gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Fused in sarcoma

This gene encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The hnRNP complex is involved in pre-mRNA splicing and the export of fully processed mRNA to the cytoplasm. This protein belongs to the FET family of RNA-binding proteins which have been implicated in cellular processes that include regulation of gene expression, maintenance of genomic integrity and mRNA/microRNA processing. Alternative splicing results in multiple transcript variants. Defects in this gene result in amyotrophic lateral sclerosis type 6. [provided by RefSeq, Sep 2009] (from NCBI)
Top mentioned proteins: Als, TDP-43, CAN, POLYMERASE, Ubiquitin
Papers on FUS
Cytogenetically confirmed low-grade fibromyxoid sarcoma arising from the tibia.
Zhang et al., Philadelphia, United States. In Hum Pathol, Feb 2016
This diagnosis often hinges on the presence of the hallmark cytogenetic aberration, a balanced 7;16 translocation resulting in a FUS-CREB3L2 fusion gene.
Utility of whole exome sequencing in evaluation of juvenile motor neuron disease.
Lotze et al., Houston, United States. In Muscle Nerve, Feb 2016
Results This study identified a heterozygous de novo variant of unknown clinical significance (VUS) in the fused in sarcoma (FUS) gene [c.1554_1557del].
New in vitro models to study amyotrophic lateral sclerosis.
Ferraiuolo et al., Sheffield, United Kingdom. In Brain Pathol, Feb 2016
The identification of mutations in transactive response DNA-binding protein gene (TARDBP), fused in sarcoma (FUS) and, more recently, a GGGGCC-hexanucleotide repeat expansion in chromosome 9 open reading frame 72 (C9ORF72) and their link with familial ALS have provided new avenues of investigation and hypotheses on the pathophysiology of this devastating disease.
Orthogonal matrix factorization enables integrative analysis of multiple RNA binding proteins.
Curk et al., Ljubljana, Slovenia. In Bioinformatics, Feb 2016
We have integrated the largest data compendium to date, which includes 31 CLIP experiments on 19 RBPs involved in splicing (such as hnRNPs, U2AF2, ELAVL1, TDP-43, and FUS) and processing of 3'UTR (Ago, IGF2BP).
Tumor lysis syndrome in the era of novel and targeted agents in patients with hematologic malignancies: a systematic review.
McBride et al., Memphis, United States. In Ann Hematol, Feb 2016
However, their propensity to cause tumor lysis syndrome (TLS) has not been systematically examined.
Drug and gene delivery across the blood-brain barrier with focused ultrasound.
Price et al., Charlottesville, United States. In J Control Release, Jan 2016
It is now well-established that focused ultrasound (FUS) in conjunction with contrast agent microbubbles may be used to non-invasively and temporarily disrupt the BBB, allowing localized delivery of systemically administered therapeutic agents as large as 100nm in size to the CNS.
Noninvasive, Targeted, and Non-Viral Ultrasound-Mediated GDNF-Plasmid Delivery for Treatment of Parkinson's Disease.
Yeh et al., Taiwan. In Sci Rep, Dec 2015
Cationic microbubbles as gene carriers were developed to allow the stable formation of a bubble-GDNF gene complex, and transcranial focused ultrasound (FUS) exposure concurrently interacting with the bubble-gene complex allowed transient gene permeation and induced local GDNF expression.
Neural immune modulation and immunotherapy assisted by focused ultrasound induced blood-brain barrier opening.
Liu et al., Taiwan. In Hum Vaccin Immunother, Dec 2015
Exposure of low-energy focused ultrasound (FUS) with the presence of microbubbles has been found to provide a temporary and targeted opening of the BBB without inflicting brain damage or inflammation, and is thus an attractive means of delivering CNS therapeutic agents and raising the potential for targeted CNS immunotherapy.
Long noncoding RNAs in TDP-43 and FUS/TLS-related frontotemporal lobar degeneration (FTLD).
Halliday et al., Sydney, Australia. In Neurobiol Dis, Oct 2015
Two of the major pathologies, FTLD-TDP and FTLD-FUS, are characterized by the abnormal accumulation in cytoplasmic inclusions of RNA-binding proteins (RBPs) - TDP-43 and FUS/TLS, respectively.
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.
Alberti et al., Dresden, Germany. In Cell, Sep 2015
Here, we study FUS, a prion-like protein containing intrinsically disordered domains associated with the neurodegenerative disease ALS.
Biochemical Properties and Biological Functions of FET Proteins.
Parker et al., Boulder, United States. In Annu Rev Biochem, 2014
Members of the FET protein family, consisting of FUS, EWSR1, and TAF15, bind to RNA and contribute to the control of transcription, RNA processing, and the cytoplasmic fates of messenger RNAs in metazoa.
Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?
Vande Velde et al., Montréal, Canada. In Front Cell Neurosci, 2014
Of note, both ALS and FTD are characterized by pathological inclusions, where some well-known SG markers localize with the ALS related proteins TDP-43 and FUS.
The structural basis of transfer RNA mimicry and conformational plasticity by a viral RNA.
Kieft et al., Aurora, United States. In Nature, 2014
To address this gap it is useful to study examples from single-stranded positive-sense RNA viruses, a prototype being the tRNA-like structure (TLS) found at the 3' end of the turnip yellow mosaic virus (TYMV).
Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events.
Shorter et al., Philadelphia, United States. In Cell, 2014
Here, we reprogram Hsp104 to rescue TDP-43, FUS, and α-synuclein proteotoxicity by mutating single residues in helix 1, 2, or 3 of the middle domain or the small domain of nucleotide-binding domain 1.
Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains.
McKnight et al., Dallas, United States. In Cell, 2013
The low-complexity (LC) domains of the products of the fused in sarcoma (FUS), Ewings sarcoma (EWS), and TAF15 genes are translocated onto a variety of different DNA-binding domains and thereby assist in driving the formation of cancerous cells.
FUS/TLS-immunoreactive neuronal and glial cell inclusions increase with disease duration in familial amyotrophic lateral sclerosis with an R521C FUS/TLS mutation.
Aoki et al., Sendai, Japan. In J Neuropathol Exp Neurol, 2012
This study emonstrated a widespread occurrence of FUS/TLS-ir neuronal and glial structures in R521C-FUS/TLS-mutated familial amyotrophic lateral sclerosis.
Exome sequencing identifies FUS mutations as a cause of essential tremor.
Rouleau et al., Montréal, Canada. In Am J Hum Genet, 2012
We identified FUS c.868C>T as the pathogenic variant that causes essential tremor.
Loss of fused in sarcoma (FUS) promotes pathological Tau splicing.
Edbauer et al., München, Germany. In Embo Rep, 2012
Tau mRNA is identified as a physiological splicing target of FUS.
Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS).
Chook et al., Dallas, United States. In Proc Natl Acad Sci U S A, 2012
Thermodynamic analyses of ALS mutations in the FUS proline/tyrosine-nuclear localization signal show that the weakening of FUS-Kapbeta2 binding affinity, the degree of cytoplasmic mislocalization, and ALS disease severity are correlated.
[Amyotrophic lateral sclerosis (ALS) and fused in sarcoma/translocated in liposarcoma (FUS/TLS)].
Aoki et al., In Nihon Rinsho, 2011
Analysis of post-translational modification of FUS/TLS and that at micro RNA and mRNA levels in autopsy cases contribute greatly to comprehensive understandng of ALS with FUS/TLS mutations.
share on facebooktweetadd +1mail to friends