| pubmed-article:15556604 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15556604 | lifeskim:mentions | umls-concept:C0007367 | lld:lifeskim |
| pubmed-article:15556604 | lifeskim:mentions | umls-concept:C0020275 | lld:lifeskim |
| pubmed-article:15556604 | lifeskim:mentions | umls-concept:C1335280 | lld:lifeskim |
| pubmed-article:15556604 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:15556604 | lifeskim:mentions | umls-concept:C1149880 | lld:lifeskim |
| pubmed-article:15556604 | lifeskim:mentions | umls-concept:C1706701 | lld:lifeskim |
| pubmed-article:15556604 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15556604 | pubmed:dateCreated | 2004-11-23 | lld:pubmed |
| pubmed-article:15556604 | pubmed:abstractText | Here, we examined whether catalase binds SHP2 and alters SHP2 susceptibility to H2O2. Our results indicated that serum and fibrinogen commonly evoked catalase binding to SHP2 in HeLa and A549 cells in a herbimycin-A and TNFalpha sensitive manner. Expression of active catalase nearly 15-fold over control levels in tet-off HeLa cells substantially increased the SHP2 binding, and the catalase-associated SHP2 displayed significantly high phosphatase activities with a H2O2-resistance compared to those with little catalase. Site-directed mutagenesis at 280 abolished the binding capability of catalase to SHP2-SH2 in vitro. These results suggest that catalase-280pYIQV binds SHP2 via integrin-signaling to increase a H2O2-resistant SHP2 activity. | lld:pubmed |
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| pubmed-article:15556604 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15556604 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15556604 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15556604 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15556604 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15556604 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556604 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15556604 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15556604 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:15556604 | pubmed:author | pubmed-author:YanoSumioS | lld:pubmed |
| pubmed-article:15556604 | pubmed:author | pubmed-author:YanoNorikoN | lld:pubmed |
| pubmed-article:15556604 | pubmed:author | pubmed-author:ArroyoNellyN | lld:pubmed |
| pubmed-article:15556604 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15556604 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:15556604 | pubmed:volume | 577 | lld:pubmed |
| pubmed-article:15556604 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15556604 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15556604 | pubmed:pagination | 327-32 | lld:pubmed |
| pubmed-article:15556604 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:15556604 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15556604 | pubmed:articleTitle | SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling. | lld:pubmed |
| pubmed-article:15556604 | pubmed:affiliation | Department of Biochemistry, Ponce School of Medicine, Ponce, PR 00731, USA. yanos@coqui.net | lld:pubmed |
| pubmed-article:15556604 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15556604 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15556604 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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