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1.2 DESCRIPCIÓN DEL PROYECTO

1.3.8 ESPACIOS EXTERIORES ADSCRITOS:

1. Rub, U, Schols, L, Paulson, H, Auburger, G, Kermer, P, Jen, JC, et al. (2013). Clinical features, neurogenetics and neuropathology of the polyglutamine spinocerebellar ataxias type 1, 2, 3, 6 and 7.

Prog Neurobiol104: 38-66.

2. Riess, O, Rub, U, Pastore, A, Bauer, P, and Schols, L (2008). SCA3: neurological features, pathogenesis and animal models. Cerebellum (London, England)7: 125-137.

3. Orr, HT, and Zoghbi, HY (2007). Trinucleotide repeat disorders. Annual review of neuroscience30: 575-621. 4. Kawaguchi, Y, Okamoto, T, Taniwaki, M, Aizawa, M, Inoue, M, Katayama, S, et al. (1994). CAG expansions

in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nature genetics8: 221-228. 5. Cummings, CJ, and Zoghbi, HY (2000). Trinucleotide repeats: mechanisms and pathophysiology.

Annual review of genomics and human genetics1: 281-328.

6. Matos, CA, de Macedo-Ribeiro, S, and Carvalho, AL (2011). Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease. Prog Neurobiol95: 26-48.

7. Bettencourt, C, Raposo, M, Ros, R, Montiel, R, Bruges-Armas, J, and Lima, M (2013). Transcript diversity of Machado-Joseph disease gene (ATXN3) is not directly determined by SNPs in exonic or flanking intronic regions. Journal of molecular neuroscience : MN49: 539-543.

8. Harris, GM, Dodelzon, K, Gong, L, Gonzalez-Alegre, P, and Paulson, HL (2010). Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties. PloS one5: e13695.

9. Schmidt, T, Landwehrmeyer, GB, Schmitt, I, Trottier, Y, Auburger, G, Laccone, F, et al. (1998). An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Brain pathology (Zurich, Switzerland)8: 669-679.

10. Chai, Y, Berke, SS, Cohen, RE, and Paulson, HL (2004). Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways. J Biol Chem279: 3605-3611. 11. Mao, Y, Senic-Matuglia, F, Di Fiore, PP, Polo, S, Hodsdon, ME, and De Camilli, P (2005).

Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.

Proceedings of the National Academy of Sciences of the United States of America102: 12700-12705. 12. Winborn, BJ, Travis, SM, Todi, SV, Scaglione, KM, Xu, P, Williams, AJ, et al. (2008). The deubiquitinating

enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. The Journal of biological chemistry283: 26436-26443.

13. Alves, S, Nascimento-Ferreira, I, Dufour, N, Hassig, R, Auregan, G, Nobrega, C, et al. (2010). Silencing ataxin-3 mitigates degeneration in a rat model of Machado-Joseph disease: no role for wild-type ataxin-3? Hum Mol Genet19: 2380-2394.

14. Alves, S, Nascimento-Ferreira, I, Auregan, G, Hassig, R, Dufour, N, Brouillet, E, et al. (2008). Allele- specific RNA silencing of mutant ataxin-3 mediates neuroprotection in a rat model of Machado- Joseph disease. PLoS One3: e3341.

15. Conceicao, M, Mendonca, L, Nobrega, C, Gomes, C, Costa, P, Hirai, H, et al. (2015). Intravenous administration of brain-targeted stable nucleic acid lipid particles alleviates Machado-Joseph disease neurological phenotype. Biomaterials82: 124-137.

16. Nobrega, C, Nascimento-Ferreira, I, Onofre, I, Albuquerque, D, Hirai, H, Deglon, N, et al. (2013). Silencing mutant ataxin-3 rescues motor deficits and neuropathology in Machado-Joseph disease transgenic mice. PloS one8: e52396.

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17. Evers, MM, Toonen, LJ, and van Roon-Mom, WM (2015). Antisense oligonucleotides in therapy for neurodegenerative disorders. Advanced drug delivery reviews87: 90-103.

18. Aartsma-Rus, A (2012). Overview on AON design. Methods Mol Biol867: 117-129.

19. Aartsma-Rus, A, van Vliet, L, Hirschi, M, Janson, AA, Heemskerk, H, de Winter, CL, et al. (2009). Guidelines for antisense oligonucleotide design and insight into splice-modulating mechanisms.

Molecular therapy : the journal of the American Society of Gene Therapy17: 548-553.

20. Desmet, FO, Hamroun, D, Lalande, M, Collod-Beroud, G, Claustres, M, and Beroud, C (2009). Human Splicing Finder: an online bioinformatics tool to predict splicing signals. Nucleic Acids Res37: e67. 21. Swayze, EE, Siwkowski, AM, Wancewicz, EV, Migawa, MT, Wyrzykiewicz, TK, Hung, G, et al. (2007).

