The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
about
Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcriptionThe role of LANP and ataxin 1 in E4F-mediated transcriptional repressionAtaxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptorsAtaxin-1 with an expanded glutamine tract alters nuclear matrix-associated structuresBoat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1.Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signalingProtein ligands to HuR modulate its interaction with target mRNAs in vivoNopp140 functions as a molecular link between the nucleolus and the coiled bodiesPolyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation.Targeted ANP32E mutant mice do not demonstrate obvious movement defectsCpd-1 null mice display a subtle neurological phenotypeThe crystal structure of the tumor suppressor protein pp32 (Anp32a): Structural insights into Anp32 family of proteinsStructural bases for recognition of Anp32/LANP proteinsThe promise and perils of HDAC inhibitors in neurodegenerationMapmodulin/leucine-rich acidic nuclear protein binds the light chain of microtubule-associated protein 1B and modulates neuritogenesisIdentification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenaseLHX3 interacts with inhibitor of histone acetyltransferase complex subunits LANP and TAF-1β to modulate pituitary gene regulationCXCL12-mediated regulation of ANP32A/Lanp, a component of the inhibitor of histone acetyl transferase (INHAT) complex, in cortical neuronsNeuronal differentiation is regulated by leucine-rich acidic nuclear protein (LANP), a member of the inhibitor of histone acetyltransferase complexPathogenesis of inclusion bodies in (CAG)n/Qn-expansion diseases with special reference to the role of tissue transglutaminase and to selective vulnerability.Intracellular inclusions, pathological markers in diseases caused by expanded polyglutamine tracts?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.Progress in pathogenesis studies of spinocerebellar ataxia type 1.Novel small molecules relieve prothymosin alpha-mediated inhibition of apoptosome formation by blocking its interaction with Apaf-1.An out-of-frame overlapping reading frame in the ataxin-1 coding sequence encodes a novel ataxin-1 interacting proteinProtein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations.Interaction of expanded polyglutamine stretches with nuclear transcription factors leads to aberrant transcriptional regulation in polyglutamine diseases.Cracking the ANP32 whips: important functions, unequal requirement, and hints at disease implications.A Drosophila model of the neurodegenerative disease SCA17 reveals a role of RBP-J/Su(H) in modulating the pathological outcome.Prion disease induced alterations in gene expression in spleen and brain prior to clinical symptoms.Transgenic mice expressing mutated full-length HD cDNA: a paradigm for locomotor changes and selective neuronal loss in Huntington's disease.Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans.Nonneural nuclear inclusions of androgen receptor protein in spinal and bulbar muscular atrophy.Pathways to motor incoordination: the inherited ataxias.Mechanisms of neural cell death: implications for development of neuroprotective treatment strategiesThe perinucleolar compartment and transcription.Trinucleotide repeats and neuropsychiatric disorders.The importance of serine 776 in Ataxin-1 partner selection: a FRET analysis.Genetic and molecular aspects of spinocerebellar ataxias.Generation and characterization of LANP/pp32 null mice.
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P2860
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
description
1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Nature
@fr
artículu científicu espublizáu en 1997
@ast
scientific journal article
@en
vedecký článok (publikovaný 1997/10/30)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/10/30)
@nl
наукова стаття, опублікована в жовтні 1997
@uk
مقالة علمية (نشرت في 30-10-1997)
@ar
name
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@ast
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@en
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@nl
type
label
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@ast
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@en
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@nl
prefLabel
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@ast
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@en
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@nl
P2093
P2860
P356
P1433
P1476
The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
@en
P2093
P2860
P2888
P304
P356
10.1038/40159
P407
P577
1997-10-01T00:00:00Z
P5875
P6179
1032260577