Source:http://linkedlifedata.com/resource/pubmed/id/19675642
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7257
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pubmed:dateCreated |
2009-8-13
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pubmed:abstractText |
Almost half of all enzymes must associate with a particular metal to function. An ambition is to understand why each metal-protein partnership arose and how it is maintained. Metal availability provides part of the explanation, and has changed over geological time and varies between habitats but is held within vital limits in cells. Such homeostasis needs metal sensors, and there is an ongoing search to discover the metal-sensing mechanisms. For metalloproteins to acquire the right metals, metal sensors must correctly distinguish between the inorganic elements.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1476-4687
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
460
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
823-30
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pubmed:meshHeading |
pubmed-meshheading:19675642-Allosteric Regulation,
pubmed-meshheading:19675642-Animals,
pubmed-meshheading:19675642-Bacteria,
pubmed-meshheading:19675642-Biocatalysis,
pubmed-meshheading:19675642-Gene Expression,
pubmed-meshheading:19675642-Metalloproteins,
pubmed-meshheading:19675642-Metals,
pubmed-meshheading:19675642-RNA Stability,
pubmed-meshheading:19675642-Yeasts
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pubmed:year |
2009
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pubmed:articleTitle |
Metalloproteins and metal sensing.
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pubmed:affiliation |
Cell & Molecular Biosciences, Medical School, Newcastle University, Newcastle NE2 4HH, UK.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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