Antisense oligonucleotides containing locked nucleic acid improve potency but cause significant hepatotoxicity in animals. Nucleic acids research35: 687-700.

22. Bauer, S, Kirschning, CJ, Hacker, H, Redecke, V, Hausmann, S, Akira, S, et al. (2001). Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition. Proceedings of the National Academy of Sciences of the United States of America98: 9237-9242.

23. Janicki, SM, Tsukamoto, T, Salghetti, SE, Tansey, WP, Sachidanandam, R, Prasanth, KV, et al. (2004). From Silencing to Gene Expression: Real-Time Analysis in Single Cells. Cell116: 683-698.

24. Evers, MM, Tran, HD, Zalachoras, I, Pepers, BA, Meijer, OC, den Dunnen, JT, et al. (2013). Ataxin-3 protein modification as a treatment strategy for spinocerebellar ataxia type 3: removal of the CAG containing exon. Neurobiology of disease58: 49-56.

25. Toonen, LJ, Schmidt, I, Luijsterburg, MS, van Attikum, H, and van Roon-Mom, WM (2016). Antisense oligonucleotide-mediated exon skipping as a strategy to reduce proteolytic cleavage of ataxin-3.

Sci Rep6: 35200.

26. Cemal, CK, Carroll, CJ, Lawrence, L, Lowrie, MB, Ruddle, P, Al-Mahdawi, S, et al. (2002). YAC transgenic mice carrying pathological alleles of the MJD1 locus exhibit a mild and slowly progressive cerebellar deficit. Human molecular genetics11: 1075-1094.

27. Schneider, CA, Rasband, WS, and Eliceiri, KW (2012). NIH Image to ImageJ: 25 years of image analysis. Nature methods9: 671-675.

28. Luijsterburg, MS, Acs, K, Ackermann, L, Wiegant, WW, Bekker‐Jensen, S, Larsen, DH, et al. (2012). A new non‐catalytic role for ubiquitin ligase RNF8 in unfolding higher‐order chromatin structure.

The EMBO Journal31: 2511-2527.

29. Pfeiffer, A, Luijsterburg, MS, Acs, K, Wiegant, WW, Helfricht, A, Herzog, LK, et al. (2017). Ataxin-3 consolidates the MDC1-dependent DNA double-strand break response by counteracting the SUMO- targeted ubiquitin ligase RNF4. Embo j.

30. Gaspar, C, Lopes-Cendes, I, Hayes, S, Goto, J, Arvidsson, K, Dias, A, et al. (2001). Ancestral origins of the Machado-Joseph disease mutation: a worldwide haplotype study. American journal of human genetics68: 523-528.

31. Michlewski, G, and Krzyzosiak, WJ (2004). Molecular architecture of CAG repeats in human disease related transcripts. J Mol Biol340: 665-679.

32. Burnett, B, Li, F, and Pittman, RN (2003). The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Human molecular genetics12: 3195-3205.

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33. Costa Mdo, C, Luna-Cancalon, K, Fischer, S, Ashraf, NS, Ouyang, M, Dharia, RM, et al. (2013). Toward RNAi therapy for the polyglutamine disease Machado-Joseph disease. Molecular therapy : the journal of the American Society of Gene Therapy21: 1898-1908.

34. Rodriguez-Lebron, E, Costa Mdo, C, Luna-Cancalon, K, Peron, TM, Fischer, S, Boudreau, RL, et al. (2013). Silencing mutant ATXN3 expression resolves molecular phenotypes in SCA3 transgenic mice. Molecular therapy : the journal of the American Society of Gene Therapy21: 1909-1918. 35. Chen, S, Ferrone, FA, and Wetzel, R (2002). Huntington’s disease age-of-onset linked to polyglutamine

aggregation nucleation. Proceedings of the National Academy of Sciences of the United States of America99: 11884-11889.

36. Holmes, WM, Klaips, CL, and Serio, TR (2014). Defining the limits: Protein aggregation and toxicity in vivo. Critical reviews in biochemistry and molecular biology49: 294-303.

37. Koch, P, Breuer, P, Peitz, M, Jungverdorben, J, Kesavan, J, Poppe, D, et al. (2011). Excitation-induced ataxin-3 aggregation in neurons from patients with Machado-Joseph disease. Nature480: 543-546. 38. Wanker, EE, Scherzinger, E, Heiser, V, Sittler, A, Eickhoff, H, and Lehrach, H (1999). Membrane

filter assay for detection of amyloid-like polyglutamine-containing protein aggregates. Methods in enzymology309: 375-386.

39. Bichelmeier, U, Schmidt, T, Hubener, J, Boy, J, Ruttiger, L, Habig, K, et al. (2007). Nuclear localization of ataxin-3 is required for the manifestation of symptoms in SCA3: in vivo evidence. The Journal of neuroscience : the official journal of the Society for Neuroscience27: 7418-7428.

