Virulence Factors of Bordetella Pertussis, Annual Review of Microbiology, vol.40, issue.1, pp.661-686, 1986. ,
DOI : 10.1146/annurev.mi.40.100186.003305
Bordetella pertussis adenylate cyclase: a toxin with multiple talents, Trends in Microbiology, vol.7, issue.4, pp.172-176, 1999. ,
DOI : 10.1016/S0966-842X(99)01468-7
Bordetella adenylate cyclase toxin: a swift saboteur of host defense, Current Opinion in Microbiology, vol.9, issue.1, pp.69-75, 2006. ,
DOI : 10.1016/j.mib.2005.12.011
Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis, EMBO J, vol.7, pp.3997-4004, 1988. ,
Synthesis and secretion of Bordetella pertussis adenylate cyclase as a 200-kilodalton protein, Infect. Immun, vol.58, pp.1195-1200, 1990. ,
Distinct steps in the penetration of adenylate cyclase toxin of Bordetella pertussis into sheep erythrocytes. Translocation of the toxin across the membrane, J. Biol. Chem, vol.267, pp.22599-22605, 1992. ,
Phagocyte impotence caused by an invasive bacterial adenylate cyclase, Science, vol.217, issue.4563, pp.948-950, 1982. ,
DOI : 10.1126/science.6287574
Bordetella pertussis invasive adenylate cyclase. Partial resolution and properties of its cellular penetration, J. Biol. Chem, vol.260, pp.5526-5532, 1985. ,
Bordetella pertussis adenylate cyclase: purification and characterization of the toxic form of the enzyme, EMBO J, vol.8, pp.2755-2760, 1989. ,
Bordetella pertussis induces apoptosis in macrophages: role of adenylate cyclase-hemolysin, Infect. Immun, vol.61, pp.4064-4071, 1993. ,
Adenylate Cyclase Toxin, Biochemistry, vol.49, issue.2, pp.318-328, 2010. ,
DOI : 10.1021/bi9016389
URL : https://hal.archives-ouvertes.fr/hal-00512114
Integrin (Cd11b/Cd18), The Journal of Experimental Medicine, vol.162, issue.9, pp.1035-1044, 2001. ,
DOI : 10.1073/pnas.94.7.3314
RTX cytotoxins recognize b2 integrin receptors through N-linked oligosaccharides, Proc. Natl. Acad. Sci. USA, pp.5355-5360, 2008. ,
DOI : 10.1073/pnas.0711400105
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2291121
Pore-forming cytolysins of Gram-negative bacteria, Molecular Microbiology, vol.42, issue.3, pp.521-528, 1991. ,
DOI : 10.1007/BF01869107
Structural and functional relationships among the RTX toxin determinants of Gram-negative bacteria, FEMS Microbiology Letters, vol.88, issue.2, pp.137-161, 1992. ,
DOI : 10.1111/j.1574-6968.1992.tb04961.x
RTX Toxin Structure and Function: A Story of Numerous Anomalies and Few Analogies in Toxin Biology, Curr. Top. Microbiol. Immunol, vol.257, pp.85-111, 2001. ,
DOI : 10.1007/978-3-642-56508-3_5
Interaction of Calcium with Bordetella pertussis Adenylate Cyclase Toxin: CHARACTERIZATION OF MULTIPLE CALCIUM-BINDING SITES AND CALCIUM-INDUCED CONFORMATIONAL CHANGES, Journal of Biological Chemistry, vol.270, issue.44, pp.26370-26376, 1995. ,
DOI : 10.1074/jbc.270.44.26370
Structural and Functional Characterization of an Essential RTX Subdomain of Bordetella pertussis Adenylate Cyclase Toxin, Journal of Biological Chemistry, vol.281, issue.25, pp.16914-16926, 2006. ,
DOI : 10.1074/jbc.M601594200
RTX Calcium Binding Motifs Are Intrinsically Disordered in the Absence of Calcium: IMPLICATION FOR PROTEIN SECRETION, Journal of Biological Chemistry, vol.284, issue.3, pp.1781-1789, 2009. ,
DOI : 10.1074/jbc.M807312200
URL : https://hal.archives-ouvertes.fr/pasteur-00364637
Adenylate Cyclase, Biochemistry, vol.48, issue.47, pp.11273-11282, 2009. ,
DOI : 10.1021/bi901447j
