| pubmed-article:17082481 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0025545 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0043481 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0019868 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:17082481 | lifeskim:mentions | umls-concept:C0332453 | lld:lifeskim |
| pubmed-article:17082481 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17082481 | pubmed:dateCreated | 2006-12-22 | lld:pubmed |
| pubmed-article:17082481 | pubmed:abstractText | L-homocysteine and/or L-homocystine interact in vivo with albumin and other extracellular proteins by forming mixed-disulfide conjugates. Because of its extremely rich cysteine content, we hypothesized that metallothionein, a ubiquitous intracellular zinc-chaperone and superoxide anion radical scavenger, reacts with L-homocysteine and that homocysteinylated-metallothionein suffers loss of function. | lld:pubmed |
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| pubmed-article:17082481 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17082481 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17082481 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17082481 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17082481 | pubmed:issn | 1524-4636 | lld:pubmed |
| pubmed-article:17082481 | pubmed:author | pubmed-author:BarbatoJohn... | lld:pubmed |
| pubmed-article:17082481 | pubmed:author | pubmed-author:DiBelloPatric... | lld:pubmed |
| pubmed-article:17082481 | pubmed:author | pubmed-author:JacobsenDonal... | lld:pubmed |
| pubmed-article:17082481 | pubmed:author | pubmed-author:CatanescuOtil... | lld:pubmed |
| pubmed-article:17082481 | pubmed:author | pubmed-author:MurrayKelseyK | lld:pubmed |
| pubmed-article:17082481 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17082481 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:17082481 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17082481 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17082481 | pubmed:pagination | 49-54 | lld:pubmed |
| pubmed-article:17082481 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
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| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
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| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:meshHeading | pubmed-meshheading:17082481... | lld:pubmed |
| pubmed-article:17082481 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17082481 | pubmed:articleTitle | Targeting of metallothionein by L-homocysteine: a novel mechanism for disruption of zinc and redox homeostasis. | lld:pubmed |
| pubmed-article:17082481 | pubmed:affiliation | Department Cell Biology, Lerner Research Institute, The Cleveland Clinic, Cleveland, OH 44195, USA. | lld:pubmed |
| pubmed-article:17082481 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17082481 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
