Table 1. List of diseases with proven alterations in SNAP29 (see text for details).

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46. Sprecher E, Ishida-Yamamoto A, Mizrahi-Koren M, Rapaport D, Goldsher D, Indelman M, Topaz O, Chefetz I, Keren H, O’Brien T J, Bercovich D, Shalev S, Geiger D, Bergman R, Horowitz M, Mandel H (2005). A mutation in SNAP29, coding for a SNARE protein involved in intracellular trafficking, causes a novel neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma. Am J Hum Genet 77(2): 242-251. http://dx.doi.org/10.1086/432556

47. Fuchs-Telem D, Stewart H, Rapaport D, Nousbeck J, Gat A, Gini M, Lugassy Y, Emmert S, Eckl K, Hennies HC, Sarig O, Goldsher D, Meilik B, Ishida-Yamamoto A, Horowitz M, Sprecher E (2011). CEDNIK syndrome results from loss-of-function mutations in SNAP29. Br J Dermatol 164(3): 610-616. http://dx.doi.org/10.1111/j.1365-2133.2010.10133.x

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49. Diggle CP, Martinez-Garay I, Molnar Z, Brinkworth MH, White E, Fowler E, Hughes R, Hayward BE, Carr IM, Watson CM, Crinnion L, Asipu A, Woodman B, Coletta PL, Markham AF, Dear TN, Bonthron DT, Peckham M, Morrison EE, Sheridan E (2017). A tubulin alpha 8 mouse knockout model indicates a likely role in spermatogenesis but not in brain development. PLoS One 12(4): e0174264. http://dx.doi.org/10.1371/journal.pone.0174264

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51. Rapaport D, Lugassy Y, Sprecher E, Horowitz M (2010). Loss of SNAP29 impairs endocytic recycling and cell motility. PloS one 5(3): e9759. http://dx.doi.org/10.1371/journal.pone.0009759

52. McDonald-McGinn DM, Fahiminiya S, Revil T, Nowakowska BA, Suhl J, Bailey A, Mlynarski E, Lynch DR, Yan AC, Bilaniuk LT, Sullivan KE, Warren ST, Emanuel BS, Vermeesch JR, Zackai EH, Jerome-Majewska LA (2013). Hemizygous mutations in SNAP29 unmask autosomal recessive conditions and contribute to atypical findings in patients with 22q11.2DS. J Med Genet 50(2): 80-90. http://dx.doi.org/10.1136/jmedgenet-2012-101320

53. Cordovez JA, Capasso J, Lingao MD, Sadagopan KA, Spaeth GL, Wasserman BN, Levin AV (2014). Ocular manifestations of 22q11.2 microduplication. Ophthalmology 121(1): 392-398. http://dx.doi.org/10.1016/j.ophtha.2013.06.040

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55. Ding B, Zhang G, Yang X, Zhang S, Chen L, Yan Q, Xu M, Banerjee AK, Chen M (2014). Phosphoprotein of human parainfluenza virus type 3 blocks autophagosome-lysosome fusion to increase virus production. Cell Host Microbe 15(5): 564-577. http://dx.doi.org/10.1016/j.chom.2014.04.004

56. Lai JKF, Sam IC, Verlhac P, Baguet J, Eskelinen EL, Faure M, Chan YF (2017). 2BC Non-Structural Protein of Enterovirus A71 Interacts with SNARE Proteins to Trigger Autolysosome Formation. Viruses 9(7). http://dx.doi.org/10.3390/v9070169