Emil Axell
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View article: Galectin-3 deletion modulates microglial phenotype and Aβ response via TREM2 activation while attenuating neuroinflammation
Galectin-3 deletion modulates microglial phenotype and Aβ response via TREM2 activation while attenuating neuroinflammation Open
Summary Galectin-3 (Gal3) is a regulator of microglial activation implicated in Alzheimer’s disease (AD). However, Gal3 role in modulating microglial phenotype towards amyloid-beta (Aβ) remains poorly understood. We demonstrate that Gal3 a…
View article: On the reversibility of amyloid fibril formation
On the reversibility of amyloid fibril formation Open
Amyloids are elongated supramolecular protein self-assemblies. Their formation is a non-covalent assembly process and as such is fully reversible. Amyloid formation is associated with several neurodegenerative diseases, and the reversibili…
View article: General integrated rate law for complex self-assembly reactions reveals the mechanism of amyloid-beta coaggregation
General integrated rate law for complex self-assembly reactions reveals the mechanism of amyloid-beta coaggregation Open
A highly general integrated rate law for complex amyloid fibril formation reactions is developed. Its global fitting to data from multiple kinetic experiments reveals the molecular mechanism of Abeta alloform coaggregation in unprecedented…
View article: The role of shear forces in primary and secondary nucleation of amyloid fibrils
The role of shear forces in primary and secondary nucleation of amyloid fibrils Open
Shear forces affect self-assembly processes ranging from crystallization to fiber formation. Here, the effect of mild agitation on amyloid fibril formation was explored for four peptides and investigated in detail for A 42, which is ass…
View article: The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation State
The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation State Open
For many chaperones, a propensity to self-assemble correlates with function. The highly efficient amyloid suppressing chaperone DNAJB6b has been reported to oligomerize. A key question is whether the DNAJB6b self-assemblies or their subuni…
View article: A label-free high-throughput protein solubility assay and its application to A<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si14.svg"><mml:mi mathvariant="bold-italic">β</mml:mi></mml:math>40
A label-free high-throughput protein solubility assay and its application to A40 Open
A major hallmark of Alzheimer's disease is the accumulation of aggregated amyloid β peptide (Aβ) in the brain. Here we develop a solubility assay for proteins and measure the solubility of Aβ40. In brief, the method utilizes 96-well filter…
View article: A Comparison of the Transglycosylation Capacity between the Guar GH27 Aga27A and Bacteroides GH36 BoGal36A α-Galactosidases
A Comparison of the Transglycosylation Capacity between the Guar GH27 Aga27A and Bacteroides GH36 BoGal36A α-Galactosidases Open
The transglycosylation behavior and capacity of two clan GH-D α-galactosidases, BoGal36A from the gut bacterium Bacteroides ovatus and Aga27A from the guar plant, was investigated and compared. The enzymes were screened for the ability to …
View article: Proliferation of Tau 304–380 Fragment Aggregates through Autocatalytic Secondary Nucleation
Proliferation of Tau 304–380 Fragment Aggregates through Autocatalytic Secondary Nucleation Open
The self-assembly of the protein tau into neurofibrillary tangles is one of the hallmarks of Alzheimer's disease and related tauopathies. Still, the molecular mechanism of tau aggregation is largely unknown. This problem may be addressed b…
View article: Tau AD fragment aggregates proliferate through autocatalytic secondary nucleation
Tau AD fragment aggregates proliferate through autocatalytic secondary nucleation Open
The self-assembly of the protein tau into neurofibrillary tangles is one of the hallmarks of Alzheimer’s disease and related tauopathies. Still, the molecular mechanism of tau aggregation is largely unknown. This problem may be addressed b…
View article: A calorimetric study of α-synuclein fibril formation & peptide induced vesicle leakage
A calorimetric study of α-synuclein fibril formation & peptide induced vesicle leakage Open
The small protein α-synuclein is strongly associated with Parkinson’s disease. This protein is found in inclusion bodies, named lewy bodies inside neurons of people suffering from the disease. α-synuclein is very abundant in the human brai…