M. Van-der-knaap, P. Barth, F. Gabreëls, E. Franzoni, J. Begeer et al., A new leukoencephalopathy with vanishing white matter, Neurology, vol.48, issue.4, pp.845-55, 1997.
DOI : 10.1212/WNL.48.4.845

P. Leegwater, G. Vermeulen, A. Könst, S. Naidu, J. Mulders et al., Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter, Nature Genetics, vol.29, issue.4, pp.383-88, 2001.
DOI : 10.1038/ng764

M. Van-der-knaap, P. Leegwater, A. Könst, A. Visser, S. Naidu et al., Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter, Annals of Neurology, vol.100, issue.2, pp.264-70, 2002.
DOI : 10.1002/ana.10112

A. Fogli, D. Rodriguez, E. Eymard-pierre, F. Bouhour, P. Labauge et al., Ovarian Failure Related to Eukaryotic Initiation Factor 2B Mutations, The American Journal of Human Genetics, vol.72, issue.6, pp.1544-50, 2003.
DOI : 10.1086/375404

A. Fogli and O. Boespflug-tanguy, The large spectrum of eIF2B-related diseases, Biochemical Society Transactions, vol.34, issue.1, pp.22-29, 2006.
DOI : 10.1042/BST0340022

A. Fogli, R. Schiffmann, L. Hugendubler, P. Combes, E. Bertini et al., Decreased guanine nucleotide exchange factor activity in eIF2B-mutated patients, European Journal of Human Genetics, vol.12, issue.7, pp.561-567, 2004.
DOI : 10.1038/sj.ejhg.5201189

G. Pavitt, K. Ramaiah, S. Kimball, and A. Hinnebusch, eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide??exchange, Genes & Development, vol.12, issue.4, pp.2514-2540, 1998.
DOI : 10.1101/gad.12.4.514

L. Kantor, H. Harding, R. D. Schiffmann, R. Kaneski, C. Kimball et al., Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients, Human Genetics, vol.100, issue.1, pp.99-106, 2005.
DOI : 10.1007/s00439-005-0024-x

J. Richardson, S. Mohammad, and G. Pavitt, Mutations Causing Childhood Ataxia with Central Nervous System Hypomyelination Reduce Eukaryotic Initiation Factor 2B Complex Formation and Activity, Molecular and Cellular Biology, vol.24, issue.6, pp.2352-63, 2004.
DOI : 10.1128/MCB.24.6.2352-2363.2004

W. Li, X. Wang, M. Van-der-knaap, and C. Proud, Mutations Linked to Leukoencephalopathy with Vanishing White Matter Impair the Function of the Eukaryotic Initiation Factor 2B Complex in Diverse Ways, Molecular and Cellular Biology, vol.24, issue.8, pp.3295-306, 2004.
DOI : 10.1128/MCB.24.8.3295-3306.2004

L. Kantor, D. Pinchasi, M. Mintz, Y. Hathout, A. Vanderver et al., A Point Mutation in Translation Initiation Factor 2B Leads to a Continuous Hyper Stress State in Oligodendroglial-Derived Cells, PLoS ONE, vol.262, issue.11, p.3783, 2008.
DOI : 10.1371/journal.pone.0003783.g005

J. Van-der-voorn, B. Van-kollenburg, G. Bertrand, K. Van-haren, G. Scheper et al., The Unfolded Protein Response in Vanishing White Matter Disease, Journal of Neuropathology & Experimental Neurology, vol.64, issue.9, pp.770-775, 2005.
DOI : 10.1097/01.jnen.0000178446.41595.3a

B. Van-kollenburg, J. Van-dijk, J. Garbern, A. Thomas, G. Scheper et al., Glia-Specific Activation of All Pathways of the Unfolded Protein Response in Vanishing White Matter Disease, Journal of Neuropathology and Experimental Neurology, vol.65, issue.7, pp.707-722, 2006.
DOI : 10.1097/01.jnen.0000228201.27539.50

G. Pavitt and C. Proud, Protein synthesis and its control in neuronal cells with a focus on vanishing white matter disease, Biochemical Society Transactions, vol.37, issue.6, pp.1298-1310, 2009.
DOI : 10.1042/BST0371298

L. Horzinski, A. Huyghe, M. Cardoso, C. Gonthier, L. Ouchchane et al., Eukaryotic Initiation Factor 2B (eIF2B) GEF Activity as a Diagnostic Tool for EIF2B-Related Disorders, PLoS ONE, vol.4, issue.12, p.8318, 2009.
DOI : 10.1371/journal.pone.0008318.t002

B. Van-kollenburg, A. Thomas, G. Vermeulen, G. Bertrand, C. Van-berkel et al., Regulation of protein synthesis in lymphoblasts from vanishing white matter patients, Neurobiology of Disease, vol.21, issue.3, pp.496-504, 2006.
DOI : 10.1016/j.nbd.2005.08.009

H. Neitzel, A routine method for the establishment of permanent growing lymphoblastoid cell lines, Human Genetics, vol.67, issue.4, pp.320-326, 1986.
DOI : 10.1007/BF00279094

G. Sivan, N. Kedersha, and O. Elroy-stein, Ribosomal Slowdown Mediates Translational Arrest during Cellular Division, Molecular and Cellular Biology, vol.27, issue.19, pp.6639-6685, 2007.
DOI : 10.1128/MCB.00798-07

P. Young, E. Anderton, K. Paschos, R. White, and M. Allday, Epstein-Barr virus nuclear antigen (EBNA) 3A induces the expression of and interacts with a subset of chaperones and co-chaperones, Journal of General Virology, vol.89, issue.4, pp.866-77, 2008.
DOI : 10.1099/vir.0.83414-0

D. Mosser, A. Caron, L. Bourget, A. Meriin, M. Sherman et al., The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis, Molecular and Cellular Biology, vol.20, issue.19, pp.7146-59, 2000.
DOI : 10.1128/MCB.20.19.7146-7159.2000

S. Balachandran and G. Barber, Defective translational control facilitates vesicular stomatitis virus oncolysis, Cancer Cell, vol.5, issue.1, pp.51-65, 2004.
DOI : 10.1016/S1535-6108(03)00330-1

J. Dietrich, M. Lacagnina, D. Gass, E. Richfield, M. Mayer-pröschel et al., EIF2B5 mutations compromise GFAP+ astrocyte generation in vanishing white matter leukodystrophy, Nature Medicine, vol.21, issue.3, pp.277-83, 2005.
DOI : 10.1038/nm1195