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Phase 1/1b Studies of UCB0599, an Oral Inhibitor of α‐Synuclein Misfolding, Including a Randomized Study in Parkinson's Disease

Movement disorders, 2022-10, Vol.37 (10), p.2045-2056

2022

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In vivo effects of the alpha-synuclein misfolding inhibitor minzasolmin supports clinical development in Parkinson's disease

NPJ Parkinson's Disease, 2023-07, Vol.9 (1), p.114-114, Article 114

2023

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Reply to Matters Arising: In vivo effects of the alpha-synuclein misfolding inhibitor minzasolmin supports clinical development in Parkinson's disease

NPJ Parkinson's Disease, 2024-03, Vol.10 (1), p.60-60, Article 60

2024

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Evidence that the 42- and 40-Amino Acid Forms of Amyloid β Protein are Generated from the β -amyloid Precursor Protein by Different Protease Activities

Proceedings of the National Academy of Sciences - PNAS, 1996-11, Vol.93 (23), p.13170-13175

1996

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Preclinical In Vivo Characterization of UCB0599, an Orally Available, Small Molecule Inhibitor of α-Synuclein Misfolding in Development for Parkinson’s Disease (S36.007)

Neurology, 2022-05, Vol.98 (18_supplement)

2022

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Anti-inflammatory drug therapy alters beta-amyloid processing and deposition in an animal model of Alzheimer's disease

The Journal of neuroscience, 2003-08, Vol.23 (20), p.7504-7509

2003

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β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Science (American Association for the Advancement of Science), 1999-10, Vol.286 (5440), p.735-741

1999

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alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease

The Journal of biological chemistry, 1999-07, Vol.274 (28), p.19509-19512

1999

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Permeability and Residual Plasma Volume of Human, Dutch Variant, and Rat Amyloid β-Protein 1-40 at the Blood–Brain Barrier

Neurobiology of disease, 1997, Vol.4 (1), p.27-34

1997

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Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation

The Journal of biological chemistry, 1999-04, Vol.274 (14), p.9843-9846

1999

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Co-expression of β-amyloid precursor protein (βAPP) and apolipoprotein E in cell culture: analysis of βAPP processing

Neurobiology of disease, 1995-06, Vol.2 (3), p.177-187

1995

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Oxidative Dimer Formation Is the Critical Rate-Limiting Step for Parkinson's Disease α-Synuclein Fibrillogenesis

Biochemistry (Easton), 2003-01, Vol.42 (3), p.829-837

2003

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Amyloid β-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma

The Journal of biological chemistry, 1996-12, Vol.271 (51), p.32916-32922

1996

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Parkinson's Disease-associated α-Synuclein Is More Fibrillogenic than β- and γ-Synuclein and Cannot Cross-seed Its Homologs

The Journal of biological chemistry, 2000-11, Vol.275 (44), p.34574-34579

2000

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[25] Analysis of fibril elongation using surface plasmon resonance biosensors

Methods in Enzymology, 1999, Vol.309, p.386-402

1999

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Î±-Synuclein Fibrillogenesis Is Nucleation-dependent

The Journal of biological chemistry, 1999-07, Vol.274 (28), p.19509

1999

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α-Synuclein Fibrillogenesis Is Nucleation-dependent

The Journal of biological chemistry, 1999-07, Vol.274 (28), p.19509-19512

1999

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Parkinson's Disease-associated Î±-Synuclein Is More Fibrillogenic than Î²- and Î³-Synuclein and Cannot Cross-seed Its Homologs

The Journal of biological chemistry, 2000-11, Vol.275 (44), p.34574

2000

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Both familial Parkinson's disease mutations accelerate α-synuclein aggregation

The Journal of biological chemistry, 1999-05, Vol.274 (19), p.13728-13728

1999

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Transcriptional control via translational repression by c4 antisense RNA of bacteriophages P1 and P7

Genes & development, 1992-12, Vol.6 (12A), p.2409-2416

1992

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Both Familial Parkinsonâs Disease Mutations Accelerate Î±-Synuclein Aggregation

The Journal of biological chemistry, 1999-04, Vol.274 (14), p.9843

1999

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Amyloid Î²-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma

The Journal of biological chemistry, 1996-12, Vol.271 (51), p.32916

1996

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[Beta]-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Science (American Association for the Advancement of Science), 1999-10, Vol.286 (5440), p.735-735

1999

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Anti-Inflammatory Drug Therapy Alters {beta}-Amyloid Processing and Deposition in an Animal Model of Alzheimer's Disease

The Journal of neuroscience, 2003-08, Vol.23 (20), p.7504

2003

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Phase 1/1b Studies of UCB0599, an Oral Inhibitor of α‐Synuclein Misfolding, Including a Randomized Study in Parkinson's Disease

In vivo effects of the alpha-synuclein misfolding inhibitor minzasolmin supports clinical development in Parkinson's disease

Reply to Matters Arising: In vivo effects of the alpha-synuclein misfolding inhibitor minzasolmin supports clinical development in Parkinson's disease

Evidence that the 42- and 40-Amino Acid Forms of Amyloid β Protein are Generated from the β -amyloid Precursor Protein by Different Protease Activities

Preclinical In Vivo Characterization of UCB0599, an Orally Available, Small Molecule Inhibitor of α-Synuclein Misfolding in Development for Parkinson’s Disease (S36.007)

Anti-inflammatory drug therapy alters beta-amyloid processing and deposition in an animal model of Alzheimer's disease

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease

Permeability and Residual Plasma Volume of Human, Dutch Variant, and Rat Amyloid β-Protein 1-40 at the Blood–Brain Barrier

Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation

Co-expression of β-amyloid precursor protein (βAPP) and apolipoprotein E in cell culture: analysis of βAPP processing

Oxidative Dimer Formation Is the Critical Rate-Limiting Step for Parkinson's Disease α-Synuclein Fibrillogenesis

Amyloid β-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma

Parkinson's Disease-associated α-Synuclein Is More Fibrillogenic than β- and γ-Synuclein and Cannot Cross-seed Its Homologs

[25] Analysis of fibril elongation using surface plasmon resonance biosensors

Î±-Synuclein Fibrillogenesis Is Nucleation-dependent

α-Synuclein Fibrillogenesis Is Nucleation-dependent

Parkinson's Disease-associated Î±-Synuclein Is More Fibrillogenic than Î²- and Î³-Synuclein and Cannot Cross-seed Its Homologs

Both familial Parkinson's disease mutations accelerate α-synuclein aggregation

Transcriptional control via translational repression by c4 antisense RNA of bacteriophages P1 and P7

Both Familial Parkinsonâs Disease Mutations Accelerate Î±-Synuclein Aggregation

Amyloid Î²-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma

[Beta]-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Anti-Inflammatory Drug Therapy Alters {beta}-Amyloid Processing and Deposition in an Animal Model of Alzheimer's Disease

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