What planar lipid membranes tell us about the pore-forming activity of cholesterol-dependent cytolysins.
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[1] G. Anderluh,et al. Effects of MACPF/CDC proteins on lipid membranes , 2013, Cellular and Molecular Life Sciences.
[2] S. Cassidy,et al. More Than a Pore: The Cellular Response to Cholesterol-Dependent Cytolysins , 2013, Toxins.
[3] H. Bayley,et al. Lipid-coated hydrogel shapes as components of electrical circuits and mechanical devices , 2012, Scientific Reports.
[4] R. Tweten,et al. Identification and Characterization of the First Cholesterol-Dependent Cytolysins from Gram-Negative Bacteria , 2012, Infection and Immunity.
[5] Minchen Chien,et al. PEG-Labeled Nucleotides and Nanopore Detection for Single Molecule DNA Sequencing by Synthesis , 2012, Scientific Reports.
[6] D. DeVoe,et al. Dynamics of Ceramide Channels Detected Using a Microfluidic System , 2012, PloS one.
[7] P. Cossart,et al. Listeriolysin O: the Swiss army knife of Listeria. , 2012, Trends in microbiology.
[8] K. Mann,et al. Targeting Her-2+ breast cancer cells with bleomycin immunoliposomes linked to LLO. , 2012, Molecular pharmaceutics.
[9] R. Tweten,et al. Membrane assembly of the cholesterol-dependent cytolysin pore complex. , 2012, Biochimica et biophysica acta.
[10] M. Pangburn,et al. Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9. , 2012, Cell reports.
[11] M. Parker,et al. Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity. , 2012, Structure.
[12] B. Konforti,et al. More than the sum of its parts. , 2012, Cell reports.
[13] B. Le Pioufle,et al. Activity monitoring of functional OprM using a biomimetic microfluidic device. , 2012, The Analyst.
[14] R. Liddington,et al. Structure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)*♦ , 2012, The Journal of Biological Chemistry.
[15] H. Bayley,et al. Protein Detection by Nanopores Equipped with Aptamers , 2012, Journal of the American Chemical Society.
[16] J. Lakey,et al. pH dependence of listeriolysin O aggregation and pore‐forming ability , 2012, The FEBS journal.
[17] M. Serra,et al. Pore-forming Toxins , 2011 .
[18] H. Bayley,et al. Rapid assembly of a multimeric membrane protein pore. , 2011, Biophysical journal.
[19] R. Collier,et al. Ultrasensitive detection of protein translocated through toxin pores in droplet-interface bilayers , 2011, Proceedings of the National Academy of Sciences.
[20] G. Anderluh,et al. Human Perforin Employs Different Avenues to Damage Membranes* , 2010, The Journal of Biological Chemistry.
[21] A. Berezhkovskii,et al. Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor. , 2010, Biophysical journal.
[22] Xuemei Li,et al. Crystal structure of cytotoxin protein suilysin from Streptococcus suis , 2010, Protein & Cell.
[23] B. Bishop,et al. Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis* , 2009, Journal of Biological Chemistry.
[24] H. Bayley,et al. Continuous base identification for single-molecule nanopore DNA sequencing. , 2009, Nature nanotechnology.
[25] H. Bayley,et al. Simultaneous measurement of ionic current and fluorescence from single protein pores. , 2009, Journal of the American Chemical Society.
[26] Kyung-Dall Lee,et al. Enhanced gene delivery using disulfide-crosslinked low molecular weight polyethylenimine with listeriolysin o-polyethylenimine disulfide conjugate. , 2008, Journal of controlled release : official journal of the Controlled Release Society.
[27] J. Lakey,et al. Disparate proteins use similar architectures to damage membranes. , 2008, Trends in biochemical sciences.
[28] P. E. Granum,et al. Demonstration of a cholesterol-dependent cytolysin in a noninsecticidal Bacillus sphaericus strain and evidence for widespread distribution of the toxin within the species. , 2008, FEMS microbiology letters.
[29] Ashley M Buckle,et al. The MACPF/CDC family of pore-forming toxins , 2008, Cellular microbiology.
[30] F. G. van der Goot,et al. Pore formation: an ancient yet complex form of attack. , 2008, Biochimica et biophysica acta.
