Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis

scientific article published on 17 June 2016

Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis is …
instance of (P31):
review articleQ7318358
scholarly articleQ13442814

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P356DOI10.1007/5584_2016_32
P698PubMed publication ID27311318

P50authorYoshiaki FurukawaQ57339180
Eiichi TokudaQ84352374
P2860cites workAtaxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALSQ24297462
Rules for nuclear localization sequence recognition by karyopherin beta 2Q24600321
Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosisQ24605104
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALSQ24629495
ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear importQ24630100
A new subtype of frontotemporal lobar degeneration with FUS pathologyQ24647697
Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)Q27670694
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosisQ28131672
Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisQ28131805
Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formationQ28138179
Identification of an RNA binding specificity for the potential splicing factor TLSQ28138875
Human POMp75 is identified as the pro-oncoprotein TLS/FUS: both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferationQ28141846
Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosisQ28236796
Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6Q28236805
RNA granules: post-transcriptional and epigenetic modulators of gene expressionQ28245899
TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosisQ28270779
TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementiaQ28294001
Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosisQ28730723
Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogelsQ29614781
Mutations of optineurin in amyotrophic lateral sclerosisQ29614836
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosisQ29615597
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosisQ29616311
RNA seeds higher-order assembly of FUS proteinQ30457170
Biochemical Properties and Biological Functions of FET ProteinsQ30459373
FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stressQ30577079
Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domainsQ30577537
The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress responseQ33351073
Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLSQ33889532
FUS immunogold labeling TEM analysis of the neuronal cytoplasmic inclusions of neuronal intermediate filament inclusion disease: a frontotemporal lobar degeneration with FUS proteinopathyQ33908722
Glutamine repeats and neurodegenerationQ33938576
The TET family of proteins: functions and roles in diseaseQ33999337
Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an updateQ34020227
FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutationsQ34209561
Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granulesQ34308339
A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosisQ34342425
Male sterility and enhanced radiation sensitivity in TLS(-/-) miceQ34662602
Tyrosine Phosphorylation in the C-Terminal Nuclear Localization and Retention Signal (C-NLS) of the EWS ProteinQ35013235
A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathiesQ35206942
A yeast functional screen predicts new candidate ALS disease genesQ35641365
Emerging principles of conformation-based prion inheritanceQ35799989
Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutationQ35869162
Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS.Q35928701
ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule FunctionQ36320469
Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.Q36408540
The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site.Q36501107
TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysisQ36536399
ALS-associated mutant FUS induces selective motor neuron degeneration through toxic gain of functionQ36548825
Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAsQ36650975
Sarcomas: genetics, signalling, and cellular origins. Part 1: The fellowship of TET.Q36906766
Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS.Q37087752
TDP-43 A315T mutation in familial motor neuron diseaseQ37354490
RNA-binding proteins with prion-like domains in ALS and FTLD-U.Q37918720
The changing scene of amyotrophic lateral sclerosisQ38086771
Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosisQ39054098
Ataxin-2 interacts with FUS and intermediate-length polyglutamine expansions enhance FUS-related pathology in amyotrophic lateral sclerosisQ39240882
The seeds of neurodegeneration: prion-like spreading in ALSQ39247056
Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies.Q39349822
Identification and characterization of FUS/TLS as a new target of ATM.Q39962311
RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cellsQ40028993
Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid.Q41341998
Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons.Q41469956
Widespread binding of FUS along nascent RNA regulates alternative splicing in the brainQ41955381
Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptionsQ42246467
Expression and subcellular localization of Ewing sarcoma (EWS) protein is affected by the methylation processQ44547089
Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivoQ45294913
The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseasesQ45295489
The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology.Q46409672
Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutationsQ46624207
Transportin 1 accumulates in FUS inclusions in adult-onset ALS without FUS mutationQ48187879
FUS-immunoreactive intranuclear inclusions in neurodegenerative disease.Q48433435
Identification of a tripartite import signal in the Ewing Sarcoma protein (EWS)Q57931910
P407language of work or nameEnglishQ1860
P921main subjectamyotrophic lateral sclerosisQ206901
P304page(s)1-12
P577publication date2016-06-17
P1433published inAdvances in Experimental Medicine and BiologyQ4686385
P1476titleAggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis
P478volume925

Reverse relations

Q47693846The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degenerationcites workP2860