Amyloid-like aggregates of expanded polyglutamines are present in nuclei from affected neurons in Huntington and related neurodegenerative diseases.
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References
Paulson H.L. & Fishbeck, K.H. Trinucleotide repeats in neurogenetic disorders. Ann. Rev. Neurosci. 19, 79–107 (1997).
Zoghbi, H.Y. CAG repeats in SCA6: anticipating new clues. Neurology in the press.
Davies, S.W. et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537–548 (1997).
Mangiarini, L. et al. Exon l of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87, 493–506 (1996).
Skinner, P.J. et al. SCA1 pathogenesis involves alterations in nuclear matrix-associated structures. Nature in the press.
Difiglia, M. et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990–1993 (1997).
Paulson, H.L. et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19, 333–344 (1997).
Clark, H.B. et al. Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviours followed by a progressive cerebellar dysfunction and histologies! alterations. J. Neurosci. in the press.
Matilla, A. et al. The cerebellar leucine-rich acidic nuclear protein (LANP) interacts with ataxin-l. Nature in the press.
Kalchman, M.A. et al. HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nature Genet 16, 44–53 (1997).
Jarrett, J.T. & Lansbury, P.T. Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie. Cell 73, 1055–1058 (1993).
Goldberg, Y.P. et al. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nature Genet. 13, 442–449 (1996).
Scherzinger, E. et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90, 549–558 (1997).
Stott, K., Blackburn, J.M., Butler, P.J. & Perutz, M. Incorporation of glutamine repeats make proteins oligomerize: Implications for neurodegenerative diseases. Proc. Notl. Acad. Sci. U.S.A. 92, 6509–6513 (1995).
Trottier, Y. et al. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature 378, 403–406 (1995).
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Lunkes, A., Mandel, JL. Polyglutamines, nuclear inclusions and neurodegeneration. Nat Med 3, 1201–1202 (1997). https://doi.org/10.1038/nm1197-1201
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DOI: https://doi.org/10.1038/nm1197-1201
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