[1] B. Boonyawat et al., “HHS Public Access,” Iran. J. Public Health, vol. 21, no. 1, pp. 281–285, 2015.
[2] B. Boonyawat, T. Phetthong, C. Nabangchang, and P. Suwanpakdee, “A novel frameshift mutation of HEXA gene in the first family with classical infantile Tay-Sachs disease in Thailand,” Neurol. Asia, vol. 21, no. 3, pp. 281–285, 2016.
[3] S. Zampieri et al., “Sequence and Copy Number Analyses of HEXB Gene in Patients Affected by Sandhoff Disease : Functional Characterization of 9 Novel Sequence Variants,” vol. 7, no. 7, pp. 1–10, 2012.
[4] W. Zhang, H. Zeng, Y. Huang, T. Xie, and J. Zheng, “Clinical , biochemical and molecular analysis of five Chinese patients with Sandhoff disease,” 2016.
[5] R. Ebrahimzadeh-Vesal, S. Hosseini, M. Moghaddassian, and M. R. Abbaszadegan, “Identification of novel missense HEXB gene mutation in Iranian-child with juvenile Sandhoff disease,” Meta Gene, vol. 12, pp. 83–87, 2017.
[6] K. Neote, B. Mcinnes, D. J. Mahuran, and R. A. Gravel, “Structure and Distribution of an Alu-type Deletion Mutation in Sandhoff Disease.”
[7] L. Gort, N. De Olano, J. Macías-vidal, and M. Josep, “GM2 gangliosidoses in Spain : Analysis of the HEXA and HEXB genes in 34 Tay – Sachs and 14 Sandhoff patients ☆,” Gene, vol. 506, no. 1, pp. 25–30, 2012.
[8] P. Gaignard et al., “Characterization of seven novel mutations on the HEXB gene in French Sandhoff patients,” Gene, vol. 512, no. 2, pp. 521–526, 2013.
[9] S. Lakshmi, G. Anitha, and S. Vinoth, “A rare case of Sandhoff disease: two in the same family,” Int. J. Contemp. Pediatr., vol. 2, no. 1, p. 42, 2015.
[10] H. Aryan, O. Aryani, K. Banihashemi, T. Zaman, and M. Houshmand, “Novel mutations in sandhoff disease: A molecular analysis among Iranian cohort of infantile patients,” Iran. J. Public Health, vol. 41, no. 3, pp. 112–118, 2012.
[11] M. Abiri, S. Talebi, J. Uitto, L. Youssefian, H. Vahidnezhad, and T. Shirzad, “Co-existence of phenylketonuria either with maple syrup urine disease or Sandhoff disease in two patients from Iran : emphasizing the role of consanguinity,” 2016.
[12] K. Sandhoff, H. Christomanou, M. Psychiatrie, and N. Abteilung, “Biochemistry and Genetics of Gangliosidoses,” vol. 143, pp. 107–108, 1979.
[13] T. N. and K. Suzuki, “Genetic Cause of a Juvenile Form of Sandhoff Disease,” DNA Seq., vol. 264, no. 9, pp. 5155–5158, 1989.
[14] W. Biochemical, G. Unit, and C. D. Centre, “Juvenile Sandho ¡ diseaseöNine new cases and a review of the literature,” vol. 27, pp. 241–249, 2004.
[15] P. A. Bolhuis, N. J. Ponne, H. Bikker, F. Baas, and J. M. B. V. de Jong, “Molecular basis of an adult form of Sandhoff disease: Substitution of glutamine for arginine at position 505 of the ??-chain of ??-hexosaminidase results in a labile enzyme,” BBA - Mol. Basis Dis., vol. 1182, no. 2, pp. 142–146, 1993.
[16] M. G. A. Sangalli, M. Mottes, C. Perusi, P. Franco, N. Rizzuto, and A. Salviati, “A common hexosaminidase gene mutation in adult Sandhoff disease patients,” pp. 417–418, 1995.
[17] N. A. Chamoles, M. Blanco, D. Gaggioli, and C. Casentini, “Tay-Sachs and Sandhoff diseases: Enzymatic diagnosis in dried blood spots on filter paper: Retrospective diagnoses in newborn-screening cards,” Clin. Chim. Acta, vol. 318, no. 1–2, pp. 133–137, 2002.
[18] A. R. Tavasoli, N. Parvaneh, M. R. Ashrafi, Z. Rezaei, J. Zschocke, and P. Rostami, “Clinical presentation and outcome in infantile Sandhoff disease: A case series of 25 patients from Iranian neurometabolic bioregistry with five novel mutations Dr. Segolene Ayme,” Orphanet J. Rare Dis., vol. 13, no. 1, pp. 1–8, 2018.
[19] I. A. Adzhubei et al., “A method and server for predicting damaging missense mutations a,” Nat. Publ. Gr., vol. 7, no. 4, pp. 248–249, 2010.
[20] P. Kumar, S. Henikoff, and P. C. Ng, “Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm,” vol. 4, no. 8, pp. 1073–1082, 2009.
[21] L. A. Kelly, S. Mezulis, C. Yates, M. Wass, and M. Sternberg, “The Phyre2 web portal for protein modelling, prediction, and analysis,” Nat. Protoc., vol. 10, no. 6, pp. 845–858, 2015.
[22] H. M. Berman et al., “The protein data bank.,” Nucleic Acids Res., vol. 28, no. 1, pp. 235–242, 2000.
