Source:http://linkedlifedata.com/resource/pubmed/id/18989099
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
2008-12-29
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| pubmed:abstractText |
Lysosomes contain most of the cell's supply of labile iron, which makes them sensitive to oxidative stress. To keep lysosomal labile iron at a minimum, a cellular strategy might be to autophagocytose iron binding proteins that temporarily would chelate iron in a non-redox-active form. Previously we have shown that autophagy of metallothioneins, as well as of non-Fe-saturated ferritin, meets this goal. Here we add another stress-regulated protein to the list, namely HSP70.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
1554-8635
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| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
93-5
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| pubmed:dateRevised |
2011-6-30
|
| pubmed:meshHeading |
pubmed-meshheading:18989099-Autophagy,
pubmed-meshheading:18989099-Ferritins,
pubmed-meshheading:18989099-HSP70 Heat-Shock Proteins,
pubmed-meshheading:18989099-Iron,
pubmed-meshheading:18989099-Iron Chelating Agents,
pubmed-meshheading:18989099-Lysosomes,
pubmed-meshheading:18989099-Oxidation-Reduction,
pubmed-meshheading:18989099-Oxidative Stress
|
| pubmed:year |
2009
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| pubmed:articleTitle |
Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form.
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| pubmed:affiliation |
Division of Pharmacology, Faculty of Health Sciences, Linköping University, Linköping, Sweden.
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| pubmed:publicationType |
Journal Article
|