pubmed-article:16329988 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16329988 | lifeskim:mentions | umls-concept:C1417769 | lld:lifeskim |
pubmed-article:16329988 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:16329988 | lifeskim:mentions | umls-concept:C2609570 | lld:lifeskim |
pubmed-article:16329988 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:16329988 | pubmed:dateCreated | 2005-12-13 | lld:pubmed |
pubmed-article:16329988 | pubmed:abstractText | It is well established that growth-factor-induced reactive oxygen species (ROS) act as second messengers in cell signaling. We have previously reported that betaPix, a guanine nucleotide exchange factor for Rac, interacts with NADPH oxidase 1 (Nox1) leading to EGF-induced ROS generation. Here, we report the identification of the domains of Nox1 and betaPix responsible for the interaction between the two proteins. GST pull-down assays show that the PH domain of betaPix binds to the FAD-binding region of Nox1. We also show that overexpression of the PH domain of betaPix results in inhibition of superoxide anion generation in response to EGF. Additionally, NADPH oxidase Organizer 1 (NoxO1) is shown to interact with the NADPH-binding region of Nox1. These results suggest that the formation of the complex consisting of Nox1, betaPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation. | lld:pubmed |
pubmed-article:16329988 | pubmed:language | eng | lld:pubmed |
pubmed-article:16329988 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16329988 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16329988 | pubmed:month | Jan | lld:pubmed |
pubmed-article:16329988 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:16329988 | pubmed:author | pubmed-author:ParkDongeunD | lld:pubmed |
pubmed-article:16329988 | pubmed:author | pubmed-author:BaeYun SooYS | lld:pubmed |
pubmed-article:16329988 | pubmed:author | pubmed-author:ParkHye SunHS | lld:pubmed |
pubmed-article:16329988 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16329988 | pubmed:day | 20 | lld:pubmed |
pubmed-article:16329988 | pubmed:volume | 339 | lld:pubmed |
pubmed-article:16329988 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16329988 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16329988 | pubmed:pagination | 985-90 | lld:pubmed |
pubmed-article:16329988 | pubmed:dateRevised | 2008-9-11 | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:meshHeading | pubmed-meshheading:16329988... | lld:pubmed |
pubmed-article:16329988 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16329988 | pubmed:articleTitle | Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1. | lld:pubmed |
pubmed-article:16329988 | pubmed:affiliation | Center for Cell Signaling Research, Division of Molecular Life Sciences, Ewha Womans University, Seoul 120-750, Republic of Korea. | lld:pubmed |
pubmed-article:16329988 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16329988 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:8874 | entrezgene:pubmed | pubmed-article:16329988 | lld:entrezgene |
entrez-gene:27035 | entrezgene:pubmed | pubmed-article:16329988 | lld:entrezgene |
entrez-gene:124056 | entrezgene:pubmed | pubmed-article:16329988 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16329988 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16329988 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16329988 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16329988 | lld:pubmed |