, Academic Cell, vol.11, pp.365-392, 2016.
, Pharmaceutical Sciences Encyclopedia, 2015.
Disparate proteins use similar architectures to damage membranes, Trends in Biochemical Sciences, vol.33, issue.10, pp.482-490, 2008. ,
DOI : 10.1016/j.tibs.2008.07.004
Membrane pore formation at protein???lipid interfaces, Trends in Biochemical Sciences, vol.39, issue.11, pp.510-516, 2014. ,
DOI : 10.1016/j.tibs.2014.09.002
Engineered transmembrane pores, Current Opinion in Chemical Biology, vol.34, pp.117-126, 2016. ,
DOI : 10.1016/j.cbpa.2016.08.005
URL : http://europepmc.org/articles/pmc5123773?pdf=render
Channel-Forming Bacterial Toxins in Biosensing and Macromolecule Delivery, Toxins, vol.278, issue.8, pp.2483-2540, 2014. ,
DOI : 10.1007/s00210-010-0581-y
URL : https://www.mdpi.com/2072-6651/6/8/2483/pdf
Nucleobase Recognition by Truncated ??-Hemolysin Pores, ACS Nano, vol.9, issue.8, pp.7895-7903, 2015. ,
DOI : 10.1021/nn5060317
URL : http://europepmc.org/articles/pmc4830132?pdf=render
Detection of 3???-End RNA Uridylation with a Protein Nanopore, ACS Nano, vol.8, issue.2, pp.1364-1374, 2014. ,
DOI : 10.1021/nn4050479
URL : http://europepmc.org/articles/pmc3936189?pdf=render
Nanopore-Based Identification of Individual Nucleotides for Direct RNA Sequencing, Nano Letters, vol.13, issue.12, pp.6144-6150, 2013. ,
DOI : 10.1021/nl403469r
URL : http://europepmc.org/articles/pmc3899427?pdf=render
Real-time, portable genome sequencing for Ebola surveillance, Nature, vol.504, issue.7589, pp.228-232, 2016. ,
DOI : 10.1093/bioinformatics/btp163
URL : http://europepmc.org/articles/pmc4817224?pdf=render
Semisynthetic Nanoreactor for Reversible Single-Molecule Covalent Chemistry, ACS Nano, vol.10, issue.9, pp.8843-8850, 2016. ,
DOI : 10.1021/acsnano.6b04663
URL : http://doi.org/10.1021/acsnano.6b04663
The evolution and epidemiology of Listeria monocytogenes in Europe and the United States, Infection, Genetics and Evolution, vol.35, pp.172-183, 2015. ,
DOI : 10.1016/j.meegid.2015.08.008
, Scientific RepoRts | 7:42231 | DOI: 10.1038/srep42231 13. Birmingham, C. L. et al. Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles, Nature, vol.451, pp.350-354, 2008.
Listeria monocytogenes exploits efferocytosis to promote cell-to-cell spread, Nature, vol.3, issue.7499, pp.230-234, 2014. ,
DOI : 10.1046/j.1462-5822.2001.00087.x
Listeriolysin O: the Swiss army knife of Listeria, Trends in Microbiology, vol.20, issue.8, pp.360-368, 2012. ,
DOI : 10.1016/j.tim.2012.04.006
, Proteins -Agents of Defence, vol.9, pp.161-195, 2014.
Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation, Nature Communications, vol.248, issue.1, p.3690, 2014. ,
DOI : 10.1093/nar/gkm276
The Unique Molecular Choreography of Giant Pore Formation by the Cholesterol-Dependent Cytolysins of Gram-Positive Bacteria, Annual Review of Microbiology, vol.69, issue.1, pp.323-340, 2015. ,
DOI : 10.1146/annurev-micro-091014-104233
, Biochemistry, vol.46, issue.14, pp.4425-4437, 2007.
DOI : 10.1021/bi602497g
Plasticity of Listeriolysin O Pores and its Regulation by pH and Unique Histidine, Scientific Reports, vol.9, issue.1, p.9623, 2015. ,
DOI : 10.1038/nmeth.2089
Listeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic Vacuole, PLOS Pathogens, vol.60, issue.4, p.1005597, 2016. ,
DOI : 10.1371/journal.ppat.1005597.s011
URL : https://hal.archives-ouvertes.fr/inserm-01307112
Molecular basis of listeriolysin O pH dependence, Proc. Natl. Acad. Sci. USA, pp.12537-12542, 2005. ,
DOI : 10.1002/elps.1150181505
pH dependence of listeriolysin O aggregation and pore-forming ability, FEBS Journal, vol.145, issue.1, pp.126-141, 2012. ,
DOI : 10.1016/j.chemphyslip.2006.02.010
Trastuzumab-targeted gene delivery to Her2-overexpressing breast cancer cells, Cancer Gene Therapy, vol.12, issue.7, pp.221-228, 2016. ,
DOI : 10.1007/s12094-011-0744-4
, , pp.117-129, 2015.