[31] P. Andrew,et al. Pneumolysin generates multiple conductance pores in the membrane of nucleated cells. , 2008, Biochemical and biophysical research communications.
[32] S. Gelber,et al. Functional and Phylogenetic Characterization of Vaginolysin, the Human-Specific Cytolysin from Gardnerella vaginalis , 2008, Journal of bacteriology.
[33] R. Lemmens‐Gruber,et al. IFN-β Increases Listeriolysin O-Induced Membrane Permeabilization and Death of Macrophages1 , 2008, The Journal of Immunology.
[34] Helen R Saibil,et al. Friend or foe: the same fold for attack and defense. , 2008, Trends in immunology.
[35] Y. Santoso,et al. Enhanced stability and fluidity in droplet on hydrogel bilayers for measuring membrane protein diffusion. , 2007, Nano letters.
[36] R. Benz,et al. Anthrax lethal factor (LF) mediated block of the anthrax protective antigen (PA) ion channel: effect of ionic strength and voltage. , 2006, Biochemistry.
[37] R. Tweten,et al. Cholesterol-Dependent Cytolysins, a Family of Versatile Pore-Forming Toxins , 2005, Infection and Immunity.
[38] R. Gilbert. Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us. , 2005, Structure.
[39] M. Parker,et al. Pore-forming protein toxins: from structure to function. , 2005, Progress in biophysics and molecular biology.
[40] M. Parker,et al. Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[41] P. Sims,et al. Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin , 2004, Nature Structural &Molecular Biology.
[42] R. Collier,et al. Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[43] Zhifeng Shao,et al. Vertical collapse of a cytolysin prepore moves its transmembrane β‐hairpins to the membrane , 2004, The EMBO journal.
[44] R. Tweten,et al. Assembly and Topography of the Prepore Complex in Cholesterol-dependent Cytolysins* , 2003, Journal of Biological Chemistry.
[45] R. Tweten,et al. Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin , 2002, Nature Structural Biology.
[46] E. Domann,et al. Listeriolysin of Listeria monocytogenes forms Ca2+‐permeable pores leading to intracellular Ca2+ oscillations , 2002, Cellular microbiology.
[47] R. Gilbert,et al. Pore-forming toxins , 2002, Cellular and Molecular Life Sciences CMLS.
[48] R. Tweten,et al. The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins. , 2000, Biochemistry.
[49] C. Boulin,et al. Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter , 2000 .
[50] S. Bezrukov,et al. Polymeric nonelectrolytes to probe pore geometry: application to the alpha-toxin transmembrane channel. , 1999, Biophysical journal.
[51] Y. Korchev,et al. A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers. , 1998, The Biochemical journal.
[52] Michael W Parker,et al. Structure of a Cholesterol-Binding, Thiol-Activated Cytolysin and a Model of Its Membrane Form , 1997, Cell.
[53] Y. Korchev,et al. Differential sensitivity of pneumolysin-induced channels to gating by divalent cations , 1992, The Journal of Membrane Biology.
[54] J. Shiver,et al. Formation of ion-conducting channels by the membrane attack complex proteins of complement. , 1991, Biophysical journal.
[55] A. Delcour,et al. Electrophysiological characterization of bacterial pore-forming proteins in planar lipid bilayers. , 2013, Methods in molecular biology.
[56] R. Gilbert. Cholesterol-dependent cytolysins. , 2010, Advances in experimental medicine and biology.
[57] G. Menestrina,et al. Liposomes in the study of pore-forming toxins. , 2003, Methods in enzymology.
[58] '. Robertblumenthal. Mechanism of Tetanolysin-Induced Membrane Damage : Studies with Black Lipid Membranes , 2003 .
[59] M. Parker,et al. The cholesterol-dependent cytolysins. , 2001, Current topics in microbiology and immunology.
[60] G. Menestrina,et al. Characterization of molecular properties of pore-forming toxins with planar lipid bilayers. , 2000, Methods in molecular biology.
[61] G. Menestrina,et al. Pore-forming toxins: experiments with S. aureus alpha-toxin, C. perfringens theta-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells. , 1990, Toxicon : official journal of the International Society on Toxinology.
[62] G. Menestrina,et al. Pore-forming toxins: Experiments with S. aureus α-toxin, C. perfringens θ-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells , 1990 .
[63] S. Spragg. Biophysical chemistry , 1979, Nature.