| pubmed-article:1334098 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1334098 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:1334098 | lifeskim:mentions | umls-concept:C0026769 | lld:lifeskim |
| pubmed-article:1334098 | lifeskim:mentions | umls-concept:C0007806 | lld:lifeskim |
| pubmed-article:1334098 | lifeskim:mentions | umls-concept:C0027765 | lld:lifeskim |
| pubmed-article:1334098 | lifeskim:mentions | umls-concept:C0206528 | lld:lifeskim |
| pubmed-article:1334098 | lifeskim:mentions | umls-concept:C0333348 | lld:lifeskim |
| pubmed-article:1334098 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1334098 | pubmed:dateCreated | 1993-1-12 | lld:pubmed |
| pubmed-article:1334098 | pubmed:abstractText | A substrate conversion assay was used to detect gelatinase activity in the cerebrospinal fluid (CSF) of patients with various neurological disorders. Two main forms of gelatinase with an apparent molecular mass of 65 and 85 kDa, respectively, could be discerned. The high molecular mass gelatinase was detectable only in samples of patients with multiple sclerosis or other inflammatory neurological disorders. A statistically significant correlation was found between the level of the 85-kDa gelatinase and the CSF cytosis. This protease could play a role in the process of demyelination and breakdown of the blood-brain barrier in certain neurological disorders, such as multiple sclerosis. | lld:pubmed |
| pubmed-article:1334098 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1334098 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1334098 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1334098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1334098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1334098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1334098 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1334098 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1334098 | pubmed:issn | 0165-5728 | lld:pubmed |
| pubmed-article:1334098 | pubmed:author | pubmed-author:CartonHH | lld:pubmed |
| pubmed-article:1334098 | pubmed:author | pubmed-author:OpdenakkerGG | lld:pubmed |
| pubmed-article:1334098 | pubmed:author | pubmed-author:MasureSS | lld:pubmed |
| pubmed-article:1334098 | pubmed:author | pubmed-author:GijbelsKK | lld:pubmed |
| pubmed-article:1334098 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1334098 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:1334098 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1334098 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1334098 | pubmed:pagination | 29-34 | lld:pubmed |
| pubmed-article:1334098 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1334098 | pubmed:meshHeading | pubmed-meshheading:1334098-... | lld:pubmed |
| pubmed-article:1334098 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1334098 | pubmed:articleTitle | Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders. | lld:pubmed |
| pubmed-article:1334098 | pubmed:affiliation | Rega Institute, Leuven, Belgium. | lld:pubmed |
| pubmed-article:1334098 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1334098 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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