about
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's diseaseA High Power-Density, Mediator-Free, Microfluidic Biophotovoltaic Device for Cyanobacterial CellsDynamic microfluidic control of supramolecular peptide self-assembly.A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicityDynamics of protein aggregation and oligomer formation governed by secondary nucleation.N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineeringDirect observation of the interconversion of normal and toxic forms of α-synucleinNanoscale spatially resolved infrared spectra from single microdroplets.Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates.Role of intermolecular forces in defining material properties of protein nanofibrils.Crucial role of nonspecific interactions in amyloid nucleation.Highly specific label-free protein detection from lysed cells using internally referenced microcantilever sensors.Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.Self-Assembly of Amyloid Fibrils That Display Active Enzymes.Preventing peptide and protein misbehavior.Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity.Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.Force generation by the growth of amyloid aggregates.Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperonesChemical and biophysical insights into the propagation of prion strains.Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces.Nanomechanics of functional and pathological amyloid materials.Protein micro- and nano-capsules for biomedical applications.Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials.Tetracycline nanoparticles as antibacterial and gene-silencing agents.Physical principles of filamentous protein self-assembly kinetics.Dynamics of heteromolecular filament formation.Expanding the solvent chemical space for self-assembly of dipeptide nanostructures.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.Silk micrococoons for protein stabilisation and molecular encapsulationDiffuse transition state structure for the unfolding of a leucine-rich repeat protein.Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variantsEasyworm: an open-source software tool to determine the mechanical properties of worm-like chains.Kinetic constraints on self-assembly into closed supramolecular structures.Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoformsRole of elongation and secondary pathways in S6 amyloid fibril growth.
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description
researcher
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wetenschapper
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հետազոտող
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name
Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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type
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
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Tuomas P. J. Knowles
@nl
P106
P2456
P2798
P31
P496
0000-0002-7879-0140