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- 2021
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Mark
Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation
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- Contribution to journal › Article
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Expression, purification and characterisation of large quantities of recombinant human IAPP for mechanistic studies
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- Contribution to journal › Article
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A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
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- Contribution to journal › Article
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Proliferation of Tau 304-380 Fragment Aggregates through Autocatalytic Secondary Nucleation
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- Contribution to journal › Article
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Mark
Transient Lipid-Protein Structures and Selective Ganglioside Uptake During α-Synuclein-Lipid Co-aggregation
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- Contribution to journal › Article
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Mark
Solubility of Aβ40 peptide
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- Contribution to journal › Article
- 2020
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The catalytic nature of protein aggregation
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- Contribution to journal › Article
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Single Step Purification of Glycogen Synthase Kinase Isoforms from Small Scale Transient Expression in HEK293 Cells with a Calcium-Dependent Fragment Complementation System
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- Contribution to journal › Article
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Mark
The properties of α-synuclein secondary nuclei are dominated by the solution conditions rather than the seed fibril strain
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- Contribution to journal › Article
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Mark
Anomalous Salt Dependence Reveals an Interplay of Attractive and Repulsive Electrostatic Interactions in α-synuclein Fibril Formation
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- Contribution to journal › Article
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Mark
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
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- Contribution to journal › Article
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Mark
The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils
2020) In Proceedings of the National Academy of Sciences of the United States of America 117(41). p.25272-25283(
- Contribution to journal › Article
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Mark
On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide
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- Contribution to journal › Article
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Mark
Kinetic diversity of amyloid oligomers
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- Contribution to journal › Article
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Mark
Identification of on- And off-pathway oligomers in amyloid fibril formation
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- Contribution to journal › Article