Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.
about
NMR Meets Tau: Insights into Its Function and PathologyThe Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a CostPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Tau StructuresAssigning backbone NMR resonances for full length tau isoforms: efficient compromise between manual assignments and reduced dimensionalityCell signaling, post-translational protein modifications and NMR spectroscopyA relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synucleinMinute time scale prolyl isomerization governs antibody recognition of an intrinsically disordered immunodominant epitopeTau as a therapeutic target in neurodegenerative disease.Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.Protein phosphorylation in neurodegeneration: friend or foe?Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.OGlcNAcylation and phosphorylation have similar structural effects in α-helices: post-translational modifications as inducible start and stop signals in α-helices, with greater structural effects on threonine modification.Implications of peptide assemblies in amyloid diseases.Effect of Phosphorylation on a Human-like Osteopontin Peptide.A Novel Antibody Targeting Tau Phosphorylated at Serine 235 Detects Neurofibrillary Tangles.Loss of intramolecular electrostatic interactions and limited conformational ensemble may promote self-association of cis-tau peptide.Structural evaluations of tau protein conformation: methodologies and approaches.
P2860
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P2860
Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
@zh
2011年学术文章
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2011年学术文章
@zh-hans
2011年学术文章
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name
Structural characterization by ...... of the disordered Tau protein.
@en
Structural characterization by ...... of the disordered Tau protein.
@nl
type
label
Structural characterization by ...... of the disordered Tau protein.
@en
Structural characterization by ...... of the disordered Tau protein.
@nl
prefLabel
Structural characterization by ...... of the disordered Tau protein.
@en
Structural characterization by ...... of the disordered Tau protein.
@nl
P2093
P2860
P50
P356
P1433
P1476
Structural characterization by ...... of the disordered Tau protein.
@en
P2093
Arnaud Leroy
Caroline Fauquant
Dries Verdegem
Laziza Amniai
P2860
P304
P356
10.1002/PROT.23210
P407
P577
2011-11-09T00:00:00Z