Christopher M. Dobson

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.

Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.

The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation.

Altered aggregation properties of mutant gamma-crystallins cause inherited cataract.

De novo designed peptide-based amyloid fibrils.

Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.

Calculation of mutational free energy changes in transition states for protein folding.

Chemical modification of insulin in amyloid fibrils.

The circularization of amyloid fibrils formed by apolipoprotein C-II.

Structures and relative free energies of partially folded states of proteins.

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.

Exploring amyloid formation by a de novo design.

Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.

Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes.

The formation of spherulites by amyloid fibrils of bovine insulin.

A glimpse at the organization of the protein universe.

Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.

Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.

Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.

Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.

Characterization of the nanoscale properties of individual amyloid fibrils.

Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides.

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

Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy.

Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.

Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity.

Molecular determinants of the aggregation behavior of alpha- and beta-synuclein.

A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction.

Immunological features of alpha-synuclein in Parkinson's disease.

Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.

Recombinant amyloid beta-peptide production by coexpression with an affibody ligand.

A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.

Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.

Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate.

Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy.

Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy.

Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.

Analysis of sub-tauc and supra-tauc motions in protein Gbeta1 using molecular dynamics simulations.

Folding study of Venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions.

Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.

Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy.

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

Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo.

A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis.

Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.

Physicochemical determinants of chaperone requirements.

Structure and properties of a complex of α-synuclein and a single-domain camelid antibody.

The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity.

Surface attachment of protein fibrils via covalent modification strategies.

High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .

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

Frequency factors in a landscape model of filamentous protein aggregation.

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.

Glial innate immunity generated by non-aggregated alpha-synuclein in mouse: differences between wild-type and Parkinson's disease-linked mutants.

Transient tertiary structure formation within the ribosome exit port.

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

New scenarios of protein folding can occur on the ribosome.

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

Protein dynamics: Moore's law in molecular biology.

A FRET sensor for non-invasive imaging of amyloid formation in vivo.

Detection of early locomotor abnormalities in a Drosophila model of Alzheimer's disease.

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

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

¹H, ¹³C and ¹⁵N resonance assignments of human muscle acylphosphatase.

Metastability of native proteins and the phenomenon of amyloid formation.

Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.

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

The iFly tracking system for an automated locomotor and behavioural analysis of Drosophila melanogaster.

Probing protein aggregation with quartz crystal microbalances.

Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.

In situ measurements of the formation and morphology of intracellular β-amyloid fibrils by super-resolution fluorescence imaging.

Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris.

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

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.

Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster.

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.

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility.

The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.

The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila.

From macroscopic measurements to microscopic mechanisms of protein aggregation.

Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity.

Detailed analysis of the energy barriers for amyloid fibril growth.

Intrinsic disorder modulates protein self-assembly and aggregation.

Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances.

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

Prediction of variable translation rate effects on cotranslational protein folding.

Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions.

Characterizing intermolecular interactions that initiate native-like protein aggregation.

Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.

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

Nanobodies as structural probes of protein misfolding and fibril formation.

Twisting transition between crystalline and fibrillar phases of aggregated peptides.

Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones.

Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.

In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome.

Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.

Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms.

Protein amyloids develop an intrinsic fluorescence signature during aggregation.

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.

Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.

A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence.

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

α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.

Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.

Characterization of the interdomain motions in hen lysozyme using residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations.

In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells.

Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.

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

Preconditioning of microglia by α-synuclein strongly affects the response induced by toll-like receptor (TLR) stimulation.

Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.

Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.

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

Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.

A simple lattice model that captures protein folding, aggregation and amyloid formation.

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.

Dynamics and timekeeping in biological systems.

Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage.

Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies.

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

Understanding the influence of codon translation rates on cotranslational protein folding.

Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.

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

The amyloid state and its association with protein misfolding diseases.

Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation.

Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.

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.

Antibodies and protein misfolding: From structural research tools to therapeutic strategies.

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

Single-molecule imaging reveals that small amyloid-β1-42 oligomers interact with the cellular prion protein (PrP(C)).

A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein.

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

Protein microgels from amyloid fibril networks.

Structure of a low-population intermediate state in the release of an enzyme product.

Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.

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

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

Investigating the mechanisms of amylolysis of starch granules by solution-state NMR.

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

Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression.

Chaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype.

Widespread Proteome Remodeling and Aggregation in Aging C. elegans.

The influence of novel gemini surfactants containing cycloalkyl side-chains on the structural phases of DNA in solution.

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

Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity.

Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies.

Force generation by the growth of amyloid aggregates.

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

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.

Conformational Effects of the A21G Flemish Mutation on the Aggregation of Amyloid β Peptide.

Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response.

Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins.

Identification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for Tauopathies.

SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.

The length distribution of frangible biofilaments.

Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide.

Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease.

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.

Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.

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.

A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.

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

Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing.

Quantitative thermophoretic study of disease-related protein aggregates.

Ca2+ is a key factor in α-synuclein-induced neurotoxicity.

Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons.

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

A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation.

Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.

Structural Effects of Two Camelid Nanobodies Directed to Distinct C-Terminal Epitopes on α-Synuclein.

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

Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity.

Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein.

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

Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.

Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies.

Towards a structural biology of the hydrophobic effect in protein folding.

The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity.

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

A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease.

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

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.

Structural basis of synaptic vesicle assembly promoted by α-synuclein.

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

Bifunctional Anti-Non-Amyloid Component α-Synuclein Nanobodies Are Protective In Situ.

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.

Multi-dimensional super-resolution imaging enables surface hydrophobicity mapping.

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

The Amyloid Phenomenon and Its Links with Human Disease.

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

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

Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.

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

Amyloid-like Fibrils from an α-Helical Transmembrane Protein.

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.

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

Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.

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.

The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases.

The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis.

Silk micrococoons for protein stabilisation and molecular encapsulation.

Sequential Release of Proteins from Structured Multishell Microcapsules.

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

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.

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

Immunization with α-synuclein/Grp94 reshapes peripheral immunity and suppresses microgliosis in a chronic Parkinsonism model.

Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation.

Clusterin protects neurons against intracellular proteotoxicity.

Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles.

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

Inhibiting the Ca Influx Induced by Human CSF.

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers.

Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity.

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

Optical Structural Analysis of Individual α-Synuclein Oligomers.

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

Biophotonics of Native Silk Fibrils.

The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.

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.

Bifunctional fluorescent probes for detection of amyloid aggregates and reactive oxygen species.

Microfluidic approaches for probing amyloid assembly and behaviour.

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

Molecular determinants of the interaction of EGCG with ordered and disordered proteins.

Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding.

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

Cooperative Assembly of Hsp70 Subdomain Clusters.

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

Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers.

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

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.

Structural differences between toxic and nontoxic HypF-N oligomers.

Conserved S/T Residues of the Human Chaperone DNAJB6 Are Required for Effective Inhibition of Aβ42 Amyloid Fibril Formation.

Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.

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

Obituary: Nico van Nuland 1961-2017.

Proteasome-targeted nanobodies alleviate pathology and functional decline in an α-synuclein-based Parkinson's disease model.

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

SAR by kinetics for drug discovery in protein misfolding diseases.

Statistical Mechanics of Globular Oligomer Formation by Protein Molecules.

Quantifying Co-Oligomer Formation by α-Synuclein.

Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale.