about
Dynamic microfluidic control of supramolecular peptide self-assembly.Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.Force generation by the growth of amyloid aggregates.Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces.Physical principles of filamentous protein self-assembly kinetics.Dynamics of heteromolecular filament formation.Molecular mechanisms of protein aggregation from global fitting of kinetic models.The length distribution of frangible biofilaments.Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.Kinetic constraints on self-assembly into closed supramolecular structures.Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoformsβ-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces.Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.Quantitative Analysis of Diffusive Reactions at the Solid-Liquid Interface in Finite Systems.Thermodynamics of Polypeptide Supramolecular Assembly in the Short-Chain Limit.Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2.Fluctuations in the Kinetics of Linear Protein Self-Assembly.Hamiltonian Dynamics of Protein Filament Formation.Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.Scaling theory of electric-field-assisted tunnelling.Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization.Asymptotic solutions of the Oosawa model for the length distribution of biofilaments.Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly.Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.Budding-like division of all-aqueous emulsion droplets modulated by networks of protein nanofibrils.Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.Physical determinants of the self-replication of protein fibrilsSAR by kinetics for drug discovery in protein misfolding diseasesSecondary nucleation in amyloid formationSelf-Assembly-Mediated Release of Peptide Nanoparticles through Jets Across Microdroplet InterfacesCooperative Assembly of Hsp70 Subdomain ClustersCholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranesKinetic Analysis of Amyloid FormationTrodusquemine enhances Aβ aggregation but suppresses its toxicity by displacing oligomers from cell membranesSpatial control of irreversible protein aggregationThe catalytic nature of protein aggregationDynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptideAuthor Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide
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description
Forscher
@de
investigador
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researcher
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ricercatore
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wetenschapper
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հետազոտող
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研究者
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name
Thomas C. T. Michaels
@en
Thomas Michaels
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Thomas Michaels
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Thomas Michaels
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type
label
Thomas C. T. Michaels
@en
Thomas Michaels
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Thomas Michaels
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Thomas Michaels
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prefLabel
Thomas C. T. Michaels
@en
Thomas Michaels
@ast
Thomas Michaels
@es
Thomas Michaels
@nl
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P1153
55638714700
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0000-0001-6931-5041