Source:http://linkedlifedata.com/resource/pubmed/id/10400992
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
1999-9-14
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| pubmed:abstractText |
Mutations in superoxide dismutase 1 (SOD1) polypeptides cause a form of familial amyotrophic lateral sclerosis (FALS). In different kindreds, harboring different mutations, the duration of illness tends to be similar for a given mutation. For example, patients inheriting a substitution of valine for alanine at position four (A4V) average a 1.5 year life expectancy after the onset of symptoms, whereas patients harboring a substitution of arginine for histidine at position 46 (H46R) average an 18 year life expectancy after disease onset. Here, we examine a number of biochemical and biophysical properties of nine different FALS variants of SOD1 polypeptides, including enzymatic activity (which relates indirectly to the affinity of the enzyme for copper), polypeptide half-life, resistance to proteolytic degradation and solubility, in an effort to determine whether a specific property of these enzymes correlates with clinical progression. We find that although all the mutants tested appear to be soluble, the different mutants show a remarkable degree of variation with respect to activity, polypeptide half-life and resistance to proteolysis. However, these variables do not stratify in a manner that correlates with clinical progression. We conclude that the basis for the different life expectancies of patients in different kindreds of sod1-linked FALS may result from an as yet unidentified property of these mutant enzymes.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/superoxide dismutase 1
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
|
| pubmed:issn |
0964-6906
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1451-60
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:10400992-Amino Acid Substitution,
pubmed-meshheading:10400992-Amyotrophic Lateral Sclerosis,
pubmed-meshheading:10400992-Animals,
pubmed-meshheading:10400992-COS Cells,
pubmed-meshheading:10400992-Centrifugation,
pubmed-meshheading:10400992-Copper,
pubmed-meshheading:10400992-Disease Progression,
pubmed-meshheading:10400992-Endopeptidase K,
pubmed-meshheading:10400992-Family Health,
pubmed-meshheading:10400992-Genetic Variation,
pubmed-meshheading:10400992-Glycine,
pubmed-meshheading:10400992-Histidine,
pubmed-meshheading:10400992-Humans,
pubmed-meshheading:10400992-Mice,
pubmed-meshheading:10400992-Mice, Transgenic,
pubmed-meshheading:10400992-Mutation,
pubmed-meshheading:10400992-Protein Binding,
pubmed-meshheading:10400992-Solubility,
pubmed-meshheading:10400992-Superoxide Dismutase,
pubmed-meshheading:10400992-Time Factors,
pubmed-meshheading:10400992-Tumor Cells, Cultured
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| pubmed:year |
1999
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| pubmed:articleTitle |
Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds.
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| pubmed:affiliation |
Department of Pathology, Johns Hopkins School of Medicine, 558 Ross Building, 720 Rutland Avenue, Baltimore, MD 21205, USA,
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|