D. Dennis, T. Inglesby, D. Henderson, J. Bartlett, and M. Ascher, Tularemia as a Biological Weapon, JAMA, vol.285, issue.21, pp.2763-2773, 2001.
DOI : 10.1001/jama.285.21.2763

A. Sjostedt, Virulence determinants and protective antigens of Francisella tularensis, Current Opinion in Microbiology, vol.6, issue.1, pp.66-71, 2003.
DOI : 10.1016/S1369-5274(03)00002-X

I. Golovliov, V. Baranov, Z. Krocova, H. Kovarova, and A. Sjostedt, An Attenuated Strain of the Facultative Intracellular Bacterium Francisella tularensis Can Escape the Phagosome of Monocytic Cells, Infection and Immunity, vol.71, issue.10, pp.5940-5950, 2003.
DOI : 10.1128/IAI.71.10.5940-5950.2003

A. Chong, T. Wehrly, V. Nair, E. Fischer, and J. Barker, The Early Phagosomal Stage of Francisella tularensis Determines Optimal Phagosomal Escape and Francisella Pathogenicity Island Protein Expression, Infection and Immunity, vol.76, issue.12, pp.5488-5499, 2008.
DOI : 10.1128/IAI.00682-08

D. Clemens, B. Lee, and M. Horwitz, Virulent and Avirulent Strains of Francisella tularensis Prevent Acidification and Maturation of Their Phagosomes and Escape into the Cytoplasm in Human Macrophages, Infection and Immunity, vol.72, issue.6, pp.3204-3217, 2004.
DOI : 10.1128/IAI.72.6.3204-3217.2004

M. Rajaram, J. Butchar, K. Parsa, T. Cremer, and A. Amer, Akt and SHIP Modulate Francisella Escape from the Phagosome and Induction of the Fas-Mediated Death Pathway, PLoS ONE, vol.4, issue.11, p.7919, 2009.
DOI : 10.1371/journal.pone.0007919.g012

M. Santic, G. Pavokovic, S. Jones, R. Asare, and Y. Kwaik, Regulation of apoptosis and anti-apoptosis signalling by Francisella tularensis, Microbes and Infection, vol.12, issue.2, pp.126-134, 2010.
DOI : 10.1016/j.micinf.2009.11.003

H. Thomas and M. Denise, Activation of the inflammasome upon Francisella tularensis infection: interplay of innate immune pathways and virulence factors, Cell Microbiol, vol.9, pp.2543-2551, 2007.

D. Clemens, B. Lee, and M. Horwitz, Francisella tularensis Enters Macrophages via a Novel Process Involving Pseudopod Loops, Infection and Immunity, vol.73, issue.9, pp.5892-5902, 2005.
DOI : 10.1128/IAI.73.9.5892-5902.2005
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1231130

A. Balagopal, A. Macfarlane, N. Mohapatra, S. Soni, and J. Gunn, Characterization of the Receptor-Ligand Pathways Important for Entry and Survival of Francisella tularensis in Human Macrophages, Infection and Immunity, vol.74, issue.9, pp.5114-5125, 2006.
DOI : 10.1128/IAI.00795-06

L. Pierini, Uptake of serum-opsonized Francisella tularensis by macrophages can be mediated by class A scavenger receptors, Cellular Microbiology, vol.42, issue.8, pp.1361-1370, 2006.
DOI : 10.1046/j.1432-1033.2002.03321.x

G. Schulert and L. Allen, Differential infection of mononuclear phagocytes by Francisella tularensis: role of the macrophage mannose receptor, Journal of Leukocyte Biology, vol.80, issue.3, pp.563-571, 2006.
DOI : 10.1189/jlb.0306219

M. Barel, A. Hovanessian, K. Meibom, J. Briand, and M. Dupuis, A novel receptor ??? ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu, BMC Microbiology, vol.8, issue.1, pp.145-153, 2008.
DOI : 10.1186/1471-2180-8-145
URL : https://hal.archives-ouvertes.fr/hal-00324631

