| pubmed-article:2714436 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2714436 | lifeskim:mentions | umls-concept:C0015879 | lld:lifeskim |
| pubmed-article:2714436 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:2714436 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:2714436 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:2714436 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:2714436 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2714436 | pubmed:dateCreated | 1989-6-16 | lld:pubmed |
| pubmed-article:2714436 | pubmed:abstractText | Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation. | lld:pubmed |
| pubmed-article:2714436 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2714436 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2714436 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2714436 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2714436 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2714436 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2714436 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2714436 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2714436 | pubmed:author | pubmed-author:HarrisonP MPM | lld:pubmed |
| pubmed-article:2714436 | pubmed:author | pubmed-author:CesareniGG | lld:pubmed |
| pubmed-article:2714436 | pubmed:author | pubmed-author:TreffryAA | lld:pubmed |
| pubmed-article:2714436 | pubmed:author | pubmed-author:LuzzagoAA | lld:pubmed |
| pubmed-article:2714436 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2714436 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:2714436 | pubmed:volume | 247 | lld:pubmed |
| pubmed-article:2714436 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2714436 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2714436 | pubmed:pagination | 268-72 | lld:pubmed |
| pubmed-article:2714436 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
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| pubmed-article:2714436 | pubmed:meshHeading | pubmed-meshheading:2714436-... | lld:pubmed |
| pubmed-article:2714436 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2714436 | pubmed:articleTitle | Recombinant H-chain ferritins: effects of changes in the 3-fold channels. | lld:pubmed |
| pubmed-article:2714436 | pubmed:affiliation | Department of Molecular Biology and Biotechnology, The University, Sheffield, England. | lld:pubmed |
| pubmed-article:2714436 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2714436 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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