| pubmed-article:1312261 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1312261 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:1312261 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
| pubmed-article:1312261 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
| pubmed-article:1312261 | lifeskim:mentions | umls-concept:C2267219 | lld:lifeskim |
| pubmed-article:1312261 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1312261 | pubmed:dateCreated | 1992-4-16 | lld:pubmed |
| pubmed-article:1312261 | pubmed:abstractText | Phenylketonuria (PKU) is a metabolic disorder secondary to a deficiency of the hepatic enzyme phenylalanine hydroxylase (PAH). The recent creation of a mouse strain for PAH deficiency has provided an excellent model system to explore the possibility of its phenotypic correction by hepatic gene therapy. A recombinant retrovirus containing the mouse PAH cDNA under the transcriptional control of the human CMV promoter was constructed and used to transduce hepatocytes isolated from PAH-deficient mice. Viral-transduced hepatocytes produced dramatically higher levels of mouse PAH mRNA as compared to control mock-infected hepatocytes. The PAH mRNA was translated efficiently into PAH protein that is capable of converting phenylalanine to tyrosine in vitro. These results demonstrate that the PAH-deficient mouse hepatocytes can be readily reconstituted by retroviral-mediated gene transduction, which is a crucial step towards somatic gene therapy for PKU. | lld:pubmed |
| pubmed-article:1312261 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1312261 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1312261 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1312261 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1312261 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1312261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1312261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1312261 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1312261 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1312261 | pubmed:issn | 0740-7750 | lld:pubmed |
| pubmed-article:1312261 | pubmed:author | pubmed-author:KayM AMA | lld:pubmed |
| pubmed-article:1312261 | pubmed:author | pubmed-author:WooS LSL | lld:pubmed |
| pubmed-article:1312261 | pubmed:author | pubmed-author:DarlingtonG... | lld:pubmed |
| pubmed-article:1312261 | pubmed:author | pubmed-author:DAWH THT | lld:pubmed |
| pubmed-article:1312261 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1312261 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:1312261 | pubmed:geneSymbol | PAH | lld:pubmed |
| pubmed-article:1312261 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1312261 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1312261 | pubmed:pagination | 89-96 | lld:pubmed |
| pubmed-article:1312261 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:meshHeading | pubmed-meshheading:1312261-... | lld:pubmed |
| pubmed-article:1312261 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1312261 | pubmed:articleTitle | Reconstitution of enzymatic activity in hepatocytes of phenylalanine hydroxylase-deficient mice. | lld:pubmed |
| pubmed-article:1312261 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Cell Biology, Houston, Texas 77030. | lld:pubmed |
| pubmed-article:1312261 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1312261 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1312261 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:18478 | entrezgene:pubmed | pubmed-article:1312261 | lld:entrezgene |
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