| pubmed-article:16681429 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C0002736 | lld:lifeskim |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C0241888 | lld:lifeskim |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C1862941 | lld:lifeskim |
| pubmed-article:16681429 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:16681429 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16681429 | pubmed:dateCreated | 2006-5-9 | lld:pubmed |
| pubmed-article:16681429 | pubmed:abstractText | Overproduction of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)) may be an important factor in the pathogenesis of amyotrophic lateral sclerosis (ALS). Owing to their ability to permeate through biological membranes, excess NO and H(2)O(2) may be present in the media surrounding motor neurones. Anti-oxidative defence enzymes (ADEs) in erythrocytes are capable of detoxifying reactive oxygen species (produced endogenously or exogenously), but may also be structurally modified and inactivated by reactive oxygen and nitrogen species. Both balanced and coordinated ADE activities are of utmost importance for their correct physiological function. | lld:pubmed |
| pubmed-article:16681429 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16681429 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16681429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681429 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16681429 | pubmed:issn | 1434-6621 | lld:pubmed |
| pubmed-article:16681429 | pubmed:author | pubmed-author:JonesDavid... | lld:pubmed |
| pubmed-article:16681429 | pubmed:author | pubmed-author:Spasi?Mihajlo... | lld:pubmed |
| pubmed-article:16681429 | pubmed:author | pubmed-author:Stevi?ZoricaZ | lld:pubmed |
| pubmed-article:16681429 | pubmed:author | pubmed-author:Nikoli?-Koki... | lld:pubmed |
| pubmed-article:16681429 | pubmed:author | pubmed-author:Blagojevi?Dus... | lld:pubmed |
| pubmed-article:16681429 | pubmed:author | pubmed-author:Davidovi?Bilj... | lld:pubmed |
| pubmed-article:16681429 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16681429 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:16681429 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16681429 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16681429 | pubmed:pagination | 589-93 | lld:pubmed |
| pubmed-article:16681429 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
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| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:meshHeading | pubmed-meshheading:16681429... | lld:pubmed |
| pubmed-article:16681429 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16681429 | pubmed:articleTitle | Alterations in anti-oxidative defence enzymes in erythrocytes from sporadic amyotrophic lateral sclerosis (SALS) and familial ALS patients. | lld:pubmed |
| pubmed-article:16681429 | pubmed:affiliation | Department of Physiology, Institute for Biological Research Sinisa Stankovi?, Bulevar Despota Stefana 142, 11060 Belgrade, Serbia and Montenegro. san@ibiss.bg.ac.yu | lld:pubmed |
| pubmed-article:16681429 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16681429 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16681429 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16681429 | lld:pubmed |