Characterization of the Regions Involved in the Calcium-Induced Folding of the Intrinsically Disordered RTX Motifs from the Bordetella pertussis Adenylate Cyclase Toxin, Journal of Molecular Biology, vol.397, issue.2, pp.534-549, 2010. ,
DOI : 10.1016/j.jmb.2010.01.031
Identification by in vitro complementation of regions required for cell-invasive activity of Bordetella pertussis adenylate cyclase toxin, Molecular Microbiology, vol.17, issue.6, pp.1015-1024, 1995. ,
DOI : 10.1111/j.1365-2958.1995.mmi_17061015.x
Characterization of the C-terminal domain essential for toxic activity of adenylate cyclase toxin, Molecular Microbiology, vol.77, issue.1, pp.381-392, 1999. ,
DOI : 10.1074/jbc.270.44.26370
Newly secreted adenylate cyclase toxin is responsible for intoxication of target cells by Bordetella pertussis, Molecular Microbiology, vol.45, issue.6, pp.1709-1719, 2004. ,
DOI : 10.1111/j.1365-2958.2004.04227.x
Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a twodomain protein with a calcium binding parallel b roll motif, EMBO J, vol.12, pp.3357-3364, 1993. ,
Folding of a synthetic parallel ??-roll protein, FEBS Letters, vol.362, issue.2, pp.173-177, 2000. ,
DOI : 10.1016/S0014-5793(00)01308-9
A Calcium-gated Lid and a Large beta-Roll Sandwich Are Revealed by the Crystal Structure of Extracellular Lipase from Serratia marcescens, Journal of Biological Chemistry, vol.282, issue.43, pp.31477-31483, 2007. ,
DOI : 10.1074/jbc.M704942200
Type I secretion in gram-negative bacteria, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1694, issue.1-3, pp.149-161, 2004. ,
DOI : 10.1016/j.bbamcr.2004.05.001
URL : https://hal.archives-ouvertes.fr/hal-00020359
Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (Review), Molecular Membrane Biology, vol.249, issue.1-2, pp.29-39, 2005. ,
DOI : 10.1080/09687860500042013
Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin, Microbiology, vol.156, issue.8, pp.2495-2505, 2010. ,
DOI : 10.1099/mic.0.038562-0
URL : https://hal.archives-ouvertes.fr/hal-00603831
Adenylate Cyclase with CD11b/CD18, Journal of Biological Chemistry, vol.278, issue.40, pp.38514-38521, 2003. ,
DOI : 10.1074/jbc.M304387200
Classification of Spectra of Cata???Condensed Hydrocarbons, The Journal of Chemical Physics, vol.7, issue.5, pp.484-495, 1949. ,
DOI : 10.1021/cr60129a004
Study of the ?molten globule? intermediate state in protein folding by a hydrophobic fluorescent probe, Biopolymers, vol.263, issue.1, pp.119-128, 1991. ,
DOI : 10.1002/bip.360310111
Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding, The Protein Journal, vol.22, issue.Suppl 1, pp.305-325, 2009. ,
DOI : 10.1007/s10930-009-9201-4
Circular dichroism of intrinsically disordered proteins In Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation, pp.303-321, 2010. ,
Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule, Biochemistry, vol.32, issue.48, pp.13288-13298, 1993. ,
DOI : 10.1021/bi00211a042
What does it mean to be natively unfolded?, European Journal of Biochemistry, vol.39, issue.1, pp.2-12, 2002. ,
DOI : 10.1046/j.0014-2956.2001.02649.x
Circular dichroism of the parallel ?? helical proteins pectate lyase C and E, Proteins: Structure, Function, and Genetics, vol.98, issue.1, pp.32-37, 1995. ,
DOI : 10.1002/prot.340230105
binding motifs at the C-terminus, FEBS Letters, vol.18, issue.1, pp.17-21, 2001. ,
DOI : 10.1016/S0014-5793(01)03108-8
Comparison of the Conformational Stability of the Molten Globule and Native States of Horse Cytochrome c, Journal of Molecular Biology, vol.237, issue.3, pp.336-348, 1994. ,
DOI : 10.1006/jmbi.1994.1234