ABSTRACT, Clinical and Vaccine Immunology, vol.20, issue.1, pp.77-84, 2013. ,
DOI : 10.1128/CVI.00488-12
Adjuvant properties of listeriolysin O protein in a DNA vaccination strategy, Cancer Immunology, Immunotherapy, vol.39, issue.6, pp.797-806, 2006. ,
DOI : 10.4049/jimmunol.171.6.2970
Irreversible loss of membrane-binding activity of Listeria-derived cytolysins in non-acidic conditions: a distinct difference from allied cytolysins produced by other Gram-positive bacteria, Microbiology, vol.153, issue.7, pp.2250-2258, 2007. ,
DOI : 10.1099/mic.0.2007/005843-0
Structures of Perfringolysin O Suggest a Pathway for Activation of Cholesterol-dependent Cytolysins, Journal of Molecular Biology, vol.367, issue.5, pp.1227-1236, 2007. ,
DOI : 10.1016/j.jmb.2007.01.042
URL : http://europepmc.org/articles/pmc3674820?pdf=render
A New Model for Pore Formation by Cholesterol-Dependent Cytolysins, PLoS Computational Biology, vol.66, issue.8, p.1003791, 2014. ,
DOI : 10.1371/journal.pcbi.1003791.s019
URL : https://doi.org/10.1371/journal.pcbi.1003791
The Pore-Forming Toxin Listeriolysin O Mediates a Novel Entry Pathway of L. monocytogenes into Human Hepatocytes, PLoS Pathogens, vol.13, issue.11, p.1002356, 2011. ,
DOI : 10.1371/journal.ppat.1002356.s017
URL : https://doi.org/10.1371/journal.ppat.1002356
Filming Biomolecular Processes by High-Speed Atomic Force Microscopy, Chemical Reviews, vol.114, issue.6, pp.3120-3188, 2014. ,
DOI : 10.1021/cr4003837
URL : https://doi.org/10.1021/cr4003837
Glasslike Membrane Protein Diffusion in a Crowded Membrane, ACS Nano, vol.10, issue.2, pp.2584-2590, 2016. ,
DOI : 10.1021/acsnano.5b07595
URL : http://www.hal.inserm.fr/inserm-01285787/file/Munguira_et_al_ACS-Nano-Manuscript_Corrected.pdf
Assemblies of pore-forming toxins visualized by atomic force microscopy, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1858, issue.3, pp.500-511, 2016. ,
DOI : 10.1016/j.bbamem.2015.11.005
URL : https://doi.org/10.1016/j.bbamem.2015.11.005
Human perforin permeabilizing activity, but not binding to lipid membranes, is affected by pH, Molecular Immunology, vol.47, issue.15, pp.2492-2504, 2010. ,
DOI : 10.1016/j.molimm.2010.06.001
Listeriolysin O Affects the Permeability of Caco-2 Monolayer in a Pore-Dependent and Ca 2+ -Independent Manner, PLoS ONE, vol.10, p.130471, 2015. ,
Illumination of the Spatial Order of Intracellular pH by Genetically Encoded pH-Sensitive Sensors, Sensors, vol.32, issue.12, pp.16736-16758, 2013. ,
DOI : 10.1038/emboj.2013.124
Engineering color variants of green fluorescent protein (GFP) for thermostability, pH-sensitivity, and improved folding kinetics, Applied Microbiology and Biotechnology, vol.279, issue.3, pp.1205-1216, 2014. ,
DOI : 10.1074/jbc.M402405200
Engineering pH responsive fibronectin domains for biomedical applications, Journal of Biological Engineering, vol.1, issue.2, p.6, 2015. ,
DOI : 10.1038/nprot.2006.94
URL : https://jbioleng.biomedcentral.com/track/pdf/10.1186/s13036-015-0004-1?site=jbioleng.biomedcentral.com
pH-dependent Binding Engineering Reveals an FcRn Affinity Threshold That Governs IgG Recycling, Journal of Biological Chemistry, vol.158, issue.7, pp.4282-4290, 2015. ,
DOI : 10.1093/protein/gzq009
URL : http://www.jbc.org/content/290/7/4282.full.pdf
Construction of pH-sensitive Her2-binding IgG1-Fc by directed evolution, Biotechnology Journal, vol.26, issue.8, pp.1013-1022, 2014. ,
DOI : 10.1093/protein/gzt041
URL : http://onlinelibrary.wiley.com/doi/10.1002/biot.201300483/pdf
A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches, Protein Science, vol.60, issue.9, pp.1619-1631, 2011. ,
DOI : 10.1107/S0907444904019158
URL : http://onlinelibrary.wiley.com/doi/10.1002/pro.696/pdf
Structure-based histidine substitution for optimizing pH-sensitive Staphylococcus protein A, Journal of Chromatography B, vol.929, pp.155-160, 2013. ,
DOI : 10.1016/j.jchromb.2013.04.029
GALA: a designed synthetic pH-responsive amphipathic peptide with applications in drug and gene delivery, Advanced Drug Delivery Reviews, vol.56, issue.7, pp.967-985, 2004. ,
DOI : 10.1016/j.addr.2003.10.041
Engineering allostery, Trends in Genetics, vol.30, issue.12, pp.521-528, 2014. ,
DOI : 10.1016/j.tig.2014.09.004
URL : https://manuscript.elsevier.com/S0168952514001401/pdf/S0168952514001401.pdf
Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA, Analytical Biochemistry, vol.319, issue.2, pp.335-336, 2003. ,
DOI : 10.1016/S0003-2697(03)00286-0
GROMACS 4:?? Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation, Journal of Chemical Theory and Computation, vol.4, issue.3, pp.435-447, 2008. ,
DOI : 10.1021/ct700301q
Comparison of simple potential functions for simulating liquid water, The Journal of Chemical Physics, vol.79, issue.2, pp.926-935, 1983. ,
DOI : 10.1016/0009-2614(80)85344-9
All-atom empirical force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data, Journal of Computational Chemistry, vol.7, issue.2, pp.86-104, 2000. ,
DOI : 10.1007/978-1-4684-8580-6_2
Canonical sampling through velocity rescaling, The Journal of Chemical Physics, vol.126, issue.1, p.14101, 2007. ,
DOI : 10.1007/978-3-642-61544-3
URL : http://arxiv.org/pdf/0803.4060
Polymorphic transitions in single crystals: A new molecular dynamics method, Journal of Applied Physics, vol.52, issue.12, pp.7182-7190, 1981. ,
DOI : 10.1103/PhysRevA.22.1690
A smooth particle mesh Ewald method, The Journal of Chemical Physics, vol.100, issue.19, pp.8577-8593, 1995. ,
DOI : 10.1063/1.470043
The PyMOL Molecular Graphics System, Version 1, p.2015 ,
VMD: Visual molecular dynamics, Journal of Molecular Graphics, vol.14, issue.1, pp.33-38, 1996. ,
DOI : 10.1016/0263-7855(96)00018-5
H++ 3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations, Nucleic Acids Research, vol.25, issue.16, pp.537-541, 2012. ,
DOI : 10.1002/jcc.20139
H++: a server for estimating pKas and adding missing hydrogens to macromolecules, Nucleic Acids Research, vol.33, issue.Web Server, pp.368-371, 2005. ,
DOI : 10.1093/nar/gki464
URL : https://academic.oup.com/nar/article-pdf/33/suppl_2/W368/7623463/gki464.pdf
A simple clustering algorithm can be accurate enough for use in calculations of pKs in macromolecules, Proteins: Structure, Function, and Bioinformatics, vol.40, issue.12, pp.928-938, 2006. ,
DOI : 10.1021/jp963412w
pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model, Biochemistry, vol.29, issue.44, pp.10219-10225, 1990. ,
DOI : 10.1021/bi00496a010
Fiji: an open-source platform for biological-image analysis, Nature Methods, vol.27, issue.7, pp.676-682, 2012. ,
DOI : 10.1093/bioinformatics/btr390
URL : http://europepmc.org/articles/pmc3855844?pdf=render
Atomic force microscopy of supported lipid bilayers, Nature Protocols, vol.3, issue.10, pp.1654-1659, 2008. ,
DOI : 10.1038/nprot.2008.149
Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation, Cell, vol.163, issue.4, pp.866-879, 2015. ,
DOI : 10.1016/j.cell.2015.10.017
URL : https://hal.archives-ouvertes.fr/hal-01238262
High-speed atomic force microscopy shows that annexin V stabilizes membranes on the second timescale, Nature Nanotechnology, vol.13, issue.9, pp.783-790, 2016. ,
DOI : 10.1002/jcc.540130805
The ImageJ ecosystem: An open platform for biomedical image analysis, Molecular Reproduction and Development, vol.15, issue.7-8, pp.518-529, 2015. ,
DOI : 10.1038/nmeth.2089
URL : https://onlinelibrary.wiley.com/doi/pdf/10.1002/mrd.22489
Software for drift compensation, particle tracking and particle analysis of high-speed atomic force microscopy image series, Journal of Molecular Recognition, vol.70, issue.11, pp.292-298, 2012. ,
DOI : 10.1063/1.1150069
URL : https://hal.archives-ouvertes.fr/inserm-01363229