| pubmed-article:6201617 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6201617 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
| pubmed-article:6201617 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:6201617 | lifeskim:mentions | umls-concept:C0035544 | lld:lifeskim |
| pubmed-article:6201617 | lifeskim:mentions | umls-concept:C0041525 | lld:lifeskim |
| pubmed-article:6201617 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:6201617 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:6201617 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6201617 | pubmed:dateCreated | 1984-6-14 | lld:pubmed |
| pubmed-article:6201617 | pubmed:abstractText | U1 small nuclear RNA is thought to be involved in messenger RNA splicing by binding to complementary sequences in pre-mRNA. We have investigated intermolecular base-pairing between pre-mRNA (hnRNA) and U1 small nuclear RNA by psoralen crosslinking in situ, with emphasis on ribonucleoprotein structure. HeLa cells were pulse-labeled with [3H]uridine under conditions in which hnRNA is preferentially labeled. Isolated nuclei were treated with aminomethyltrioxsalen , which produces interstrand crosslinks at sites of base-pairing between hnRNA and U1 RNA. hnRNA-ribonucleoprotein (hnRNP) particles were isolated in sucrose gradients containing 50% formamide, to dissociate non-crosslinked U1 RNA, and then analyzed by immunoaffinity chromatography using a human autoantibody that is specific for the ribonucleoprotein form of U1 RNA (anti-U1 RNP). After psoralen crosslinking, pulse-labeled hnRNA in hnRNP particles reproducibly bound to anti-U1 RNP. The amount of hnRNA bound to anti-U1 RNP was reduced 80 to 85% when psoralen crosslinking of nuclei was omitted, or if the crosslinks between U1 RNA and hnRNA were photo-reversed prior to immunoaffinity chromatography. Analysis of the proteins bound to anti-U1 RNP after crosslink reversal revealed polypeptides having molecular weights similar to those previously described for U1 RNP. These proteins did not bind to control, non-immune human immunoglobulin G. These results indicate that the subset of nuclear U1 RNA that is base-paired with hnRNA at a given time in the cell is a ribonucleoprotein. This raises the possibility that these proteins, as well as U1 RNA itself, may participate in pre-mRNA splice site recognition by U1 RNP. | lld:pubmed |
| pubmed-article:6201617 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6201617 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6201617 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6201617 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:6201617 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:6201617 | pubmed:author | pubmed-author:SetyonoBB | lld:pubmed |
| pubmed-article:6201617 | pubmed:author | pubmed-author:PedersonTT | lld:pubmed |
| pubmed-article:6201617 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6201617 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:6201617 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:6201617 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6201617 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6201617 | pubmed:pagination | 285-95 | lld:pubmed |
| pubmed-article:6201617 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:6201617 | pubmed:meshHeading | pubmed-meshheading:6201617-... | lld:pubmed |
| pubmed-article:6201617 | pubmed:meshHeading | pubmed-meshheading:6201617-... | lld:pubmed |
| pubmed-article:6201617 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6201617 | pubmed:articleTitle | Ribonucleoprotein organization of eukaryotic RNA. XXX. Evidence that U1 small nuclear RNA is a ribonucleoprotein when base-paired with pre-messenger RNA in vivo. | lld:pubmed |
| pubmed-article:6201617 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6201617 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6201617 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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