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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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Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease

Biochemistry (Easton), 2001-07, Vol.40 (26), p.7812-7819

2001

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Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

Biochemistry (Easton), 2000-03, Vol.39 (10), p.2552-2563

2000

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NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

Biochemistry (Easton), 1996-10, Vol.35 (43), p.13709-13715

1996

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Seeding one-dimensional crystallization of amyloid : a pathogenic mechanism in Alzheimer's disease and scrapie ?

Cell, 1993-06, Vol.73 (6), p.1055-1058

1993

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Acceleration of Oligomerization, Not Fibrillization, Is a Shared Property of Both α -Synuclein Mutations Linked to Early-Onset Parkinson's Disease: Implications for Pathogenesis and Therapy

Proceedings of the National Academy of Sciences - PNAS, 2000-01, Vol.97 (2), p.571-576

2000

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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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Inhibition of Fibrillization and Accumulation of Prefibrillar Oligomers in Mixtures of Human and Mouse α-Synuclein

Biochemistry (Easton), 2000-09, Vol.39 (35), p.10619-10626

2000

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Amyloid fibrillogenesis: themes and variations

Current Opinion in Structural Biology, 2000-02, Vol.10 (1), p.60-68

2000

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A detergent-insoluble membrane compartment contains A beta in vivo

Nature medicine, 1998-06, Vol.4 (6), p.730-734

1998

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Is there a cause-and-effect relationship between α -synuclein fibrillization and Parkinson's disease?

Nature cell biology, 2000-07, Vol.2 (7), p.E115-E119

2000

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The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Biochemistry (Easton), 1993-05, Vol.32 (18), p.4693-4697

1993

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A Kinetic Model for Amyloid Formation in the Prion Diseases: Importance of Seeding

Proceedings of the National Academy of Sciences - PNAS, 1993-07, Vol.90 (13), p.5959-5963

1993

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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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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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Accelerated Oligomerization by Parkinson's Disease Linked α-Synuclein Mutants

Annals of the New York Academy of Sciences, 2000-01, Vol.920 (1), p.42-45

2000

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Structural neurology: are seeds at the root of neuronal degeneration?

Neuron (Cambridge, Mass.), 1997-12, Vol.19 (6), p.1151-1154

Lansbury, Jr, P T

1997

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Species Specificity in the Cell-Free Conversion of Prion Protein to Protease-Resistant Forms: A Model for the Scrapie Species Barrier

Proceedings of the National Academy of Sciences - PNAS, 1995-04, Vol.92 (9), p.3923-3927

1995

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Apolipoprotein E is a Kinetic But not as a Thermodynamic Inhibitor of Amyloid Formation: Implications for the Pathogenesis and Treatment of Alzheimer Disease

Proceedings of the National Academy of Sciences - PNAS, 1995-01, Vol.92 (3), p.763-767

1995

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Molecular assessment of the potential transmissibilities of BSE and scrapie to humans

Nature (London), 1997-07, Vol.388 (6639), p.285-288

1997

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Cell-free formation of protease-resistant prion protein

Nature (London), 1994-08, Vol.370 (6489), p.471-474

1994

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Synthesis and Amyloid Binding Properties of Rhenium Complexes: Preliminary Progress Toward a Reagent for SPECT Imaging of Alzheimer's Disease Brain

Journal of medicinal chemistry, 1999-07, Vol.42 (15), p.2805-2815

1999

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Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB

Biochemistry (Easton), 1992-12, Vol.31 (49), p.12345-12352

1992

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Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's Disease

Biochemistry (Easton), 1999-07, Vol.38 (28), p.8972-8980

1999

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Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies

Journal of Virology, 1997-05, Vol.71 (5), p.4107-4110

1997

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

Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease

Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

Seeding one-dimensional crystallization of amyloid : a pathogenic mechanism in Alzheimer's disease and scrapie ?

Acceleration of Oligomerization, Not Fibrillization, Is a Shared Property of Both α -Synuclein Mutations Linked to Early-Onset Parkinson's Disease: Implications for Pathogenesis and Therapy

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

Inhibition of Fibrillization and Accumulation of Prefibrillar Oligomers in Mixtures of Human and Mouse α-Synuclein

Amyloid fibrillogenesis: themes and variations

A detergent-insoluble membrane compartment contains A beta in vivo

Is there a cause-and-effect relationship between α -synuclein fibrillization and Parkinson's disease?

The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

A Kinetic Model for Amyloid Formation in the Prion Diseases: Importance of Seeding

Amyloid Diseases: Abnormal Protein Aggregation in Neurodegeneration

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

Accelerated Oligomerization by Parkinson's Disease Linked α-Synuclein Mutants

Structural neurology: are seeds at the root of neuronal degeneration?

Species Specificity in the Cell-Free Conversion of Prion Protein to Protease-Resistant Forms: A Model for the Scrapie Species Barrier

Apolipoprotein E is a Kinetic But not as a Thermodynamic Inhibitor of Amyloid Formation: Implications for the Pathogenesis and Treatment of Alzheimer Disease

Molecular assessment of the potential transmissibilities of BSE and scrapie to humans

Cell-free formation of protease-resistant prion protein

Synthesis and Amyloid Binding Properties of Rhenium Complexes: Preliminary Progress Toward a Reagent for SPECT Imaging of Alzheimer's Disease Brain

Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB

Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's Disease

Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies

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