| pubmed-article:9659908 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0032592 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0066030 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0016667 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0205082 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C1414649 | lld:lifeskim |
| pubmed-article:9659908 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:9659908 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9659908 | pubmed:dateCreated | 1998-7-24 | lld:pubmed |
| pubmed-article:9659908 | pubmed:abstractText | Fragile X mental retardation is caused by the lack of FMRP, a selective RNA-binding protein associated with ribosomes. A missense mutation, I304N, has been found to result in an unusually severe phenotype. We show here that normal FMRP associates with elongating polyribosomes via large mRNP particles. Despite normal expression and cytoplasmic mRNA association, the I304N FMRP is incorporated into abnormal mRNP particles that are not associated with polyribosomes. These data indicate that association of FMRP with polyribosomes must be functionally important and imply that the mechanism of the severe phenotype in the I304N patient lies in the sequestration of bound mRNAs in nontranslatable mRNP particles. In the absence of FMRP, these same mRNAs may be partially translated via alternative mRNPs, although perhaps abnormally localized or regulated, resulting in typical fragile X syndrome. | lld:pubmed |
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| pubmed-article:9659908 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9659908 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9659908 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9659908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9659908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9659908 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9659908 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9659908 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:9659908 | pubmed:author | pubmed-author:BrownVV | lld:pubmed |
| pubmed-article:9659908 | pubmed:author | pubmed-author:FengYY | lld:pubmed |
| pubmed-article:9659908 | pubmed:author | pubmed-author:WarrenS TST | lld:pubmed |
| pubmed-article:9659908 | pubmed:author | pubmed-author:MalterH EHE | lld:pubmed |
| pubmed-article:9659908 | pubmed:author | pubmed-author:AbsherDD | lld:pubmed |
| pubmed-article:9659908 | pubmed:author | pubmed-author:EberhartD EDE | lld:pubmed |
| pubmed-article:9659908 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9659908 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:9659908 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9659908 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9659908 | pubmed:pagination | 109-18 | lld:pubmed |
| pubmed-article:9659908 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
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| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:meshHeading | pubmed-meshheading:9659908-... | lld:pubmed |
| pubmed-article:9659908 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9659908 | pubmed:articleTitle | FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. | lld:pubmed |
| pubmed-article:9659908 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA. | lld:pubmed |
| pubmed-article:9659908 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9659908 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9659908 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2332 | entrezgene:pubmed | pubmed-article:9659908 | lld:entrezgene |
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