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- 2024
-
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
- 2022
-
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
-
Mark
Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation
(
- Contribution to journal › Article
-
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
- 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
-
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
-
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
-
Mark
Kinetic diversity of amyloid oligomers
(
- Contribution to journal › Article
-
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
-
Mark
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
(
- Contribution to journal › Article
-
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
-
Mark
Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid
(
- Contribution to journal › Article
-
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
-
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
- 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
Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification
(
- 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
-
Mark
Scaling behaviour and rate-determining steps in filamentous self-assembly
(
- Contribution to journal › Article
- 2016
-
Mark
Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide.
(
- Contribution to journal › Article
-
Mark
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
(
- Contribution to journal › Article
-
Mark
Physical determinants of the self-replication of protein fibrils
(
- Contribution to journal › Article
- 2015
-
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
-
Mark
N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42.
(
- Contribution to journal › Article
- 2014
-
Mark
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.
(
- Contribution to journal › Article