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Cover Image for Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells

Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells

W Chen, LJ Young, M Lu, A Zaccone, F Ströhl, N Yu, GS Kaminski Schierle, CF Kaminski

Feb 24, 2017

FLIM SIM Self-quenching amyloid aggregation Super-resolution

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Structural characterization of toxic oligomers that are kinetically trapped during alpha-synuclein fibril formation

Serene W Chen, Srdja Drakulic, Emma Deas, Myriam M Ouberai, Francesco A Aprile, Rocío Arranz, Samuel Ness, Cintia Roodveldt, Tim Guilliams, Genst Erwin De, David Klenerman, Nicholas W Wood, Tuomas PJ Knowles, Carlos Alfonso, Germán Rivas, Andrey Y Abramov, José María Valpuesta, Christopher M Dobson, Nunilo Cremades

May 21, 2015

amyloid aggregation Cryoelectron Microscopy neurodegeneration protein misfolding toxic oligomer

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Library-Derived Peptide Aggregation Modulators of Parkinson's Disease Early-Onset α-Synuclein Variants

Kathryn J. C. Watt, Richard M. Meade, Robert J. Williams, Jody M. Mason

Jun 15, 2022

Parkinson's Disease (PD) is characterized by the accumulation of Lewy bodies in dopaminergic neurons. The main protein component of Lewy bodies, α-synuclein (αS), is also firmly linked to PD through the identification of a...

amyloid aggregation early-onset Parkinson's disease Peptides /dk/atira/pure/subjectarea/asjc/1300/1303 name=Biochemistry /dk/atira/pure/subjectarea/asjc/1300/1314 name=Physiology /dk/atira/pure/subjectarea/asjc/2800/2805 name=Cognitive Neuroscience /dk/atira/pure/subjectarea/asjc/1300/1307 name=Cell Biology

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Anionic lipid vesicles have differential effects on the aggregation of early onset-associated α-synuclein missense mutants

Kathryn J. C. Watt, Richard M. Meade, Robert J. Williams, Jody M. Mason

Dec 31, 2022

α-synuclein (αS) is the key component of synucleinopathies such as Parkinson's disease (PD), dementia with Lewy bodies, and multiple system atrophy. αS was first linked to PD through the identification of point mutations in...

amyloid aggregation early onset Parkinson's disease Lipid vesicles Peptide /dk/atira/pure/subjectarea/asjc/1300/1303 name=Biochemistry /dk/atira/pure/subjectarea/asjc/1300/1312 name=Molecular Biology /dk/atira/pure/subjectarea/asjc/1300/1307 name=Cell Biology

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

Marija Iljina, Gonzalo A Garcia, Mathew H Horrocks, Laura Tosatto, Minee L Choi, Kristina A Ganzinger, Andrey Y Abramov, Sonia Gandhi, Nicholas W Wood, Nunilo Cremades, Christopher M Dobson, Tuomas PJ Knowles, David Klenerman

Feb 04, 2016

amyloid aggregation kinetic analysis neurodegeneration prion-like propagation templated seeding Fluorescence Resonance Energy Transfer Kinetics Models Biological Prions Reactive Oxygen Species ALPHA-SYNUCLEIN

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Library-Derived Peptide Aggregation Modulators of Parkinson's Disease Early-Onset α-Synuclein Variants

Kathryn J. C. Watt, Richard M. Meade, Robert J. Williams, Jody M. Mason

Jun 15, 2022

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Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation

Mantas Ziaunys, Andrius Sakalauskas, Tomas Sneideris, Vytautas Smirnovas

Feb 11, 2021

Protein aggregation into amyloid fibrils is linked to multiple disorders. The understanding of how natively non-harmful proteins convert to these highly cytotoxic amyloid aggregates is still not sufficient, with new ideas and...

insulin fibrils lysozyme fibrils amyloid aggregation aggregation mechanism

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Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation.

Mantas Ziaunys, Andrius Sakalauskas, Tomas Sneideris, Vytautas Smirnovas

May 03, 2021

aggregation mechanism amyloid aggregation insulin fibrils lysozyme fibrils Amyloid Animals Chickens Humans Insulin Muramidase Protein Aggregates protein aggregation Pathological Recombinant Proteins

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Cover Image for A downsized and optimised intracellular library-derived peptide prevents alpha-synuclein primary nucleation and toxicity without impacting upon lipid binding

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A downsized and optimised intracellular library-derived peptide prevents alpha-synuclein primary nucleation and toxicity without impacting upon lipid binding

Richard M. Meade, Kathryn J. C. Watt, Robert J. Williams, Jody M. Mason

Dec 03, 2021

Misfolding and aggregation of alpha-synuclein (αS) within dopaminergic neurons is a key factor in the development and progression of a group of age-related neurodegenerative diseases, termed synucleinopathies, that include...

Parkinson's Disease amyloid aggregation Lipid vesicles Peptide primary nucleation /dk/atira/pure/subjectarea/asjc/1300/1304 name=Biophysics /dk/atira/pure/subjectarea/asjc/1300/1315 name=Structural Biology /dk/atira/pure/subjectarea/asjc/1300/1312 name=Molecular Biology

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A downsized and optimised intracellular library-derived peptide prevents alpha-synuclein primary nucleation and toxicity without impacting upon lipid binding

Richard M. Meade, Kathryn J. C. Watt, Robert J. Williams, Jody M. Mason

Dec 03, 2021

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Anionic lipid vesicles have differential effects on the aggregation of early onset-associated α-synuclein missense mutants

Kathryn J. C. Watt, Richard M. Meade, Robert J. Williams, Jody M. Mason

Dec 31, 2022

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