Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
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Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALSRedox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linkingThe genetics and neuropathology of frontotemporal lobar degenerationAccumulation of transactive response DNA binding protein 43 in mild cognitive impairment and Alzheimer diseaseNeuroinflammation in motor neuron diseaseCell biology of spinocerebellar ataxiaThe involvement of microRNAs in neurodegenerative diseasesEngineering enhanced protein disaggregases for neurodegenerative diseaseALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosisPhosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy.Neuropathology of Amyotrophic Lateral Sclerosis and Its Variants.Development of a novel nonradiometric assay for nucleic acid binding to TDP-43 suitable for high-throughput screening using AlphaScreen technology.A Drosophila model for TDP-43 proteinopathy.TDP-43 regulates its mRNA levels through a negative feedback loop.Profiling the genes affected by pathogenic TDP-43 in astrocytesIdentification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes.Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLSA yeast model of FUS/TLS-dependent cytotoxicity.TAR DNA-binding protein 43 in neurodegenerative disease.Genetics and biology of Alzheimer's disease and frontotemporal lobar degenerationThe influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS.Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.Nuclear TAR DNA-binding protein 43: A new target for amyotrophic lateral sclerosis treatmentDeletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism.TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor.Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA.Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins.Clinical phenotypes and genetic biomarkers of FTLD.Similar intracellular peptide profile of TAP1/β2 microglobulin double-knockout mice and C57BL/6 wild-type mice as revealed by peptidomic analysis.Knockdown of the Drosophila fused in sarcoma (FUS) homologue causes deficient locomotive behavior and shortening of motoneuron terminal branches.Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice.Ataxin-2 intermediate-length polyglutamine expansions in European ALS patientsTDP-1, the Caenorhabditis elegans ortholog of TDP-43, limits the accumulation of double-stranded RNA.Targeting RNA binding proteins involved in neurodegeneration.Risk genotypes at TMEM106B are associated with cognitive impairment in amyotrophic lateral sclerosis.A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport.Building an integrated neurodegenerative disease database at an academic health center.Loss of nuclear TDP-43 in amyotrophic lateral sclerosis (ALS) causes altered expression of splicing machinery and widespread dysregulation of RNA splicing in motor neurones.
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Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on October 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@en
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@nl
type
label
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@en
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@nl
prefLabel
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@en
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@nl
P2860
P356
P1476
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
@en
P2093
G Scott Pesiridis
Virginia M-Y Lee
P2860
P304
P356
10.1093/HMG/DDP303
P577
2009-10-01T00:00:00Z