A. Kharrat, J. Derancourt, M. Doree, F. Amalric, and M. Erard, Synergistic effect of histone H1 and nucleolin on chromatin condensation in mitosis: role of a phosphorylated heteromer, Biochemistry, vol.30, issue.42, pp.10329-10336, 1991.
DOI : 10.1021/bi00106a034

D. Hirata, M. Iwamoto, T. Yoshio, H. Okazaki, and J. Masuyama, Nucleolin as the Earliest Target Molecule of Autoantibodies Produced in MRL/lpr Lupus-Prone Mice, Clinical Immunology, vol.97, issue.1, pp.50-58, 2000.
DOI : 10.1006/clim.2000.4916

P. Bouvet, J. Diaz, K. Kindbeiter, J. Madjar, and F. Amalric, Nucleolin Interacts with Several Ribosomal Proteins through Its RGG Domain, Journal of Biological Chemistry, vol.273, issue.30, pp.19025-19029, 1998.
DOI : 10.1074/jbc.273.30.19025
URL : https://hal.archives-ouvertes.fr/hal-00180283

D. Legrand, K. Vigie, E. Said, E. Elass, and M. Masson, Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells, European Journal of Biochemistry, vol.84, issue.2, pp.303-317, 2004.
DOI : 10.1023/A:1026205603217
URL : https://hal.archives-ouvertes.fr/hal-00104916

C. Checroun, T. Wehrly, E. Fischer, S. Hayes, and J. Celli, Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication, Proceedings of the National Academy of Sciences, vol.103, issue.39, pp.14578-14583, 2006.
DOI : 10.1073/pnas.0601838103

M. Santic, M. Molmeret, K. Klose, S. Jones, and Y. Kwaik, The Francisella tularensis pathogenicity island protein IglC and its regulator MglA are essential for modulating phagosome biogenesis and subsequent bacterial escape into the cytoplasm, Cellular Microbiology, vol.70, issue.7, pp.969-979, 2005.
DOI : 10.1111/j.1462-5822.2005.00526.x

L. Bonquist, H. Lindgren, I. Golovliov, T. Guina, and A. Sjostedt, MglA and Igl Proteins Contribute to the Modulation of Francisella tularensis Live Vaccine Strain-Containing Phagosomes in Murine Macrophages, Infection and Immunity, vol.76, issue.8, pp.3502-3510, 2008.
DOI : 10.1128/IAI.00226-08

C. Gahan, O. Mahony, J. Hill, and C. , Characterization of the groESL Operon in Listeria monocytogenes: Utilization of Two Reporter Systems (gfp and hly) for Evaluating In Vivo Expression, Infection and Immunity, vol.69, issue.6, pp.3924-3932, 2001.
DOI : 10.1128/IAI.69.6.3924-3932.2001

X. Lai, I. Golovliov, and A. Sjostedt, Expression of IglC is necessary for intracellular growth and induction of apoptosis in murine macrophages by Francisella tularensis, Microbial Pathogenesis, vol.37, issue.5, pp.225-230, 2004.
DOI : 10.1016/j.micpath.2004.07.002

E. Eskelinen, Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy, Molecular Aspects of Medicine, vol.27, issue.5-6, pp.495-502, 2006.
DOI : 10.1016/j.mam.2006.08.005

B. Tooker and P. Coussens, Phagocytosis of M. paratuberculosis fails to activate expression of NADH dehydrogenase and nucleolin-related protein in bovine macrophages, Immunology Letters, vol.93, issue.2-3, pp.137-142, 2004.
DOI : 10.1016/j.imlet.2004.03.005

K. Hirano, Y. Miki, Y. Hirai, R. Sato, and T. Itoh, A Multifunctional Shuttling Protein Nucleolin Is a Macrophage Receptor for Apoptotic Cells, Journal of Biological Chemistry, vol.280, issue.47, pp.39284-39293, 2005.
DOI : 10.1074/jbc.M505275200

