Identification of an aggregation-prone structure of tau.
about
A flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceShedding light on protein folding, structural and functional dynamics by single molecule studiesMultiply labeling proteins for studies of folding and stabilityIdentification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for TauopathiesPhosphoregulation of Tau modulates inhibition of kinesin-1 motility.Tau mutants bind tubulin heterodimers with enhanced affinity.Structural Insight into Tau Protein's Paradox of Intrinsically Disordered Behavior, Self-Acetylation Activity, and AggregationStructure and mechanism of action of tau aggregation inhibitors.Hyperphosphorylation of intrinsically disordered tau protein induces an amyloidogenic shift in its conformational ensemble.An evolutionary roadmap to the microtubule-associated protein MAP TauDistinct Therapeutic Mechanisms of Tau Antibodies: Promoting Microglial Clearance Versus Blocking Neuronal Uptake.The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations.Fluorescence correlation spectroscopy reveals highly efficient cytosolic delivery of certain penta-arg proteins and stapled peptidesRemodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer.Simple method to enhance the photostability of the fluorescence reporter R6G for prolonged single-molecule studies.Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations.Single-molecule FRET reveals the native-state dynamics of the IκBα ankyrin repeat domainThe role of crowded physiological environments in prion and prion-like protein aggregationA functional role for intrinsic disorder in the tau-tubulin complex.Shedding light on protein folding landscapes by single-molecule fluorescence.Cellular factors modulating the mechanism of tau protein aggregation.A co-expression strategy to achieve labeling of individual subunits within a dimeric protein for single molecule analysis.OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth.Alternative conformations of the Tau repeat domain in complex with an engineered binding protein.Conformation determines the seeding potencies of native and recombinant Tau aggregates.A protein-based electrochemical biosensor for detection of tau protein, a neurodegenerative disease biomarker.Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.Tau-based therapies in neurodegeneration: opportunities and challenges.Probing Conformational Dynamics of Tau Protein by Hydrogen/Deuterium Exchange Mass Spectrometry.Structural evaluations of tau protein conformation: methodologies and approaches.Tau Internalization is Regulated by 6-O Sulfation on Heparan Sulfate Proteoglycans (HSPGs).
P2860
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P2860
Identification of an aggregation-prone structure of tau.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Identification of an aggregation-prone structure of tau.
@ast
Identification of an aggregation-prone structure of tau.
@en
type
label
Identification of an aggregation-prone structure of tau.
@ast
Identification of an aggregation-prone structure of tau.
@en
prefLabel
Identification of an aggregation-prone structure of tau.
@ast
Identification of an aggregation-prone structure of tau.
@en
P2860
P356
P1476
Identification of an aggregation-prone structure of tau.
@en
P2093
Elizabeth Rhoades
Shana Elbaum-Garfinkle
P2860
P304
16607-16613
P356
10.1021/JA305206M
P407
P577
2012-10-01T00:00:00Z