Amino acids in a region of ataxin-1 outside of the polyglutamine tract influence the course of disease in SCA1 transgenic mice
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Huda Y. Zoghbi | Harry T. Orr | H. Zoghbi | E. Emamian | H. Orr | P. Skinner | C. Vierra-Green | Pamela J. Skinner | Cynthia A. Vierra-Green | Effat Emamian
[1] S. Kish,et al. Structural and immunocytochemical features of olivopontocerebellar atrophy caused by the spinocerebellar ataxia type 1 (SCA-1) mutation define a unique phenotype , 2004, Acta Neuropathologica.
[2] I. Kanazawa,et al. SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. , 2001, Human molecular genetics.
[3] Harry T Orr,et al. SCA1 transgenic mice: A model for neurodegeneration caused by an expanded CAG trinucleotide repeat , 1995, Cell.
[4] H. Zoghbi,et al. Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures , 1997, Nature.
[5] H. Zoghbi,et al. The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1 , 1997, Nature.
[6] Huda Y. Zoghbi,et al. Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1 , 2000, Nature Neuroscience.
[7] H. Zoghbi,et al. Altered trafficking of membrane proteins in purkinje cells of SCA1 transgenic mice. , 2001, The American journal of pathology.
[8] H. Zoghbi,et al. Expression analysis of the ataxin–1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals , 1995, Nature Genetics.
[9] M. MacDonald,et al. Huntingtin interacts with a family of WW domain proteins. , 1998, Human molecular genetics.
[10] Michael A. Mancini,et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 , 1998, Nature Genetics.
[11] J. M. Boutell,et al. Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin. , 1999, Human molecular genetics.
[12] H. Lehrach,et al. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. , 1997, Human molecular genetics.
[13] P. Howley,et al. The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. , 2000, Molecular cell.
[14] H. Zoghbi,et al. Purkinje Cell Expression of a Mutant Allele of SCA1in Transgenic Mice Leads to Disparate Effects on Motor Behaviors, Followed by a Progressive Cerebellar Dysfunction and Histological Alterations , 1997, The Journal of Neuroscience.
[15] Harry T Orr,et al. Mutation of the E6-AP Ubiquitin Ligase Reduces Nuclear Inclusion Frequency While Accelerating Polyglutamine-Induced Pathology in SCA1 Mice , 1999, Neuron.
[16] Max F. Perutz,et al. Glutamine repeats and neurodegenerative diseases: molecular aspects. , 1999, Trends in biochemical sciences.
[17] S. Snyder,et al. A huntingtin-associated protein enriched in brain with implications for pathology , 1995, Nature.
[18] Harry T Orr,et al. Ataxin-1 Nuclear Localization and Aggregation Role in Polyglutamine-Induced Disease in SCA1 Transgenic Mice , 1998, Cell.
[19] H. Zoghbi,et al. Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein. , 2000, Human molecular genetics.
[20] J. Yewdell,et al. Intracellular Localization of Proteasomal Degradation of a Viral Antigen , 1999, The Journal of cell biology.
[21] H. Zoghbi,et al. Identification of a self-association region within the SCA1 gene product, ataxin-1. , 1997, Human molecular genetics.