Alexander K Buell researcher
Büll, Alexander Kai
VIAF ID: 2811159035163101380008 (Personal)
Permalink: http://viaf.org/viaf/2811159035163101380008
Preferred Forms
- 100 0 _ ‡a Alexander K Buell ‡c researcher
- 100 1 _ ‡a Büll, Alexander Kai
4xx's: Alternate Name Forms (4)
5xx's: Related Names (1)
Works
Title | Sources |
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Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy | |
Biosensor-based label-free assays of amyloid growth | |
C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH | |
Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation | |
Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein | |
Compact fibril-like structure of amyloid β-peptide (1-42) monomers | |
Correction to: Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study | |
Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth | |
Detection and Characterization of Small Molecule Interactions with Fibrillar Protein Aggregates Using Microscale Thermophoresis | |
Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy | |
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. | |
An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils | |
The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG | |
Expanding the solvent chemical space for self-assembly of dipeptide nanostructures. | |
Frequency Factors in a Landscape Model of Filamentous Protein Aggregation | |
The growth of amyloid fibrils: rates and mechanisms | |
The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth | |
Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2 | |
Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils | |
Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors | |
Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils | |
The length distribution of frangible biofilaments. | |
Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils | |
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation | |
Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances | |
Mécanismes fondamentaux de formation de fibres amyloïdes par la protéine α-synucléine dans la maladie de Parkinson | |
A microfluidic diffusion platform for characterizing the size of lipid vesicles and the thermodynamics of protein-lipid interactions. | |
Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species | |
Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons | |
Nanostructured films from hierarchical self-assembly of amyloidogenic proteins | |
The Nucleation of Protein Aggregates - From Crystals to Amyloid Fibrils | |
Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth | |
Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers | |
Photodissociation dynamics of the reaction H2CO-->H+HCO via the singlet (S0) and triplet (T1) surfaces | |
The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation | |
Population of nonnative states of lysozyme variants drives amyloid fibril formation | |
Position-dependent electrostatic protection against protein aggregation. | |
Probing small molecule binding to amyloid fibrils | |
The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril Strain | |
Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation | |
Protein Aggregation in Crowded Environments | |
Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways | |
Quantitative Analysis of Diffusive Reactions at the Solid-Liquid Interface in Finite Systems. | |
Quantitative thermophoretic study of disease-related protein aggregates | |
Relationship between prion propensity and the rates of individual molecular steps of fibril assembly | |
Role of Hydrophobicity and Charge of Amyloid-Beta Oligomer Eliminating d-Peptides in the Interaction with Amyloid-Beta Monomers | |
Scaling behaviour and rate-determining steps in filamentous self-assembly | |
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation | |
Spatial Propagation of Protein Polymerization | |
Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation | |
Surface attachment of protein fibrils via covalent modification strategies | |
Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform. | |
Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease | |
Thermodynamics of amyloid fibril formation from chemical depolymerization | |
Thermodynamics of Polypeptide Supramolecular Assembly in the Short-Chain Limit. | |
Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase | |
α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation | |
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. |