Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M113.492017
Title: Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice
Authors: Shelkovnikova, T.A
Peters, O.M
Deykin, A.V
Connor-Robson, N
Robinson, H
Ustyugov, A.A
Bachurin, S.O
Ermolkevich, T.G
Goldman, I.L
Sadchikova, E.R
Kovrazhkina, E.A
Skvortsova, V.I
Ling, S.-C 
Da Cruz, S
Parone, P.A
Buchman, V.L
Ninkina, N.N
Keywords: Amyotrophic lateral sclerosis
Fused in sarcomata
Nuclear localization signal
Protein aggregation
RNA-binding motif
Transgenic mice
Mammals
Neurodegenerative diseases
Proteins
fused in sarcoma protein
amyotrophic lateral sclerosis
animal cell
animal experiment
animal model
animal tissue
article
clinical feature
controlled study
disease course
disease severity
lifespan
mortality
motoneuron
motor dysfunction
mouse
nerve cell lesion
nerve fiber
nervous system inflammation
nonhuman
nuclear localization signal
pathophysiology
phenotype
priority journal
protein defect
protein expression
protein motif
RNA binding
transgenic mouse
Amyotrophic Lateral Sclerosis (Lou Gehrig's Disease)
Animal Models
Motor Neuron Disease
Neurodegeneration
Protein Aggregation
Proteinopathy
RNA Metabolism
RNA-binding Proteins
TDP-43
Transgenic Mouse
Amino Acid Motifs
Amino Acid Sequence
Amyotrophic Lateral Sclerosis
Animals
Axons
Cytoplasm
Humans
Mice
Mice, Transgenic
Motor Neurons
Nuclear Localization Signals
Phenotype
RNA
RNA-Binding Protein FUS
Sequence Deletion
Issue Date: 2013
Citation: Shelkovnikova, T.A, Peters, O.M, Deykin, A.V, Connor-Robson, N, Robinson, H, Ustyugov, A.A, Bachurin, S.O, Ermolkevich, T.G, Goldman, I.L, Sadchikova, E.R, Kovrazhkina, E.A, Skvortsova, V.I, Ling, S.-C, Da Cruz, S, Parone, P.A, Buchman, V.L, Ninkina, N.N (2013). Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice. Journal of Biological Chemistry 288 (35) : 25266-25274. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M113.492017
Rights: Attribution 4.0 International
Abstract: Background: FUS inclusions are hallmarks of certain neurodegenerative diseases. Results: Expression of a highly aggregate prone FUS variant in transgenic mice causes proteinopathy and severe motor phenotype. Conclusion: Aggregation of FUS is sufficient to recapitulate motor pathology typical for amyotrophic lateral sclerosis. Significance: Understanding the role of protein aggregation in the development of human neurodegenerative diseases is crucial for designing efficient therapeutic approaches. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
Source Title: Journal of Biological Chemistry
URI: https://scholarbank.nus.edu.sg/handle/10635/180783
ISSN: 0021-9258
DOI: 10.1074/jbc.M113.492017
Rights: Attribution 4.0 International
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1074_jbc_M113_492017.pdf3.27 MBAdobe PDF

OPEN

NoneView/Download

Google ScholarTM

Check

Altmetric


This item is licensed under a Creative Commons License Creative Commons