Lewis, Huw D.Liddle, JohnCoote, Jim E.Atkinson, Stephen J.Barker, Michael D.Bax, Benjamin D.Bicker, Kevin L.Bingham, Ryan P.Campbell, MatthewChen, Yu HuaChung, Chun-waCraggs, Peter D.Davis, Rob P.Eberhard, DirkJoberty, GerardLind, Kenneth E.Locke, KellyMaller, ClaireMartinod, KimberlyPatten, ChrisPolyakova, OxanaRise, Cecil E.Rüdiger, MartinSheppard, Robert J.Slade, Daniel J.Thomas, PamelaThorpe, JimYao, GangDrewes, GerardWagner, Denisa D.Thompson, Paul R.Prinjha, Rab K.Wilson, David M.2016-11-092016-11-092015-03http://hdl.handle.net/10919/73404PAD4 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.189 - 191 page(s)application/pdfenIn CopyrightAnimalsBenzimidazolesBinding, CompetitiveCalciumCitrullineEnzyme InhibitorsHEK293 CellsHistonesHumansHydrolasesIn Vitro TechniquesMiceModels, MolecularNeutrophilsSmall Molecule LibrariesSubstrate SpecificityArticle - Refereedhttps://doi.org/10.1038/nchembio.17351131552-4469