Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
about
Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptorsHIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brainThe structure of the AXH domain of spinocerebellar ataxin-1Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtinS-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 bindingThe diverse functions of GAPDH: views from different subcellular compartmentsIdentification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenaseThe cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeatsReduction 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.Polyglutamine pathogenesis.Analysis of exon 1 mutations in the androgen receptor gene.Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegenerationETS1 regulates the expression of ATXN2.Mutant huntingtin: nuclear translocation and cytotoxicity mediated by GAPDHNonneural nuclear inclusions of androgen receptor protein in spinal and bulbar muscular atrophy.Ataxin-1 poly(Q)-induced proteotoxic stress and apoptosis are attenuated in neural cells by docosahexaenoic acid-derived neuroprotectin D1.Impaired GAPDH-induced mitophagy contributes to the pathology of Huntington's disease.Glyceraldehyde-3-phosphate dehydrogenase: nuclear translocation participates in neuronal and nonneuronal cell death.Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological lengthPharmacological protein targets in polyglutamine diseases: mutant polypeptides and their interactors.Glyceraldehyde-3-phosphate dehydrogenase enhances transcriptional activity of androgen receptor in prostate cancer cells.Intracellular processing and toxicity of the truncated androgen receptor: nuclear congophilia-associated cell death.Polyglutamine domain proteins with expanded repeats bind neurofilament, altering the neurofilament network.The dual role of a yeast metacaspase: What doesn't kill you makes you stronger.Molecular genetics and neurobiology of neurodegenerative and neurodevelopmental disorders.The CAG/polyglutamine tract diseases: gene products and molecular pathogenesis.Toward understanding the molecular pathology of Huntington's disease.Huntington's disease and dentatorubral-pallidoluysian atrophy: proteins, pathogenesis and pathology.Characterization of proteins associated with polyglutamine aggregates: a novel approach towards isolation of aggregates from protein conformation disorders.Induction of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) expression in rat brain after focal ischemia/reperfusion.Glyceraldehyde 3-phosphate dehydrogenase augments the intercellular transmission and toxicity of polyglutamine aggregates in a cell model of Huntington disease.Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis.Urinary diagnostic proteomic markers for dynapenia in cancer patients.Inhibition of α-ketoglutarate-and pyruvate dehydrogenase complexes in E. coli by a glutathione S-transferase containing a pathological length poly-Q domain: A possible role of energy deficit in neurological diseases associated with poly-Q expansionsThe AXH module: an independently folded domain common to ataxin-1 and HBP1
P2860
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P2860
Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@ast
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@en
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@nl
type
label
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@ast
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@en
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@nl
prefLabel
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@ast
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@en
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@nl
P2093
P356
P1476
Spinocerebellar ataxia type-1 ...... hyde-3-phosphate dehydrogenase
@en
P2093
P304
P356
10.1093/HMG/5.9.1311
P407
P577
1996-09-01T00:00:00Z