40. Evers, MM, Toonen, LJ, and van Roon-Mom, WM (2014). Ataxin-3 protein and RNA toxicity in spinocerebellar ataxia type 3: current insights and emerging therapeutic strategies. Mol Neurobiol49: 1513-1531.

41. Evert, BO, Araujo, J, Vieira-Saecker, AM, de Vos, RA, Harendza, S, Klockgether, T, et al. (2006). Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation. The Journal of neuroscience : the official journal of the Society for Neuroscience26: 11474-11486. 42. Moore, LR, Rajpal, G, Dillingham, IT, Qutob, M, Blumenstein, KG, Gattis, D, et al. (2017). Evaluation of Antisense Oligonucleotides Targeting ATXN3 in SCA3 Mouse Models. Molecular therapy Nucleic acids7: 200-210.

43. Schmitt, I, Linden, M, Khazneh, H, Evert, BO, Breuer, P, Klockgether, T, et al. (2007). Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination. Biochemical and biophysical research communications362: 734-739.

44. Switonski, PM, Fiszer, A, Kazmierska, K, Kurpisz, M, Krzyzosiak, WJ, and Figiel, M (2011). Mouse ataxin-3 functional knock-out model. Neuromolecular Med13: 54-65.

45. Boeddrich, A, Gaumer, S, Haacke, A, Tzvetkov, N, Albrecht, M, Evert, BO, et al. (2006). An arginine/ lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis. The EMBO journal25: 1547-1558.

46. Nicastro, G, Todi, SV, Karaca, E, Bonvin, AM, Paulson, HL, and Pastore, A (2010). Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3. PloS one5: e12430. 47. Donaldson, KM, Li, W, Ching, KA, Batalov, S, Tsai, CC, and Joazeiro, CA (2003). Ubiquitin-mediated

sequestration of normal cellular proteins into polyglutamine aggregates. Proceedings of the National Academy of Sciences of the United States of America100: 8892-8897.

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48. Tzvetkov, N, and Breuer, P (2007). Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes. Biological chemistry388: 973-978.

49. Laco, MN, Cortes, L, Travis, SM, Paulson, HL, and Rego, AC (2012). Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3. PloS one7: e43563.

50. Zhong, X, and Pittman, RN (2006). Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates. Hum Mol Genet15: 2409-2420.

51. Hubener, J, Vauti, F, Funke, C, Wolburg, H, Ye, Y, Schmidt, T, et al. (2011). N-terminal ataxin-3 causes neurological symptoms with inclusions, endoplasmic reticulum stress and ribosomal dislocation.

Brain : a journal of neurology134: 1925-1942.

52. Liu, J, Yu, D, Aiba, Y, Pendergraff, H, Swayze, EE, Lima, WF, et al. (2013). ss-siRNAs allele selectively inhibit ataxin-3 expression: multiple mechanisms for an alternative gene silencing strategy. Nucleic acids research41: 9570-9583.

53. Bonanomi, M, Visentin, C, Invernizzi, G, Tortora, P, and Regonesi, ME (2015). The Toxic Effects of Pathogenic Ataxin-3 Variants in a Yeast Cellular Model. PloS one10: e0129727.

54. Pellistri, F, Bucciantini, M, Invernizzi, G, Gatta, E, Penco, A, Frana, AM, et al. (2013). Different ataxin-3 amyloid aggregates induce intracellular Ca(2+) deregulation by different mechanisms in cerebellar granule cells. Biochimica et biophysica acta1833: 3155-3165.

55. Chen, X, Tang, TS, Tu, H, Nelson, O, Pook, M, Hammer, R, et al. (2008). Deranged calcium signaling and neurodegeneration in spinocerebellar ataxia type 3. The Journal of neuroscience : the official journal of the Society for Neuroscience28: 12713-12724.

56. Rigo, F, Chun, SJ, Norris, DA, Hung, G, Lee, S, Matson, J, et al. (2014). Pharmacology of a central nervous system delivered 2’-O-methoxyethyl-modified survival of motor neuron splicing oligonucleotide in mice and nonhuman primates. The Journal of pharmacology and experimental therapeutics350: 46-55.

57. Chiriboga, CA, Swoboda, KJ, Darras, BT, Iannaccone, ST, Montes, J, De Vivo, DC, et al. (2016). Results from a phase 1 study of nusinersen (ISIS-SMN(Rx)) in children with spinal muscular atrophy.

Neurology86: 890-897.

58. Boy, J, Schmidt, T, Wolburg, H, Mack, A, Nuber, S, Bottcher, M, et al. (2009). Reversibility of symptoms in a conditional mouse model of spinocerebellar ataxia type 3. Hum Mol Genet18: 4282-4295. 59. Kordasiewicz, HB, Stanek, LM, Wancewicz, EV, Mazur, C, McAlonis, MM, Pytel, KA, et al. (2012).

Sustained therapeutic reversal of Huntington’s disease by transient repression of huntingtin synthesis.

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