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Microbiol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0370","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1009001","article-title":"Fluorescent secreted bacterial effectors reveal active intravacuolar proliferation of Listeria monocytogenes in epithelial cells","volume":"16","author":"Peron-Cane","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbamem.2021.183604_bb0375","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1111\/j.1462-5822.2005.00665.x","article-title":"Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles","volume":"8","author":"Shaughnessy","year":"2006","journal-title":"Cell. Microbiol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0380","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1038\/nature07344","article-title":"GILT is a critical host factor for Listeria monocytogenes infection","volume":"455","author":"Singh","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2021.183604_bb0385","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1083\/jcb.200201081","article-title":"The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells","volume":"156","author":"Glomski","year":"2002","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0390","doi-asserted-by":"crossref","first-page":"42231","DOI":"10.1038\/srep42231","article-title":"Engineering a pH responsive pore forming protein","volume":"7","author":"Kisovec","year":"2017","journal-title":"Sci. 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Dis."},{"key":"10.1016\/j.bbamem.2021.183604_bb0445","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0008610","article-title":"Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection","volume":"5","author":"Meyer-Morse","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamem.2021.183604_bb0450","doi-asserted-by":"crossref","first-page":"3066","DOI":"10.1038\/emboj.2013.234","article-title":"Listeria phospholipases subvert host autophagic defenses by stalling pre-autophagosomal structures","volume":"32","author":"Tattoli","year":"2013","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamem.2021.183604_bb0455","doi-asserted-by":"crossref","first-page":"48","DOI":"10.15698\/mic2014.01.124","article-title":"Stalling autophagy: a new function for Listeria phospholipases","volume":"1","author":"Tattoli","year":"2014","journal-title":"Microb Cell"},{"key":"10.1016\/j.bbamem.2021.183604_bb0460","doi-asserted-by":"crossref","first-page":"E210","DOI":"10.1073\/pnas.1716055115","article-title":"Listeria monocytogenes triggers noncanonical autophagy upon phagocytosis, but avoids subsequent growth-restricting xenophagy","volume":"115","author":"Mitchell","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2021.183604_bb0465","doi-asserted-by":"crossref","first-page":"13467","DOI":"10.1073\/pnas.0702729104","article-title":"Histone modifications induced by a family of bacterial toxins","volume":"104","author":"Hamon","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2021.183604_bb0470","doi-asserted-by":"crossref","first-page":"7859","DOI":"10.4049\/jimmunol.180.12.7859","article-title":"Dependency of caspase-1 activation induced in macrophages by Listeria monocytogenes on cytolysin, listeriolysin O, after evasion from phagosome into the cytoplasm","volume":"180","author":"Hara","year":"2008","journal-title":"J. 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Microbiol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0485","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1002\/j.1460-2075.1994.tb06318.x","article-title":"The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton","volume":"13","author":"Pistor","year":"1994","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamem.2021.183604_bb0490","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1083\/jcb.109.4.1597","article-title":"Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes","volume":"109","author":"Tilney","year":"1989","journal-title":"J Cell Biol"},{"key":"10.1016\/j.bbamem.2021.183604_bb0495","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/sj.emboj.7600595","article-title":"Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell","volume":"24","author":"Pust","year":"2005","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamem.2021.183604_bb0500","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1093\/infdis\/jiu546","article-title":"The diaphanous-related formins promote protrusion formation and cell-to-cell spread of Listeria monocytogenes","volume":"211","author":"Fattouh","year":"2015","journal-title":"J. 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Microbiol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0535","doi-asserted-by":"crossref","first-page":"5755","DOI":"10.1021\/bi972948k","article-title":"General base catalysis by the phosphatidylcholine-preferring phospholipase C from Bacillus cereus: the role of Glu4 and Asp55","volume":"37","author":"Martin","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2021.183604_bb0540","doi-asserted-by":"crossref","first-page":"6639","DOI":"10.1128\/IAI.73.10.6639-6646.2005","article-title":"Characterization of Listeria monocytogenes expressing Anthrolysin O and phosphatidylinositol-specific phospholipase C from Bacillus anthracis","volume":"73","author":"Wei","year":"2005","journal-title":"Infect. 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Bacteriol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0550","doi-asserted-by":"crossref","first-page":"3578","DOI":"10.1021\/bi802312d","article-title":"Listeria monocytogenes phosphatidylinositol-specific phospholipase C: kinetic activation and homing in on different interfaces","volume":"48","author":"Chen","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2021.183604_bb0555","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.bbapap.2016.03.008","article-title":"Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH","volume":"1864","author":"Huang","year":"2016","journal-title":"Biochim. Biophys. 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Rev."},{"key":"10.1016\/j.bbamem.2021.183604_bb0575","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/338357a0","article-title":"High-resolution (1.5 \u00c5) crystal structure of phospholipase C from Bacillus cereus","volume":"338","author":"Hough","year":"1989","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2021.183604_bb0580","doi-asserted-by":"crossref","first-page":"3010","DOI":"10.4049\/jimmunol.161.6.3010","article-title":"Two distinct phospholipases C of Listeria monocytogenes induce ceramide generation, nuclear factor-kappa B activation, and E-selectin expression in human endothelial cells","volume":"161","author":"Schwarzer","year":"1998","journal-title":"J. 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A."},{"key":"10.1016\/j.bbamem.2021.183604_bb0635","doi-asserted-by":"crossref","first-page":"3690","DOI":"10.1038\/ncomms4690","article-title":"Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation","volume":"5","author":"Koster","year":"2014","journal-title":"Nature Comm"},{"key":"10.1016\/j.bbamem.2021.183604_bb0640","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/S0092-8674(00)80251-2","article-title":"Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form","volume":"89","author":"Rossjohn","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.bbamem.2021.183604_bb0645","doi-asserted-by":"crossref","first-page":"14352","DOI":"10.1038\/srep14352","article-title":"Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation","volume":"5","author":"Lawrence","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2021.183604_bb0650","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.jmb.2013.11.020","article-title":"Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration","volume":"426","author":"Feil","year":"2014","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2021.183604_bb0655","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1007\/s13238-010-0012-3","article-title":"Crystal structure of cytotoxin protein suilysin from Streptococcus suis","volume":"1","author":"Xu","year":"2010","journal-title":"Protein Cell"},{"key":"10.1016\/j.bbamem.2021.183604_bb0660","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1016\/j.str.2016.06.017","article-title":"Structural basis for receptor recognition by the human CD59-responsive cholesterol-dependent cytolysins","volume":"24","author":"Lawrence","year":"2016","journal-title":"Structure"},{"key":"10.1016\/j.bbamem.2021.183604_bb0665","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1111\/j.1348-0421.2005.tb03661.x","article-title":"Involvement of reactive oxygen intermediate in the enhanced expression of virulence-associated genes of Listeria monocytogenes inside activated macrophages","volume":"49","author":"Makino","year":"2005","journal-title":"Microbiol. 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