Oligomer Diversity during the Aggregation of the Repeat Region of Tau (Q57986225)

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3 April 2020

title

Oligomer Diversity during the Aggregation of the Repeat Region of Tau (English)

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3 April 2020

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3 April 2020

Alexander J Dear

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3 April 2020

Franziska Kundel

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3 April 2020

Georg Meisl

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3 April 2020

Tuomas Knowles

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author name string

Seema Qamar

4

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3 April 2020

David Klenerman

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publication date

17 July 2018

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ACS Chemical Neuroscience

3 April 2020

published in

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volume

9

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issue

12

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3 April 2020

page(s)

3060-3071

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Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

3 April 2020

cites work

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Modulation of neurodegeneration by molecular chaperones

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Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions

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Different species of alpha-synuclein oligomers induce calcium influx and seeding.

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Structural polymorphism of 441-residue tau at single residue resolution

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Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.

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An analytical solution to the kinetics of breakable filament assembly

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The role of the lipid bilayer in tau aggregation

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Frequency Factors in a Landscape Model of Filamentous Protein Aggregation

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Observation of spatial propagation of amyloid assembly from single nuclei

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Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein

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Single Molecule Fluorescence under Conditions of Fast Flow

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Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth

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Direct observation of the interconversion of normal and toxic forms of α-synuclein

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Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution

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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

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The structural basis for optimal performance of oligothiophene-based fluorescent amyloid ligands: conformational flexibility is essential for spectral assignment of a diversity of protein aggregates

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Spatial Propagation of Protein Polymerization

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12 December 2020

Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry.

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The amyloid state and its association with protein misfolding diseases.

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12 December 2020

Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

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12 December 2020

Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats

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12 December 2020

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

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12 December 2020

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers

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12 December 2020

Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants

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Molecular mechanisms of protein aggregation from global fitting of kinetic models.

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Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids

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Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading

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Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism

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β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces.

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Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors

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Cryo-EM structures of tau filaments from Alzheimer's disease.

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Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.

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12 December 2020

Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity

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12 December 2020

Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2.

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12 December 2020

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.

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12 December 2020

Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.

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12 December 2020

10.1021/ACSCHEMNEURO.8B00250

Identifiers

DOI

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3 April 2020

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3 April 2020

PubMed publication ID

29953200

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