pubmed-article:9808564 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C1511359 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C1307126 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:9808564 | lifeskim:mentions | umls-concept:C2700400 | lld:lifeskim |
pubmed-article:9808564 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:9808564 | pubmed:dateCreated | 1998-12-21 | lld:pubmed |
pubmed-article:9808564 | pubmed:abstractText | The human blood coagulation factor VIII C2 domain (Ser2173-Tyr2332) contains an epitope recognized by most polyclonal inhibitory anti-factor VIII alloantibodies and autoantibodies. We took advantage of the differential reactivity of inhibitory antibodies with human and porcine factor VIII and mapped a major determinant of the C2 epitope by using a series of active recombinant hybrid human/porcine factor VIII molecules. A series of five C2-specific human antibodies and a murine anti-factor VIII monoclonal antibody, NMC-VIII/5, inhibited a hybrid containing a substitution of porcine sequence for Glu2181-Val2243 significantly less than human factor VIII. In contrast, four of the five patient antibodies and NMC-VIII/5 inhibited a hybrid containing a substitution of porcine sequence for Thr2253-Tyr2332 equally well as human factor VIII. Thus, a major factor VIII inhibitor epitope determinant is bounded by Glu2181-Val2243 at the NH2-terminal end of the C2 domain. Because C2 inhibitors block the binding of factor VIII to phospholipid and von Willebrand factor, for which binding sites have been localized to Thr2303-Tyr2332, these results imply that the segment bounded by Glu2181-Val2243 also is involved in these macromolecular interactions. | lld:pubmed |
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pubmed-article:9808564 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9808564 | pubmed:language | eng | lld:pubmed |
pubmed-article:9808564 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9808564 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:9808564 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9808564 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9808564 | pubmed:month | Nov | lld:pubmed |
pubmed-article:9808564 | pubmed:issn | 0006-4971 | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:ScandellaDD | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:HealeyJ FJF | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:ShimaMM | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:LollarPP | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:LubinI MIM | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:BarrowR TRT | lld:pubmed |
pubmed-article:9808564 | pubmed:author | pubmed-author:TamimH MHM | lld:pubmed |
pubmed-article:9808564 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9808564 | pubmed:day | 15 | lld:pubmed |
pubmed-article:9808564 | pubmed:volume | 92 | lld:pubmed |
pubmed-article:9808564 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9808564 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9808564 | pubmed:pagination | 3701-9 | lld:pubmed |
pubmed-article:9808564 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:9808564 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9808564 | pubmed:articleTitle | Residues Glu2181-Val2243 contain a major determinant of the inhibitory epitope in the C2 domain of human factor VIII. | lld:pubmed |
pubmed-article:9808564 | pubmed:affiliation | Emory University, Atlanta, GA; Holland Laboratory, American Red Cross, Rockville, MD, USA. | lld:pubmed |
pubmed-article:9808564 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9808564 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:9808564 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9808564 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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