Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion (original) (raw)
Martin, J.B. & Gusella, J.F. Huntington's disease: pathogenesis and management. N. Engl. J. Med.315, 1267–1276 (1986). ArticleCASPubMed Google Scholar
Vonsattel, J.P. et al. Neuropathological classification of Huntington's disease. J. Neuropathol. Exp. Neuml.44, 559–577 (1985). ArticleCAS Google Scholar
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell.72, 971–983 (1993). Article Google Scholar
McNeil, S.M. et al. Reduced penetrance of the Huntington's disease mutation. Hum. Mol. Genet.6, 775–779 (1997). ArticleCASPubMed Google Scholar
Rubinsztein, D.C. et al. Phenotypic characterization of individuals with 30–40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36–39 repeats. Am. J. Hum. Genet.59, 16–22 (1996). CASPubMedPubMed Central Google Scholar
Gusella, J.F., Persichetti, F. & MacDonald, M.E. The genetic defect causing Huntington's disease: repeated in other contexts. Mol. Med.3, 238–246 (1997). ArticleCASPubMedPubMed Central Google Scholar
Ide, K. et al. Abnormal gene product identified in Huntington's disease lymphocytes and brain. Biochem. Biophys. Res. Commun.209, 1119–1125 (1995). ArticleCASPubMed Google Scholar
Trottier, Y. et al. Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form. Nature Genet.10, 104–110 (1995). ArticleCASPubMed Google Scholar
Jou, Y.S. & Myers, R.M. Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein. Hum. Mol. Genet.4, 465–469 (1995). ArticleCASPubMed Google Scholar
Sharp, A.H. et al. Widespread expression of Huntington's disease gene (IT15) protein product. Neuron.14, 1065–1074 (1995). ArticleCASPubMed Google Scholar
DiFiglia, M. et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron.14, 1075–1081 (1995). ArticleCASPubMed Google Scholar
Gutekunst, C.-A. et al. Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc. Natl. Acad. Sci. USA.92, 8710–8714 (1995). ArticleCASPubMedPubMed Central Google Scholar
Persichetti, F. et al. Normal and expanded Huntington's disease alleles produce distinguishable proteins due to translation across the CAG repeat. Mol. Med.1, 374–383 (1995). ArticleCASPubMedPubMed Central Google Scholar
Trottier, Y. et al. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature.378, 403–406 (1995). ArticleCASPubMed Google Scholar
Persichetti, F. et al. Huntington's disease CAG trinucleotide repeats in neuropathologically confirmed post-mortem brains. Neurobiol. Dis.1, 159–166 (1995). Article Google Scholar
Li, X.J. et al. A huntingtin-associated protein enriched in brain with implications for pathology. Nature.378, 398–402 (1995). ArticleCASPubMed Google Scholar
Bao, J. et al. Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin. Proc. Natl. Acad. Sci. USA.93, 5037–5042 (1996). ArticleCASPubMedPubMed Central Google Scholar
Burke, J.R. et al. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nature Med.2, 347–350 (1996). ArticleCASPubMed Google Scholar
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). ArticleCASPubMed Google Scholar
Wanker, E.E. et al. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. Hum. Mol. Genet.6, 487–495 (1997). ArticleCASPubMed Google Scholar
Ambrose, C.M. et al. Structure and expression of the Huntington's disease gene: evidence against simple inactivation due to an expanded CAG repeat. Somatic Cell Mol. Genet.20, 27–38 (1994). ArticleCAS Google Scholar
Duyao, M.P. et al. Homozygous inactivation of the mouse Hdh gene does not produce a Huntington's disease-like phenotype. Science.269, 407–410 (1995). ArticleCASPubMed Google Scholar
Zeitlin, S. et al. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nature Genet.11, 155–162 (1995). ArticleCASPubMed Google Scholar
Nasir, J. et al. Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes. Cell.81, 811–823 (1995). ArticleCASPubMed Google Scholar
MacDonald, M.E. & Gusella, J.F. Huntington's disease: translating a CAG repeat into a pathogenic mechanism. Curr. Opin. Neurobiol.6, 638–650 (1996). ArticleCASPubMed Google Scholar
