The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. - Wikidata - wikimedia - TriplyDB

The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins.

The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins.

http://www.wikidata.org/entity/Q35629026

about

Alzheimer mechanisms and therapeutic strategies A role for FKBP52 in Tau protein function Cdc5L interacts with ATR and is required for the S-phase cell-cycle checkpoint Hsp90-Tau complex reveals molecular basis for specificity in chaperone action Novel therapeutics for Alzheimer's disease: an update Akt and CHIP coregulate tau degradation through coordinated interactions Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing Glial Tau Pathology in Tauopathies: Functional Consequences The Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a Cost Proteomics in Traditional Chinese Medicine with an Emphasis on Alzheimer's Disease Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases FKBP51 and FKBP52 in signaling and disease Heat shock proteins at the crossroads between cancer and Alzheimer's disease Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models Protein homeostasis as a therapeutic target for diseases of protein conformation The role of tau in neurodegenerative diseases and its potential as a therapeutic target Tau-targeted treatment strategies in Alzheimer's disease Functions of the Hsp90 chaperone system: lifting client proteins to new heights Tau and tauopathies Rescue from tau-induced neuronal dysfunction produces insoluble tau oligomers Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer Dysregulation of Ubiquitin-Proteasome System in Neurodegenerative Diseases The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease Ubiquitin-dependent proteasomal degradation of human liver cytochrome P450 2E1: identification of sites targeted for phosphorylation and ubiquitination Hsp90 chaperone inhibitor 17-AAG attenuates Aβ-induced synaptic toxicity and memory impairment A novel calcium-binding protein is associated with tau proteins in tauopathy Zebrafish models of Tauopathy Heat shock proteins: cellular and molecular mechanisms in the central nervous system.A critical role for CHIP in the aggresome pathway Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden.Heat shock protein 90: translation from cancer to Alzheimer's disease treatment?The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP To fold or not to fold: modulation and consequences of Hsp90 inhibition.Roles of tau protein in health and disease.Facilitating Akt clearance via manipulation of Hsp70 activity and levels.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

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P2860

The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins.

http://www.wikidata.org/entity/Q35629026

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

@zh-hk

2007年論文

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2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@ast

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@en

type

label

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@ast

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@en

prefLabel

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@ast

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@en

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P1433

Journal of Clinical Investigation

P1476

The high-affinity HSP90-CHIP c ...... horylated tau client proteins.

@en

P2093

Adeela Kamal

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

Cam Patterson

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

Chad A Dickey

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

Christopher B Eckman

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

Francis Burrows

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

Jelena Zlatkovic

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

Judith Dunmore

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

Karen Lundgren

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

Michael Hutton

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

N Stanley Nahman

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

P2860

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays

Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity.

A potential role for RNA interference in controlling the activity of the human LINE-1 retrotransposon

Neuropathological stageing of Alzheimer-related changes

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

Identification of the gene for vitamin K epoxide reductase

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

New insights into proteasome function: from archaebacteria to drug development

P304

648-658

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P31

scholarly article

P356

10.1172/JCI29715

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P407

P433

3

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P478

117

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P50

Dennis W. Dickson

Leonard Petrucelli

P577

2007-02-15T00:00:00Z

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P698

17304350

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

P921

phosphorylation

P932

1794119

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