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The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

Nature communications, 2021-03, Vol.12 (1), p.1814-16, Article 1814

2021

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α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity

Nature communications, 2021-06, Vol.12 (1), p.3752-14, Article 3752

2021

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The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases

Neurobiology of disease, 2018-01, Vol.109 (Pt B), p.178-190

2018

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Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

Science (American Association for the Advancement of Science), 2017-12, Vol.358 (6369), p.1440-1443

2017

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The role of water in the primary nucleation of protein amyloid aggregation

Biophysical chemistry, 2021-02, Vol.269, p.106520, Article 106520

2021

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Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease

International journal of molecular sciences, 2020-10, Vol.21 (21), p.8043

2020

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

Proceedings of the National Academy of Sciences - PNAS, 2015-04, Vol.112 (16), p.E1994-E2003

2015

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

Proceedings of the National Academy of Sciences - PNAS, 2016-03, Vol.113 (9), p.E1206-E1215

2016

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Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

Nature communications, 2022-08, Vol.13 (1), p.4586-16, Article 4586

2022

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

Scientific reports, 2015-11, Vol.5 (1), p.16696, Article 16696

2015

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Characterisation of Amyloid Aggregation and Inhibition by Diffusion-Based Single-Molecule Fluorescence Techniques

Biophysica, 2022-12, Vol.2 (4), p.506-524

2022

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Antiparasitic Drug Nitazoxanide Inhibits the Pyruvate Oxidoreductases of Helicobacter pylori, Selected Anaerobic Bacteria and Parasites, and Campylobacter jejuni

Antimicrobial Agents and Chemotherapy, 2007-03, Vol.51 (3), p.868-876

2007

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Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria

The Journal of clinical investigation, 2008-08, Vol.118 (8), p.2858-2867

2008

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The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity

Molecules (Basel, Switzerland), 2022-02, Vol.27 (4), p.1293

2022

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Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain

PloS one, 2013-06, Vol.8 (6), p.e67961-e67961

2013

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Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

Communications biology, 2020-08, Vol.3 (1), p.435-435, Article 435

2020

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Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation

Journal of the American Chemical Society, 2011-05, Vol.133 (20), p.7737-7743

2011

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Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Journal of the American Chemical Society, 2010-11, Vol.132 (44), p.15580-15588

2010

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Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies

Cellular and molecular life sciences : CMLS, 2022-03, Vol.79 (3), p.174-174, Article 174

2022

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The Flavodoxin from Helicobacter pylori: Structural Determinants of Thermostability and FMN Cofactor Binding

Biochemistry (Easton), 2008-01, Vol.47 (2), p.627-639

2008

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The native-state ensemble of proteins provides clues for folding, misfolding and function

Trends in biochemical sciences (Amsterdam. Regular ed.), 2006-09, Vol.31 (9), p.494-496

2006

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Flavodoxin:Quinone Reductase (FqrB): a Redox Partner of Pyruvate:Ferredoxin Oxidoreductase That Reversibly Couples Pyruvate Oxidation to NADPH Production in Helicobacter pylori and Campylobacter jejuni

Journal of Bacteriology, 2007-07, Vol.189 (13), p.4764-4773

2007

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Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases

Accounts of chemical research, 2023-06, Vol.56 (12), p.1395-1405

2023

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Filling Small, Empty Protein Cavities: Structural and Energetic Consequences

Journal of molecular biology, 2006-05, Vol.358 (3), p.701-712

2006

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The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity

The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

The role of water in the primary nucleation of protein amyloid aggregation

Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease

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

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

Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

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

Characterisation of Amyloid Aggregation and Inhibition by Diffusion-Based Single-Molecule Fluorescence Techniques

Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease

Antiparasitic Drug Nitazoxanide Inhibits the Pyruvate Oxidoreductases of Helicobacter pylori, Selected Anaerobic Bacteria and Parasites, and Campylobacter jejuni

Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria

The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation

Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies

The Flavodoxin from Helicobacter pylori: Structural Determinants of Thermostability and FMN Cofactor Binding

The native-state ensemble of proteins provides clues for folding, misfolding and function

Flavodoxin:Quinone Reductase (FqrB): a Redox Partner of Pyruvate:Ferredoxin Oxidoreductase That Reversibly Couples Pyruvate Oxidation to NADPH Production in Helicobacter pylori and Campylobacter jejuni

Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases

Filling Small, Empty Protein Cavities: Structural and Energetic Consequences

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