Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS - sprookjes - yvandenbroek - TriplyDB

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS

http://www.wikidata.org/entity/Q24629495

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Symptomatic treatments for amyotrophic lateral sclerosis/motor neuron disease C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking Altered ribostasis: RNA-protein granules in degenerative disorders Motor neuron involvement in multisystem proteinopathy: implications for ALS The hnRNP family: insights into their role in health and disease Inside out: the role of nucleocytoplasmic transport in ALS and FTLD Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis Extracellular Vesicles and a Novel Form of Communication in the Brain Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease Toward precision medicine in amyotrophic lateral sclerosis Immunoprecipitation and mass spectrometry defines an extensive RBM45 protein-protein interaction network Genotype-phenotype correlations of amyotrophic lateral sclerosis Matrin3: connecting gene expression with the nuclear matrix Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?Phenotypic Heterogeneity of Monogenic Frontotemporal Dementia Clinical and genetic basis of familial amyotrophic lateral sclerosis Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders Insights into muscle degeneration from heritable inclusion body myopathies The multiple molecular facets of fragile X-associated tremor/ataxia syndrome Yeast prions and human prion-like proteins: sequence features and prediction methods Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis Role of stress granules and RNA-binding proteins in neurodegeneration: a mini-review State of play in amyotrophic lateral sclerosis genetics Neuronal RNA-binding proteins in health and disease Sumoylation of critical proteins in amyotrophic lateral sclerosis: emerging pathways of pathogenesis The function of RNA-binding proteins at the synapse: implications for neurodegeneration Evolutionary conservation and expression of human RNA-binding proteins and their role in human genetic disease Remote control of gene function by local translation Prion-like polymerization as a signaling mechanism Self-propagation of pathogenic protein aggregates in neurodegenerative diseases RNA-binding proteins in neurodegeneration: Seq and you shall receive What we have learned from the next-generation sequencing: Contributions to the genetic diagnoses and understanding of pathomechanisms of neurodegenerative diseases Neurodegenerative diseases: expanding the prion concept RNA-processing protein TDP-43 regulates FOXO-dependent protein quality control in stress response ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.The neurogenetics of alternative splicing Phase separation in biology; functional organization of a higher order Defective control of pre-messenger RNA splicing in human disease Mutations in the Human AAA+ Chaperone p97 and Related Diseases TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets.

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Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS

http://www.wikidata.org/entity/Q24629495

description

2013 nî lūn-bûn

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2013 թուականի Մարտին հրատարակուած գիտական յօդուած

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2013 թվականի մարտին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

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Mutations in prion-like domain ...... tisystem proteinopathy and ALS

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Mutations in prion-like domain ...... tisystem proteinopathy and ALS

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type

label

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

@ast

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

@en

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

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prefLabel

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

@ast

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

@en

Mutations in prion-like domain ...... tisystem proteinopathy and ALS

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Mutations in prion-like domain ...... tisystem proteinopathy and ALS

@en

P2093

Aaron D Gitler

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

Alan Pestronk

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

Aleksandra M Wojtas

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Alice Flynn Ford

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

Amandine Molliex

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Anderson P Kanagaraj

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Athina-Soragia Gkazi

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Bradley N Smith

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

Brian Freibaum

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

Bryan J Traynor

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P2860

Exome sequencing reveals VCP mutations as a cause of familial ALS

Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

A systematic survey identifies prions and illuminates sequence features of prionogenic proteins

Transformation of intact yeast cells treated with alkali cations

Getting RNA and protein in phase

TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing

Search and clustering orders of magnitude faster than BLAST

Multiple alignment of DNA sequences with MAFFT

Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

P2888

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467-73

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scholarly article

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158411

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10.1038/NATURE11922

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P433

7442

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P478

495

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Michael Benatar

Janbernd Kirschner

Rosa Rademakers

John Q. Trojanowski

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2013-03-28T00:00:00Z

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235770144

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1037021180

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23455423

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amyotrophic lateral sclerosis

Prion protein family

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3756911

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