Tuomas P.J. Knowles

The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner.

Spatial persistence of angular correlations in amyloid fibrils.

Characterization of the nanoscale properties of individual amyloid fibrils.

Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass.

Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.

Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements.

Highly specific label-free protein detection from lysed cells using internally referenced microcantilever sensors.

Position-dependent electrostatic protection against protein aggregation.

Chemical and biophysical insights into the propagation of prion strains.

Biosensor-based label-free assays of amyloid growth.

Fabrication and characterisation of protein fibril-elastomer composites.

An analytical solution to the kinetics of breakable filament assembly.

Nanostructured films from hierarchical self-assembly of amyloidogenic proteins.

The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.

Protein aggregation in crowded environments.

Surface attachment of protein fibrils via covalent modification strategies.

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering.

Frequency factors in a landscape model of filamentous protein aggregation.

Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors.

Relationship between prion propensity and the rates of individual molecular steps of fibril assembly.

Population of nonnative states of lysozyme variants drives amyloid fibril formation.

Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions.

Metastability of native proteins and the phenomenon of amyloid formation.

Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein.

Probing protein aggregation with quartz crystal microbalances.

Nanomechanics of functional and pathological amyloid materials.

Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.

Label-free detection of amyloid growth with microcantilever sensors.

Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.

Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.

Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations.

Observation of spatial propagation of amyloid assembly from single nuclei.

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.

Probing small molecule binding to amyloid fibrils.

Nucleated polymerisation in the presence of pre-formed seed filaments.

Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation.

From macroscopic measurements to microscopic mechanisms of protein aggregation.

Detailed analysis of the energy barriers for amyloid fibril growth.

Direct observation of the interconversion of normal and toxic forms of α-synuclein.

Role of elongation and secondary pathways in S6 amyloid fibril growth.

Connecting macroscopic observables and microscopic assembly events in amyloid formation using coarse grained simulations.

Twisting transition between crystalline and fibrillar phases of aggregated peptides.

Electrostatic effects in filamentous protein aggregation.

Atomic structure and hierarchical assembly of a cross-β amyloid fibril.

Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

Single-molecule measurements of transient biomolecular complexes through microfluidic dilution.

Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptide.

Quantification of the concentration of Aβ42 propagons during the lag phase by an amyloid chain reaction assay.

A clear view of polymorphism, twist, and chirality in amyloid fibril formation.

Expanding the solvent chemical space for self-assembly of dipeptide nanostructures.

Nanoscale spatially resolved infrared spectra from single microdroplets.

Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease.

Chemical kinetics for drug discovery to combat protein aggregation diseases.

Density-gradient-free microfluidic centrifugation for analytical and preparative separation of nanoparticles.

Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters.

Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.

Asymptotic solutions of the Oosawa model for the length distribution of biofilaments.

The amyloid state and its association with protein misfolding diseases.

Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization.

Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.

The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.

Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.

Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers.

Multiphase protein microgels.

Tetracycline nanoparticles as antibacterial and gene-silencing agents.

Crucial role of nonspecific interactions in amyloid nucleation.

Protein microgels from amyloid fibril networks.

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.

On the lag phase in amyloid fibril formation.

Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.

A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution.

Preventing peptide and protein misbehavior.

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers.

Self-Assembly of Amyloid Fibrils That Display Active Enzymes.

Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.

Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry.

A High Power-Density, Mediator-Free, Microfluidic Biophotovoltaic Device for Cyanobacterial Cells.

Molecular Rotors Provide Insights into Microscopic Structural Changes During Protein Aggregation.

Force generation by the growth of amyloid aggregates.

Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.

Fast flow microfluidics and single-molecule fluorescence for the rapid characterization of α-synuclein oligomers.

Quantitative Analysis of Diffusive Reactions at the Solid-Liquid Interface in Finite Systems.

Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.

Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.

The length distribution of frangible biofilaments.

Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants.

Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.

Molecular mechanisms of protein aggregation from global fitting of kinetic models.

Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide.

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.

Hamiltonian Dynamics of Protein Filament Formation.

An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation.

Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.

A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.

Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.

Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions.

Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation.

Quantitative thermophoretic study of disease-related protein aggregates.

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.

Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation.

Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones.

Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism.

The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model.

Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials.

A Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions.

Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.

Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly.

Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.

Fluctuations in the Kinetics of Linear Protein Self-Assembly.

Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.

Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation.

Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces.

Dynamic microfluidic control of supramolecular peptide self-assembly.

β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces.

Dynamics of heteromolecular filament formation.

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease.

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.

Physical principles of filamentous protein self-assembly kinetics.

Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.

Microfluidic devices fabricated using fast wafer-scale LED-lithography patterning.

Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers.

Acceleration of α-synuclein aggregation.

Ultrasensitive Measurement of Ca Influx into Lipid Vesicles Induced by Protein Aggregates.

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

Selective targeting of primary and secondary nucleation pathways in Aβ42 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.

Silk micrococoons for protein stabilisation and molecular encapsulation.

Sequential Release of Proteins from Structured Multishell Microcapsules.

Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.

Gradient-free determination of isoelectric points of proteins on chip.

Kinetic constraints on self-assembly into closed supramolecular structures.

Hierarchical Biomolecular Emulsions Using 3-D Microfluidics with Uniform Surface Chemistry.

Absolute Quantification of Amyloid Propagons by Digital Microfluidics.

Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants.

Enhanced Quality Factor Label-free Biosensing with Micro-Cantilevers Integrated into Microfluidic Systems.

Nanoscale click-reactive scaffolds from peptide self-assembly.

Thermodynamics of Polypeptide Supramolecular Assembly in the Short-Chain Limit.

Scaling behaviour and rate-determining steps in filamentous self-assembly.

Mechanism of biosurfactant adsorption to oil/water interfaces from millisecond scale tensiometry measurements.

On-chip label-free protein analysis with downstream electrodes for direct removal of electrolysis products.

Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification.

Microfluidics for Protein Biophysics.

Microfluidic Diffusion Platform for Characterizing the Sizes of Lipid Vesicles and the Thermodynamics of Protein-Lipid Interactions.

Direct Observation of Oligomerization by Single Molecule Fluorescence Reveals a Multistep Aggregation Mechanism for the Yeast Prion Protein Ure2.

Biophotonics of Native Silk Fibrils.

Real-Time Intrinsic Fluorescence Visualization and Sizing of Proteins and Protein Complexes in Microfluidic Devices.

Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery.

Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.

Microfluidic approaches for probing amyloid assembly and behaviour.

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.

Water-Dispersible Polydopamine-Coated Nanofibers for Stimulation of Neuronal Growth and Adhesion.

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes.

Cooperative Assembly of Hsp70 Subdomain Clusters.

Rapid Growth of Acetylated Aβ(16-20) into Macroscopic Crystals.

On-chip measurements of protein unfolding from direct observations of micron-scale diffusion.

Budding-like division of all-aqueous emulsion droplets modulated by networks of protein nanofibrils.

Kinetic Analysis of Amyloid Formation.

On the role of sidechain size and charge in the aggregation of A42 with familial mutations.

Determination of Polypeptide Conformation with Nanoscale Resolution in Water.

Enhancing the Resolution of Micro Free Flow Electrophoresis through Spatially Controlled Sample Injection.

Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils.

Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils.

Oligomer Diversity during the Aggregation of the Repeat Region of Tau.

Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine.

Stabilization and Characterization of Cytotoxic Aβ Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc Ions.

Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution.

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH.

Combining Affinity Selection and Specific Ion Mobility for Microchip Protein Sensing.

Origin of metastable oligomers and their effects on amyloid fibril self-assembly.

Self-Assembly-Mediated Release of Peptide Nanoparticles through Jets Across Microdroplet Interfaces.

DNA-Coated Functional Oil Droplets.

Identification of Oxidative Stress in Red Blood Cells with Nanoscale Chemical Resolution by Infrared Nanospectroscopy.

Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity.

SAR by kinetics for drug discovery in protein misfolding diseases.

Observation of molecular self-assembly events in massively parallel microdroplet arrays.

Statistical Mechanics of Globular Oligomer Formation by Protein Molecules.

Direct Observation of Murine Prion Protein Replication in Vitro.

Quantifying Co-Oligomer Formation by α-Synuclein.