A. Samba-louaka, F. Taieb, J. P. Nougayrede, and E. Oswald, Cif type III effector protein: a smart hijacker of the host cell cycle, Future Microbiol, vol.4, pp.867-877, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02935476

J. P. Nougayrede, F. Taieb, J. De-rycke, and O. E. , Cyclomodulins: bacterial effectors that modulate the eukaryotic cell cycle, Trends Microbiol, vol.13, pp.103-110, 2005.
URL : https://hal.archives-ouvertes.fr/hal-02935444

E. Oswald, J. P. Nougayrede, F. Taieb, and M. Sugai, Bacterial toxins that modulate host cell-cycle progression, Curr Opin Microbiol, vol.8, pp.83-91, 2005.
URL : https://hal.archives-ouvertes.fr/hal-02682548

O. Marches, T. N. Ledger, M. Boury, M. Ohara, and X. Tu, Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G2/M transition, Mol Microbiol, vol.50, pp.1553-1567, 2003.
URL : https://hal.archives-ouvertes.fr/hal-02682122

Q. Yao, J. Cui, Y. Zhu, G. Wang, and L. Hu, A bacterial type III effector family uses the papain-like hydrolytic activity to arrest the host cell cycle, Proc Natl Acad Sci U S A, vol.106, pp.3716-3721, 2009.

G. Jubelin, C. V. Chavez, F. Taieb, M. J. Banfield, and A. Samba-louaka, Cycle inhibiting factors (CIFs) are a growing family of functional cyclomodulins present in invertebrate and mammal bacterial pathogens, PLoS ONE, vol.4, p.4855, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02659269

Y. Hsu, G. Jubelin, F. Taieb, J. P. Nougayrede, and E. Oswald, Structure of the cyclomodulin Cif from pathogenic Escherichia coli, J Mol Biol, vol.384, pp.465-477, 2008.
URL : https://hal.archives-ouvertes.fr/hal-02660834

A. Samba-louaka, J. P. Nougayrede, C. Watrin, E. Oswald, and F. Taieb, The EPEC effector Cif induces delayed apoptosis in epithelial cells, Infect Immun, vol.77, pp.5471-5477, 2009.

F. Taieb, J. P. Nougayrede, C. Watrin, A. Samba-louaka, and E. Oswald, Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway, Cell Microbiol, vol.8, pp.1910-1921, 2006.
URL : https://hal.archives-ouvertes.fr/hal-02660102

A. Samba-louaka, J. P. Nougayrede, C. Watrin, G. Jubelin, and E. Oswald, Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclindependent kinase inhibitors p21 and p27, Cell Microbiol, vol.10, pp.2496-2508, 2008.
URL : https://hal.archives-ouvertes.fr/hal-02658405

G. Rabut and M. Peter, Protein modifications: beyond the usual suspects' review series, EMBO Rep, vol.9, pp.969-976, 2008.

K. I. Nakayama and K. Nakayama, Regulation of the cell cycle by SCF-type ubiquitin ligases, Semin Cell Dev Biol, vol.16, pp.323-333, 2005.

J. Yu and R. L. Finley, Combining multiple positive training sets to generate confidence scores for protein-protein interactions, Bioinformatics, vol.25, pp.105-111, 2009.

T. Kamitani, K. Kito, H. P. Nguyen, and E. T. Yeh, Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein, J Biol Chem, vol.272, pp.28557-28562, 1997.

D. P. Xirodimas, Novel substrates and functions for the ubiquitin-like molecule NEDD8, Biochem Soc Trans, vol.36, pp.802-806, 2008.

J. Jones, K. Wu, Y. Yang, C. Guerrero, and N. Nillegoda, A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins, J Proteome Res, vol.7, pp.1274-1287, 2008.

D. R. Bosu and E. T. Kipreos, Cullin-RING ubiquitin ligases: global regulation and activation cycles, Cell Div, vol.3, p.7, 2008.

M. Welcker and B. E. Clurman, FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation, Nat Rev Cancer, vol.8, pp.83-93, 2008.

X. Ye, G. Nalepa, M. Welcker, B. M. Kessler, and E. Spooner, Recognition of phosphodegron motifs in human cyclin E by the SCF(Fbw7) ubiquitin ligase, J Biol Chem, vol.279, pp.50110-50119, 2004.

G. Kleiger, A. Saha, S. Lewis, B. Kuhlman, and R. J. Deshaies, Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates, Cell, vol.139, pp.957-968, 2009.

N. W. Pierce, G. Kleiger, S. O. Shan, and R. J. Deshaies, Detection of sequential polyubiquitylation on a millisecond timescale, Nature, vol.462, pp.615-619, 2009.

M. D. Petroski and R. J. Deshaies, Function and regulation of cullin-RING ubiquitin ligases, Nat Rev Mol Cell Biol, vol.6, pp.9-20, 2005.

J. Merlet, J. Burger, J. E. Gomes, and L. Pintard, Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization, Cell Mol Life Sci, vol.66, pp.1924-1938, 2009.
URL : https://hal.archives-ouvertes.fr/hal-00363831

E. H. Chew and T. Hagen, Substrate-mediated regulation of cullin neddylation, J Biol Chem, vol.282, pp.17032-17040, 2007.

G. Bornstein, D. Ganoth, and A. Hershko, Regulation of neddylation and deneddylation of cullin1 in SCFSkp2 ubiquitin ligase by F-box protein and substrate, Proc Natl Acad Sci U S A, vol.103, pp.11515-11520, 2006.

Y. Chen, Z. Yang, M. Meng, Y. Zhao, and N. Dong, Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement, Mol Cell, vol.35, pp.841-855, 2009.

J. Jin, E. E. Arias, J. Chen, J. W. Harper, and J. C. Walter, A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1, Mol Cell, vol.23, pp.709-721, 2006.

H. Nishitani, N. Sugimoto, V. Roukos, Y. Nakanishi, and M. Saijo, Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for proteolysis, EMBO J, vol.25, pp.1126-1136, 2006.

T. Senga, U. Sivaprasad, W. Zhu, J. H. Park, and E. E. Arias, PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination, J Biol Chem, vol.281, pp.6246-6252, 2006.

G. Xouri, M. Dimaki, P. I. Bastiaens, and Z. Lygerou, Cdt1 interactions in the licensing process: a model for dynamic spatiotemporal control of licensing, Cell Cycle, vol.6, pp.1549-1552, 2007.

H. Clevers, Wnt/beta-catenin signaling in development and disease, Cell, vol.127, pp.469-480, 2006.