Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. - Wikidata - awgldk - TriplyDB

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

http://www.wikidata.org/entity/Q45291767

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Huntingtin interacting proteins are genetic modifiers of neurodegeneration A human HAP1 homologue. Cloning, expression, and interaction with huntingtin HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system Huntingtin in health and disease The localization and interactions of huntingtin A dual-light reporter system to determine the efficiency of protein-protein interactions in mammalian cells Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin Glyceraldehyde-3-phosphate dehydrogenase, the putative target of the antiapoptotic compounds CGP 3466 and R-(-)-deprenyl Nuclear localization of glyceraldehyde-3-phosphate dehydrogenase is not involved in the initiation of apoptosis induced by 1-Methyl-4-phenyl-pyridium iodide (MPP+)The diverse functions of GAPDH: views from different subcellular compartments Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase Deletion of the triplet repeat encoding polyglutamine within the mouse Huntington's disease gene results in subtle behavioral/motor phenotypes in vivo and elevated levels of ATP with cellular senescence in vitro Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion An integrated strategy for evaluation of metabolic and oxidative defects in neurodegenerative illness using magnetic resonance techniques.Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeats Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts.Neurotoxicity of advanced glycation end-products for cultured cortical neurons.Pathogenesis of inclusion bodies in (CAG)n/Qn-expansion diseases with special reference to the role of tissue transglutaminase and to selective vulnerability.Are there multiple pathways in the pathogenesis of Huntington's disease?Polyglutamine pathogenesis.Evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease in cell culture and in transgenic mice expressing mutant huntingtin.CAG-polyglutamine-repeat mutations: independence from gene context.Recent advances in the genetics of epilepsy: insights from human and animal studies.The advantage of channeling nucleotides for very processive functions Of mice and men: solving the molecular mysteries of Huntington's disease.Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration Interaction of expanded polyglutamine stretches with nuclear transcription factors leads to aberrant transcriptional regulation in polyglutamine diseases.The selective vulnerability of nerve cells in Huntington's disease.Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase.ETS1 regulates the expression of ATXN2.Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2.Mutant huntingtin: nuclear translocation and cytotoxicity mediated by GAPDH Amyloid deposits: protection against toxic protein species?Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.Huntington's Disease: From Mutant Huntingtin Protein to Neurotrophic Factor Therapy.Transgenic mice expressing mutated full-length HD cDNA: a paradigm for locomotor changes and selective neuronal loss in Huntington's disease.Transcriptional modulator H2A histone family, member Y (H2AFY) marks Huntington disease activity in man and mouse

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P2860

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

http://www.wikidata.org/entity/Q45291767

description

1996 nî lūn-bûn

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1996年学术文章

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1996年學術文章

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1996年學術文章

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name

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

@en

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

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type

label

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

@en

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

@nl

prefLabel

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

@en

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

@nl

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Nature Medicine

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Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH.

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P2093

A D Roses

http://www.w3.org/2001/XMLSchema#string

J M Vance

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J R Burke

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M E Martin

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R M Myers

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W J Strittmatter

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Y S Jou

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P2860

Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals

Abnormal gene product identified in hereditary dentatorubral-pallidoluysian atrophy (DRPLA) brain

CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1

Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p

Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA)

The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease

Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA)

Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form

Glycolytic enzyme levels in synaptosomes

Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy.

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347-350

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10.1038/NM0396-347

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