Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies. - Test2 - elhamkhani - TriplyDB

Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

http://www.wikidata.org/entity/Q34281671

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Experimental characterization of the human non-sequence-specific nucleic acid interactome Inside out: the role of nucleocytoplasmic transport in ALS and FTLD Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?Role of stress granules and RNA-binding proteins in neurodegeneration: a mini-review Stress Granules Modulate SYK to Cause Microglial Cell Dysfunction in Alzheimer's Disease.Ageing, neurodegeneration and brain rejuvenation Legal but lethal: functional protein aggregation at the verge of toxicity Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1 Deficiency of G3BP1, the stress granules assembly factor, results in abnormal synaptic plasticity and calcium homeostasis in neurons.YB-1 regulates stress granule formation and tumor progression by translationally activating G3BP1.Mutant human FUS Is ubiquitously mislocalized and generates persistent stress granules in primary cultured transgenic zebrafish cells An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.C. elegans sirtuin SIR-2.4 and its mammalian homolog SIRT6 in stress response.miRNAs at the interface of cellular stress and disease The small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assembly Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity.Dysregulation of RNA Binding Protein Aggregation in Neurodegenerative Disorders.Aggregation properties of the small nuclear ribonucleoprotein U1-70K in Alzheimer disease.RNA recognition and stress granule formation by TIA proteins.Single point mutations result in the miss-sorting of Glut4 to a novel membrane compartment associated with stress granule proteins.Non-aggregating tau phosphorylation by cyclin-dependent kinase 5 contributes to motor neuron degeneration in spinal muscular atrophy.Altered mRNP granule dynamics in FTLD pathogenesis.Frontotemporal dementia-associated N279K tau mutant disrupts subcellular vesicle trafficking and induces cellular stress in iPSC-derived neural stem cells.Pathological Tau Promotes Neuronal Damage by Impairing Ribosomal Function and Decreasing Protein Synthesis Stress granules as crucibles of ALS pathogenesis.Relationships between Stress Granules, Oxidative Stress, and Neurodegenerative Diseases.Regulated protein aggregation: stress granules and neurodegeneration Stress granules in neurodegeneration--lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma.Physiological protein aggregation run amuck: stress granules and the genesis of neurodegenerative disease.RNA binding proteins: a common denominator of neuronal function and dysfunction.Syk and Yea Shall Find.A Non-Invasive NMR Method Based on Histidine Imidazoles to Analyze the pH-Modulation of Protein-Nucleic Acid Interfaces.Dysregulated expression of lipid storage and membrane dynamics factors in Tia1 knockout mouse nervous tissue.Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau.TIA1 oxidation inhibits stress granule assembly and sensitizes cells to stress-induced apoptosis.Principles and Properties of Stress Granules Prion-like propagation as a pathogenic principle in frontotemporal dementia.Robust cytoplasmic accumulation of phosphorylated TDP-43 in transgenic models of tauopathy.Regulatory region genetic variation is associated with FYN expression in Alzheimer's disease.Antagonistic roles for STYX pseudophosphatases in neurite outgrowth.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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2012 nî lūn-bûn

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2012年の論文

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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JNEUROSCI.1592-12.2012

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Journal of Neuroscience

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Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies.

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Allison Citro

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Benjamin Wolozin

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Haung Yu

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Karen Duff

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Liqun Liu-Yesucevitz

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Megan Varnum

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Tara Vanderweyde

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Tsuneya Ikezu

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P2860

Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats

DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4)

Stress granule assembly is mediated by prion-like aggregation of TIA-1

Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport.

Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23.

The proximal region of the 3'-untranslated region of cyclooxygenase-2 is recognized by a multimeric protein complex containing HuR, TIA-1, TIAR, and the heterogeneous nuclear ribonucleoprotein U

Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease

Mutations in the gene encoding immunoglobulin mu-binding protein 2 cause spinal muscular atrophy with respiratory distress type 1

Stress granules: sites of mRNA triage that regulate mRNA stability and translatability

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10.1523/JNEUROSCI.1592-12.2012

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24

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22699908

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