A. Hovanessian, Midkine, a cytokine that inhibits HIV infection by binding to the cell surface expressed nucleolin, Cell Research, vol.271, issue.2, pp.174-181, 2006.
DOI : 10.1056/NEJM199302043280508
URL : https://hal.archives-ouvertes.fr/hal-00104911

L. Roy, S. Laboissiere, E. Abdou, G. Thibault, and N. Hamel, Proteomic analysis of the transitional endoplasmic reticulum in hepatocellular carcinoma: An organelle perspective on cancer, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1804, issue.9
DOI : 10.1016/j.bbapap.2010.05.008

M. Derby, P. Gleeson, and W. Kwang, New Insights into Membrane Trafficking and Protein Sorting, International Review of Cytology, pp.47-116, 2007.
DOI : 10.1016/S0074-7696(07)61002-X

C. Akimana, S. Al-khodor, A. Kwaik, and Y. , Host Factors Required for Modulation of Phagosome Biogenesis and Proliferation of Francisella tularensis within the Cytosol, PLoS ONE, vol.101, issue.6, p.11025, 2010.
DOI : 10.1371/journal.pone.0011025.s001

A. Sjostedt, J. Conlan, and R. North, Neutrophils are critical for host defense against primary infection with the facultative intracellular bacterium Francisella tularensis in mice and participate in defense against reinfection, Infect Immun, vol.62, pp.2779-2783, 1994.

T. Maier, A. Havig, M. Casey, F. Nano, and D. Frank, Construction and Characterization of a Highly Efficient Francisella Shuttle Plasmid, Applied and Environmental Microbiology, vol.70, issue.12, pp.7511-7519, 2004.
DOI : 10.1128/AEM.70.12.7511-7519.2004

P. Glaser, L. Frangeul, C. Buchrieser, C. Rusniok, and A. Amend, Comparative genomics of Listeria species, Science, vol.294, pp.849-852, 2001.

N. Fortineau, P. Trieu-cuot, O. Gaillot, E. Pellegrini, and P. Berche, Optimization of green fluorescent protein expression vectors for in vitro and in vivo detection of Listeria monocytogenes, Research in Microbiology, vol.151, issue.5, pp.353-360, 2000.
DOI : 10.1016/S0923-2508(00)00158-3

J. Deng, B. Ballou, and J. Hofmeister, Internalization of anti-nucleolin antibody into viable HEp-2 cells, Molecular Biology Reports, vol.2680, issue.3-4, pp.191-195, 1996.
DOI : 10.1007/BF00351168

P. Sanchez-corral, L. Anton, J. Alcolea, G. Marques, and A. Sanchez, Separation of active and inactive forms of the third component of human complement, C3, by fast protein liquid chromatography (FPLC), Journal of Immunological Methods, vol.122, issue.1, pp.105-113, 1989.
DOI : 10.1016/0022-1759(89)90340-2

E. Manders, J. Stap, G. Brakenhoff, R. Van-driel, and J. Aten, Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy, J Cell Sci, vol.103, pp.857-862, 1992.

J. Adler, S. Pagakys, and I. Parmryd, Replicate-based noise corrected correlation for accurate measurements of colocalization, Journal of Microscopy, vol.3, issue.1, pp.121-133, 2008.
DOI : 10.2307/1412159

B. Van-steensel, E. Van-binnendijk, C. Hornsby, H. Van-der-voort, and Z. Krozowski, Partial colocalization of glucocorticoid and mineralocorticoid receptors in discrete compartments in nuclei of rat hippocampus neurons, J Cell Sci, vol.109, pp.787-792, 1996.

S. Bolte and F. Cordelieres, A guided tour into subcellular colocalization analysis in light microscopy, Journal of Microscopy, vol.56, issue.3, pp.213-232, 2006.
DOI : 10.1016/S0014-5793(03)00521-0
URL : https://hal.archives-ouvertes.fr/hal-00132481