FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. - Test2 - elhamkhani - TriplyDB

FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations.

FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations.

http://www.wikidata.org/entity/Q34209561

about

Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS Inside out: the role of nucleocytoplasmic transport in ALS and FTLD Molecular Pathological Classification of Neurodegenerative Diseases: Turning towards Precision Medicine RNA-Binding Proteins in the Regulation of miRNA Activity: A Focus on Neuronal Functions Phenotypic Heterogeneity of Monogenic Frontotemporal Dementia RNA-Binding Proteins: Splicing Factors and Disease Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders The function of RNA-binding proteins at the synapse: implications for neurodegeneration Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)EWS and FUS bind a subset of transcribed genes encoding proteins enriched in RNA regulatory functions Frontotemporal Dementia.Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion.Wild type human TDP-43 potentiates ALS-linked mutant TDP-43 driven progressive motor and cortical neuron degeneration with pathological features of ALS.A model-based approach to identify binding sites in CLIP-Seq data.Gene expression responses to FUS, EWS, and TAF15 reduction and stress granule sequestration analyses identifies FET-protein non-redundant functions.Protein Quality Control and the Amyotrophic Lateral Sclerosis/Frontotemporal Dementia Continuum FUS is phosphorylated by DNA-PK and accumulates in the cytoplasm after DNA damage dCLIP: a computational approach for comparative CLIP-seq analyses.Transportin-1 and Transportin-2: protein nuclear import and beyond.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Targeted exon capture and sequencing in sporadic amyotrophic lateral sclerosis.Analysis of nuclear export sequence regions of FUS-Related RNA-binding proteins in essential tremor Prevalence of mixed pathologies in the aging brain Aggregation properties of the small nuclear ribonucleoprotein U1-70K in Alzheimer disease.Aberrant RNA homeostasis in amyotrophic lateral sclerosis: potential for new therapeutic targets?Increasing prion propensity by hydrophobic insertion.Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine.Evidence for fungal infection in cerebrospinal fluid and brain tissue from patients with amyotrophic lateral sclerosis.Inactivation of EWS reduces PGC-1α protein stability and mitochondrial homeostasis.Trials of antidiabetic drugs in amyotrophic lateral sclerosis: proceed with caution?A Systematic Analysis of Factors Localized to Damaged Chromatin Reveals PARP-Dependent Recruitment of Transcription Factors A yeast functional screen predicts new candidate ALS disease genes FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors Design and bioinformatics analysis of genome-wide CLIP experiments.Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS.Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects Amyotrophic lateral sclerosis: update and new developments.Nuclear carrier and RNA-binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes.Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.

P2860

Q24605104-6806ACC0-A255-43A1-A188-5924A5E57E37 Q24629495-D4E2F3EA-A31C-4E15-A6A7-CE44B60B82B0 Q26748482-2615286E-4551-4A21-84A7-F538B14CE55C Q26768648-E9F50833-E1BA-4B8E-8179-1A0152232F5F Q26782020-041A6239-40DA-4E43-9979-860312B0F220 Q26782984-E5F182D2-6CF7-4EE1-83EC-07CE420621FF Q26823957-71A608A6-1E32-4806-AF42-A4C821BFCCEE Q26828357-54B6FB7C-B862-4B1D-A6CC-4DBB9D2E87B3 Q26991684-D2A74B6E-8CDA-492F-B366-C6617E200C1A Q27670694-8B01DA4C-D6CE-4D4F-9391-E29F77DE29A5 Q28607398-D27D0F66-70C4-4130-9C84-477E109ED2BF Q30234793-FAADB35A-4194-4923-A038-C17C9CB24ED2 Q30532680-CF803E5C-146A-48E8-AA19-65772B1E0A67 Q30655551-BAD3D87F-BFD0-4E44-92F5-CB03EDA516E0 Q30796706-21D702C6-1AB1-4E4F-8F60-38B5E5122DA5 Q31104690-ACACC605-EC77-47C4-9854-409A95FF9324 Q33653996-8B573DA1-485C-4BDE-B265-C636FF8A0550 Q33707858-2CECA514-2C1F-4B77-B3DA-3C5B62991971 Q33742972-ACBF290E-4319-43D6-8935-8BFB71C6004B Q34040766-3E2D5271-8E9E-4161-9CDC-1A6ECA5C616A Q34263380-74F993E7-1AA1-422A-981B-8C982254827D Q34315110-11D8F41A-E087-4D88-951A-DE137C5CFC61 Q34465916-0F4B8EB3-7B7A-4226-9387-67C1FF8FACDF Q34551519-24A0C51B-4794-40D8-8707-F61F44E433A2 Q34737880-AF4E3D6C-8C38-44C9-9C5A-634D6ACB217B Q35019375-FC984D0D-6D65-4A93-912C-3CFC7BFA65B1 Q35106999-1F3E1BEF-F50A-458E-B4AB-F06995EF556C Q35204586-F7D5129C-7250-4A55-BF20-20E37B47338B Q35451557-01387676-2905-440E-A426-080B408331D6 Q35616315-22CAD5CA-8269-47CF-B390-36A23F16C32C Q35618724-FFCEB2D2-582D-4C26-A631-A890EBF446B1 Q35640249-40ECA569-9112-4E59-9FEF-6D86D893C664 Q35641365-0D6A2A4E-601E-49DD-9A03-D82B50F4C1EF Q35739332-1E6DEC70-70F3-46AA-8998-C7FA6C379284 Q35770670-FE128102-1ECA-4C1D-B464-04C329CBC536 Q35928701-535B6931-6D36-418E-AF22-606CA40006A8 Q36241872-09019BDE-34ED-447D-9056-E6B6681A0B91 Q36278310-A454E0F7-EB8D-47B3-B277-32909E129431 Q36342066-3124DDB5-75F9-4792-B841-4A2D883AE01B Q36408540-74A61B1B-33DE-47BB-8438-F4E6DFC52281

