| pubmed-article:2005884 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2005884 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2005884 | lifeskim:mentions | umls-concept:C0117720 | lld:lifeskim |
| pubmed-article:2005884 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:2005884 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2005884 | pubmed:dateCreated | 1991-4-22 | lld:pubmed |
| pubmed-article:2005884 | pubmed:abstractText | We have analyzed the biosynthesis of human fibroblast growth factor-5 (FGF-5) at the translational and posttranslational levels. FGF-5 RNA synthesized in vitro can be translated in rabbit reticulocyte lysates to yield a 29,500-Da protein, which is consistent with the molecular weight predicted from the coding sequence. The efficiency of FGF-5 translation is dramatically enhanced if an upstream open reading frame (ORF-1) in the RNA is deleted or if both AUG codons in ORF-1 are destroyed by point mutations, while partial enhancement is achieved by individual mutation of either ORF-1 AUG codon. These data suggest that FGF-5 synthesis requires the scanning of ribosomes past the two ORF-1 AUG codons. The introduction of these ORF-1 mutations into a eukaryotic FGF-5 expression vector increases its capacity to transform mouse NIH 3T3 cells up to 50-fold upon transfection. FGF-5 is secreted from transfected 3T3 cells and from human tumor cells as glycoproteins containing heterogeneous amounts of sialic acid. Glycosidase treatments suggest that the growth factor bears both N-linked and O-linked sugars. | lld:pubmed |
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| pubmed-article:2005884 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2005884 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2005884 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2005884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2005884 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2005884 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2005884 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:2005884 | pubmed:author | pubmed-author:GoldfarbMM | lld:pubmed |
| pubmed-article:2005884 | pubmed:author | pubmed-author:HardinJJ | lld:pubmed |
| pubmed-article:2005884 | pubmed:author | pubmed-author:BatesBB | lld:pubmed |
| pubmed-article:2005884 | pubmed:author | pubmed-author:DrickamerKK | lld:pubmed |
| pubmed-article:2005884 | pubmed:author | pubmed-author:ZhanXX | lld:pubmed |
| pubmed-article:2005884 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2005884 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:2005884 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2005884 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2005884 | pubmed:pagination | 1840-5 | lld:pubmed |
| pubmed-article:2005884 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2005884 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2005884 | pubmed:articleTitle | Biosynthesis of human fibroblast growth factor-5. | lld:pubmed |
| pubmed-article:2005884 | pubmed:affiliation | Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, New York 10032. | lld:pubmed |
| pubmed-article:2005884 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2005884 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2005884 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2250 | entrezgene:pubmed | pubmed-article:2005884 | lld:entrezgene |
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