Heat shock protein 90 in Alzheimer's disease - Wikidata - thesis-toulmin - TriplyDB

Heat shock protein 90 in Alzheimer's disease

Heat shock protein 90 in Alzheimer's disease

http://www.wikidata.org/entity/Q34413279

about

The ubiquitin proteasomal system: a potential target for the management of Alzheimer's disease The Role of Oxidative Damage in the Pathogenesis and Progression of Alzheimer's Disease and Vascular Dementia Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls.Identification of chaperones in a MPP+-induced and ATRA/TPA-differentiated SH-SY5Y cell PD model.Mitochondrial dysfunction and oxidative stress in aging and cancer.The Role of PGRN in Alzheimer's Disease.The mechanisms of Mallory-Denk body formation are similar to the formation of aggresomes in Alzheimer's disease and other neurodegenerative disorders.Cannabidiol Modulates the Expression of Alzheimer's Disease-Related Genes in Mesenchymal Stem Cells.Formal Models of Biological Systems.Heat Shock Proteins in Multiple Sclerosis.Heat Shock Proteins in Alzheimer's Disease: Role and Targeting

P2860

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P2860

Heat shock protein 90 in Alzheimer's disease

http://www.wikidata.org/entity/Q34413279

description

2014 nî lūn-bûn

@nan

2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Heat shock protein 90 in Alzheimer's disease

@ast

Heat shock protein 90 in Alzheimer's disease

@en

Heat shock protein 90 in Alzheimer's disease

@nl

type

label

Heat shock protein 90 in Alzheimer's disease

@ast

Heat shock protein 90 in Alzheimer's disease

@en

Heat shock protein 90 in Alzheimer's disease

@nl

prefLabel

Heat shock protein 90 in Alzheimer's disease

@ast

Heat shock protein 90 in Alzheimer's disease

@en

Heat shock protein 90 in Alzheimer's disease

@nl

P1433

Q34413279-1D736692-9AA4-462D-95B8-714C4915AF5A

P1476

Q34413279-0BF35802-661E-45FD-8E2C-93E0C3C047E6

P2093

Q34413279-794A0D00-F93C-4B6B-B3E8-24B355E5ECFC

Q34413279-B71AB96E-3057-436B-85CF-67392C891326

Q34413279-F04CD2BE-EC58-4251-B1D1-6F2633873363

P275

Q34413279-0C02B79A-40D7-4BF3-970E-1AF392DE4779

P2860

Q34413279-0065AA7E-6330-4CA9-8CD1-B2AFF6F56323

Q34413279-02B14BC7-3E21-4E33-8A1B-B230D7351DD4

Q34413279-0721D379-4C8D-4CBD-AA39-15CD8189C161

Q34413279-089A1CF8-3435-40F9-AFA6-5E84F5F90F20

Q34413279-0A924B6C-A61A-4AD3-8C7A-21686C1A3BDD

Q34413279-0CC1C08F-2949-4F59-BD17-1726AF372159

Q34413279-0D701103-6E11-404C-B2C6-E32C40FF82D4

Q34413279-0ED950DB-E6EA-494C-909B-F292009188C3

Q34413279-12502264-7011-4090-A918-41777E80E80B

Q34413279-173C2B86-98C7-4C1B-980D-ED386F7F11EC

P304

Q34413279-764355F3-1BCC-4C24-A0B2-AB5AAB156B2E

P31

Q34413279-00DC4E53-350A-42A8-A89B-DC857613180A

Q34413279-74BC0F56-D048-4905-BE69-3E2E0F07F19A

P356

Q34413279-DF05EF61-0573-432A-B1BF-9AB2252E3F7A

P407

Q34413279-0482A682-605E-4FD1-8AC4-65A7016755C1

P478

Q34413279-69AC881C-A322-45CF-AE0F-50B942138AB1

P50

Q34413279-B241F9DB-DD73-4B9E-A81C-3AC3D64D012B

Q34413279-B313A856-5C81-4EE9-B3FB-0E0FBFDDA242

P5008

Q34413279-01FA294C-739F-45FD-AF6B-58ECB8F74614

P577

Q34413279-A4249B43-E015-48D0-9D0F-F0E069F1F1AA

P5875

Q34413279-A21DD700-8347-4EF2-A7D7-F31605872CAF

P698

Q34413279-D0E26139-0612-41A7-AAD7-FC33A5E6E4AB

P921

Q34413279-3179221C-DB07-4D32-9502-2B7F6DCC7A9D

P932

Q34413279-19939C22-88C8-4D00-96F8-87B3B7CFB9EC

P356

P1433

BioMed Research International

P1476

Heat shock protein 90 in Alzheimer's disease

@en

P2093

An-Mu Xie

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

Jiang-Rong Ou

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

Meng-Shan Tan

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

P275

Creative Commons Attribution 3.0 Unported

P2860

Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Akt and CHIP coregulate tau degradation through coordinated interactions

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones

Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons

Structure and mechanism of the Hsp90 molecular chaperone machinery

P304

796869

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

P31

scholarly article

P356

10.1155/2014/796869

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

P407

P478

2014

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

P50

P5008

P577

2014-10-13T00:00:00Z

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

P5875

267872504

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P698

25374890

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

P921

Alzheimer's disease

P932

4211323

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