pubmed-article:15225554 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15225554 | lifeskim:mentions | umls-concept:C0633227 | lld:lifeskim |
pubmed-article:15225554 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
pubmed-article:15225554 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
pubmed-article:15225554 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:15225554 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:15225554 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:15225554 | pubmed:dateCreated | 2004-6-30 | lld:pubmed |
pubmed-article:15225554 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:abstractText | Oxidative stress-induced cell damage is an important component of many diseases and ageing. In eukaryotes, activation of JNK/p38 stress-activated protein kinase (SAPK) signaling pathways is critical for the cellular response to stress. 2-Cys peroxiredoxins (2-Cys Prx) are highly conserved, extremely abundant antioxidant enzymes that catalyze the breakdown of peroxides to protect cells from oxidative stress. Here we reveal that Tpx1, the single 2-Cys Prx in Schizosaccharomyces pombe, is required for the peroxide-induced activation of the p38/JNK homolog, Sty1. Tpx1 activates Sty1, downstream of previously identified redox sensors, by a mechanism that involves formation of a peroxide-induced disulphide complex between Tpx1 and Sty1. We have identified conserved cysteines in Tpx1 and Sty1 that are essential for normal peroxide-induced Tpx1-Sty1 disulphide formation and Tpx1-dependent regulation of peroxide-induced Sty1 activation. Thus we provide new insight into the response of SAPKs to diverse stimuli by revealing a mechanism for SAPK activation specifically by oxidative stress. | lld:pubmed |
pubmed-article:15225554 | pubmed:language | eng | lld:pubmed |
pubmed-article:15225554 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15225554 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15225554 | pubmed:month | Jul | lld:pubmed |
pubmed-article:15225554 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:QuinnJanetJ | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:FindlayVictor... | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:MorganBrian... | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:VealElizabeth... | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:DayAlison MAM | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:BozonetStepha... | lld:pubmed |
pubmed-article:15225554 | pubmed:author | pubmed-author:EvansJennifer... | lld:pubmed |
pubmed-article:15225554 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15225554 | pubmed:day | 2 | lld:pubmed |
pubmed-article:15225554 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:15225554 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15225554 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15225554 | pubmed:pagination | 129-39 | lld:pubmed |
pubmed-article:15225554 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:15225554 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15225554 | pubmed:articleTitle | A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase. | lld:pubmed |
pubmed-article:15225554 | pubmed:affiliation | Institute of Cell and Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne, NE2 4HH, United Kingdom. e.a.veal@ncl.ac.uk | lld:pubmed |
pubmed-article:15225554 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15225554 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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