Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation - Wikidata - wikimedia - TriplyDB

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

http://www.wikidata.org/entity/Q34267286

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HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease Histone deacetylase 6 inhibition improves memory and reduces total tau levels in a mouse model of tau deposition.Severe amygdala dysfunction in a MAPT transgenic mouse model of frontotemporal dementia Tau deposition drives neuropathological, inflammatory and behavioral abnormalities independently of neuronal loss in a novel mouse model Acetylation: a new key to unlock tau's role in neurodegeneration MAP3K4 Controls the Chromatin Modifier HDAC6 during Trophoblast Stem Cell Epithelial-to-Mesenchymal Transition.The development prospection of HDAC inhibitors as a potential therapeutic direction in Alzheimer's disease.Trehalose improves human fibroblast deficits in a new CHIP-mutation related ataxia.Epigenetic memory: the Lamarckian brain Tubulin acetylation: responsible enzymes, biological functions and human diseases.Quantification of histone deacetylase isoforms in human frontal cortex, human retina, and mouse brain Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila.Amyloid β oligomers elicit mitochondrial transport defects and fragmentation in a time-dependent and pathway-specific manner Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance.Regulated protein aggregation: stress granules and neurodegeneration MAPping out distribution routes for kinesin couriers.Inclusion body formation, macroautophagy, and the role of HDAC6 in neurodegeneration.Tau-induced neurodegeneration: mechanisms and targets.An acetylation switch controls TDP-43 function and aggregation propensity.Cellular factors modulating the mechanism of tau protein aggregation.Histone Acetylation Modifiers in the Pathogenesis of Alzheimer's Disease.Cullin 3SPOP ubiquitin E3 ligase promotes the poly-ubiquitination and degradation of HDAC6.Monoaminergic neuropathology in Alzheimer's disease.The E3 ubiquitin ligase CHIP mediates ubiquitination and proteasomal degradation of PRMT5.Impact of acetylation on tumor metabolism.Therapeutic Strategies for Restoring Tau Homeostasis.Signaling pathways and posttranslational modifications of tau in Alzheimer's disease: the humanization of yeast cells.Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies.An acetylation-phosphorylation switch that regulates tau aggregation propensity and function.Increased acetylation of microtubules rescues human tau-induced microtubule defects and neuromuscular junction abnormalities in Drosophila.Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies.Tauopathies: Mechanisms and Therapeutic Strategies.Structure-Activity Relationship of Propargylamine-Based HDAC Inhibitors.Histone deacetylases (HDACs) in frontotemporal lobar degeneration.A First-in-Class Small-Molecule that Acts as a Dual Inhibitor of HDAC and PDE5 and that Rescues Hippocampal Synaptic Impairment in Alzheimer's Disease Mice.Class II HDACs and neuronal regeneration.

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P2860

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

http://www.wikidata.org/entity/Q34267286

description

2012 nî lūn-bûn

@nan

2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@ast

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@en

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@nl

type

label

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@ast

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@en

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@nl

prefLabel

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@ast

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@en

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@nl

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P1433

Human Molecular Genetics

P1476

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

@en

P2093

Casey Cook

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

Judy Dunmore

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

Kristyn Scheffel

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

Michael DeTure

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

Tania F Gendron

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

Yari Carlomagno

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

P2860

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

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor

Histone deacetylase 6 interacts with the microtubule-associated protein tau

HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates

CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Mechanisms of disease: the role of heat-shock protein 90 in genitourinary malignancy

Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion

The ubiquitin-proteasome proteolytic pathway

Hsp90 & Co. - a holding for folding.

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2936-2945

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scholarly article

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10.1093/HMG/DDS125

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13

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21

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Leonard Petrucelli

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2012-04-05T00:00:00Z

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223974370

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22492994

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3373241

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