Inhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation.

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dc.contributor.authorLewis, Huw D.en
dc.contributor.authorLiddle, Johnen
dc.contributor.authorCoote, Jim E.en
dc.contributor.authorAtkinson, Stephen J.en
dc.contributor.authorBarker, Michael D.en
dc.contributor.authorBax, Benjamin D.en
dc.contributor.authorBicker, Kevin L.en
dc.contributor.authorBingham, Ryan P.en
dc.contributor.authorCampbell, Matthewen
dc.contributor.authorChen, Yu Huaen
dc.contributor.authorChung, Chun-waen
dc.contributor.authorCraggs, Peter D.en
dc.contributor.authorDavis, Rob P.en
dc.contributor.authorEberhard, Dirken
dc.contributor.authorJoberty, Gerarden
dc.contributor.authorLind, Kenneth E.en
dc.contributor.authorLocke, Kellyen
dc.contributor.authorMaller, Claireen
dc.contributor.authorMartinod, Kimberlyen
dc.contributor.authorPatten, Chrisen
dc.contributor.authorPolyakova, Oxanaen
dc.contributor.authorRise, Cecil E.en
dc.contributor.authorRüdiger, Martinen
dc.contributor.authorSheppard, Robert J.en
dc.contributor.authorSlade, Daniel J.en
dc.contributor.authorThomas, Pamelaen
dc.contributor.authorThorpe, Jimen
dc.contributor.authorYao, Gangen
dc.contributor.authorDrewes, Gerarden
dc.contributor.authorWagner, Denisa D.en
dc.contributor.authorThompson, Paul R.en
dc.contributor.authorPrinjha, Rab K.en
dc.contributor.authorWilson, David M.en
dc.contributor.departmentBiochemistryen
dc.contributor.departmentCenter for Drug Discoveryen
dc.coverage.spatialUnited Statesen
dc.date.accessioned2016-11-09T02:59:20Zen
dc.date.available2016-11-09T02:59:20Zen
dc.date.issued2015-03en
dc.description.abstractPAD4 has been strongly implicated in the pathogenesis of autoimmune, cardiovascular and oncological diseases through clinical genetics and gene disruption in mice. New selective PAD4 inhibitors binding a calcium-deficient form of the PAD4 enzyme have validated the critical enzymatic role of human and mouse PAD4 in both histone citrullination and neutrophil extracellular trap formation for, to our knowledge, the first time. The therapeutic potential of PAD4 inhibitors can now be explored.en
dc.description.versionPublished versionen
dc.format.extent189 - 191 page(s)en
dc.identifier.doihttps://doi.org/10.1038/nchembio.1735en
dc.identifier.eissn1552-4469en
dc.identifier.issue3en
dc.identifier.urihttp://hdl.handle.net/10919/73404en
dc.identifier.volume11en
dc.language.isoenen
dc.relation.urihttp://www.ncbi.nlm.nih.gov/pubmed/25622091en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectAnimalsen
dc.subjectBenzimidazolesen
dc.subjectBinding, Competitiveen
dc.subjectCalciumen
dc.subjectCitrullineen
dc.subjectEnzyme Inhibitorsen
dc.subjectHEK293 Cellsen
dc.subjectHistonesen
dc.subjectHumansen
dc.subjectHydrolasesen
dc.subjectIn Vitro Techniquesen
dc.subjectMiceen
dc.subjectModels, Molecularen
dc.subjectNeutrophilsen
dc.subjectSmall Molecule Librariesen
dc.subjectSubstrate Specificityen
dc.titleInhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation.en
dc.title.serialNature Chemical Biologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherResearch Support, N.I.H., Extramuralen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biochemistryen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen

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