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FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Additionally we are shipping FUS Kits (3) and FUS Proteins (2) and many more products for this protein.
Showing 10 out of 45 products:
Human Monoclonal FUS Primary Antibody for IF, WB - ABIN968508
Hallier, Lerga, Barnache, Tavitian, Moreau-Gachelin: The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS. in The Journal of biological chemistry 1998
Show all 5 Pubmed References
Human Monoclonal FUS Primary Antibody for IF, WB - ABIN968509
Morohoshi, Ootsuka, Arai, Ichikawa, Mitani, Munakata, Ohki: Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes. in Gene 1998
Show all 5 Pubmed References
The review describes the main physiological functions of FUS and considers evidence for each of the theories of amyotrophic lateral sclerosis pathogenesis.
Authors used solid-state nuclear magnetic resonance methods to characterize the molecular structure of self-assembling fibrils formed by the LC domain of the fused in sarcoma (FUS) RNA-binding protein (show PTBP1 Antibodies). From the 214-residue LC domain of FUS (FUS-LC), a segment of only 57 residues forms the fibril core, while other segments remain dynamically disordered.
Nuclear magnetic resonance spectroscopy demonstrates the intrinsically disordered structure of FUS's nearly uncharged, aggregation-prone, yeast prion (show PRNP Antibodies)-like, low sequence-complexity domain is preserved after phosphorylation.
Long noncoding RNA SchLAH functions through interaction with fused in sarcoma protein (FUS).
Results expand the spectrum of tumor types harboring EWSR1 (show EWSR1 Antibodies)/FUS-ATF1 (show AFT1 Antibodies) gene fusions to include a subgroup of conventional epithelioid malignant mesothelioma.
Aggregation of FET proteins FUS, EWSR1 (show EWSR1 Antibodies), and TAF15 (show TAF15 Antibodies) mediate a pathological change in amyotrophic lateral sclerosis. (Review)
Focus on the recent advances on approaches to uncover the mechanisms of wild type and mutant FUS proteins during development and in neurodegeneration (review).
FUS-induced reductions to ER-mitochondria associations and are linked to activation of glycogen synthase kinase-3beta (GSK-3beta (show GSK3b Antibodies)), a kinase already strongly associated with ALS (show IGFALS Antibodies)/FTD (show FTL Antibodies).
Motor-neuron disease (MND (show CLN8 Antibodies))-linked RNA-binding proteins (RBPs), TDP-43 (show TARDBP Antibodies), FUS, and hnRNPA2B1 (show HNRNPA2B1 Antibodies), bind to and induce structural alteration of UGGAAexp. These RBPs suppress UGGAAexp-mediated toxicity in Drosophila by functioning as RNA chaperones for proper UGGAAexp folding and regulation of pentapeptide repeat translation.
we analyzed fast axonal transport in larval motor neurons of Drosophila models of TARDBP (TDP-43 (show TARDBP Antibodies)), FUS and C9orf72 (show C9ORF72 Antibodies). We also analyzed the effect of loss-of-function mutants of the Drosophila orthologs of TDP-43 (show TARDBP Antibodies) and FUS, TBPH and caz, respectively. The motor activities of larvae and adults in these models were assessed to correlate potential defects in axonal transport with locomotor deficits
FUS-induced reductions to ER-mitochondria associations and are linked to activation of glycogen synthase kinase-3beta (GSK-3beta (show GSK3b Antibodies)), a kinase already strongly associated with ALS/FTD (show FTL Antibodies).
our findings indicate that cytoplasmic FUS mislocalization not only leads to nuclear loss of function, but also triggers motor neuron death through a toxic gain of function within motor neurons.
The data of this study support the notion that expression of cytoplasmically mislocalized FUS with compromised RNA-binding capacity causes particularly prominent and harmful FUS pathology in the mouse nervous system.
These results highlight the pivotal role of FUS in regulating GluA1 (show GRIA1 Antibodies) mRNA stability, post-synaptic function and fronto-temporal lobar degeneration-like animal behaviors.
these studies establish potentially converging disease mechanisms in amyotrophic lateral sclerosis (ALS) and spinal muscular atrophy, with ALS-causative mutants acquiring properties representing both gain and loss of function.
FUS/TLS depletion causes phenotypes possibly related to neuropsychiatric and neurodegenerative conditions, but distinct from ALS and ET, together with specific alterations in RNA metabolisms.
It is associated with amyotrophic lateral sclerosis and its mutation causes accumulation of fus positive stress granules in neurons.
Study provides evidence for loss of PRMT1 (show PRMT1 Antibodies) function as a consequence of cytoplasmic accumulation of FUS in the pathogenesis of amyotrophic lateral sclerosis, including changes in the histone code regulating gene transcription.
our study provided evidence that a multistep process of FUS aggregation in the cell cytoplasm includes RNA-dependent and RNA-independent mechanisms.
Activation of metabotropic glutamate (show GRIN1 Antibodies) receptors 1/5 in neocortical slices and isolated synaptoneurosomes increases endogenous mouse FUS and FUS(WT) protein levels but decreases the FUS(R521G) protein
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.
75 kDa DNA-pairing protein
, RNA-binding protein FUS
, fus-like protein
, fusion gene in myxoid liposarcoma
, heterogeneous nuclear ribonucleoprotein P2
, oncogene FUS
, oncogene TLS
, translocated in liposarcoma protein
, fusion, derived from t(12;16) malignant liposarcoma
, hnRNP P2
, pigpen protein
, protein pigpen
, translocated in liposarcoma
, fusion (involved in t(12;16) in malignant liposarcoma)
, 16) in malignant liposarcoma)
, 16) malignant liposarcoma
, fusion (involved in t(12
, fusion, derived from t(12