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FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Additionally we are shipping FUS Antibodies (45) and FUS Kits (3) and many more products for this protein.
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Human FUS Protein expressed in HEK-293 Cells - ABIN2721461
Groen, Fumoto, Blokhuis, Engelen-Lee, Zhou, van den Heuvel, Koppers, van Diggelen, van Heest, Demmers, Kirby, Shaw, Aronica, Spliet, Veldink, van den Berg, Pasterkamp: ALS-associated mutations in FUS disrupt the axonal distribution and function of SMN. in Human molecular genetics 2013
Show all 3 Pubmed References
Results suggest that RBM45 (show RBM45 Proteins) serves as a negative regulator to prevent FUS-mediated excessive recruitment of HDAC1 (show HDAC1 Proteins) to the sites of DNA damage.
Authors found that FUS, EWS (show EWSR1 Proteins) and TAF15 (show TAF15 Proteins) expression is differentially regulated during brain development, both in time and in space. In particular, this study identifies a fine-tuned regulation of FUS and EWS (show EWSR1 Proteins) during neuronal differentiation.
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 Proteins). 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 Proteins)-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 Proteins)/FUS-ATF1 (show AFT1 Proteins) gene fusions to include a subgroup of conventional epithelioid malignant mesothelioma.
Aggregation of FET proteins FUS, EWSR1 (show EWSR1 Proteins), and TAF15 (show TAF15 Proteins) 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), a kinase already strongly associated with ALS (show IGFALS Proteins)/FTD (show FTL Proteins).
Study characterizes a heterozygous knock-in mouse model of ALS and demonstrates that mutations in FUS result in a toxic gain of function leading to motor neuron disease through cell autonomous and non-cell autonomous mechanisms; shows that mutant FUS triggers toxic events in both motor neurons and neighboring cells to elicit motor neuron disease.
FUS-induced reductions to ER-mitochondria associations and are linked to activation of glycogen synthase kinase-3beta (GSK-3beta), a kinase already strongly associated with ALS/FTD (show FTL Proteins).
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 Proteins) 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 Proteins) 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.
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