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- 2024
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Mark
Kinetic models reveal the interplay of protein production and aggregation
2024) In Chemical Science(
- Contribution to journal › Article
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Mark
Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites
2024) In Proceedings of the National Academy of Sciences of the United States of America 121(7). p.2220075121-2220075121(
- Contribution to journal › Article
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Mark
A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions
(
- Contribution to journal › Article
- 2023
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Mark
Amyloid formation as a protein phase transition
(
- Contribution to journal › Scientific review
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Mark
A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ42 Aggregation
(
- Contribution to journal › Article
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Mark
Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates
(
- Contribution to journal › Article
- 2022
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Mark
Influence of denaturants on amyloid β42 aggregation kinetics
(
- Contribution to journal › Article
- 2021
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Mark
The unhappy chaperone
(
- Contribution to journal › Article
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Mark
Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation
(
- Contribution to journal › Article
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Mark
pH-Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide
(
- Contribution to journal › Article
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Mark
Proliferation of Tau 304-380 Fragment Aggregates through Autocatalytic Secondary Nucleation
(
- Contribution to journal › Article
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Mark
Surface-Catalyzed Secondary Nucleation Dominates the Generation of Toxic IAPP Aggregates
(
- Contribution to journal › Article
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Mark
Elongation rate and average length of amyloid fibrils in solution using isotope-labelled small-angle neutron scattering
(
- Contribution to journal › Article
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Mark
A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
(
- Contribution to journal › Article
- 2020
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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
The catalytic nature of protein aggregation
(
- Contribution to journal › Article
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Mark
Identification of on- And off-pathway oligomers in amyloid fibril formation
(
- Contribution to journal › Article
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Mark
Ultrastructural evidence for self-replication of alzheimer-associated Aβ42 amyloid along the sides of fibrils
2020) In Proceedings of the National Academy of Sciences of the United States of America 117(21). p.11265-11273(
- Contribution to journal › Article
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Mark
A microfluidic strategy for the detection of membrane protein interactions
(
- Contribution to journal › Article
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Mark
Kinetic diversity of amyloid oligomers
(
- Contribution to journal › Article
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Mark
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
2020) In Proceedings of the National Academy of Sciences of the United States of America 117(39). p.24251-24257(
- Contribution to journal › Article
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Mark
Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
(
- Contribution to journal › Article
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Mark
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation
(
- Contribution to journal › Article
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Mark
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
(
- Contribution to journal › Article
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Mark
On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide
(
- Contribution to journal › Article
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Mark
Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies
(
- Contribution to journal › Article
- 2019
-
Mark
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli
(
- Contribution to journal › Article
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Mark
Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid
(
- Contribution to journal › Article
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Mark
Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42
2019) In ACS Chemical Neuroscience(
- Contribution to journal › Article
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Mark
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-b aggregates
(
- Contribution to journal › Article
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Mark
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
(
- Contribution to journal › Article
- 2018
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Mark
Kinetic analysis of amyloid formation
(
- Chapter in Book/Report/Conference proceeding › Book chapter
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Mark
On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations
2018) In Proceedings of the National Academy of Sciences of the United States of America 115(26). p.5849-5858(
- Contribution to journal › Article
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Mark
Secondary nucleation in amyloid formation
(
- Contribution to journal › Article
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Mark
SAR by kinetics for drug discovery in protein misfolding diseases
2018) In Proceedings of the National Academy of Sciences of the United States of America 115(41). p.10245-10250(
- Contribution to journal › Article
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Mark
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide
(
- Contribution to journal › Article
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Mark
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes
(
- Contribution to journal › Article
- 2017
-
Mark
Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method
(
- Contribution to journal › Article
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Mark
Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification
(
- Contribution to journal › Article
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Mark
On-chip label-free protein analysis with downstream electrodes for direct removal of electrolysis products
(
- Contribution to journal › Article