Barnes, G.T. et al. Mouse Huntington's disease gene homolog (Hdh). Somat. Cell Mol. Genet.20, 87–97 (1994). ArticleCASPubMed Google Scholar
Lin, B. et al. Sequence of the murine Huntington disease gene: evidence for conservation, alternate splicing and polymorphism in a triplet (CCG) repeat [published erratum appears in Hum. Mol. Genet.3, 530 (1994)]. Hum. Mol. Genet.3, 85–92 (1994). Google Scholar
MacDonald, M.E. et al. Targeted inactivation of the mouse Huntington disease homologue Hdh . Cold Spring Harbor Symp Quant. Biol.61, 627–638 (1996). ArticleCASPubMed Google Scholar
Lin, B. et al. Structural analysis of the 5′ region of mouse and human Huntington disease genes reveals conservation of putative promoter region and di- and trinucleotide polymorphisms. Genomics.25, 707–715 (1995). ArticleCASPubMed Google Scholar
Stumpo, D.J. et al. MARCKS deficiency in mice leads to abnormal brain development and perinatal death. Proc. Natl. Acad. Sci. USA.92, 944–948 (1995). ArticleCASPubMedPubMed Central Google Scholar
Wu, M. et al. Neural tube defects and abnormal brain development in F52-deficient mice. Proc. Natl. Acad. Sci. USA.93, 2110–2115 (1996). ArticleCASPubMedPubMed Central Google Scholar
Hui, C.-C. & Joyner,, A.L A mouse model of Greig cephalo-polysyndactyly syndrome: the extra-toesJ mutation contains an intragenic deletion of the GH3 gene. Nature Genet.3, 241–246 (1993). ArticleCASPubMed Google Scholar
Shah, V. et al. A subset of p53-deficient embryos exhibit exencephaly. Nature Genet.10, 175–180 (1995). Article Google Scholar
Kuida, K. et al. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature.384, 368–372 (1996). ArticleCASPubMed Google Scholar
Gusella, J.F., Persichetti, F. & MacDonald, M.E. The genetic defect causing Huntington's disease: repeated in other contexts. Mol. Med.3, 238–246 (1997). ArticleCASPubMedPubMed Central Google Scholar
Bingham, P.M. et al. Stability of an expanded trinucleotide repeat in the androgen receptor gene in transgenic mice [published erratum appears in. _Nature Genet._ **9**, 191–196 (1995). ArticleCASPubMed Google Scholar
Goldberg, Y.P. et al. Absence of disease phenotype and intergenerational stability of the CAG repeat in transgenic mice expressing the human Huntington disease transcript. Hum. Mol. Genet.5, 177–185 (1996). ArticleCASPubMed Google Scholar
Ikeda, H. et al. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo . Nature Genet.13, 196–202 (1996). ArticleCASPubMed Google Scholar
Burright, E.N. et al. SCA1 transgenic mice: a model for neurodegeneration caused by an expanded CAG trinucleotide repeat. Cell.82, 937–948 (1995). ArticleCASPubMed Google Scholar
Mangiarini, L.E. et al. Exon 1 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). ArticleCASPubMed Google Scholar
Hanks, M. et al. Rescue of the En-1 mutant phenotype by replacement of En-1 with En-2 . Science.269, 679–682 (1995). ArticleCASPubMed Google Scholar
Warner, J.P., Barren, L.H. & Brock, D.J. A new polymerase chain reaction (PCR) assay for the trinucleotide repeat that is unstable and expanded on Huntington's disease chromosomes. Mol. Cell. Probes.7, 235–239 (1993). ArticleCASPubMed Google Scholar
Nagy, A. et al. Derivation of completely cell culture–derived mice from early-passage embryonic stem cells. Proc Natl. Acad. Sci. USA.90, 8424–8428 (1993). ArticleCASPubMedPubMed Central Google Scholar
Wurst, W. & Joyner, A.L. Production of targeted embryonic stem cell clones in Gene Targeting: A Practical Approach (ed. A.L. Joyner) 33–62 (Oxford University Press, Oxford, UK, 1993). Google Scholar
Nagy, A. & Rossant, J. Production of completely ES cell-derived fetuses. in Gene Targeting: A Practical Approach (ed. A.L. Joyner) 147–180 (Oxford University Press, Oxford, UK, 1993).
Miller, M.W. & Nowakowski, R.S. Use of bromodeoxyuridine-immunohistochemistry to examine the proliferation, migration and time of origin of cells in the central nervous system. Brain Res.457, 44–52 (1988). ArticleCASPubMed Google Scholar