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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
1997-10-23
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pubmed:databankReference |
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pubmed:abstractText |
Copper is distributed to distinct localizations in the cell through diverse pathways. We demonstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated through a soluble factor identified as Saccharomyces cerevisiae LYS7 and human CCS (copper chaperone for SOD). This factor is specific for SOD1 and does not deliver copper to proteins in the mitochondria, nucleus, or secretory pathway. Yeast cells containing a lys7Delta null mutation have normal levels of SOD1 protein, but fail to incorporate copper into SOD1, which is therefore devoid of superoxide scavenging activity. LYS7 and CCS specifically restore the biosynthesis of holoSOD1 in vivo. Elucidation of the CCS copper delivery pathway may permit development of novel therapeutic approaches to human diseases that involve SOD1, including amyotrophic lateral sclerosis.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/COX17 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/COX17 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LYS7 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23469-72
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9295278-Amino Acid Sequence,
pubmed-meshheading:9295278-Carrier Proteins,
pubmed-meshheading:9295278-Cation Transport Proteins,
pubmed-meshheading:9295278-Copper,
pubmed-meshheading:9295278-Fungal Proteins,
pubmed-meshheading:9295278-Humans,
pubmed-meshheading:9295278-Molecular Chaperones,
pubmed-meshheading:9295278-Molecular Sequence Data,
pubmed-meshheading:9295278-Protein Binding,
pubmed-meshheading:9295278-Proteins,
pubmed-meshheading:9295278-Recombinant Proteins,
pubmed-meshheading:9295278-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9295278-Sequence Homology, Amino Acid,
pubmed-meshheading:9295278-Subcellular Fractions,
pubmed-meshheading:9295278-Superoxide Dismutase
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pubmed:year |
1997
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pubmed:articleTitle |
The copper chaperone for superoxide dismutase.
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pubmed:affiliation |
Division of Toxicological Sciences, Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, Maryland 21205, USA. vculotta@phnet.sph.jhu.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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