P2860

FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations.

http://www.wikidata.org/entity/Q34209561

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@ast

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@en

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@nl

type

label

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@ast

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@en

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@nl

prefLabel

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@ast

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@en

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@nl

P1433

Q34209561-A09AA384-B79E-4BFF-9751-C180BBB65F6A

P1476

Q34209561-8F16DBD7-6BAA-4DF9-B186-6786B216FBB6

P2093

Q34209561-04110B7C-4C81-4C8D-8C75-A3B3C6CE4395

Q34209561-2D104C6F-806B-415F-9119-3833499B6C40

Q34209561-3665972E-7994-48D7-B4B8-05C4CEF56E27

Q34209561-3768DACE-018C-4240-87DF-579BD3B05A61

Q34209561-429DC197-965B-4BEC-BB38-E30B06D00777

Q34209561-42E64B0C-2541-40E7-94E4-FBCB30429C20

Q34209561-4AA4B2D6-882C-4A54-9935-FAABC7DD5C85

Q34209561-78AB05BE-9F4A-493F-A7CB-3D3155FFAEB4

Q34209561-7EBD06F4-193B-4030-9E43-8967779BEF7F

Q34209561-867C0D0A-24FE-4803-AF7F-8DE366830D7F

P2860

Q34209561-03630796-EEA7-43C0-8F26-06BF6500B639

Q34209561-03E18969-437B-4C21-96C6-679FD52ADECC

Q34209561-189BE948-7583-4A30-B8EF-C60D210D9535

Q34209561-19C5840D-2765-46EC-A243-CA20B3AFEBC0

Q34209561-27B08992-9E87-4F37-A1DB-C3161DBA96F5

Q34209561-2C222682-E4F8-43E6-877E-BCA023F0BA55

Q34209561-2E6AE3B4-8524-4CF7-991B-9BEAB3C42DE9

Q34209561-31D59451-AA9A-4E3A-9630-3DB45BC38270

Q34209561-3D6B9C84-7BFB-459D-ABBA-4FFF722DFCAA

Q34209561-4109A2BD-A87F-461B-B94A-E19526C4E62A

P304

Q34209561-054D9A63-4278-47C7-B4C2-E58E60D6983E

P31

Q34209561-7C82D3FE-9F48-4485-A3F7-D2ACF866642F

P356

Q34209561-1F1F1BF1-8723-4142-A8D6-CD22AB32E695

P407

Q34209561-6F9EAE29-F0EE-4B7D-8D7C-8933819E3DC3

P433

Q34209561-F5985642-079E-427C-A004-005AC7FEED50

P478

Q34209561-8BF12169-A46A-4FE6-A77F-A8414CC3515E

P50

Q34209561-4E9563C1-9251-4BC6-824A-FD8F8FD7AC9C

Q34209561-5425A3AA-B765-4DC8-B2EE-26445717CF79

Q34209561-C0D2967D-4583-4C40-81F1-F6E0B992579A

Q34209561-F6A60E51-0D77-47B2-A802-5C9CF57DFFCD

Q34209561-FE94F976-D389-4705-93AF-407A2A9499CA

P577

Q34209561-76BF088A-9764-4BF0-88C2-52372C928271

P5875

Q34209561-34C99BBA-1C9A-415B-B434-27E97A73B1FA

P698

Q34209561-984A20CF-6A34-4D61-ABCD-96F634DC2C1A

P921

Q34209561-6f06f8da-8364-4906-9199-68b8ea7ba256

Q34209561-E7B460B1-58BF-41A0-8C18-667D34365CB4

P932

Q34209561-96055CCC-5269-4C62-9CD8-730A44D03007

P356

P1433

P1476

FET proteins TAF15 and EWS are ...... sclerosis with FUS mutations.

@en

P2093

Ali Jawaid

http://www.w3.org/2001/XMLSchema#string

Dorothee Dormann

http://www.w3.org/2001/XMLSchema#string

Eva Bentmann

http://www.w3.org/2001/XMLSchema#string

Hans A Kretzschmar

http://www.w3.org/2001/XMLSchema#string

Hirofumi Kusaka

http://www.w3.org/2001/XMLSchema#string

Ian R A Mackenzie

http://www.w3.org/2001/XMLSchema#string

Juan Bilbao

http://www.w3.org/2001/XMLSchema#string

Lee-Cyn Ang

http://www.w3.org/2001/XMLSchema#string

Olaf Ansorge

http://www.w3.org/2001/XMLSchema#string

Osamu Yokota

http://www.w3.org/2001/XMLSchema#string

P2860

PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function

Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state

Rules for nuclear localization sequence recognition by karyopherin beta 2

Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease

ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import

Heterogeneity of ubiquitin pathology in frontotemporal lobar degeneration: classification and relation to clinical phenotype

A new subtype of frontotemporal lobar degeneration with FUS pathology

Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis

Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6

P304

2595-2609

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1093/BRAIN/AWR201

http://www.w3.org/2001/XMLSchema#string

P407

P433

Pt 9

http://www.w3.org/2001/XMLSchema#string

P478

134

http://www.w3.org/2001/XMLSchema#string

P50

Christian Haass

Rosa Rademakers

Mariely DeJesus-Hernandez

Manuela Neumann

P577

2011-08-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51585646

http://www.w3.org/2001/XMLSchema#string

P698

21856723

http://www.w3.org/2001/XMLSchema#string

P921

amyotrophic lateral sclerosis

P932

3170539

http://www.w3.org/2001/XMLSchema#string