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- 2024
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Mark
Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces
2024) In ACS Chemical Neuroscience(
- Contribution to journal › Article
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Mark
The role of shear forces in primary and secondary nucleation of amyloid fibrils
2024) In Proceedings of the National Academy of Sciences of the United States of America 121(25). p.2322572121-2322572121(
- Contribution to journal › Article
- 2022
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Mark
Uncovering the universality of self-replication in protein aggregation and its link to disease
(
- Contribution to journal › Article
- 2017
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Mark
Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants
(
- Contribution to journal › Article
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Mark
Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates
2017) In Proceedings of the National Academy of Sciences of the United States of America 114(30). p.8005-8010(
- Contribution to journal › Article
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Mark
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication
2017) In Proceedings of the National Academy of Sciences of the United States of America 114(25). p.6444-6449(
- Contribution to journal › Article
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Mark
Scaling behaviour and rate-determining steps in filamentous self-assembly
(
- Contribution to journal › Article
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Mark
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease
2017) In Proceedings of the National Academy of Sciences of the United States of America 114(2). p.200-208(
- Contribution to journal › Article
- 2016
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Mark
Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation
(
- Contribution to journal › Article
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Mark
Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide.
(
- Contribution to journal › Article
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Mark
A Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions
(
- Contribution to journal › Article
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Mark
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
(
- Contribution to journal › Article
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Mark
Physical determinants of the self-replication of protein fibrils
(
- Contribution to journal › Article
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Mark
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
(
- Contribution to journal › Article
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Mark
Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.
(
- Contribution to journal › Article
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Mark
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
(
- Contribution to journal › Article
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Mark
The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model
(
- Contribution to journal › Article
- 2015
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Mark
On the lag phase in amyloid fibril formation
(
- Contribution to journal › Article
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Mark
A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution
(
- Contribution to journal › Article
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Mark
The A beta 40 and A beta 42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation
(
- Contribution to journal › Article
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Mark
Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity
(
- Contribution to journal › Article
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Mark
Protein Microgels from Amyloid Fibril Networks
(
- Contribution to journal › Article
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Mark
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
(
- Contribution to journal › Article
- 2014
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Mark
Quantification of the Concentration of A beta 42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay
(
- Contribution to journal › Article
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Mark
Solution conditions determine the relative importance of nucleation and growth processes in alpha-synuclein aggregation
(
- Contribution to journal › Article
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Mark
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.
(
- Contribution to journal › Article
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Mark
Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.
(
- Contribution to journal › Article
- 2013
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Mark
Single-molecule measurements of transient biomolecular complexes through microfluidic dilution
(
- Contribution to journal › Article
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Mark
Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism
(
- Contribution to journal › Article