<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hassan, Ihab H.</style></author><author><style face="normal" font="default" size="100%">Zhang, Michael S.</style></author><author><style face="normal" font="default" size="100%">Powers, Linda S.</style></author><author><style face="normal" font="default" size="100%">Shao, Jian Q.</style></author><author><style face="normal" font="default" size="100%">Baltrusaitis, Jonas</style></author><author><style face="normal" font="default" size="100%">Rutkowski, D. Thomas</style></author><author><style face="normal" font="default" size="100%">Legge, Kevin</style></author><author><style face="normal" font="default" size="100%">Monick, Martha M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Influenza A Viral Replication Is Blocked by Inhibition of the Inositol-requiring Enzyme 1 (IRE1) Stress Pathway.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">influenza viral replication IRE1 stress pathway inhibition</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012///</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">American Society for Biochemistry and Molecular Biology</style></publisher><volume><style face="normal" font="default" size="100%">287</style></volume><pages><style face="normal" font="default" size="100%">4679 - 4689</style></pages><isbn><style face="normal" font="default" size="100%">0021-9258</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Known therapies for influenza A virus infection are complicated by the frequent emergence of resistance.  A therapeutic strategy that may escape viral resistance is targeting host cellular mechanisms involved in viral replication and pathogenesis.  The endoplasmic reticulum (ER) stress response, also known as the unfolded protein response (UPR), is a primitive, evolutionary conserved mol. signaling cascade that has been implicated in multiple biol. phenomena including innate immunity and the pathogenesis of certain viral infections.  We investigated the effect of influenza A viral infection on ER stress pathways in lung epithelial cells.  Influenza A virus induced ER stress in a pathway-specific manner.  We showed that the virus activates the IRE1 pathway with little or no concomitant activation of the PERK and the ATF6 pathways.  When we examd. the effects of modulating the ER stress response on the virus, we found that the mol. chaperone tauroursodeoxycholic acid (TUDCA) significantly inhibits influenza A viral replication.  In addn., a specific inhibitor of the IRE1 pathway also blocked viral replication.  Our findings constitute the first evidence that ER stress plays a role in the pathogenesis of influenza A viral infection.  Decreasing viral replication by modulating the host ER stress response is a novel strategy that has important therapeutic implications. [on SciFinder(R)]</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><notes><style face="normal" font="default" size="100%">CAPLUS AN 2012:212308(Journal; Online Computer File)</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Reisetter, Anna C.</style></author><author><style face="normal" font="default" size="100%">Stebounova, Larissa V.</style></author><author><style face="normal" font="default" size="100%">Baltrusaitis, Jonas</style></author><author><style face="normal" font="default" size="100%">Powers, Linda</style></author><author><style face="normal" font="default" size="100%">Gupta, Amit</style></author><author><style face="normal" font="default" size="100%">Grassian, Vicki H.</style></author><author><style face="normal" font="default" size="100%">Monick, Martha M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Induction of Inflammasome-dependent Pyroptosis by Carbon Black Nanoparticles.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">carbon black nanoparticle immunotoxicity inflammasome pyroptosis</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011///</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">American Society for Biochemistry and Molecular Biology</style></publisher><volume><style face="normal" font="default" size="100%">286</style></volume><pages><style face="normal" font="default" size="100%">21844 - 21852</style></pages><isbn><style face="normal" font="default" size="100%">0021-9258</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Inhalation of nanoparticles has been implicated in respiratory morbidity and mortality.  In particular, carbon black nanoparticles are found in many different environmental exposures.  Macrophages take up inhaled nanoparticles and respond via release of inflammatory mediators and in some cases cell death.  Based on new data, we propose that exposure of macrophages (both a macrophage cell line and primary human alveolar macrophages) to carbon black nanoparticles induces pyroptosis, an inflammasome-dependent form of cell death.  Exposure of macrophages to carbon black nanoparticles resulted in inflammasome activation as defined by cleavage of caspase 1 to its active form and downstream IL-1β release.  The cell death that occurred with carbon black nanoparticle exposure was identified as pyroptosis by the protective effect of a caspase 1 inhibitor and a pyroptosis inhibitor.  These data demonstrate that carbon black nanoparticle exposure activates caspase 1, increases IL-1β release after LPS priming, and induces the proinflammatory cell death, pyroptosis.  The identification of pyroptosis as a cellular response to carbon nanoparticle exposure is novel and relates to environmental and health impacts of carbon-based particulates. [on SciFinder(R)]</style></abstract><issue><style face="normal" font="default" size="100%">24</style></issue><notes><style face="normal" font="default" size="100%">CAPLUS AN 2011:737835(Journal)</style></notes></record></records></xml>