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Hydrophobic, Aromatic, and Electrostatic Interactions Play a Central Role in Amyloid Fibril Formation and Stability

Biochemistry (Easton), 2011-03, Vol.50 (12), p.2061-2071

2011

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Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target

Frontiers in neurology, 2020-11, Vol.11, p.590754

2020

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PrP Knockout Cells Expressing Transmembrane PrP Resist Prion Infection

Journal of virology, 2017-01, Vol.91 (2)

2017

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The relationship between amyloid structure and cytotoxicity

Prion, 2014-03, Vol.8 (2), p.192-196

2014

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Misfolded amyloid-β-42 impairs the endosomal–lysosomal pathway

Cellular and molecular life sciences : CMLS, 2020-12, Vol.77 (23), p.5031-5043

2020

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Corrigendum: The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length tau

Frontiers in molecular biosciences, 2023-09, Vol.10, p.1276677-1276677

2023

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Structural integrity of beta-sheet assembly

Biochemical Society transactions, 2009-08, Vol.37 (Pt 4), p.671

2009

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The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides

Interface focus, 2017-12, Vol.7 (6), p.20170027-20170027

2017

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The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau

Frontiers in molecular biosciences, 2021-10, Vol.8, p.779240-779240

2021

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Internalisation and toxicity of amyloid‐β 1‐42 are influenced by its conformation and assembly state rather than size

FEBS letters, 2020-11, Vol.594 (21), p.3490-3503

2020

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Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid‐β 1‐42

FEBS letters, 2017-03, Vol.591 (5), p.822-830

2017

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The Common Architecture of Cross-β Amyloid

Journal of molecular biology, 2010-01, Vol.395 (4), p.717-727

2010

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Correlative cryo-soft X-ray tomography and cryo-structured illumination microscopy reveal changes to lysosomes in amyloid-β-treated neurons

Structure (London), 2024-05, Vol.32 (5), p.585-593.e3

2024

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Paired Helical Filament-Forming Region of Tau (297–391) Influences Endogenous Tau Protein and Accumulates in Acidic Compartments in Human Neuronal Cells

Journal of molecular biology, 2020-08, Vol.432 (17), p.4891-4907

2020

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A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration

Scientific reports, 2016-07, Vol.6 (1), p.30182, Article 30182

2016

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Characterizing the Assembly of the Sup35 Yeast Prion Fragment, GNNQQNY: Structural Changes Accompany a Fiber-to-Crystal Switch

Biophysical journal, 2010-01, Vol.98 (2), p.330-338

2010

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Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeation

FEBS letters, 2015-10, Vol.589 (21), p.3228-3236

2015

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Glycosylphosphatidylinositol Anchoring Directs the Assembly of Sup35NM Protein into Non-fibrillar, Membrane-bound Aggregates

The Journal of biological chemistry, 2014-05, Vol.289 (18), p.12245-12263

2014

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Fibres, crystals and polymorphism: the structural promiscuity of amyloidogenic peptides

Soft matter, 2010-01, Vol.6 (1), p.211-2114

2010

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Flow Linear Dichroism of Some Prototypical Proteins

Journal of the American Chemical Society, 2009-09, Vol.131 (37), p.13305-13314

2009

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Insights into the Structure of Amyloid Fibrils

The open biology journal, 2009-12, Vol.2 (1), p.185-192

2009

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Prions: Protein Rebels with a Cause

School science review, 2017-09, Vol.99 (366), p.51

2017

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Identification of zinc-binding ligands in the Class II fructose- 1,6-bisphosphate aldolase of Escherichia coli

FEBS letters, 1993-02, Vol.318 (1), p.11-16

1993

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Insights into the Structure of Amyloid Fibrils~!2009-04-21~!2009-07-09~!2010-01-02

The open biology journal, 2010-01, Vol.2 (2), p.185-192

2010

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Reagent Quality Control in Bacteriology: Cost-Effective, Easy-to-Use Methodology

Journal of Clinical Microbiology, 1981-07, Vol.14 (1), p.119-120

1981

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Hydrophobic, Aromatic, and Electrostatic Interactions Play a Central Role in Amyloid Fibril Formation and Stability

Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target

PrP Knockout Cells Expressing Transmembrane PrP Resist Prion Infection

The relationship between amyloid structure and cytotoxicity

Misfolded amyloid-β-42 impairs the endosomal–lysosomal pathway

Corrigendum: The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length tau

Structural integrity of beta-sheet assembly

The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides

The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau

Internalisation and toxicity of amyloid‐β 1‐42 are influenced by its conformation and assembly state rather than size

Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid‐β 1‐42

The Common Architecture of Cross-β Amyloid

Correlative cryo-soft X-ray tomography and cryo-structured illumination microscopy reveal changes to lysosomes in amyloid-β-treated neurons

Paired Helical Filament-Forming Region of Tau (297–391) Influences Endogenous Tau Protein and Accumulates in Acidic Compartments in Human Neuronal Cells

A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration

Characterizing the Assembly of the Sup35 Yeast Prion Fragment, GNNQQNY: Structural Changes Accompany a Fiber-to-Crystal Switch

Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeation

Glycosylphosphatidylinositol Anchoring Directs the Assembly of Sup35NM Protein into Non-fibrillar, Membrane-bound Aggregates

Fibres, crystals and polymorphism: the structural promiscuity of amyloidogenic peptides

Flow Linear Dichroism of Some Prototypical Proteins

Insights into the Structure of Amyloid Fibrils

Prions: Protein Rebels with a Cause

Identification of zinc-binding ligands in the Class II fructose- 1,6-bisphosphate aldolase of Escherichia coli

Insights into the Structure of Amyloid Fibrils~!2009-04-21~!2009-07-09~!2010-01-02

Reagent Quality Control in Bacteriology: Cost-Effective, Easy-to-Use Methodology

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