[23] E. F. Pettersen et al., “UCSF Chimera - A visualization system for exploratory research and analysis,” J. Comput. Chem., vol. 25, no. 13, pp. 1605–1612, 2004.
[24] A. Mohebbi, S. Mohammadi, and A. Memarian, “Prediction of HBF-0259 interactions with hepatitis B Virus receptors and surface antigen secretory factors,” VirusDisease, vol. 27, no. 3, pp. 234–241, 2016.
[25] R. Apweiler et al., “The Universal Protein resource (UniProt) 2009,” Nucleic Acids Res., vol. 37, no. SUPPL. 1, pp. 169–174, 2009.
[26] E. a Akl et al., “Parenteral anticoagulation may prolong the survival of patients with limited small cell lung cancer : a Cochrane systematic review,” Proteins Struct. Funct. Bioinforma., vol. 10, no. SUPPL. 10, pp. 1–10, 2008.
[27] T. Maier, N. Strater, C. G. Schuette, R. Klingenstein, K. Sandhoff, and W. Saenger, “The X-ray crystal structure of human β-hexosaminidase B provides new insights into Sandhoff disease,” J. Mol. Biol., vol. 328, no. 3, pp. 669–681, 2003.
[28] E. M. Leslie, R. G. Deeley, and S. P. C. Cole, “Multidrug resistance proteins: Role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense,” Toxicol. Appl. Pharmacol., vol. 204, no. 3, pp. 216–237, 2005.
[29] Y. Hou, D. Vocadlo, S. Withers, and D. Mahuran, “Role of Arg 211 in the Active Site of Human -Hexosaminidase B †,” Society, vol. 39, no. 20, pp. 6219–6227, 2000.
[30] Y. Yun and S. Lee, “A case refort of Sandhoff disease.,” Korean J. Ophthalmol., vol. 19, no. 1, pp. 68–72, 2005.
[31] S. Z. Wang et al., “A novel HEXB mutation and its structural effects in juvenile Sandhoff disease,” Mol. Genet. Metab., vol. 95, no. 4, pp. 236–238, 2008.
[32] M. Santoro et al., “Chronic GM2 gangliosidosis type Sandhoff associated with a novel missense HEXB gene mutation causing a double pathogenic effect,” Mol. Genet. Metab., vol. 91, no. 1, pp. 111–114, 2007.
[33] M. Gomez-Lira et al., “A novel 4-bp deletion creates a premature stop codon and dramatically decreases HEXB mRNA levels in a severe case of Sandhoff disease,” Mol. Cell. Probes, vol. 15, no. 2, pp. 75–79, 2001.
[34] M. Gomez???Lira et al., “A 48???bp insertion between exon 13 and 14 of the HEXB gene causes infantile???onset sandhoff disease,” Hum. Mutat., vol. 6, no. 3, pp. 260–262, 1995.
[35] K. Yamada, Y. Takado, Y. S. Kato, Y. Yamada, H. Ishiguro, and N. Wakamatsu, “Characterization of the mutant β-subunit of β-hexosaminidase for dimer formation responsible for the adult form of Sandhoff disease with the motor neuron disease phenotype,” J. Biochem., vol. 153, no. 1, pp. 111–119, 2013.
[36] P. Banerjee et al., “Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease.,” Biochem. Biophys. Res. Commun., vol. 181, no. 1, pp. 108–15, 1991.
[37] T. Yoshizawa, Y. Kohno, S. Nissato, and S. Shoji, “Compound heterozygosity with two novel mutations in the HEXB gene produces adult Sandhoff disease presenting as a motor neuron disease phenotype,” J. Neurol. Sci., vol. 195, no. 2, pp. 129–138, 2002.
[38] M. Rubin, G. Karpati, L. S. Wolfe, S. Carpenter, M. H. Klavins, and D. J. Mahuran, “Adult onset motor neuronopathy in the juvenile type of hexosaminidase A and B deficiency,” J. Neurol. Sci., vol. 87, no. 1, pp. 103–119, 1988.
[39] Y. Hou, B. McInnes, A. Hinek, G. Karpati, and D. Mahuran, “A Pro504 → Ser substitution in the β-subunit of β-hexosaminidase A inhibits α-subunit hydrolysis of G(M2) ganglioside, resulting in chronic Sandhoff disease,” J. Biol. Chem., vol. 273, no. 33, pp. 21386–21392, 1998.
[40] J. P. Overington, B. Al-Lazikani, and A. L. Hopkins, “How many drug targets are there?,” Nat. Rev. Drug Discov., vol. 5, no. 12, pp. 993–996, 2006.
[41] P. Imming, C. Sinning, and A. Meyer, “Drugs, their targets and the nature and number of drug targets,” Nat. Rev. Drug Discov., vol. 5, no. 10, pp. 821–834, 2006.
[42] G. H. B. Maegawa et al., “Pyrimethamine as a potential pharmacological chaperone for late-onset forms of GM2 gangliosidosis,” J. Biol. Chem., vol. 282, no. 12, pp. 9150–9161, 2007.
[43] M. B. Cachon-Gonzalez, S. Z. Wang, A. Lynch, R. Ziegler, S. H. Cheng, and T. M. Cox, “Effective gene therapy in an authentic model of Tay-Sachs-related diseases,” Proc. Natl. Acad. Sci., vol. 103, no. 27, pp. 10373–10378, 2006.