| pubmed-article:2469649 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0009013 | lld:lifeskim |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0034792 | lld:lifeskim |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0752087 | lld:lifeskim |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0024779 | lld:lifeskim |
| pubmed-article:2469649 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:2469649 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2469649 | pubmed:dateCreated | 1989-6-12 | lld:pubmed |
| pubmed-article:2469649 | pubmed:abstractText | Myasthenia gravis (MG) is an autoimmune disease of man caused by antibodies directed against the acetylcholine receptor (AChR). In the experimental model of MG in mice, murine experimental autoimmune myasthenia gravis (EAMG), an anti-AChR immune response is induced by immunization with Torpedo AChR, and anti-AChR antibodies. AChR-sensitized T cells, and neuromuscular dysfunction result. The production of antibodies to AChR is thymus-dependent. In order to define the epitopes of the AChR identified by AChR-specific T cells, we generated T cell populations and T cell hybridoma clones and tested their reactivity to synthetic uniform-sized overlapping peptides representing the entire extracellular portion of the alpha-chain of the AChR. The predominant reactivity of the T cell clones and the parent lines was to a peptide corresponding to residues 146-162 of Torpedo AChR. This data is consistent with a highly limited recognition of AChR determinants in murine EAMG by AChR-specific T cells. | lld:pubmed |
| pubmed-article:2469649 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2469649 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2469649 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2469649 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2469649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2469649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2469649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2469649 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2469649 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2469649 | pubmed:issn | 0165-2478 | lld:pubmed |
| pubmed-article:2469649 | pubmed:author | pubmed-author:AtassiM ZMZ | lld:pubmed |
| pubmed-article:2469649 | pubmed:author | pubmed-author:KantorF SFS | lld:pubmed |
| pubmed-article:2469649 | pubmed:author | pubmed-author:PachnerA RAR | lld:pubmed |
| pubmed-article:2469649 | pubmed:author | pubmed-author:Mulac-Jericev... | lld:pubmed |
| pubmed-article:2469649 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2469649 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:2469649 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2469649 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2469649 | pubmed:pagination | 199-204 | lld:pubmed |
| pubmed-article:2469649 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:meshHeading | pubmed-meshheading:2469649-... | lld:pubmed |
| pubmed-article:2469649 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2469649 | pubmed:articleTitle | An immunodominant site of acetylcholine receptor in experimental myasthenia mapped with T lymphocyte clones and synthetic peptides. | lld:pubmed |
| pubmed-article:2469649 | pubmed:affiliation | Department of Neurology, Georgetown University Hospital, Washington, DC 20007. | lld:pubmed |
| pubmed-article:2469649 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2469649 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2469649 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2469649 | lld:pubmed |
