| pubmed-article:11090361 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11090361 | lifeskim:mentions | umls-concept:C0043405 | lld:lifeskim |
| pubmed-article:11090361 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:11090361 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:11090361 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:11090361 | lifeskim:mentions | umls-concept:C0332453 | lld:lifeskim |
| pubmed-article:11090361 | lifeskim:mentions | umls-concept:C0949455 | lld:lifeskim |
| pubmed-article:11090361 | pubmed:issue | 5496 | lld:pubmed |
| pubmed-article:11090361 | pubmed:dateCreated | 2000-11-30 | lld:pubmed |
| pubmed-article:11090361 | pubmed:abstractText | Homologs of the Yersinia virulence effector YopJ are found in both plant and animal bacterial pathogens, as well as plant symbionts. These YopJ family members were shown to act as cysteine proteases. The catalytic triad of the protease was required for inhibition of the mitogen-activated protein kinase (MAPK) and nuclear factor kappaB (NF-kappaB) signaling in animal cells and for induction of localized cell death in plants. The substrates for YopJ were shown to be highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ family members exert their pathogenic effect on cells by disrupting this posttranslational modification. | lld:pubmed |
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| pubmed-article:11090361 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11090361 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11090361 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11090361 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11090361 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:DixonJ EJE | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:XuZZ | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:MangelW FWF | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:TamH SHS | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:BliskaJ BJB | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:OrthKK | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:StaskawiczBB | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:PalmerL ELE | lld:pubmed |
| pubmed-article:11090361 | pubmed:author | pubmed-author:MudgettM BMB | lld:pubmed |
| pubmed-article:11090361 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11090361 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:11090361 | pubmed:volume | 290 | lld:pubmed |
| pubmed-article:11090361 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11090361 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11090361 | pubmed:pagination | 1594-7 | lld:pubmed |
| pubmed-article:11090361 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11090361 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11090361 | pubmed:articleTitle | Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. | lld:pubmed |
| pubmed-article:11090361 | pubmed:affiliation | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA. | lld:pubmed |
| pubmed-article:11090361 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11090361 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11090361 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11090361 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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