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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
-
Mark
Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces
2024) In ACS Chemical Neuroscience(
- Contribution to journal › Article
-
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
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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
Amyloids and protein aggregation
(
- Contribution to journal › Scientific review
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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
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Mark
Uncovering the universality of self-replication in protein aggregation and its link to disease
(
- 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
-
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
-
Mark
Kinetic analysis of amyloid formation
(
- Chapter in Book/Report/Conference proceeding › Book chapter
-
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
-
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
-
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
Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants
(
- Contribution to journal › Article
-
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
-
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
-
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
-
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
-
Mark
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
(
- Contribution to journal › Article
-
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
N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42.
(
- 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
-
Mark
Quantification of the Concentration of A beta 42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay
(
- Contribution to journal › Article
-
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
-
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
-
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