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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2011-5-10
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pubmed:abstractText |
Huntington's disease (HD) is associated with impaired energy metabolism in the brain. Creatine kinase (CK) catalyzes ATP-dependent phosphorylation of creatine (Cr) into phosphocreatine (PCr), thereby serving as readily available high-capacity spatial and temporal ATP buffering.
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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 |
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pubmed:status |
MEDLINE
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pubmed:issn |
1660-2862
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 S. Karger AG, Basel.
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pubmed:issnType |
Electronic
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
194-201
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pubmed:meshHeading |
pubmed-meshheading:21124007-Animals,
pubmed-meshheading:21124007-Brain,
pubmed-meshheading:21124007-Brain Chemistry,
pubmed-meshheading:21124007-Chromatography, High Pressure Liquid,
pubmed-meshheading:21124007-Creatine Kinase, BB Form,
pubmed-meshheading:21124007-Disease Models, Animal,
pubmed-meshheading:21124007-Huntington Disease,
pubmed-meshheading:21124007-Mice,
pubmed-meshheading:21124007-Mice, Transgenic,
pubmed-meshheading:21124007-Mitochondria,
pubmed-meshheading:21124007-Phosphocreatine
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pubmed:year |
2011
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pubmed:articleTitle |
Impaired brain creatine kinase activity in Huntington's disease.
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pubmed:affiliation |
Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, NY 10065, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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