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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
The identification of mutations in the TARDBP and more recently the identification of mutations in the FUS gene as the cause of amyotrophic lateral sclerosis (ALS) is providing the field with new insight about the mechanisms involved in this severe neurodegenerative disease.
|
19741216 |
2009 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Landmark discoveries of mutations in the transactive response DNA-binding protein (TDP-43) and fused in sarcoma/translocated in liposarcoma (FUS/TLS) as causative of ALS and FTLD, combined with the abnormal aggregation of these proteins, have initiated a shifting paradigm for the underlying pathogenesis of multiple neurodegenerative diseases.
|
20400460 |
2010 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
TDP-43 (transactive response binding protein of 43 kDa) and FUS (fused in sarcoma) comprise the neuropathological protein aggregates of distinct subtypes of the neurodegenerative diseases frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
|
21777389 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Thus, TARDBP and FUS/TLS mutations define a novel class of neurodegenerative diseases called TDP-43- and FUS-proteinopathies, in which both misfolded proteins are novel targets for the development of therapeutics in this spectrum of diseases.
|
20655970 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Therefore, yeast cells expressing human FUS protein recapitulate key features of FUS-positive neurodegenerative diseases.
|
21327870 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
FUS protein aggregation is a major pathological hallmark of FUS proteinopathy, a group of neurodegenerative diseases characterized by FUS-immunoreactive inclusion bodies.
|
21748598 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
It also reveals a genetically defined neurodegenerative disease with both FUS and TDP-43 related pathology.
|
20721566 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
TDP-43 or FUS/TLS misaccumulation seems central not just to ALS (where it is found in almost all instances of disease), but more broadly in neurodegenerative disease, including frontal temporal lobular dementia (FTLD-U) and many examples of Alzheimer's or Huntington's disease.
|
21813273 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
This report highlights the importance of screening ALS patients, both familial and sporadic, for FUS mutations and also suggests that de novo mutations is a relevant mechanism underlying sporadic neurodegenerative disease.
|
20598774 |
2011 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
We next explore an emerging class of "RNA binding proteinopathies" where redistribution and aggregation of the RNA binding proteins TDP-43 or FUS contribute to a potentially broad range of neurodegenerative disorders.
|
22079416 |
2012 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Intracellular accumulations of wild type TDP-43 and FUS are observed in a growing number of late-onset diseases suggesting that TDP-43 and FUS proteinopathies may contribute to multiple neurodegenerative diseases.
|
22363618 |
2012 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
The DNA/RNA-binding proteins TDP-43 and FUS are found in protein aggregates in a growing number of neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and related dementia, but little is known about the neurotoxic mechanisms.
|
22848727 |
2012 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
This minireview gives an overview of the general biology of SGs and highlights the recently identified connection of SGs with TDP-43, FUS and other proteins involved in neurodegenerative diseases.
|
23587065 |
2013 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Mutations in the gene encoding Fused in Sarcoma (FUS) cause amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disorder.
|
23474818 |
2013 |
|
Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Dysfunction of two structurally and functionally related proteins, FUS and TAR DNA-binding protein of 43 kDa (TDP-43), implicated in crucial steps of cellular RNA metabolism can cause amyotrophic lateral sclerosis (ALS) and certain other neurodegenerative diseases.
|
23867462 |
2013 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
The nuclear protein fused in sarcoma (FUS) is found in cytoplasmic inclusions in a subset of patients with the neurodegenerative disorder frontotemporal lobar degeneration (FTLD-FUS).
|
23635657 |
2013 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Our findings have important implications for understanding the impact of FUS in neurodegenerative diseases and suggest that perturbations of FUS can impact the neuronal transcriptome via perturbations of RBP transcripts.
|
23389473 |
2013 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Our findings suggest that an impaired DDR and DNA repair may contribute to the pathogenesis of neurodegenerative diseases linked to FUS mutations.
|
24036913 |
2013 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Further understanding of the role of FUS in neurodegenerative diseases might lead to improvements in the treatment and prevention of these disorders.
|
24840975 |
2014 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
The RNA-binding protein fused-in-sarcoma (FUS) has been associated with amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), two neurodegenerative disorders that share similar clinical and pathological features.
|
25324524 |
2014 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Fused in sarcoma (FUS) is an RNA-binding protein involved in pathogenesis of several neurodegenerative diseases.
|
24842888 |
2014 |
|
Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Mutations in the RNA-binding protein FUS have been shown to cause the neurodegenerative disease amyotrophic lateral sclerosis (ALS).
|
25009283 |
2014 |
|
Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Mutations in fused in sarcoma (FUS), a DNA/RNA binding protein, have been associated with familial amyotrophic lateral sclerosis (fALS), which is a fatal neurodegenerative disease that causes progressive muscular weakness and has overlapping clinical and pathologic characteristics with frontotemporal lobar degeneration.
|
25216585 |
2014 |
|
Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
With the recent discoveries revealing the role of FUS in neurodegenerative diseases, namely amyotrophic lateral sclerosis and frontotemporal lobar degeneration, there has been a renewed interest in elucidating the normal functions of FUS.
|
25289647 |
2014 |
|
Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
In this analysis, we applied computational approach to filter the most deleterious and neurodegenerative disease of ALS6-associated mutation on FUS protein.
|
24738488 |
2015 |