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α-Synuclein aggregation nucleates through liquid-liquid phase separation

Nature chemistry, 2020-08, Vol.12 (8), p.705

2020

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Structural and Functional Insights into α-Synuclein Fibril Polymorphism

Biomolecules (Basel, Switzerland), 2021-09, Vol.11 (10), p.1419

2021

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p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis

Cell death and differentiation, 2017-10, Vol.24 (10), p.1784-1798

2017

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Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease

PLoS pathogens, 2024-04, Vol.20 (4), p.e1012087-e1012087

2024

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α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis

Biochimica et biophysica acta. Proteins and proteomics, 2019-10, Vol.1867 (10), p.890-908

2019

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The G51D SNCA mutation generates a slowly progressive α-synuclein strain in early-onset Parkinson's disease

Acta neuropathologica communications, 2023-05, Vol.11 (1), p.72-72, Article 72

2023

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α-synuclein aggregation and its modulation

International journal of biological macromolecules, 2017-07, Vol.100, p.37-54

2017

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Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

Chemical communications (Cambridge, England), 2018, Vol.54 (29), p.3605-3608

2018

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Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease

PLoS pathogens, 2024-04, Vol.20 (4), p.e1012087

2024

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Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α‑Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation

Biochemistry (Easton), 2018-09, Vol.57 (35), p.5183-5187

2018

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Sensitized Emission Imaging Allows Nanoscale Surface Polarity Mapping of α‑Synuclein Amyloid Fibrils

ACS chemical neuroscience, 2024-01, Vol.15 (1), p.108-118

2024

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Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils

The Journal of biological chemistry, 2018-08, Vol.293 (34), p.12975-12991

2018

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Cytotoxic Oligomers and Fibrils Trapped in a Gel‐like State of α‐Synuclein Assemblies

Angewandte Chemie International Edition, 2018-05, Vol.57 (19), p.5262-5266

International ed. in English, 2018

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Direct Demonstration of Seed Size-Dependent α‑Synuclein Amyloid Amplification

The journal of physical chemistry letters, 2022-07, Vol.13 (28), p.6427-6438

2022

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The Familial α‑Synuclein A53E Mutation Enhances Cell Death in Response to Environmental Toxins Due to a Larger Population of Oligomers

Biochemistry (Easton), 2018-08, Vol.57 (33), p.5014-5028

2018

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Lipopolysaccharide from Gut Microbiota Modulates α‑Synuclein Aggregation and Alters Its Biological Function

ACS chemical neuroscience, 2019-05, Vol.10 (5), p.2229-2236

2019

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Iron-based nano-particles for Lipolase immobilization and stabilization

New biotechnology, 2014-07, Vol.31, p.S175-S175

2014

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α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties

Journal of molecular biology, 2022-10, Vol.434 (19), p.167761-167761, Article 167761

2022

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Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensitiesElectronic supplementary information (ESI) available. See DOI: 10.1039/c7cc09597j

2018-04

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Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate

Biomolecular NMR assignments, 2024-07

2024

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α‐Synuclein Spontaneously Adopts Stable and Reversible α‐Helical Structure in Water‐Less Environment

Chemphyschem, 2019-11, Vol.20 (21), p.2783-2790

2019

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Complexation of NAC-Derived Peptide Ligands with the C‑Terminus of α‑Synuclein Accelerates Its Aggregation

Biochemistry (Easton), 2018-02, Vol.57 (5), p.791-804

2018

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Effect of Disease-Associated P123H and V70M Mutations on β‑Synuclein Fibrillation

ACS chemical neuroscience, 2020-09, Vol.11 (18), p.2836-2848

2020

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Parkinson’s Disease Associated α‑Synuclein Familial Mutants Promote Dopaminergic Neuronal Death in Drosophila melanogaster

ACS chemical neuroscience, 2018-11, Vol.9 (11), p.2628-2638

2018

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α-Synuclein aggregation nucleates through liquid-liquid phase separation

Structural and Functional Insights into α-Synuclein Fibril Polymorphism

p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis

Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease

Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids

α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis

The G51D SNCA mutation generates a slowly progressive α-synuclein strain in early-onset Parkinson's disease

α-synuclein aggregation and its modulation

Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease

Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α‑Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation

Sensitized Emission Imaging Allows Nanoscale Surface Polarity Mapping of α‑Synuclein Amyloid Fibrils

Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils

Cytotoxic Oligomers and Fibrils Trapped in a Gel‐like State of α‐Synuclein Assemblies

Direct Demonstration of Seed Size-Dependent α‑Synuclein Amyloid Amplification

The Familial α‑Synuclein A53E Mutation Enhances Cell Death in Response to Environmental Toxins Due to a Larger Population of Oligomers

Lipopolysaccharide from Gut Microbiota Modulates α‑Synuclein Aggregation and Alters Its Biological Function

Iron-based nano-particles for Lipolase immobilization and stabilization

α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties

Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensitiesElectronic supplementary information (ESI) available. See DOI: 10.1039/c7cc09597j

Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate

α‐Synuclein Spontaneously Adopts Stable and Reversible α‐Helical Structure in Water‐Less Environment

Complexation of NAC-Derived Peptide Ligands with the C‑Terminus of α‑Synuclein Accelerates Its Aggregation

Effect of Disease-Associated P123H and V70M Mutations on β‑Synuclein Fibrillation

Parkinson’s Disease Associated α‑Synuclein Familial Mutants Promote Dopaminergic Neuronal Death in Drosophila melanogaster

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