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Author Details

Christopher M Dobson
University of Cambridge
1973
796
138
Andrej Sali (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
36921387Microfluidic antibody affinity profiling of alloantibody-HLA interactions in human serum.Biosens Bioelectron2023
37186840Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains.Proc Natl Acad Sci U S A2023
35209093The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity.Molecules2022
36158582The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes.Front Mol Biosci2022
35944093N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates.Biochemistry2022
33386842Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies.J Mol Cell Biol2021
33829010Comparative Studies in the A30P and A53T α-Synuclein <i>C. elegans</i> Strains to Investigate the Molecular Origins of Parkinson's Disease.Front Cell Dev Biol2021
33767451Scaling analysis reveals the mechanism and rates of prion replication in vivo.Nat Struct Mol Biol2021
33538575Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors.ACS Chem Neurosci2021
33640796Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.Biophys Chem2021
33753734The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells.Nat Commun2021
33500508Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers.Commun Biol2021
34606279Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary Systems.J Am Chem Soc2021
34518228The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.Proc Natl Acad Sci U S A2021
34684701The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ.Molecules2021
34650037The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends.Nat Commun2021
34220435Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers.Front Neurosci2021
34043816Distinct responses of human peripheral blood cells to different misfolded protein oligomers.Immunology2021
34292154Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins.Elife2021
34206070Parallel and Sequential Pathways of Molecular Recognition of a Tandem-Repeat Protein and Its Intrinsically Disordered Binding Partner.Biomolecules2021
34234268Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response.Commun Biol2021
34312490Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response.Commun Biol2021
34257326Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans.Sci Rep2021
34109955Machine learning-aided protein identification from multidimensional signatures.Lab Chip2021
33217338Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis.Cell Chem Biol2021
33398040A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers.Commun Biol2021
30936117The Amyloid Phenomenon and Its Significance in Biology and Medicine.Cold Spring Harb Perspect Biol2020
36703335Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter.Commun Chem2020
33520152The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates.Chem Sci2020
34122915ThX - a next-generation probe for the early detection of amyloid aggregates.Chem Sci2020
31937832The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State.Sci Rep2020
31892536Proteome-wide observation of the phenomenon of life on the edge of solubility.Proc Natl Acad Sci U S A2020
32011129Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers.Biomacromolecules2020
31980482Correction: Defining α-synuclein species responsible for Parkinson's disease phenotypes in mice.J Biol Chem2020
32063829A Role of Cholesterol in Modulating the Binding of α-Synuclein to Synaptic-Like Vesicles.Front Neurosci2020
33079553Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution.Nano Lett2020
33203502Biophysical studies of protein misfolding and aggregation in <i>in vivo</i> models of Alzheimer's and Parkinson's diseases - ERRATUM.Q Rev Biophys2020
33148639Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease.Sci Adv2020
32943652A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.Sci Rep2020
32632432Half a century of amyloids: past, present and future.Chem Soc Rev2020
32824145Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers.Int J Mol Sci2020
32794533Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils.Nanoscale2020
32819579Probing the unfolded protein response in long-lived naked mole-rats.Biochem Biophys Res Commun2020
32989305Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies.Nat Struct Mol Biol2020
32929030Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.Proc Natl Acad Sci U S A2020
32778821Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation.Nat Struct Mol Biol2020
32284577Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.Nat Chem2020
32414930Kinetic diversity of amyloid oligomers.Proc Natl Acad Sci U S A2020
32303714Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.Nat Chem2020
32146327A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation.iScience2020
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Collaborators

University of Cambridge
Co-authored papers 196
Institut fur Physikalische Biologie, Heinrich-Heine-Universitat Dusseldorf
Co-authored papers 44
University of Oxford
Co-authored papers 42
University of Melbourne, The Royal Children's Hospital
Co-authored papers 42
University of Oxford
Co-authored papers 34
Harvard University
Co-authored papers 22
University of Oxford
Co-authored papers 15
Institute of Bioengineering of Catalonia (IBEC)
Co-authored papers 9
UCL Queen Square Institute of Neurology
Co-authored papers 7
Co-authored papers 6
The University of Edinburgh
Co-authored papers 5
Enterin Research Institute Inc.
Co-authored papers 5
University of Connecticut Health Center
Co-authored papers 4
Institute of Structural and Molecular Biology, University of London
Co-authored papers 4
Cambridge Institute for Medical Research, University of Cambridge
Co-authored papers 4
OncProTech LLC
Co-authored papers 4
National Health Service Blood and Transplant, University of Cambridge
Co-authored papers 3
Co-authored papers 3
Co-authored papers 3
National Institutes of Health
Co-authored papers 3
Co-authored papers 3
University of California San Francisco
Co-authored papers 2
Clinical Institute of Hematology and Oncology, Hospital Clinic Barcelona
Co-authored papers 2
Ontario Institute for Cancer Research
Co-authored papers 2
European Bioinformatics Institute (EMBL-EBI)
Co-authored papers 2
University of Oxford
Co-authored papers 2
University of Alberta
Co-authored papers 2
University of Cambridge
Co-authored papers 2
University of Exeter, Royal Devon and Exeter Hospital
Co-authored papers 2
Max Planck Institute of Molecular Plant Physiology
Co-authored papers 2