| pubmed-article:8654359 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C0050989 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1708096 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1312042 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8654359 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8654359 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:8654359 | pubmed:dateCreated | 1996-7-30 | lld:pubmed |
| pubmed-article:8654359 | pubmed:abstractText | Agrin induces both phosphorylation and aggregation of nicotinic acetylcholine receptors (AChRs) when added to myotubes in culture, apparently by binding to a specific receptor on the myotube surface. One such agrin receptor is alpha-dystroglycan, although binding to alpha-dystroglycan appears not to mediate AChR aggregation. To determine whether agrin-induced AChR phosphorylation is mediated by alpha-dystroglycan or by a different agrin receptor, fragments of recombinant agrin that differ in affinity for alpha-dystroglycan were examined for their ability to induce AChR phosphorylation and aggregation in mouse C2 myotubes. The carboxy-terminal 95 kDa agrin fragment agrin-c95(A0B0), which binds to alpha-dystroglycan with high affinity, failed to induce AChR phosphorylation and aggregation. In contrast, agrin-c95(A4B8) which binds less strongly to alpha-dystroglycan, induced both phosphorylation and aggregation, as did a small 21 kDa fragment of agrin, agrin-c21(B8), that completely lacks the binding domain for alpha-dystroglycan. We conclude that agrin-induced AChR phosphorylation and aggregation are triggered by an agrin receptor that is distinct from alpha-dystroglycan. | lld:pubmed |
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| pubmed-article:8654359 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8654359 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8654359 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8654359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8654359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8654359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8654359 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8654359 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8654359 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8654359 | pubmed:author | pubmed-author:WallaceB GBG | lld:pubmed |
| pubmed-article:8654359 | pubmed:author | pubmed-author:RueggM AMA | lld:pubmed |
| pubmed-article:8654359 | pubmed:author | pubmed-author:GesemannMM | lld:pubmed |
| pubmed-article:8654359 | pubmed:author | pubmed-author:MeierTT | lld:pubmed |
| pubmed-article:8654359 | pubmed:author | pubmed-author:CavalloPP | lld:pubmed |
| pubmed-article:8654359 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8654359 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:8654359 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:8654359 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8654359 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8654359 | pubmed:pagination | 2625-31 | lld:pubmed |
| pubmed-article:8654359 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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