| pubmed-article:15331161 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15331161 | lifeskim:mentions | umls-concept:C0002395 | lld:lifeskim |
| pubmed-article:15331161 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:15331161 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:15331161 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:15331161 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:15331161 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:15331161 | pubmed:dateCreated | 2004-8-27 | lld:pubmed |
| pubmed-article:15331161 | pubmed:abstractText | Glycosylation influences the biological activity of proteins and affects their folding and stability. Because aberrant glycosylation is associated with Alzheimer's disease (AD), we applied proteome analysis together with Pro-Q Emerald 300 glycoprotein staining to investigate changes in glycosylated cytosolic proteins in AD and control brain. Frontal cortex proteins from 10 AD patients and 7 non-demented controls were subjected to separation by two-dimensional gel electrophoresis and subsequently stained with carbohydrate-specific Pro-Q Emerald 300 dye. Changes in glycosylation of separated proteins were quantified, and proteins of interest identified by mass spectrometry. Approximately 30% of all detectable proteins in the human frontal cortex appeared glycosylated, including heat shock cognate 71 stress protein and beta isoform of creatine kinase. The glycosylation of collapsin response mediator protein 2 (CRMP-2) and an unknown protein was reduced in AD, while the glycosylation of glial fibrillary acidic protein was increased. CRMP-2 regulates the assembly and polymerization of microtubules and is associated with neurofibrillary tangles in AD. Aberrant glycosylations in AD may help understand the mechanisms of neurodegenerative diseases. | lld:pubmed |
| pubmed-article:15331161 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15331161 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15331161 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15331161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15331161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15331161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15331161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15331161 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15331161 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15331161 | pubmed:issn | 0304-3940 | lld:pubmed |
| pubmed-article:15331161 | pubmed:author | pubmed-author:GoldsteinsGun... | lld:pubmed |
| pubmed-article:15331161 | pubmed:author | pubmed-author:KoistinahoJar... | lld:pubmed |
| pubmed-article:15331161 | pubmed:author | pubmed-author:AuriolaSeppoS | lld:pubmed |
| pubmed-article:15331161 | pubmed:author | pubmed-author:AlafuzoffIrin... | lld:pubmed |
| pubmed-article:15331161 | pubmed:author | pubmed-author:KanninenKatja... | lld:pubmed |
| pubmed-article:15331161 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15331161 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:15331161 | pubmed:volume | 367 | lld:pubmed |
| pubmed-article:15331161 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15331161 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15331161 | pubmed:pagination | 235-40 | lld:pubmed |
| pubmed-article:15331161 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15331161 | pubmed:meshHeading | pubmed-meshheading:15331161... | lld:pubmed |
| pubmed-article:15331161 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15331161 | pubmed:articleTitle | Glycosylation changes in Alzheimer's disease as revealed by a proteomic approach. | lld:pubmed |
| pubmed-article:15331161 | pubmed:affiliation | Department of Neurobiology, A.I. Virtanen Institute for Molecular Sciences, University of Kuopio, Neulaniementie 2, P.O. Box 1627, FIN-70211 Kuopio, Finland. | lld:pubmed |
| pubmed-article:15331161 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15331161 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15331161 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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