Cerebellar soluble mutant ataxin-3 level decreases during disease progression in Spinocerebellar Ataxia Type 3 mice - Wikidata - awgldk - TriplyDB

Cerebellar soluble mutant ataxin-3 level decreases during disease progression in Spinocerebellar Ataxia Type 3 mice

Cerebellar soluble mutant ataxin-3 level decreases during disease progression in Spinocerebellar Ataxia Type 3 mice

http://www.wikidata.org/entity/Q34692633

about

Ataxin-3 protein and RNA toxicity in spinocerebellar ataxia type 3: current insights and emerging therapeutic strategies.From mice to men: lessons from mutant ataxic mice.miR-25 alleviates polyQ-mediated cytotoxicity by silencing ATXN3.

P2860

Q38167681-F3F37E9A-E56A-4646-800D-33DF0DD6A993 Q38578808-FBCCB5ED-6660-4C28-A966-2C8905B16D31 Q50609525-2127EF31-0A82-4E49-A500-5C92B35E5DE9

P2860

Cerebellar soluble mutant ataxin-3 level decreases during disease progression in Spinocerebellar Ataxia Type 3 mice

http://www.wikidata.org/entity/Q34692633

description

2013 nî lūn-bûn

@nan

2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@ast

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@en

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@nl

type

label

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@ast

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@en

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@nl

prefLabel

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@ast

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@en

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@nl

P1433

Q34692633-103312E6-4A95-47F2-B207-6E8EB57C3FC9

P1476

Q34692633-1B6A786E-4C3C-4140-A6DB-954DD3FEC117

P2093

Q34692633-2FDD2303-3C5F-4048-89FA-75B810C2C434

Q34692633-4AAF9803-0FC6-4AE4-A7E7-6EEDCB12C0E6

Q34692633-9D610675-F8CB-4DE4-A65B-8D9620B1B364

Q34692633-B5205CF4-7B07-4E50-9774-309AD23159DD

P2860

Q34692633-0D3FC87E-03E1-4E96-B8DB-6626DCEB94D6

Q34692633-1C01FE66-2762-4F72-8A22-6D4C52899972

Q34692633-276C5FCD-63EF-4DCA-8AB6-712A424118D8

Q34692633-2C4432A8-B06F-4D67-8A0C-692B082C30E5

Q34692633-3326E615-FC02-4039-B48A-E4513A7D5990

Q34692633-391F43B3-5076-4749-B5E4-9897A8C56ACB

Q34692633-3E6EB9B5-CBA8-42C9-A7A9-FFC088700643

Q34692633-478E2107-15B7-4748-9A4B-99F15091435C

Q34692633-481FF661-F344-4F3D-BE2E-24F92B1FDCDB

Q34692633-4A531605-27F7-41B1-BCCE-30F9FF33B79A

P304

Q34692633-46EB070D-FFF3-4FD9-A75A-540C31FE34AE

P31

Q34692633-4284DC3C-CF8E-4E82-A863-2E43831A7AC3

P356

Q34692633-5EA71AD9-AA81-4297-A071-404B24B94A25

P407

Q34692633-0789F870-F86C-497E-95E5-2A8DD690A36A

P433

Q34692633-EA65D690-D031-486C-9046-4013EA4B32CF

P478

Q34692633-6E2E634B-C480-4020-8A4B-29423757611E

P50

Q34692633-0ECB9B4B-4578-40EE-AE9A-28B4D75CA984

Q34692633-F9C296A7-95B4-40E7-894B-3E57B03B9387

P577

Q34692633-34307965-A804-400D-AEE8-F760F145946A

P5875

Q34692633-CB1BA3FF-72B4-4ABD-B5AD-DD35A688A379

P698

Q34692633-2AC7B8BB-09FA-4356-BC45-71FC0DE42EAE

P932

Q34692633-8B7C9903-EF61-44D0-B3D1-0AB23107F429

P356

JOURNAL.PONE.0062043

P1433

P1476

Cerebellar soluble mutant atax ...... ocerebellar Ataxia Type 3 mice

@en

P2093

Andreas Weiss

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

Jeannette Hübener

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

Jonasz Jeremiasz Weber

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

Stephan Grueninger

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

P2860

Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract

Non-conjugated small molecule FRET for differentiating monomers from higher molecular weight amyloid beta species

Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus

Study of subcellular localization and proteolysis of ataxin-3

Nuclear localization of ataxin-3 is required for the manifestation of symptoms in SCA3: in vivo evidence

Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice

SCA3: neurological features, pathogenesis and animal models.

A FRET sensor for non-invasive imaging of amyloid formation in vivo.

Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis.

BRET and Time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues.

P304

e62043

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0062043

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

P407

P433

4

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

P478

8

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

P50

Huu Phuc Nguyen

P577

2013-04-23T00:00:00Z

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

P5875

236461527

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

P698

23626768

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

P932

3633920

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