| pubmed-article:7506618 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C0392918 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C0129439 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C0026019 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C1522605 | lld:lifeskim |
| pubmed-article:7506618 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7506618 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:7506618 | pubmed:dateCreated | 1994-2-15 | lld:pubmed |
| pubmed-article:7506618 | pubmed:abstractText | The functional topography of the myelin-associated glycoprotein (MAG) was investigated by electron microscopic analysis of rotary-shadowed molecules of a MAG fragment (MAG 90) comprising the five immunoglobulin-like domains of the extracellular part of the molecule. MAG 90 molecules appeared as rod-like structures (18.5 +/- 1.2 nm long and 4.0 +/- 0.8 nm wide) with a globular domain at one end. Antibodies directed against the amino- and carboxy-terminus of MAG 90 interacted with the non-globular terminal region, indicating that the molecule is bent in the globular region with the amino- and carboxy-terminal arms in close apposition to each other. An antibody which interferes with the binding of MAG to neurons interacted predominantly with the globular domain of MAG 90. The fibril-forming collagen types I, III and V bound mainly to the non-globular terminal region of MAG 90, whereas the majority of heparin molecules interacted with the globular region of the molecule. The L2/HNK-1 carbohydrate structure was localized at the non-globular region in the protein fragment comprising the fourth and fifth immunoglobulin-like domains. | lld:pubmed |
| pubmed-article:7506618 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7506618 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7506618 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7506618 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7506618 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7506618 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7506618 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7506618 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7506618 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7506618 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7506618 | pubmed:issn | 0953-816X | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:SchachnerMM | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:DrescherBB | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:SpiessEE | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:ProbstmeierRR | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:FahrigTT | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:KirchhoffFF | lld:pubmed |
| pubmed-article:7506618 | pubmed:author | pubmed-author:Meyer-FrankeA... | lld:pubmed |
| pubmed-article:7506618 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7506618 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7506618 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:7506618 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7506618 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7506618 | pubmed:pagination | 1118-26 | lld:pubmed |
| pubmed-article:7506618 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:meshHeading | pubmed-meshheading:7506618-... | lld:pubmed |
| pubmed-article:7506618 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7506618 | pubmed:articleTitle | Functional topography of the myelin-associated glycoprotein. I. Mapping of domains by electron microscopy. | lld:pubmed |
| pubmed-article:7506618 | pubmed:affiliation | Department of Neurobiology, Swiss Federal Institute of Technology, Zürich. | lld:pubmed |
| pubmed-article:7506618 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7506618 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7506618 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7506618 | lld:pubmed |
