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A century-old debate on protein aggregation and neurodegeneration enters the clinic

Nature, 2006-10, Vol.443 (7113), p.774-779

2006

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Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders

Annual review of neuroscience, 2003-01, Vol.26, p.267-298

2003

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Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

The Journal of biological chemistry, 2008-06, Vol.283 (24), p.16895-16905

2008

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Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct

Science (American Association for the Advancement of Science), 2001-11, Vol.294 (5545), p.1346-1349

2001

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Membrane-associated farnesylated UCH-L1 promotes α-synuclein neurotoxicity and is a therapeutic target for Parkinson's disease

Proceedings of the National Academy of Sciences - PNAS, 2009-03, Vol.106 (12), p.4635-4640

2009

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Evolution of Amyloid: What Normal Protein Folding May Tell Us about Fibrillogenesis and Disease

Proceedings of the National Academy of Sciences - PNAS, 1999-03, Vol.96 (7), p.3342-3344

Lansbury, Peter T.

1999

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Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

Quarterly reviews of biophysics, 2006-05, Vol.39 (2), p.167-201

2006

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Stress-Induced Cellular Clearance Is Mediated by the SNARE Protein ykt6 and Disrupted by α-Synuclein

Neuron (Cambridge, Mass.), 2019-12, Vol.104 (5), p.869-884.e11

2019

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Reversible Monoubiquitination Regulates the Parkinson Disease-associated Ubiquitin Hydrolase UCH-L1

The Journal of biological chemistry, 2007-04, Vol.282 (14), p.10567-10575

2007

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Farnesyltransferase inhibitor LNK-754 attenuates axonal dystrophy and reduces amyloid pathology in mice

Molecular neurodegeneration, 2022-08, Vol.17 (1), p.54-54, Article 54

2022

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The First N-terminal Amino Acids of α-Synuclein Are Essential for α-Helical Structure Formation In Vitro and Membrane Binding in Yeast

Journal of molecular biology, 2009-06, Vol.389 (2), p.413-424

2009

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Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity

Journal of molecular biology, 2007-03, Vol.366 (5), p.1510-1522

2007

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Amyloid Diseases: Abnormal Protein Aggregation in Neurodegeneration

Proceedings of the National Academy of Sciences - PNAS, 1999-08, Vol.96 (18), p.9989-9990

1999

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Zeroing in on the Pathogenic Form of α-Synuclein and Its Mechanism of Neurotoxicity in Parkinson's Disease

Biochemistry (Easton), 2003-07, Vol.42 (26), p.7871-7878

2003

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Small-Molecule-Mediated Stabilization of Familial Amyotrophic Lateral Sclerosis-Linked Superoxide Dismutase Mutants against Unfolding and Aggregation

Proceedings of the National Academy of Sciences - PNAS, 2005-03, Vol.102 (10), p.3639-3644

2005

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Neurodegenerative disease Amyloid pores from pathogenic mutations

Nature (London), 2002-07, Vol.418 (6895), p.291-291

2002

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The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility

Cell, 2002-10, Vol.111 (2), p.209-218

2002

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N‐terminal deletion does not affect α‐synuclein membrane binding, self‐association and toxicity in human neuroblastoma cells, unlike yeast

Journal of neurochemistry, 2011-10, Vol.119 (2), p.389-397

2011

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α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils

Journal of molecular biology, 2002-10, Vol.322 (5), p.1089-1102

2002

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Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like Mechanism

Biochemistry (Easton), 2002-04, Vol.41 (14), p.4595-4602

2002

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MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE:Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins

Annual review of biochemistry, 1997, Vol.66 (1), p.385-407

1997

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The Impact of the E46K Mutation on the Properties of α-Synuclein in Its Monomeric and Oligomeric States

Biochemistry (Easton), 2007-06, Vol.46 (24), p.7107-7118

2007

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Protofibrillar Islet Amyloid Polypeptide Permeabilizes Synthetic Vesicles by a Pore-like Mechanism that May Be Relevant to Type II Diabetes

Biochemistry (Easton), 2002-09, Vol.41 (38), p.11338-11343

2002

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Structural Basis for Conformational Plasticity of the Parkinson's Disease-Associated Ubiquitin Hydrolase UCH-L1

Proceedings of the National Academy of Sciences - PNAS, 2006-03, Vol.103 (12), p.4675-4680

2006

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Annular α-Synuclein Protofibrils Are Produced When Spherical Protofibrils Are Incubated in Solution or Bound to Brain-Derived Membranes

Biochemistry (Easton), 2002-08, Vol.41 (32), p.10209-10217

2002

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A century-old debate on protein aggregation and neurodegeneration enters the clinic

Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders

Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct

Membrane-associated farnesylated UCH-L1 promotes α-synuclein neurotoxicity and is a therapeutic target for Parkinson's disease

Evolution of Amyloid: What Normal Protein Folding May Tell Us about Fibrillogenesis and Disease

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

Stress-Induced Cellular Clearance Is Mediated by the SNARE Protein ykt6 and Disrupted by α-Synuclein

Reversible Monoubiquitination Regulates the Parkinson Disease-associated Ubiquitin Hydrolase UCH-L1

Farnesyltransferase inhibitor LNK-754 attenuates axonal dystrophy and reduces amyloid pathology in mice

The First N-terminal Amino Acids of α-Synuclein Are Essential for α-Helical Structure Formation In Vitro and Membrane Binding in Yeast

Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity

Amyloid Diseases: Abnormal Protein Aggregation in Neurodegeneration

Zeroing in on the Pathogenic Form of α-Synuclein and Its Mechanism of Neurotoxicity in Parkinson's Disease

Small-Molecule-Mediated Stabilization of Familial Amyotrophic Lateral Sclerosis-Linked Superoxide Dismutase Mutants against Unfolding and Aggregation

Neurodegenerative disease Amyloid pores from pathogenic mutations

The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility

N‐terminal deletion does not affect α‐synuclein membrane binding, self‐association and toxicity in human neuroblastoma cells, unlike yeast

α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils

Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like Mechanism

MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE:Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins

The Impact of the E46K Mutation on the Properties of α-Synuclein in Its Monomeric and Oligomeric States

Protofibrillar Islet Amyloid Polypeptide Permeabilizes Synthetic Vesicles by a Pore-like Mechanism that May Be Relevant to Type II Diabetes

Structural Basis for Conformational Plasticity of the Parkinson's Disease-Associated Ubiquitin Hydrolase UCH-L1

Annular α-Synuclein Protofibrils Are Produced When Spherical Protofibrils Are Incubated in Solution or Bound to Brain-Derived Membranes

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