ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP. - Wikidata - thesis-toulmin - TriplyDB

ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP.

ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP.

http://www.wikidata.org/entity/Q35114564

about

Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis Copy Number Variations in the Survival Motor Neuron Genes: Implications for Spinal Muscular Atrophy and Other Neurodegenerative Diseases Toward precision medicine in amyotrophic lateral sclerosis FUS-mediated regulation of alternative RNA processing in neurons: insights from global transcriptome analysis A novel conditional knock-in approach defines molecular and circuit effects of the DYT1 dystonia mutation.Characterization of genetic loss-of-function of Fus in zebrafish.Motor neuron vulnerability and resistance in amyotrophic lateral sclerosis.Functional interaction between FUS and SMN underlies SMA-like splicing changes in wild-type hFUS mice.Spinal Muscular Atrophy: From Defective Chaperoning of snRNP Assembly to Neuromuscular Dysfunction.Single-Cell Analysis of SMN Reveals Its Broader Role in Neuromuscular Disease.U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP Translocated in liposarcoma regulates the distribution and function of mammalian enabled, a modulator of actin dynamics.Altered mRNP granule dynamics in FTLD pathogenesis.The hnRNP-Htt axis regulates necrotic cell death induced by transcriptional repression through impaired RNA splicing.ALS mutations in TLS/FUS disrupt target gene expression.TDP-43 and FUS en route from the nucleus to the cytoplasm.Directly converted patient-specific induced neurons mirror the neuropathology of FUS with disrupted nuclear localization in amyotrophic lateral sclerosis.A U1 snRNP-specific assembly pathway reveals the SMN complex as a versatile hub for RNP exchange Differential neuronal vulnerability identifies IGF-2 as a protective factor in ALS.Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss.Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses.Minor intron splicing is regulated by FUS and affected by ALS-associated FUS mutants Comparative interactomics analysis of different ALS-associated proteins identifies converging molecular pathways FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription Nuclear bodies reorganize during myogenesis in vitro and are differentially disrupted by expression of FSHD-associated DUX4.Sequestration of PRMT1 and Nd1-L mRNA into ALS-linked FUS mutant R521C-positive aggregates contributes to neurite degeneration upon oxidative stress.SMN deficiency in severe models of spinal muscular atrophy causes widespread intron retention and DNA damage FUS affects circular RNA expression in murine embryonic stem cell-derived motor neurons.RNA mis-splicing in disease.Roles for RNA-binding proteins in development and disease.Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins.Cajal bodies in neurons Linking amyotrophic lateral sclerosis and spinal muscular atrophy through RNA-transcriptome homeostasis: a genomics perspective.RNA-binding proteins with prion-like domains in health and disease.Faulty RNA splicing: consequences and therapeutic opportunities in brain and muscle disorders.Alternative splicing as a regulator of development and tissue identity.Expanding Axonal Transcriptome Brings New Functions for Axonally Synthesized Proteins in Health and Disease.Novel FUS mutations identified through molecular screening in a large cohort of familial and sporadic amyotrophic lateral sclerosis.

P2860

Q26749169-28382DD7-0CDE-4D2B-9CF6-E88B18EE8228 Q26750803-12AC06B1-61EE-45D7-9B20-72E015200F4D Q26764950-54A03575-AB56-493D-9CD3-2997D5E57302 Q26773038-E2E451B1-EF1A-416A-A3EA-83EC27347D78 Q30670034-5E1B3B27-3794-4288-BEF1-29182A7C44FD Q30836650-11F8FC68-1092-4418-BB7F-992EF6B32076 Q33665800-2BB765A5-25D2-404E-BF02-3A98003EC5F1 Q33700562-9DBC175D-3148-490D-8112-D065B3AF4492 Q33775770-01807123-C2C5-4FA1-8DEA-AF2D14E35A06 Q33777083-820889AE-1F05-4E0B-B5B5-8CC16C9EAFFA Q35237055-F9FC44C0-B7A6-4EE0-A892-D5BB194AEFD6 Q35739332-275CEFC5-CA66-4930-B8C5-B98A8FEF36C9 Q35865531-ECE0E3F4-D225-4BA1-9F02-67ED30654B62 Q35929154-98385A39-9B35-4E2F-88E1-7C2A73433BAC Q35944221-E59D63D2-FCEF-43EF-B2BB-B57234EA7E1D Q36002020-E7597577-0C67-4943-9B3C-EEB454391865 Q36032446-3A19CB23-DB54-4705-9A41-B4F8BAA27330 Q36336278-B3EE236D-2F8B-47B7-9FF6-0EA02DBC917F Q36489948-35C96AD5-C6DB-4684-B930-4FF4CA703B6E Q36806948-D5D7B4C3-BE47-4CE8-B4F4-81DF6F1775C7 Q36903049-2B3F9444-762A-4340-A059-98C7005F3314 Q36906420-95C75A21-7D2A-41AE-995D-D9B643AC7587 Q37072993-C52F8B12-C92B-46E3-8388-5D28F5E199DB Q37096949-EFD672E3-1413-46FD-95CB-0A7B80DD61C8 Q37099358-1BA36C66-E70F-4E27-89BB-29CF8940DBC7 Q37330498-CFB8C38F-4910-4E64-A291-FE414F21F481 Q37466448-6633126E-36D6-475F-9DC5-D23AFF482269 Q37589278-C82C2DC8-37BE-4C16-B52A-3D88FC305D07 Q37730133-8C320B14-36EC-49F8-8EE3-C4E1DA606A96 Q37736433-D0F87A34-09CE-402D-AFBF-15C9ABD0FB46 Q38642996-3251C04C-723B-4788-B9D0-A2E87B6E154F Q38772987-E166FAC1-C6F0-4428-AF29-18120788836F Q38789192-884FAB63-43BF-449A-A1CE-AC87C27973FC Q38954293-F9D89C67-C8FC-46ED-8F1B-3DDEED1E90EE Q39039061-819CF757-0A9D-4500-A5FD-B6145CAA04F9 Q39227676-1DA40278-3FF0-4ED1-A44C-7A10E649A259 Q39256785-EF7159AA-C51F-454D-BE4F-BFC3B1ECCA6A Q39295240-68805538-2419-4F13-A021-D94137F5BC9B Q39359080-AAE00BE2-99C4-45DA-AC7B-A5A63D7850C0 Q40734296-1268E32B-BF20-4212-833C-3437AFE46C78

