Source:http://linkedlifedata.com/resource/pubmed/id/11027589
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2000-10-30
|
pubmed:abstractText |
The familial form of amyotrophic lateral sclerosis is caused by mutations in the SOD1 gene encoding the cytosolic antioxidant enzyme Cu,Zn superoxide dismutase. Although there is no clear correlation between disease and dismutating catalytic activity among the various disease-associated SOD1 alleles, all of the known missense mutations significantly alter the half-life of the encoded polypeptides. Using transient transfection studies in mammalian cells, it was demonstrated that a frameshift mutation in SOD1 which results in a truncated polypeptide is similarly destabilized. Using an epitope-tagging strategy to discriminate between mutant and wild-type SOD1 polypeptides, no evidence for dominant effects on polypeptide stability was detected, including that of a positive effect of the wild-type on mutant SOD1 polypeptides or that of a negative effect of mutant on wild-type SOD1 polypeptides. These experiments thus favor a non-catalytic role of mutant forms of SOD1 in disease progression.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
|
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
276
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1056-61
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11027589-5' Untranslated Regions,
pubmed-meshheading:11027589-Animals,
pubmed-meshheading:11027589-Blotting, Western,
pubmed-meshheading:11027589-Cell Line,
pubmed-meshheading:11027589-Cricetinae,
pubmed-meshheading:11027589-Enzyme Stability,
pubmed-meshheading:11027589-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11027589-Genes, Dominant,
pubmed-meshheading:11027589-Mutation,
pubmed-meshheading:11027589-Peptides,
pubmed-meshheading:11027589-Phenotype,
pubmed-meshheading:11027589-Recombinant Fusion Proteins,
pubmed-meshheading:11027589-Superoxide Dismutase,
pubmed-meshheading:11027589-Transfection
|
pubmed:year |
2000
|
pubmed:articleTitle |
Disease-associated mutations in SOD1 are impervious to dominant positive or negative effects.
|
pubmed:affiliation |
Gene Therapy and Molecular Virology Group, John P. Robarts Research Institute, 100 Perth Drive, London, Ontario, N6A 5K8, Canada.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|