pubmed-article:17966040 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0067033 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0004358 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0162847 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0337184 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C0185111 | lld:lifeskim |
pubmed-article:17966040 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:17966040 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:17966040 | pubmed:dateCreated | 2007-10-29 | lld:pubmed |
pubmed-article:17966040 | pubmed:abstractText | Proteinase 3 (PR3)-specific antineutrophil cytoplasmic autoantibodies (PR3-ANCA) recognize conformational epitopes on PR3. This study evaluates PR3-ANCA target epitopes utilizing a novel recombinant PR3 (rPR3) produced to accommodate manipulations of the N-terminal domain. The rPR3 molecule contains an N-terminus six histidine tag, which can be removed by enterokinase (EK) cleavage of an adjacent EK cleavage site. Once cleaved the remaining amino acids correspond to the mature N-terminus of PR3. This rPR3 can be manipulated to produce three variant forms: tagged rPR3(+his), EK-cleaved (his-tag removed) rPR3(- his), and EK-cleaved, denatured/refolded rPR3(- his/dr) (the proteolytically active form). Patients with clinically positive PR3-ANCA titers (n = 40) were confirmed for reactivity against purchased native PR3 in our system. Controls included 29 healthy volunteers and 34 MPO-ANCA patients. All PR3-ANCA sera samples tested were reactive with one or more forms of the recombinant protein (greater than mean ELISA OD 405 + 2 SDs of controls). Of significance, three sera were reactive with non-active forms only and three others were more reactive with rPR3(- his/dr) than with native PR3. The results of our evaluation of PR3-ANCA sera for reactivity against the three forms of our rPR3 protein uniquely exemplify the diverse array of epitopes within the PR3-ANCA population. This new recombinant form of PR3 should provide a suitable approach to mapping ANCA epitopes using site-directed mutagenesis. | lld:pubmed |
pubmed-article:17966040 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:language | eng | lld:pubmed |
pubmed-article:17966040 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17966040 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17966040 | pubmed:month | Nov | lld:pubmed |
pubmed-article:17966040 | pubmed:issn | 1607-842X | lld:pubmed |
pubmed-article:17966040 | pubmed:author | pubmed-author:YangJ JJJ | lld:pubmed |
pubmed-article:17966040 | pubmed:author | pubmed-author:FalkRonald... | lld:pubmed |
pubmed-article:17966040 | pubmed:author | pubmed-author:JennetteJ... | lld:pubmed |
pubmed-article:17966040 | pubmed:author | pubmed-author:PrestonGloria... | lld:pubmed |
pubmed-article:17966040 | pubmed:author | pubmed-author:PendergraftWi... | lld:pubmed |
pubmed-article:17966040 | pubmed:author | pubmed-author:FarragLilaL | lld:pubmed |
pubmed-article:17966040 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17966040 | pubmed:volume | 40 | lld:pubmed |
pubmed-article:17966040 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17966040 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17966040 | pubmed:pagination | 503-11 | lld:pubmed |
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pubmed-article:17966040 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17966040 | pubmed:articleTitle | A study of conformational restraints on reactivity of human PR3-specific autoantibodies (ANCA) facilitated through protein folding manipulations of a new recombinant proteinase 3 protein. | lld:pubmed |
pubmed-article:17966040 | pubmed:affiliation | UNC Kidney Center, University of North Carolina at Chapel Hill, NC 27599, USA. | lld:pubmed |
pubmed-article:17966040 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17966040 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:17966040 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17966040 | lld:pubmed |