Sabine M. Ulamec
Leeds, ENG, United Kingdom
Last Updated: 09/26/2026
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Found 8 publications
In silico peptide self-assembly reveals the importance of N-terminal motifs and the inhibition mechanism of the mutation L38M in α-synuclein fibrillation.
Journal: Protein science : a publication of the Protein Society
Published: June 20, 2025
Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: August 12, 2024
Visualizing Viral RNA Packaging Signals in Action.
Journal: Journal of molecular biology
Published: August 01, 2024
Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: January 03, 2024
Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein.
Journal: Nature communications
Published: October 29, 2021
Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins.
Journal: Frontiers in neuroscience
Published: September 28, 2020
Spot the Difference: Function versus Toxicity in Amyloid Fibrils.
Journal: Trends in biochemical sciences
Published: March 29, 2020
A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function.
A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function.
Journal: Nature structural & molecular biology
Published: July 30, 2019
Showing 1-8 of 8
Last Updated: 09/26/2026