| pubmed-article:11134126 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11134126 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:11134126 | lifeskim:mentions | umls-concept:C0004358 | lld:lifeskim |
| pubmed-article:11134126 | lifeskim:mentions | umls-concept:C0017785 | lld:lifeskim |
| pubmed-article:11134126 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:11134126 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11134126 | pubmed:dateCreated | 2001-2-2 | lld:pubmed |
| pubmed-article:11134126 | pubmed:abstractText | Autoantibodies against the smaller isoform of glutamic acid decarboxylase (GAD) are markers for Type 1 diabetes. GAD65 autoantibody (GAD65Ab)-positive individuals in the general population are, however, mostly at low risk of developing Type 1 diabetes, suggesting that GAD65Ab phenotypes may be associated with different underlying pathogenic processes. The aim of this study was to test the hypothesis that Type 1 diabetes patients (n = 243; group I), GAD65Ab-positive healthy individuals (n = 28; group II), and healthy first-degree relatives of Type 1 diabetes patients (n = 41; group III) have antibody phenotypes that recognize different GAD65 epitopes. Sera from groups I-III were tested for their binding to GAD65 and GAD67, as well as six different GAD65/67 fusion proteins. Regardless of group, sera reactive to both GAD65 and GAD67 showed broader epitope reactivity than GAD65-specific sera. Furthermore, Type 1 diabetes patients showed a more restricted epitope binding than healthy individuals and first-degree relatives, demonstrating significantly less binding to the N-terminal part of GAD65 and to GAD67. Our analysis demonstrates that the N-terminal part is essential for full antibody binding to GAD65, in particular, to the middle epitope. It is suggested that Type 1 diabetes is associated with restricted GAD65Ab epitope specificity. | lld:pubmed |
| pubmed-article:11134126 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11134126 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:11134126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11134126 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11134126 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11134126 | pubmed:issn | 0021-972X | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:PerssonBB | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:LernmarkAA | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:HampfC RCR | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:Landin-Olsson... | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:KockumII | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:OrtqvistEE | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:RolandssonOO | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:BekrisLL | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:TörnCC | lld:pubmed |
| pubmed-article:11134126 | pubmed:author | pubmed-author:HammerleL PLP | lld:pubmed |
| pubmed-article:11134126 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11134126 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:11134126 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11134126 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11134126 | pubmed:pagination | 4671-9 | lld:pubmed |
| pubmed-article:11134126 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11134126 | pubmed:meshHeading | pubmed-meshheading:11134126... | lld:pubmed |
| pubmed-article:11134126 | pubmed:meshHeading | pubmed-meshheading:11134126... | lld:pubmed |
| pubmed-article:11134126 | pubmed:meshHeading | pubmed-meshheading:11134126... | lld:pubmed |
| pubmed-article:11134126 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11134126 | pubmed:articleTitle | Recognition of glutamic acid decarboxylase (GAD) by autoantibodies from different GAD antibody-positive phenotypes. | lld:pubmed |
| pubmed-article:11134126 | pubmed:affiliation | Department of Medicine, University of Washington, Seattle, Washington 98195, USA. champe@u.washington.edu | lld:pubmed |
| pubmed-article:11134126 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11134126 | pubmed:publicationType | Clinical Trial | lld:pubmed |
| pubmed-article:11134126 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11134126 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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