Source:http://linkedlifedata.com/resource/pubmed/id/12441251
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-11-20
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pubmed:abstractText |
Although many RNA-protein complexes or ribonucleoproteins (RNPs) assemble spontaneously in vitro, little is known about how they form in the environment of a living cell. Insight into RNP assembly has come unexpectedly from functional analyses of the survival motor neuron (SMN) protein, a gene product that is affected in the neuromuscular disease spinal muscular atrophy. These studies show that the assembly of spliceosomal U-rich small nuclear RNPs in vivo depends on the activity of two large protein complexes, one of which contains the SMN protein. These complexes might also facilitate the assembly of other cellular RNPs.
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pubmed:language |
eng
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response...,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMN Complex Proteins
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pubmed:status |
MEDLINE
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pubmed:author | |
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
472-8
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pubmed:dateRevised |
2008-11-21
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pubmed:articleTitle |
SMN-mediated assembly of RNPs: a complex story.
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pubmed:affiliation |
Max-Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152,., Martinsried, Germany.
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