Linked Life Data

12738850

Source:http://linkedlifedata.com/resource/pubmed/id/12738850

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5621
pubmed:dateCreated
2003-5-9
pubmed:abstractText
The essential transition metal ions are avidly accumulated by cells, yet they have two faces: They are put to use as required cofactors, but they also can catalyze cytotoxic reactions. Several families of proteins are emerging that control the activity of intracellular metal ions and help confine them to vital roles. These include integral transmembrane transporters, metalloregulatory sensors, and diffusible cytoplasmic metallochaperone proteins that protect and guide metal ions to targets. It is becoming clear that many of these proteins use atypical coordination chemistry to accomplish their unique goals. The different coordination numbers, types of coordinating residues, and solvent accessibilities of these sites are providing insight into the inorganic chemistry of the cytoplasm.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
300
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
931-6
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Transition metal speciation in the cell: insights from the chemistry of metal ion receptors.
pubmed:affiliation
Department of Chemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3113, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't