Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
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NMR Meets Tau: Insights into Its Function and PathologyThe Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a CostChaperones in NeurodegenerationPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulatorsModulation of the maladaptive stress response to manage diseases of protein foldingFolding of the Tau Protein on MicrotubulesSystematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 FunctionMechanistic Asymmetry in Hsp90 DimersThe Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's DiseaseCapturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingNMR Backbone Assignment of Large Proteins by Using (13) Cα -Only Triple-Resonance Experiments.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesProduction and purification of human Hsp90β in Escherichia coli.Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry.The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting ProteinConformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity.Heat Shock Protein 90 Associates with the Per-Arnt-Sim Domain of Heme-free Soluble Guanylate Cyclase: IMplications for Enzyme Maturation.The Human Tau Interactome: Binding to the Ribonucleoproteome, and Impaired Binding of the Proline-to-Leucine Mutant at Position 301 (P301L) to Chaperones and the Proteasome.Visualizing chaperone-assisted protein folding.Stressing Out Hsp90 in Neurotoxic Proteinopathies.A new molecular link between defective autophagy and erythroid abnormalities in chorea-acanthocytosis.Targeting Hsp90 and its co-chaperones to treat Alzheimer's diseaseCellular factors modulating the mechanism of tau protein aggregation.Molecular chaperones and neuronal proteostasis.HSP90AB1: Helping the good and the bad.Hsp90 activator Aha1 drives production of pathological tau aggregates.NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13C-methyl alanine.Modulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.Therapeutic strategies for the treatment of tauopathies: Hopes and challenges.Therapeutic Strategies for Restoring Tau Homeostasis.Folding while bound to chaperones.Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.Forces Driving Chaperone ActionA script to highlight hydrophobicity and charge on protein surfaces.Characterization of the Grp94/OS-9 chaperone-lectin complex.Quarterly intrinsic disorder digest (January-February-March, 2014).CCT complex restricts neuropathogenic protein aggregation via autophagy.
P2860
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P2860
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
description
2014 nî lūn-bûn
@nan
2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի փետրվարին 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
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@ast
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en-gb
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@nl
type
label
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@ast
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en-gb
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@nl
prefLabel
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@ast
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en-gb
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@nl
P2093
P2860
P50
P3181
P1433
P1476
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
@en
P2093
Afonso M S Duarte
Bryce A Nordhues
Chad A Dickey
G Elif Karagöz
Hans Ippel
Jacek Biernat
Martina Radli
Stefan G D Rüdiger
Tania Morán Luengo
Tatiana Didenko
P2860
P304
P3181
P356
10.1016/J.CELL.2014.01.037
P407
P577
2014-02-27T00:00:00Z