| pubmed-article:10862081 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10862081 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:10862081 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:10862081 | lifeskim:mentions | umls-concept:C1832200 | lld:lifeskim |
| pubmed-article:10862081 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:10862081 | pubmed:dateCreated | 2000-8-11 | lld:pubmed |
| pubmed-article:10862081 | pubmed:abstractText | The peroxisome biogenesis disorders (PBD) are characterized by neural, hepatic, and renal deficiencies, severe mental retardation, and are often lethal. These disorders are genetically and phenotypically heterogeneous and are caused by defective peroxisomal protein import and decreased peroxisomal metabolic function. Mutations in PEX10 have been identified in patients from complementation group 7 (CG7) of the PBDs and we report here an analysis of the genotypes and phenotypes of PEX10-deficient patients. All four PEX10-deficient Zellweger Syndrome (ZS) patients were found to have nonsense, frameshift, or splice site mutations that remove large portions of the PEX10 coding region. In contrast, a more mildly affected PEX10-deficient neonatal adrenoleukodystrophy patient expressed a PEX10 allele with a missense mutation, H290Q, affecting the C-terminal zinc-binding domain of the PEX10 product. These results support the hypothesis that severe, loss-of-function mutations in PEX genes cause more severe clinical phenotypes, whereas mildly affected PBD patients have PEX gene mutations that retain residual function. To quantitate the effects of the PEX10 mutations identified here and elsewhere we employed a functional complementation assay. Surprisingly, we observed that nonsense and frameshift mutations predicted to delete the C-terminal 2/3 (R125X) or 1/3 (c.704insA) of the protein displayed nearly normal PEX10 activity. Even more surprising, we found that the unexpectedly high PEX10 activity displayed by these cDNAs could be eliminated by removing or mutating segments of the PEX10 cDNA downstream of the mutations. Although these results demonstrate serious flaws in the PEX10 functional complementation assay, they do suggest that the C-terminal zinc-binding domain is critical for PEX10 function. | lld:pubmed |
| pubmed-article:10862081 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10862081 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10862081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10862081 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10862081 | pubmed:issn | 1059-7794 | lld:pubmed |
| pubmed-article:10862081 | pubmed:author | pubmed-author:GouldS JSJ | lld:pubmed |
| pubmed-article:10862081 | pubmed:author | pubmed-author:WarrenD SDS | lld:pubmed |
| pubmed-article:10862081 | pubmed:author | pubmed-author:WolfeB DBD | lld:pubmed |
| pubmed-article:10862081 | pubmed:copyrightInfo | Copyright 2000 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:10862081 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10862081 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:10862081 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10862081 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10862081 | pubmed:pagination | 509-21 | lld:pubmed |
| pubmed-article:10862081 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10862081 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10862081 | pubmed:articleTitle | Phenotype-genotype relationships in PEX10-deficient peroxisome biogenesis disorder patients. | lld:pubmed |
| pubmed-article:10862081 | pubmed:affiliation | Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. sgould@jhmi.edu | lld:pubmed |
| pubmed-article:10862081 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10862081 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:5192 | entrezgene:pubmed | pubmed-article:10862081 | lld:entrezgene |
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