Intranuclear Inclusions of Expanded Polyglutamine Protein in Spinocerebellar Ataxia Type 3
暂无分享,去创建一个
K. Fischbeck | J. Trojanowski | H. Paulson | S. Subramony | J. Mandel | Y. Trottier | J. Q Trojanowski | Y Trottier | R. Pittman | H. L Paulson | M. K Perez | S. H Subramony | S. S Das | P Vig | J.-L Mandel | K. H Fischbeck | R. N Pittman | P. Vig | P. Vig | M. K. Perez | S. Das | S. Das | S. Das | S. Das | Matthew K. Perez
[1] H. Green,et al. Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[2] H. Zoghbi,et al. Expression analysis of the ataxin–1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals , 1995, Nature Genetics.
[3] S. W. Davies,et al. Exon 1 of the HD Gene with an Expanded CAG Repeat Is Sufficient to Cause a Progressive Neurological Phenotype in Transgenic Mice , 1996, Cell.
[4] L. Schöls,et al. Trinucleotide expansion within the MJD1 gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients. , 1995, Human molecular genetics.
[5] K. Fischbeck,et al. Machado‐Joseph disease gene product is a cytoplasmic protein widely expressed in brain , 1997, Annals of neurology.
[6] P E Fraser,et al. A kinetic model for amyloid formation in the prion diseases: importance of seeding. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[7] C A Ross,et al. Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[8] Mark Turmaine,et al. Formation of Neuronal Intranuclear Inclusions Underlies the Neurological Dysfunction in Mice Transgenic for the HD Mutation , 1997, Cell.
[9] Christopher A Ross,et al. Widespread expression of Huntington's disease gene (IT15) protein product , 1995, Neuron.
[10] K. Fischbeck,et al. Trinucleotide repeats in neurogenetic disorders. , 1996, Annual review of neuroscience.
[11] R. Rosenberg. Machado‐Joseph disease: An autosomal dominant motor system degeneration , 1992, Movement disorders : official journal of the Movement Disorder Society.
[12] S. Tsuji,et al. A clinical and pathologic study of a large Japanese family with Machado‐ Joseph disease tightly linked to the DNA markers on chromosome 14q , 1994, Neurology.
[13] Shigenobu Nakamura,et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1 , 1994, Nature Genetics.
[14] G. G. Stokes. "J." , 1890, The New Yale Book of Quotations.
[15] Manish S. Shah,et al. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes , 1993, Cell.
[16] A. Roses,et al. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH , 1996, Nature Medicine.
[17] J. D. den Dunnen,et al. Subcellular localization of the Huntington's disease gene product in cell lines by immunofluorescence and biochemical subcellular fractionation. , 1996, Human molecular genetics.
[18] G. Sobue,et al. Molecular features of the CAG repeats and clinical manifestation of Machado-Joseph disease. , 1995, Human molecular genetics.
[19] P. Coutinho,et al. Machado-Joseph disease. , 1995, Clinical neuroscience.
[20] H. Zoghbi,et al. Molecular and clinical correlations in spinocerebellar ataxia type 3 and Machado‐Joseph disease , 1995, Annals of neurology.
[21] P. Chambon,et al. The N‐terminal domain of the human TATA‐binding protein plays a role in transcription from TATA‐containing RNA polymerase II and III promoters. , 1994, The EMBO journal.
[22] Harry T Orr,et al. SCA1 transgenic mice: A model for neurodegeneration caused by an expanded CAG trinucleotide repeat , 1995, Cell.
[23] H. Ehrsson,et al. An expanded CAG repeat sequence in spinocerebellar ataxia type 7. , 1996, Genome research.
[24] Í. Lopes-Cendes,et al. Correlation between CAG repeat length and clinical features in Machado-Joseph disease. , 1995, American journal of human genetics.
[25] H. Zoghbi. The expanding world of ataxins , 1996, Nature Genetics.
[26] Yves Agid,et al. Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats , 1996, Nature Genetics.
[27] D. Housman. Gain of glutamines, gain of function? , 1995, Nature Genetics.
[28] J. Beckmann,et al. The gene for the TATA binding protein (TBP) that contains a highly polymorphic protein coding CAG repeat maps to 6q27. , 1994, Genomics.
[29] H. Green. Human genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism , 1993, Cell.
