Pages that link to "Q30458567"

The following pages link to FUS is sequestered in nuclear aggregates in ALS patient fibroblasts (Q30458567):

Displaying 26 items.

• Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis (Q26749169) (← links)
• FUS-mediated regulation of alternative RNA processing in neurons: insights from global transcriptome analysis (Q26773038) (← links)
• Biochemical Properties and Biological Functions of FET Proteins (Q30459373) (← links)
• Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions (Q30661910) (← links)
• Self-assembled FUS binds active chromatin and regulates gene transcription. (Q34752975) (← links)
• U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish (Q35237055) (← links)
• Subcellular localization and RNAs determine FUS architecture in different cellular compartments. (Q35678009) (← links)
• ALS mutant FUS proteins are recruited into stress granules in induced pluripotent stem cell-derived motoneurons (Q35802889) (← links)
• FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP (Q35865531) (← links)
• Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins (Q36172705) (← links)
• Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II (Q36172715) (← links)
• TDP-43 and FUS en route from the nucleus to the cytoplasm (Q36336278) (← links)
• Directly converted patient-specific induced neurons mirror the neuropathology of FUS with disrupted nuclear localization in amyotrophic lateral sclerosis (Q36489948) (← links)
• Regulatory mechanisms underlying sepsis progression in patients with tumor necrosis factor-α genetic variations (Q37001758) (← links)
• Fibroblasts of Machado Joseph Disease patients reveal autophagy impairment. (Q37027391) (← links)
• Two familial ALS proteins function in prevention/repair of transcription-associated DNA damage (Q37474001) (← links)
• Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins (Q38789192) (← links)
• Treatment with a Global Methyltransferase Inhibitor Induces the Intranuclear Aggregation of ALS-Linked FUS Mutant In Vitro (Q38816949) (← links)
• Neuron-to-Neuron Transfer of FUS in Drosophila Primary Neuronal Culture Is Enhanced by ALS-Associated Mutations. (Q38827430) (← links)
• Position-specific binding of FUS to nascent RNA regulates mRNA length (Q38872764) (← links)
• The fused in sarcoma protein forms cytoplasmic aggregates in motor neurons derived from integration-free induced pluripotent stem cells generated from a patient with familial amyotrophic lateral sclerosis carrying the FUS-P525L mutation (Q38882417) (← links)
• The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS. (Q54967377) (← links)
• The hnRNP raly regulates PRMT1 expression and interacts with the ALS-linked protein FUS: implication for reciprocal cellular localization (Q57793297) (← links)
• Control of CNS functions by RNA-binding proteins in neurological diseases (Q58566969) (← links)
• The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization (Q58806144) (← links)
• FUS (fused in sarcoma) is a component of the cellular response to topoisomerase I-induced DNA breakage and transcriptional stress (Q64101978) (← links)