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

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scientific article published on 17 July 2018

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English	Oligomer Diversity during the Aggregation of the Repeat Region of Tau	scientific article published on 17 July 2018

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scholarly article

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Europe PubMed Central

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6302314

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3 April 2020

title

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

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Europe PubMed Central

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6302314

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main subject

cell biology

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author

Magnus Kjaergaard

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1

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Europe PubMed Central

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6302314

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3 April 2020

Alexander J Dear

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2

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6302314

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Franziska Kundel

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3

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6302314

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Georg Meisl

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5

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6302314

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Tuomas Knowles

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6

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6302314

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author name string

Seema Qamar

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4

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6302314

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David Klenerman

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7

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6302314

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3 April 2020

publication date

17 July 2018

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3 April 2020

published in

ACS Chemical Neuroscience

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PMC publication ID

6302314

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3 April 2020

volume

9

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6302314

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issue

12

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6302314

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3 April 2020

page(s)

3060-3071

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6302314

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3 April 2020

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Role of tau protein in both physiological and pathological conditions.

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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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12 December 2020

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

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Structural classification of toxic amyloid oligomers

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Direct characterization of amyloidogenic oligomers by single-molecule fluorescence

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

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

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

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12 December 2020

based on heuristic

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Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

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12 December 2020

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

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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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12 December 2020

based on heuristic

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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

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

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PubMed

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based on heuristic

inferred from PubMed ID database lookup

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

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

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reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

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reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

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reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

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reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

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reference URL

https://pubmed.ncbi.nlm.nih.gov/29953200

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1021/ACSCHEMNEURO.8B00250

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stated in

Europe PubMed Central

PMC publication ID

6302314

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29953200%20AND%20SRC:MED&resulttype=core&format=json

retrieved

3 April 2020

PMC publication ID

6302314

1 reference

stated in

Europe PubMed Central

PMC publication ID

6302314

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29953200%20AND%20SRC:MED&resulttype=core&format=json

retrieved

3 April 2020

PubMed publication ID

29953200

1 reference

stated in

Europe PubMed Central

PMC publication ID

6302314

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29953200%20AND%20SRC:MED&resulttype=core&format=json

retrieved

3 April 2020

 

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