| pubmed-article:20971110 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C0318256 | lld:lifeskim |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C0021669 | lld:lifeskim |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C0178666 | lld:lifeskim |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:20971110 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:20971110 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:20971110 | pubmed:dateCreated | 2010-11-15 | lld:pubmed |
| pubmed-article:20971110 | pubmed:abstractText | Vibrio vulnificus is an opportunistic human pathogen that causes severe infections in susceptible individuals. While the components of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system (PTS) have been shown to regulate numerous targets, little such information is available for the V. vulnificus PTS. Here we show that enzyme IIA(Glc) of the PTS regulates the peptidase activity of a mammalian insulysin homolog in V. vulnificus. While interaction of IIA(Glc) with the insulysin homolog is independent of the phosphorylation state of IIA(Glc), only unphosphorylated IIA(Glc) activates the insulysin homolog. Taken together, our results suggest that the V. vulnificus insulysin-IIA(Glc) complex plays a role in survival in the host by sensing glucose. | lld:pubmed |
| pubmed-article:20971110 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20971110 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20971110 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20971110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20971110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20971110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20971110 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20971110 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:20971110 | pubmed:issn | 1873-3468 | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:ParkSoon-Jung... | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:LeeKyu-HoKH | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:KooByoung-MoB... | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:SeokYeong-Jae... | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:KimYou-JinYJ | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:ChunSe-JinSJ | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:LeeNa YeonNY | lld:pubmed |
| pubmed-article:20971110 | pubmed:author | pubmed-author:RyuYangkyunY | lld:pubmed |
| pubmed-article:20971110 | pubmed:copyrightInfo | Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:20971110 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20971110 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:20971110 | pubmed:volume | 584 | lld:pubmed |
| pubmed-article:20971110 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20971110 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20971110 | pubmed:pagination | 4537-44 | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:meshHeading | pubmed-meshheading:20971110... | lld:pubmed |
| pubmed-article:20971110 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20971110 | pubmed:articleTitle | A mammalian insulysin homolog is regulated by enzyme IIA(Glc) of the glucose transport system in Vibrio vulnificus. | lld:pubmed |
| pubmed-article:20971110 | pubmed:affiliation | Department of Biophysics and Chemical Biology and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea. | lld:pubmed |
| pubmed-article:20971110 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20971110 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:3416 | entrezgene:pubmed | pubmed-article:20971110 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20971110 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20971110 | lld:entrezgene |
