Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis - Wikidata - thesis-toulmin - TriplyDB

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

http://www.wikidata.org/entity/Q24642141

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Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS Update in inclusion body myositis Targeting protein homeostasis in sporadic inclusion body myositis.The Myoblast C2C12 Transfected with Mutant Valosin-Containing Protein Exhibits Delayed Stress Granule Resolution on Oxidative Stress.Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6 Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations.Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease Sporadic inclusion body myositis: the genetic contributions to the pathogenesis.TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97.Theories of the pathogenesis of inclusion body myositis.Aquaporin-4 expression in distal myopathy with rimmed vacuoles.Ongoing developments in sporadic inclusion body myositis Sporadic inclusion body myositis: new insights and potential therapy.Cytosolic 5'-nucleotidase 1A autoimmunity in sporadic inclusion body myositis.Proteasome dysfunction induces muscle growth defects and protein aggregation.Molecular markers for granulovacuolar degeneration are present in rimmed vacuoles.Diagnostic value of markers of muscle degeneration in sporadic inclusion body myositis.Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D Muscleblind, BSF and TBPH are mislocalized in the muscle sarcomere of a Drosophila myotonic dystrophy model.Expression of myogenic regulatory factors and myo-endothelial remodeling in sporadic inclusion body myositis Neuronal-specific overexpression of a mutant valosin-containing protein associated with IBMPFD promotes aberrant ubiquitin and TDP-43 accumulation and cognitive dysfunction in transgenic mice.Comparative utility of LC3, p62 and TDP-43 immunohistochemistry in differentiation of inclusion body myositis from polymyositis and related inflammatory myopathies.De novo prion aggregates trigger autophagy in skeletal muscle.Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly.Widespread RNA metabolism impairment in sporadic inclusion body myositis TDP43-proteinopathy.TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration.Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers Novel therapeutic approaches for inclusion body myositis.Review: An update on inflammatory and autoimmune myopathies.State of the art and the dark side of amyotrophic lateral sclerosis.Autoimmune myopathies: autoantibodies, phenotypes and pathogenesis.TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies.Common pathways of autoimmune inflammatory myopathies and genetic neuromuscular disorders.Understanding ALS: new therapeutic approaches.Amyloid deposits and inflammatory infiltrates in sporadic inclusion body myositis: the inflammatory egg comes before the degenerative chicken.Idiopathic inflammatory myopathies: from immunopathogenesis to new therapeutic targets.New ALS-Related Genes Expand the Spectrum Paradigm of Amyotrophic Lateral Sclerosis.

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Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

http://www.wikidata.org/entity/Q24642141

description

2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

@ast

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

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Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

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type

label

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

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Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

@en

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

@nl

prefLabel

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

@ast

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

@en

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

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Muscle and Nerve

P1476

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

@en

P2093

Anthony A Amato

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

Jack L Pinkus

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

Mohammad Salajegheh

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

Remedios Nazareno

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

Robert H Baloh

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

Steven A Greenberg

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

P2860

Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs

Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Inclusion body myositis and myopathies.

Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease.

TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis.

Structural determinants of the cellular localization and shuttling of TDP-43.

Inclusion body myositis: a distinct variety of idiopathic inflammatory myopathy.

Structural diversity and functional implications of the eukaryotic TDP gene family.

TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia.

Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis.

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19-31

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scholarly article

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10.1002/MUS.21386

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1

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40

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2009-07-01T00:00:00Z

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26298795

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19533646

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2700211

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