| pubmed-article:11007483 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11007483 | lifeskim:mentions | umls-concept:C0002191 | lld:lifeskim |
| pubmed-article:11007483 | lifeskim:mentions | umls-concept:C0036764 | lld:lifeskim |
| pubmed-article:11007483 | lifeskim:mentions | umls-concept:C0165519 | lld:lifeskim |
| pubmed-article:11007483 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:11007483 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
| pubmed-article:11007483 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:11007483 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11007483 | pubmed:dateCreated | 2000-10-4 | lld:pubmed |
| pubmed-article:11007483 | pubmed:abstractText | We have identified the key protein substrate of gelatinase B/MMP-9 (GB) that is cleaved in vivo during dermal-epidermal separation triggered by antibodies to the hemidesmosomal protein BP180 (collagen XVII, BPAG2). Mice deficient in either GB or neutrophil elastase (NE) are resistant to blister formation in response to these antibodies in a mouse model of the autoimmune disease bullous pemphigoid. Disease develops upon complementation of GB -/- mice with NE -/- neutrophils or NE -/- mice with GB -/- neutrophils. Only NE degrades BP180 and produces dermal-epidermal separation in vivo and in culture. Instead, GB acts upstream to regulates NE activity by inactivating alpha1-proteinase inhibitor (alpha1-PI). Excess NE produces lesions in GB -/- mice without cleaving alpha1-PI. Excess alpha1-PI phenocopies GB and NE deficiency in wild-type mice. | lld:pubmed |
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| pubmed-article:11007483 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11007483 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11007483 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11007483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11007483 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11007483 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11007483 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:LimRR | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:TwiningS SSS | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:WerbZZ | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:DiazL ALA | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:SeniorR MRM | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:ZhouXX | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:ShapiroS DSD | lld:pubmed |
| pubmed-article:11007483 | pubmed:author | pubmed-author:ShipleyJ MJM | lld:pubmed |
| pubmed-article:11007483 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11007483 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11007483 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:11007483 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11007483 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11007483 | pubmed:pagination | 647-55 | lld:pubmed |
| pubmed-article:11007483 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:11007483 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11007483 | pubmed:articleTitle | The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. | lld:pubmed |
| pubmed-article:11007483 | pubmed:affiliation | Department of Dermatology, University of North Carolina, Chapel Hill 27599, USA. zhiliu@med.unc.edu | lld:pubmed |
| pubmed-article:11007483 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11007483 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11007483 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11007483 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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