Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
about
Structural basis for the nuclear export activity of Importin13Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseNuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1Crystal structure of human Karyopherin β2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALSIncreasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift ReagentHighly efficient cell-type-specific gene inactivation reveals a key function for the Drosophila FUS homolog cabeza in neuronsThe ALS gene FUS regulates synaptic transmission at the Drosophila neuromuscular junction.Transportin-1 and Transportin-2: protein nuclear import and beyond.Novel somatic single nucleotide variants within the RNA binding protein hnRNP A1 in multiple sclerosis patients.Activity-dependent FUS dysregulation disrupts synaptic homeostasisNuclear export inhibitors avert progression in preclinical models of inflammatory demyelination.Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS.Dysregulated expression of death, stress and mitochondrion related genes in the sciatic nerve of presymptomatic SOD1(G93A) mouse model of Amyotrophic Lateral Sclerosis.Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.Stress granules as crucibles of ALS pathogenesis.Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice.Transportin acts to regulate mitotic assembly events by target binding rather than Ran sequestration.Stress granules in neurodegeneration--lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma.Minor splicing pathway is not minor any more: implications for the pathogenesis of motor neuron diseases.The role of FUS gene variants in neurodegenerative diseases.Factors influencing the nuclear targeting ability of nuclear localization signals.Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis.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.Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis.Clinical and experimental studies of a novel P525R FUS mutation in amyotrophic lateral sclerosis.Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins.Pur-alpha functionally interacts with FUS carrying ALS-associated mutations.Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U.RNA Granules and Diseases: A Case Study of Stress Granules in ALS and FTLDGenetic mutations in RNA-binding proteins and their roles in ALS.Karyopherin-β2 Recognition of a PY-NLS Variant that Lacks the Proline-Tyrosine Motif.Nucleic acid binding proteins affect the subcellular distribution of phosphorothioate antisense oligonucleotides.Karyopherins in cancer.R521C and R521H mutations in FUS result in weak binding with Karyopherinβ2 leading to Amyotrophic lateral sclerosis: a molecular docking and dynamics study.Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1.Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like DomainsThe physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration
P2860
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P2860
Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
description
2012 nî lūn-bûn
@nan
2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@ast
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@en
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@nl
type
label
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@ast
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@en
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@nl
prefLabel
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@ast
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@en
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@nl
P2860
P356
P1476
Structural and energetic basis ...... Fused in Sarcoma protein (FUS)
@en
P2093
Yuh Min Chook
Zi Chao Zhang
P2860
P304
P356
10.1073/PNAS.1207247109
P407
P577
2012-07-24T00:00:00Z