| pubmed-article:15353322 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15353322 | lifeskim:mentions | umls-concept:C0497327 | lld:lifeskim |
| pubmed-article:15353322 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:15353322 | lifeskim:mentions | umls-concept:C0314672 | lld:lifeskim |
| pubmed-article:15353322 | lifeskim:mentions | umls-concept:C1700775 | lld:lifeskim |
| pubmed-article:15353322 | pubmed:dateCreated | 2004-9-8 | lld:pubmed |
| pubmed-article:15353322 | pubmed:abstractText | We review here the molecular mechanisms that underlie alpha1-antitrypsin deficiency and show how an understanding of this mechanism has allowed us to explain the deficiency of other members of the serine proteinase inhibitor or serpin superfamily. These include the deficiency of antithrombin, C1-inhibitor and alpha1-antichymotrypsin in association with thrombosis, angio-oedema and emphysema respectively. Moreover the accumulation of mutant neuroserpin within neurones causes the novel dementia familial encephalopathy with neuroserpin inclusion bodies (FENIB). We have grouped these conditions together as the serpinopathies as recognition of their common pathophysiology provides a platform to develop strategies to treat the associated clinical syndromes. | lld:pubmed |
| pubmed-article:15353322 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15353322 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15353322 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15353322 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15353322 | pubmed:issn | 1093-4715 | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:LomasDavid... | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:BelorgeyDidie... | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:CrowtherDamia... | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:MallyaMeeraM | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:PageRichardR | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:OndaMakiM | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:MirandaElenaE | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:KinghornKerri... | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:SharpLynda... | lld:pubmed |
| pubmed-article:15353322 | pubmed:author | pubmed-author:PhillipsRusse... | lld:pubmed |
| pubmed-article:15353322 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15353322 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15353322 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:15353322 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15353322 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15353322 | pubmed:pagination | 2873-91 | lld:pubmed |
| pubmed-article:15353322 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:meshHeading | pubmed-meshheading:15353322... | lld:pubmed |
| pubmed-article:15353322 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15353322 | pubmed:articleTitle | Polymerisation underlies alpha1-antitrypsin deficiency, dementia and other serpinopathies. | lld:pubmed |
| pubmed-article:15353322 | pubmed:affiliation | Department of Medicine, University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, United Kingdom. dal16@cam.ac.uk | lld:pubmed |
| pubmed-article:15353322 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15353322 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:15353322 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15353322 | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15353322 | lld:pubmed |
