| pubmed-article:16412514 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16412514 | lifeskim:mentions | umls-concept:C0003732 | lld:lifeskim |
| pubmed-article:16412514 | lifeskim:mentions | umls-concept:C0600435 | lld:lifeskim |
| pubmed-article:16412514 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16412514 | pubmed:issue | 5-6 | lld:pubmed |
| pubmed-article:16412514 | pubmed:dateCreated | 2006-5-8 | lld:pubmed |
| pubmed-article:16412514 | pubmed:abstractText | Oxidative stress is a universal phenomenon experienced by organisms in all domains of life. Proteins like those in the ferritin-like di-iron carboxylate superfamily have evolved to manage this stress. Here we describe the cloning, isolation, and characterization of a Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (PfDps-like). Phylogenetic analysis, primary structure alignments and higher order structural predictions all suggest that the P. furiosus protein is related to proteins within the broad superfamily of ferritin-like di-iron carboxylate proteins. The recombinant PfDps protein self-assembles into a 12 subunit quaternary structure with an outer shell diameter of approximately 10nm and an interior diameter of approximately 5 nm. Dps proteins functionally manage the toxicity of oxidative stress by sequestering intracellular ferrous iron and using it to reduce H(2)O(2) in a two electron process to form water. The iron is converted to a benign form as Fe(III) within the protein cage. This Dps-mediated reduction of hydrogen peroxide, coupled with the protein's capacity to sequester iron, contributes to its service as a multifunctional antioxidant. | lld:pubmed |
| pubmed-article:16412514 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16412514 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16412514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412514 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16412514 | pubmed:month | May | lld:pubmed |
| pubmed-article:16412514 | pubmed:issn | 0162-0134 | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:AllenMarkM | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:DouglasTrevor... | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:GaussGeorge... | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:YoungMarkM | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:WiedenheftBla... | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:LawrenceC... | lld:pubmed |
| pubmed-article:16412514 | pubmed:author | pubmed-author:RamsayBradley... | lld:pubmed |
| pubmed-article:16412514 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16412514 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:16412514 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16412514 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16412514 | pubmed:pagination | 1061-8 | lld:pubmed |
| pubmed-article:16412514 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:meshHeading | pubmed-meshheading:16412514... | lld:pubmed |
| pubmed-article:16412514 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16412514 | pubmed:articleTitle | Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus. | lld:pubmed |
| pubmed-article:16412514 | pubmed:affiliation | Thermal Biology Institute, Montana State University, 108 Gaines Hall, Bozeman, MT 59717, USA. | lld:pubmed |
| pubmed-article:16412514 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16412514 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16412514 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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