ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1
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Title
ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1
Authors
Keywords
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Journal
HUMAN MOLECULAR GENETICS
Volume 24, Issue 9, Pages 2565-2577
Publisher
Oxford University Press (OUP)
Online
2015-01-24
DOI
10.1093/hmg/ddv020
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Note: Only part of the references are listed.- UBQLN2mutation causing heterogeneous X-linked dominant neurodegeneration
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- Ubiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of TDP-43 and modulates TDP-43 levels in H4 cells: Characterization of inhibition by nucleic acids and 4-aminoquinolines
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- Pathogenic mutation of UBQLN2 impairs its interaction with UBXD8 and disrupts endoplasmic reticulum-associated protein degradation
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- Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
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- The changing scene of amyotrophic lateral sclerosis
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- Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
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- Ubiquilins in the crosstalk among proteolytic pathways
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- Understanding the role of TDP-43 and FUS/TLS in ALS and beyond
- (2011) Sandrine Da Cruz et al. CURRENT OPINION IN NEUROBIOLOGY
- Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
- (2011) Han-Xiang Deng et al. NATURE
- Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis
- (2011) Laura Ferraiuolo et al. Nature Reviews Neurology
- Ubiquilin at a crossroads in protein degradation pathways
- (2010) Cara Rothenberg et al. Autophagy
- TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
- (2010) C. Lagier-Tourenne et al. HUMAN MOLECULAR GENETICS
- Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
- (2009) G. S. Pesiridis et al. HUMAN MOLECULAR GENETICS
- Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD
- (2009) Precious J. Lim et al. JOURNAL OF CELL BIOLOGY
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