Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. - Wikidata - wikimedia - TriplyDB

Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.

Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.

http://www.wikidata.org/entity/Q36408540

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Inside out: the role of nucleocytoplasmic transport in ALS and FTLD Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1.Early lethality and neuronal proteinopathy in mice expressing cytoplasm-targeted FUS that lacks the RNA recognition motif.A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1 Pathogenesis of FUS-associated ALS and FTD: insights from rodent models Oxr1 improves pathogenic cellular features of ALS-associated FUS and TDP-43 mutations Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization Increasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift Reagent Are aberrant phase transitions a driver of cellular aging?Protein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy.Nucleic acid-binding specificity of human FUS protein.Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasm Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis.FUS is phosphorylated by DNA-PK and accumulates in the cytoplasm after DNA damage Transportin-1 and Transportin-2: protein nuclear import and beyond.Functions of FUS/TLS from DNA repair to stress response: implications for ALS.The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS.Activity-dependent FUS dysregulation disrupts synaptic homeostasis Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.Psychiatric genetics, neurogenetics, and neurodegeneration Compromised paraspeckle formation as a pathogenic factor in FUSopathies.A fruitful endeavor: modeling ALS in the fruit fly Subcellular localization and RNAs determine FUS architecture in different cellular compartments.Chemical biology of protein arginine modifications in epigenetic regulation Arginine methylation of DRBD18 differentially impacts its opposing effects on the trypanosome transcriptome.ALS mutant FUS proteins are recruited into stress granules in induced pluripotent stem cell-derived motoneurons Genotype-phenotype relationship in hereditary amyotrophic lateral sclerosis.Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS.Dysregulated expression of death, stress and mitochondrion related genes in the sciatic nerve of presymptomatic SOD1(G93A) mouse model of Amyotrophic Lateral Sclerosis.TDP-43 and FUS en route from the nucleus to the cytoplasm.Directly converted patient-specific induced neurons mirror the neuropathology of FUS with disrupted nuclear localization in amyotrophic lateral sclerosis.Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS.Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics.ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1 Sequestration of PRMT1 and Nd1-L mRNA into ALS-linked FUS mutant R521C-positive aggregates contributes to neurite degeneration upon oxidative stress.Loss of ZNF32 augments the regeneration of nervous lateral line system through negative regulation of SOX2 transcription Stress granules in neurodegeneration--lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma.Posttranslational modifications of the retinoblastoma tumor suppressor protein as determinants of function.Structural disorder and the loss of RNA homeostasis in aging and neurodegenerative disease.

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Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.

http://www.wikidata.org/entity/Q36408540

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Arginine methylation next to t ...... ing and nuclear import of FUS.

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Arginine methylation next to t ...... ing and nuclear import of FUS.

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type

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Arginine methylation next to t ...... ing and nuclear import of FUS.

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Arginine methylation next to t ...... ing and nuclear import of FUS.

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Arginine methylation next to t ...... ing and nuclear import of FUS.

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Arginine methylation next to t ...... ing and nuclear import of FUS.

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The EMBO Journal

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Arginine methylation next to t ...... ing and nuclear import of FUS.

@en

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Chiara F Valori

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Claudia Abou-Ajram

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Dorothee Dormann

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Elisabeth Kremmer

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Eva Bentmann

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

Ian R A Mackenzie

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Olaf Ansorge

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Sabina Tahirovic

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P2860

RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers

PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function

PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

Rules for nuclear localization sequence recognition by karyopherin beta 2

Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease

ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import

A new subtype of frontotemporal lobar degeneration with FUS pathology

Assembly PCR oligo maker: a tool for designing oligodeoxynucleotides for constructing long DNA molecules for RNA production.

Structure-based design of a pathway-specific nuclear import inhibitor

Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)

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4258-4275

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10.1038/EMBOJ.2012.261

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22

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31

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Christian Haass

Manuela Neumann

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2012-09-11T00:00:00Z

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230832668

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22968170

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3501225

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