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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 |
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