Linked Life Data

8351519

Source:http://linkedlifedata.com/resource/pubmed/id/8351519

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5124
pubmed:dateCreated
1993-9-14
pubmed:abstractText
Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation Ala4 to Val in exon 1 was the most frequent one; mutations were identified in exons 2, 4, and 5 but not in the active site region formed by exon 3. The 2.4 A crystal structure of human SOD, along with two other SOD structures, established that all 12 observed FALS mutant sites alter conserved interactions critical to the beta-barrel fold and dimer contact, rather than catalysis. Red cells from heterozygotes had less than 50 percent normal SOD activity, consistent with a structurally defective SOD dimer. Thus, defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of FALS.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
261
pubmed:geneSymbol
SOD1
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
1047-51
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.
pubmed:affiliation
Department of Neurology, Northwestern University Medical School, Chicago, IL 60611.
pubmed:publicationType
Journal Article, Comment, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't