[30] M. Perutz,et al. Glutamine repeats and inherited neurodegenerative diseases: molecular aspects. , 1996, Current opinion in structural biology.
[31] M. MacDonald,et al. Huntingtin Immunoreactivity in the Rat Neostriatum: Differential Accumulation in Projection and Interneurons , 1997, Experimental Neurology.
[32] C A Ross,et al. When more is less: Pathogenesis of glutamine repeat neurodegenerative diseases , 1995, Neuron.
[33] H. Lehrach,et al. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. , 1997, Human molecular genetics.
[34] Huda Y. Zoghbi,et al. Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1 , 1993, Nature Genetics.
[35] T. Yuasa,et al. Joseph's disease: Clinical and pathological studies in a Japanese family , 1986, Annals of neurology.
[36] E. Hirsch,et al. Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form , 1995, Nature Genetics.
[37] E. Mengual,et al. Immunohistochemical Distribution and Electron Microscopic Subcellular Localization of the Proteasome in the Rat CNS , 1996, The Journal of Neuroscience.
[38] J. Hodgson,et al. Huntingtin Is Ubiquitinated and Interacts with a Specific Ubiquitin-conjugating Enzyme* , 1996, The Journal of Biological Chemistry.
[39] M. MacDonald,et al. Huntington's disease: translating a CAG repeat into a pathogenic mechanism , 1996, Current Opinion in Neurobiology.
[40] G. Auburger,et al. Autosomal dominant cerebellar ataxia , 1990, Neurology.
[41] I. Kanazawa,et al. HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain , 1997, Nature Genetics.
[42] J T Finch,et al. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[43] R. Carraway,et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons , 1995, Neuron.
[44] M. Perutz,et al. Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[45] Matt L. Huffman,et al. When More is Less , 1997 .
[46] A. Sano,et al. Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p , 1994, Nature Genetics.
[47] D. Dickson,et al. Ubiquitin immunoreactive structures in normal human brains. Distribution and developmental aspects. , 1990, Laboratory investigation; a journal of technical methods and pathology.
[48] S. Prusiner,et al. Etiology and pathogenesis of prion diseases. , 1995, The American journal of pathology.
[49] L. Forno,et al. Joseph disease , 1982, Neurology.
[50] S. Narumiya,et al. Expanded polyglutamine in the Machado–Joseph disease protein induces cell death in vitro and in vivo , 1996, Nature Genetics.
[51] T D Bird,et al. Spinocerebellar ataxia type 1 and Machado-Joseph disease: incidence of CAG expansions among adult-onset ataxia patients from 311 families with dominant, recessive, or sporadic ataxia. , 1995, American journal of human genetics.
[52] K. Fischbeck,et al. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy , 1991, Nature.
[53] Georg Auburger,et al. Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2 , 1996, Nature Genetics.
[54] M. Hayden,et al. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract , 1996, Nature Genetics.
[55] A. Korczyn,et al. Intranuclear inclusions in oculopharyngeal muscular dystrophy among Bukhara Jews , 1996, Neurology.
[56] D W Dickson,et al. Intranuclear inclusion bodies in an elderly demented woman: a form of intranuclear inclusion body disease. , 1995, Clinical neuropathology.
[57] William B. Dobyns,et al. Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the α1A-voltage-dependent calcium channel , 1997, Nature Genetics.
[58] S. Hersch,et al. Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[59] S. Tsuji,et al. Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT , 1996, Nature Genetics.
[60] Y. Agid,et al. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias , 1995, Nature.
[61] G. Bates. Expanded glutamines and neurodegeneration--a gain of insight. , 1996, BioEssays : news and reviews in molecular, cellular and developmental biology.
[62] O. Onodera,et al. Unstable expansion of CAG repeat in hereditary dentatorubral–pallidoluysian atrophy (DRPLA) , 1994, Nature Genetics.
[63] S. Snyder,et al. A huntingtin-associated protein enriched in brain with implications for pathology , 1995, Nature.
[64] R. Mayer,et al. Ubiquitin in Neurodegenerative Diseases , 1993, Brain pathology.
[65] J. Palo,et al. Neurofilament subunit–related proteins in neuronal intranuclear inclusions , 1984, Annals of neurology.
[66] Alexandra Durr,et al. Spinocerebellar ataxia 3 and machado‐joseph disease: Clinical, molecular, and neuropathological features , 1996, Annals of neurology.