International Journal of Cell Biology [128] G. K. Dhaliwal and R. P. Grewal, “Mitochondrial DNA deletion mutation levels are elevated in ALS brains,” NeuroReport, vol. 11, no. 11, pp. 2507–2509, 2000. [129] R. Lodi, C. Tonon, M. L. Valentino et al., “Deﬁcit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy,” Annals of Neurology, vol. 56, no. 5, pp. 719–723, 2004. [130] C. Zanna, A. Ghelli, A. M. Porcelli et al., “OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion,” Brain, vol. 131, no. 2, pp. 352–367, 2008. [131] D. A. Mackey, R. J. Oostra, T. Rosenberg et al., “Primary pathogenic mtDNA mutations in multigeneration pedigrees with Leber hereditary optic neuropathy,” American Journal of Human Genetics, vol. 59, no. 2, pp. 481–485, 1996. [132] S. Cipolat, T. Rudka, D. Hartmann et al., “Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling,” Cell, vol. 126, no. 1, pp. 163–175, 2006. [133] N. Phasukkijwatana, B. Kunhapan, J. Stankovich et al., “Genome-wide linkage scan and association study of PARL to the expression of LHON families in Thailand,” Human Genetics, vol. 128, no. 1, pp. 39–49, 2010. [134] S. H. Chung, M. Calaﬁore, J. M. Plane, D. E. Pleasure, and W. Deng, “Apoptosis inducing factor deﬁciency causes reduced mitofusion 1 expression and patterned Purkinje cell degeneration,” Neurobiology of Disease, vol. 41, no. 2, pp. 445–457, 2011. [135] J. R. Sarna and R. Hawkes, “Patterned Purkinje cell death in the cerebellum,” Progress in Neurobiology, vol. 70, no. 6, pp. 473–507, 2003. [136] H. Chen, J. M. McCaﬀery, and D. C. Chan, “Mitochondrial fusion protects against neurodegeneration in the cerebellum,” Cell, vol. 130, no. 3, pp. 548–562, 2007. [137] T. Ilani, D. Ben-Shachar, R. D. Strous et al., “A peripheral marker for schizophrenia: increased levels of D3 dopamine receptor mRNA in blood lymphocytes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 2, pp. 625–628, 2001. [138] M. Rosenfeld, H. Brenner-Lavie, S. G. B. Ari, A. Kavushansky, and D. Ben-Shachar, “Perturbation in mitochondrial network dynamics and in complex I dependent cellular respiration in schizophrenia,” Biological Psychiatry, vol. 69, no. 10, pp. 980–988, 2011. [139] C. Verny, D. Loiseau, C. Scherer et al., “Multiple sclerosis- like disorder in OPA1-related autosomal dominant optic atrophy,” Neurology, vol. 70, no. 13, pp. 1152–1153, 2008. [140] R. Dutta, J. McDonough, X. Yin et al., “Mitochondrial dysfunction as a cause of axonal degeneration in multiple sclerosis patients,” Annals of Neurology, vol. 59, no. 3, pp. 478–489, 2006. [141] A. Makino, B. T. Scott, and W. H. Dillmann, “Mitochondrial fragmentation and superoxide anion production in coronary endothelial cells from a mouse model of type 1 diabetes,” Diabetologia, vol. 53, no. 8, pp. 1783–1794, 2010. [142] J. H. Lee, K. Hoa Nguyen, S. Mishra, and B. L. G. Nyomba, “Prohibitin is expressed in pancreatic β-cells and protects against oxidative and proapoptotic eﬀects of ethanol,” FEBS Journal, vol. 277, no. 2, pp. 488–500, 2010. [143] T. M. Bosley, C. S. Constantinescu, C. R. Tench, and K. K. Abu-Amero, “Mitochondrial changes in leukocytes of 13 patients with optic neuritis,” Molecular Vision, vol. 13, pp. 1516–1528, 2007. [144] L. Weiss, R. Or, R. C. Jones et al., “Preimplantation Factor (PIF∗) reverses neuroinﬂammation while promoting neural repair in EAE model,” Journal of the Neurological Sciences, vol. 312, no. 1-2, pp. 146–157, 2012. [145] L. Weiss, S. Bernstein, R. Jones et al., “Erratum to: preimplan- tation factor (PIF) analog prevents type I diabetes mellitus (TIDM) development by preserving pancreatic function in NOD mice,” Endocrine, vol. 40, no. 1, pp. 41–54, 2011. [146] P. H. Krammer, R. Arnold, and I. N. Lavrik, “Life and death in peripheral T cells,” Nature Reviews Immunology, vol. 7, no. 7, pp. 532–542, 2007. [147] R. L. Contento, S. Campello, A. E. Trovato, E. Magrini, F. Anselmi, and A. Viola, “Adhesion shapes T cells for prompt and sustained T-cell receptor signalling,” The EMBO Journal, vol. 29, no. 23, pp. 4035–4047, 2010. [148] E. Abarca-Rojano, S. Mun˜iz-Herna´ndez, M. M. B. Moreno- Altamirano, R. Mondrago´ n-Flores, F. Enriquez-Rinco´ n, and F. J. Sa´nchez-Garc´ıa, “Re-organization of mitochondria at the NK cell immune synapse,” Immunology Letters, vol. 122, no. 1, pp. 18–25, 2009. [149] C. Kummerow, C. Junker, K. Kruse, H. Rieger, A. Quintana, and M. Hoth, “The immunological synapse controls local and global calcium signals in T lymphocytes,” Immunological Reviews, vol. 231, no. 1, pp. 132–147, 2009. [150] P. Matarrese, A. Tinari, E. Mormone et al., “Galectin-1 sensitizes resting human T lymphocytes to Fas (CD95)- mediated cell death via mitochondrial hyperpolarization, budding, and ﬁssion,” The Journal of Biological Chemistry, vol. 280, no. 8, pp. 6969–6985, 2005. [151] M. Bras, V. J. Yuste, G. Roue´ et al., “Drp1 mediates caspase- independent type III cell death in normal and leukemic cells,” Molecular and Cellular Biology, vol. 27, no. 20, pp. 7073–7088, 2007.