P2860

ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP.

http://www.wikidata.org/entity/Q35114564

description

2015 nî lūn-bûn

@nan

2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

ALS-causative mutations in FUS ...... ciation with SMN and U1-snRNP.

@ast

ALS-causative mutations in FUS ...... ciation with SMN and U1-snRNP.

@en

type

label

ALS-causative mutations in FUS ...... ciation with SMN and U1-snRNP.

@ast

ALS-causative mutations in FUS ...... ciation with SMN and U1-snRNP.

@en

prefLabel

ALS-causative mutations in FUS ...... ciation with SMN and U1-snRNP.

@ast

ALS-causative mutations in FUS ...... ciation with SMN and U1-snRNP.

@en

P1433

Q35114564-728D7AE2-8010-433E-BF68-B7E506077C53

P1476

Q35114564-A0A2385B-B6CC-4742-87F0-35A1DA674484

P2093

Q35114564-0A398814-8D57-48C6-94CC-3482670A25B1

Q35114564-281B80E3-3082-40D8-AF8A-6C869941822A

Q35114564-3F699E88-A5E8-4E88-B069-C05BCB7F7100

Q35114564-73C19800-47DF-4FC3-8A3D-55A8CC614243

Q35114564-8ABEB614-5D6D-439A-A60C-D36635AF7D5D

Q35114564-93C261E8-E5C8-4A05-BB46-278469C67807

Q35114564-AF8E61B0-3424-43F0-AFC6-291B20C64A6B

Q35114564-B6F20E69-2901-42CA-80EF-567488319812

Q35114564-BAD6F641-567F-4457-A960-2D6AF9E738EA

Q35114564-BEB4AAFB-34F7-4861-A24F-FD76D6D0168E

P2860

Q35114564-00D542D3-D794-46DA-BC60-AF5E1394F811

Q35114564-0CA8A68B-7F89-45E0-8AA7-4CFDF418EF65

Q35114564-15E61340-C857-4654-9167-234ADF36AE9C

Q35114564-1AC0271E-1DD4-4620-B595-A1142CF0E91F

Q35114564-1E6272C4-4D02-47F6-A36C-CA44F3936CA6

Q35114564-21179EBC-244E-42B2-B3D8-E9B759AA73E2

Q35114564-21ACE8CA-32E5-48DA-A3A8-43427D2DE81C

Q35114564-3113D377-5776-4116-A67B-E59181BDE4C2

Q35114564-34C035E5-523E-4F18-8E89-F8E2E074F201

Q35114564-3586C5A5-AD5B-4B7F-A50A-24E2A5D852AC

P2888

Q35114564-72150CEB-8DB3-48A3-AB08-7934E482D296

P304

Q35114564-7A3327A2-C736-41F5-A24A-7ABE3A97585A

P31

Q35114564-A159C061-FB32-4000-B61E-9DA75AD06FE5

P356

Q35114564-DEE3FAA0-9F84-4139-BEA3-6B495317C488

P407

Q35114564-71B115A7-13BA-4A51-B82E-8584B4D27432

P478

Q35114564-4DFBF568-5DD7-4F05-85FC-26C2E66E78B3

P50

Q35114564-29C33458-3287-4DE4-A498-279623ECB231

Q35114564-FC571C80-0DF5-42A7-8087-FCD178ABB4D9

P577

Q35114564-E625531C-C0A4-4E5C-B621-72C888396C81

P5875

Q35114564-D44912BF-FD47-4E86-9113-0C14111BBAE0

P698

Q35114564-4F61EBAD-C391-433A-9B1F-4E00AC1FBF72

P921

Q35114564-72CE78C9-5F2F-4AE0-961C-E79A7A88D7C0

P932

Q35114564-9EFEBF10-1A50-4498-9934-9114C86AC247

P356

P1433

Nature Communications

P1476

ALS-causative mutations in FUS ...... ociation with SMN and U1-snRNP

@en

P2093

Anh Bui

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

Claudio P Albuquerque

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

Clotilde Lagier-Tourenne

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

Gene W Yeo

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

Hairi Li

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

Haiyan Qiu

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

Huilin Zhou

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

Jinsong Qiu

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

Kevin Eggan

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

Seiya Tokunaga

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

P2860

Ultrafast and memory-efficient alignment of short DNA sequences to the human genome

CAJAL BODIES: A Long History of Discovery

Coiled bodies and gems: Janus or gemini?

A novel nuclear structure containing the survival of motor neurons protein

Gemin proteins are required for efficient assembly of Sm-class ribonucleoproteins.

Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein

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

Cluster analysis and display of genome-wide expression patterns

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

P2888

P304

6171

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

P31

scholarly article

P356

10.1038/NCOMMS7171

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

P407

P478

6

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

P50

Don W Cleveland

P577

2015-01-27T00:00:00Z

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

P5875

271600764

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

P698

25625564

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

P921

amyotrophic lateral sclerosis

P932

4338613

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