Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.
about
Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1.Oxr1 improves pathogenic cellular features of ALS-associated FUS and TDP-43 mutationsProtein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy.FUS is sequestered in nuclear aggregates in ALS patient fibroblasts.A fruitful endeavor: modeling ALS in the fruit flySubcellular localization and RNAs determine FUS architecture in different cellular compartments.Sequestration of PRMT1 and Nd1-L mRNA into ALS-linked FUS mutant R521C-positive aggregates contributes to neurite degeneration upon oxidative stress.The role of FUS gene variants in neurodegenerative diseases.Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD.Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins.Treatment with a Global Methyltransferase Inhibitor Induces the Intranuclear Aggregation of ALS-Linked FUS Mutant In Vitro.Stress granules at the intersection of autophagy and ALS.Nuclear trafficking in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.TDP-43/FUS in motor neuron disease: Complexity and challenges.Post-translational Modifications and Protein Quality Control in Motor Neuron and Polyglutamine Diseases.ALS-FUS pathology revisited: singleton FUS mutations and an unusual case with both a FUS and TARDBP mutationRegulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders.Neurodegenerative Disease Proteinopathies Are Connected to Distinct Histone Post-translational Modification Landscapes.FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions.The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization
P2860
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P2860
Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.
description
2013 nî lūn-bûn
@nan
2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@ast
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@en
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@nl
type
label
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@ast
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@en
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@nl
prefLabel
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@ast
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@en
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@nl
P2093
P2860
P1433
P1476
Protein arginine methyltransfe ...... toxicity in vitro and in vivo.
@en
P2093
Astha Maltare
Carmelo Milioto
Chiara Scaramuzzino
Frank O Fackelmayer
John Monaghan
Maria Pennuto
Nicholas A Lanson
Tanya Aggarwal
Udai Bhan Pandey
P2860
P304
P356
10.1371/JOURNAL.PONE.0061576
P407
P577
2013-04-19T00:00:00Z