lifeskim |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C1412716 | lld:lifeskim |
pubmed-article:2444603 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:2444603 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:2444603 | pubmed:dateCreated | 1987-12-3 | lld:pubmed |
pubmed-article:2444603 | pubmed:abstractText | A monoclonal antibody to the myelin-associated glycoprotein (MAG) was prepared and characterized to probe for the involvement of MAG in cell surface interactions among neural cells in vitro. The antibody reacts specifically with oligodendrocyte cell surface and myelin-rich brain regions as expected from previous investigations. Not all O4 antigen-positive oligodendrocytes express MAG in vitro. Fab fragments of the antibody interfere with neuron to oligodendrocyte and oligodendrocyte to oligodendrocyte adhesion, but not with oligodendrocyte to astrocyte adhesion. MAG-containing liposomes bind to the cell surfaces of the appropriate target cells by a mechanism that is specifically inhibitable by Fab fragments of monoclonal MAG antibodies, demonstrating that MAG is a neural cell adhesion molecule. | lld:pubmed |
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pubmed-article:2444603 | pubmed:language | eng | lld:pubmed |
pubmed-article:2444603 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2444603 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2444603 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2444603 | pubmed:month | Oct | lld:pubmed |
pubmed-article:2444603 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:2444603 | pubmed:author | pubmed-author:SchachnerMM | lld:pubmed |
pubmed-article:2444603 | pubmed:author | pubmed-author:LandaCC | lld:pubmed |
pubmed-article:2444603 | pubmed:author | pubmed-author:PoltorakMM | lld:pubmed |
pubmed-article:2444603 | pubmed:author | pubmed-author:FahrigTT | lld:pubmed |
pubmed-article:2444603 | pubmed:author | pubmed-author:SadoulRR | lld:pubmed |
pubmed-article:2444603 | pubmed:author | pubmed-author:KeilhauerGG | lld:pubmed |
pubmed-article:2444603 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2444603 | pubmed:volume | 105 | lld:pubmed |
pubmed-article:2444603 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2444603 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2444603 | pubmed:pagination | 1893-9 | lld:pubmed |
pubmed-article:2444603 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2444603 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:2444603 | pubmed:articleTitle | Myelin-associated glycoprotein, a member of the L2/HNK-1 family of neural cell adhesion molecules, is involved in neuron-oligodendrocyte and oligodendrocyte-oligodendrocyte interaction. | lld:pubmed |
pubmed-article:2444603 | pubmed:affiliation | Department of Neurobiology, University of Heidelberg, Federal Republic of Germany. | lld:pubmed |
pubmed-article:2444603 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2444603 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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