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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-8-10
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pubmed:abstractText |
The nicotinic acetylcholine receptors (AChR) are presently the best-characterized neurotransmitter receptors. They are pentamers of homologous or identical subunits, symmetrically arranged to form a transmembrane cation channel. The AChR subunits form a family of homologous proteins, derived from a common ancestor. An autoimmune response to muscle AChR causes the disease myasthenia gravis. This review summarizes recent developments in the understanding of the AChR structure and its molecular recognition by the immune system in myasthenia.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1040-9238
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
69-123
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8026215-Amino Acid Sequence,
pubmed-meshheading:8026215-Humans,
pubmed-meshheading:8026215-Ion Channel Gating,
pubmed-meshheading:8026215-Molecular Sequence Data,
pubmed-meshheading:8026215-Muscles,
pubmed-meshheading:8026215-Myasthenia Gravis,
pubmed-meshheading:8026215-Receptors, Nicotinic,
pubmed-meshheading:8026215-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
The nicotinic acetylcholine receptor: structure and autoimmune pathology.
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pubmed:affiliation |
Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul 55108.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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