1 – 36 of 36
- show: 250
- |
- sort: year (new to old)
Close
Embed this list
<iframe src=""
width=""
height=""
allowtransparency="true"
frameborder="0">
</iframe>
- 2021
- A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
- 2020
- Structural characterization of covalently stabilized human cystatin c oligomers
- Kinetic diversity of amyloid oligomers
- Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
- Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
-
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation
Flagmeier, Patrick ; De, Suman ; Michaels, Thomas C.T. ; Yang, Xiaoting LU ; Dear, Alexander J. ; Emanuelsson, Cecilia LU
; Vendruscolo, Michele
; Linse, Sara
LU
; Klenerman, David
and Knowles, Tuomas P.J.
, et al.
(2020)
In Nature Structural and Molecular Biology
27(10).
p.886-891
Mark
- Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
- Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies
- 2019
- Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils
- Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42
- Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-b aggregates
- Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
- 2018
- SAR by kinetics for drug discovery in protein misfolding diseases
- Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide
- Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes
- 2017
- Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants
- Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method
- Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates
- Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication
- Scaling behaviour and rate-determining steps in filamentous self-assembly
-
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease
Habchi, Johnny ; Chia, Sean ; Limbocker, Ryan ; Mannini, Benedetta ; Ahn, Minkoo ; Perni, Michele ; Hansson, Oskar LU
; Arosio, Paolo
; Kumita, Janet R
and Challa, Pavan Kumar
, et al.
(2017)
In Proceedings of the National Academy of Sciences of the United States of America
114(2).
p.200-208
Mark
- 2016
- Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein
- Molecular mechanisms of protein aggregation from global fitting of kinetic models.
- Physical determinants of the self-replication of protein fibrils
-
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
Arosio, Paolo ; Michaels, Thomas C T ; Linse, Sara LU ; Månsson, Cecilia LU ; Emanuelsson, Cecilia LU
; Presto, Jenny
; Johansson, Jan
; Vendruscolo, Michele
; Dobson, Christopher M.
and Knowles, Tuomas P J
(2016)
In Nature Communications
7.
Mark
- Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.
- An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
- The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model
- 2015
- Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity
- Protein Microgels from Amyloid Fibril Networks
- A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
- 2014
- Solution conditions determine the relative importance of nucleation and growth processes in alpha-synuclein aggregation
- Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.
-
Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.
Månsson, Cecilia LU ; Arosio, Paolo ; Hussein, Rasha ; Kampinga, Harm H ; Hashem, Reem M ; Boelens, Wilbert C ; Dobson, Christopher M ; Knowles, Tuomas P J ; Linse, Sara LU and Emanuelsson, Cecilia LU
(2014)
In Journal of Biological Chemistry
289(45).
p.31066-31076
Mark
- 2013
- Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism
- 2010
-
Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution.
Dhulesia, Anne ; Cremades, Nunilo ; Kumita, Janet R ; Hsu, Shang-Te Danny ; Mossuto, Maria F ; Dumoulin, Mireille ; Nietlispach, Daniel ; Akke, Mikael LU
; Salvatella, Xavier
and Dobson, Christopher M
(2010)
In Journal of the American Chemical Society
132(44).
p.15580-15588
Mark