| pubmed-article:15526162 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15526162 | lifeskim:mentions | umls-concept:C0142661 | lld:lifeskim |
| pubmed-article:15526162 | lifeskim:mentions | umls-concept:C0147545 | lld:lifeskim |
| pubmed-article:15526162 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:15526162 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15526162 | lifeskim:mentions | umls-concept:C0237881 | lld:lifeskim |
| pubmed-article:15526162 | lifeskim:mentions | umls-concept:C0750502 | lld:lifeskim |
| pubmed-article:15526162 | pubmed:issue | 19-20 | lld:pubmed |
| pubmed-article:15526162 | pubmed:dateCreated | 2004-11-4 | lld:pubmed |
| pubmed-article:15526162 | pubmed:abstractText | The polypeptide composition of the U7 small nuclear ribonucleoprotein (snRNP) involved in histone messenger RNA (mRNA) 3' end formation has recently been elucidated. In contrast to spliceosomal snRNPs, which contain a ring-shaped assembly of seven so-called Sm proteins, in the U7 snRNP the Sm proteins D1 and D2 are replaced by U7-specific Sm-like proteins, Lsm10 and Lsm11. This polypeptide composition and the unusual structure of Lsm11, which plays a role in histone RNA processing, represent new themes in the biology of Sm/Lsm proteins. Moreover this structure has important consequences for snRNP assembly that is mediated by two complexes containing the PRMT5 methyltransferase and the SMN (survival of motor neurons) protein, respectively. Finally, the ability to alter this polypeptide composition by a small mutation in U7 snRNA forms the basis for using modified U7 snRNA derivatives to alter specific pre-mRNA splicing events, thereby opening up a new way for antisense gene therapy. | lld:pubmed |
| pubmed-article:15526162 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15526162 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15526162 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15526162 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15526162 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15526162 | pubmed:issn | 1420-682X | lld:pubmed |
| pubmed-article:15526162 | pubmed:author | pubmed-author:SchümperliDD | lld:pubmed |
| pubmed-article:15526162 | pubmed:author | pubmed-author:PillaiR SRS | lld:pubmed |
| pubmed-article:15526162 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15526162 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:15526162 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15526162 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15526162 | pubmed:pagination | 2560-70 | lld:pubmed |
| pubmed-article:15526162 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15526162 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15526162 | pubmed:articleTitle | The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein. | lld:pubmed |
| pubmed-article:15526162 | pubmed:affiliation | Institute of Cell Biology, University of Bern, Baltzerstrasse 4, 3012, Bern, Switzerland. daniel.schuemperli@izb.unibe.ch. | lld:pubmed |
| pubmed-article:15526162 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15526162 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:15526162 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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