Christopher M. Dobson

Christopher M. Dobson

Centre for Misfolding Diseases, University of Cambridge

Affiliated withUniversity of Cambridge

Research Area

Biography

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JoVE Journal Publications

ArticleTotal : 1
Year
Automated Behavioral Analysis of Large <em>C. elegans</em> Populations Using a Wide Field-of-view Tracking Platform
Publication title

Cited by 9

2018

Other Publications

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

Protein science : a publication of the Protein Society| PubMed ID: 11714922

2001
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 12374855

2002
2002
2002
De novo designed peptide-based amyloid fibrils.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 12456886

2002
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 12481032

2002
2003
Chemical modification of insulin in amyloid fibrils.

Protein science : a publication of the Protein Society| PubMed ID: 14573875

2003
2003
Structures and relative free energies of partially folded states of proteins.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 14657374

2003
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 14715898

2004
Exploring amyloid formation by a de novo design.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 15070736

2004
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 15123800

2004
Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 15263071

2004
The formation of spherulites by amyloid fibrils of bovine insulin.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 15381766

2004
A glimpse at the organization of the protein universe.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 15827120

2005
Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 15956205

2005
Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 16006528

2005
Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 16116084

2005
2005
Characterization of the nanoscale properties of individual amyloid fibrils.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 17038504

2006
Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides.

Protein science : a publication of the Protein Society| PubMed ID: 17525469

2007
Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 17540728

2007
Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 17940046

2007
2007
2007
Molecular determinants of the aggregation behavior of alpha- and beta-synuclein.

Protein science : a publication of the Protein Society| PubMed ID: 18436957

2008
A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction.

Structure (London, England : 1993)| PubMed ID: 18462678

2008
Immunological features of alpha-synuclein in Parkinson's disease.

Journal of cellular and molecular medicine| PubMed ID: 18671754

2008
Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 18796612

2008
2008
2008
Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 19416886

2009
2009
2009
Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy.

Angewandte Chemie (International ed. in English)| PubMed ID: 19562810

2009
2009
2009
2010
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 20018739

2009
2010
2010
2010
2010
2010
Physicochemical determinants of chaperone requirements.

Journal of molecular biology| PubMed ID: 20416322

2010
2010
2010
Surface attachment of protein fibrils via covalent modification strategies.

The journal of physical chemistry. B| PubMed ID: 20695458

2010
2010
Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 20713699

2010
2010
2010
2010
Transient tertiary structure formation within the ribosome exit port.

Journal of the American Chemical Society| PubMed ID: 21062068

2010
2010
New scenarios of protein folding can occur on the ribosome.

Journal of the American Chemical Society| PubMed ID: 21204555

2011
2011
Protein dynamics: Moore's law in molecular biology.

Current biology : CB| PubMed ID: 21256436

2011
A FRET sensor for non-invasive imaging of amyloid formation in vivo.

Chemphyschem : a European journal of chemical physics and physical chemistry| PubMed ID: 21308945

2011
2011
Population of nonnative states of lysozyme variants drives amyloid fibril formation.

Journal of the American Chemical Society| PubMed ID: 21528861

2011
2011
2012
Metastability of native proteins and the phenomenon of amyloid formation.

Journal of the American Chemical Society| PubMed ID: 21650202

2011
Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.

Angewandte Chemie (International ed. in English)| PubMed ID: 21671315

2011
2011
The iFly tracking system for an automated locomotor and behavioural analysis of Drosophila melanogaster.

Integrative biology : quantitative biosciences from nano to macro| PubMed ID: 21698336

2011
Probing protein aggregation with quartz crystal microbalances.

Methods in molecular biology (Clifton, N.J.)| PubMed ID: 21713635

2011
2011
2011
2011
Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.

Cold Spring Harbor perspectives in biology| PubMed ID: 21825020

2011
2011
2011
2011
Observation of spatial propagation of amyloid assembly from single nuclei.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 21876182

2011
2011
Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology| PubMed ID: 21965601

2012
Probing small molecule binding to amyloid fibrils.

Physical chemistry chemical physics : PCCP| PubMed ID: 22006124

2011
Nucleated polymerisation in the presence of pre-formed seed filaments.

International journal of molecular sciences| PubMed ID: 22016630

2011
2011
Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 22160682

2011
2011
2012
2012
2012
Detailed analysis of the energy barriers for amyloid fibril growth.

Angewandte Chemie (International ed. in English)| PubMed ID: 22489083

2012
Intrinsic disorder modulates protein self-assembly and aggregation.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 22509003

2012
Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances.

Methods in molecular biology (Clifton, N.J.)| PubMed ID: 22528086

2012
2012
2012
2012
2012
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 22802614

2012
2012
Nanobodies as structural probes of protein misfolding and fibril formation.

Methods in molecular biology (Clifton, N.J.)| PubMed ID: 22886275

2012
2012
2012
2012
In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 23256155

2013
2013
2013
2013
Electrostatic effects in filamentous protein aggregation.

Biophysical journal| PubMed ID: 23473495

2013
Atomic structure and hierarchical assembly of a cross-β amyloid fibril.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 23513222

2013
Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences| PubMed ID: 23530260

2013
2013
A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence.

Chembiochem : a European journal of chemical biology| PubMed ID: 23592254

2013
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 23703910

2013
2013
2013
2013
2013
2013
2013
2013
2014
2013
2014
Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.

Journal of the American Chemical Society| PubMed ID: 24304221

2013
2013
2014
2014
2014
Chemical kinetics for drug discovery to combat protein aggregation diseases.

Trends in pharmacological sciences| PubMed ID: 24560688

2014
Dynamics and timekeeping in biological systems.

Annual review of biochemistry| PubMed ID: 24606145

2014
2014
2014
Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters.

Physical review. E, Statistical, nonlinear, and soft matter physics| PubMed ID: 24730879

2014
2014
Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 24799681

2014
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 24817693

2014
The amyloid state and its association with protein misfolding diseases.

Nature reviews. Molecular cell biology| PubMed ID: 24854788

2014
2014
2014
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 24938782

2014
2014
2014
2014
2014
2014
2014
2015
2015
2015
2015
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.

Nature structural & molecular biology| PubMed ID: 25686087

2015
2015
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 25855634

2015
2015
2014
2015
2015
2015
2015
2015
Force generation by the growth of amyloid aggregates.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 26195762

2015
2015
2015
2015
2015
Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology| PubMed ID: 26443817

2016
2015
2015
2015
The length distribution of frangible biofilaments.

The Journal of chemical physics| PubMed ID: 26520548

2015
2015
2016
2015
2016
2016
2016
2016
Hamiltonian Dynamics of Protein Filament Formation.

Physical review letters| PubMed ID: 26849615

2016
2016
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 26884195

2016
2016
2016
2016
2016
2016
Ca2+ is a key factor in α-synuclein-induced neurotoxicity.

Journal of cell science| PubMed ID: 26989132

2016
Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 26993805

2016
2016
A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 27071083

2016
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 27092002

2016
2016
2016
2016
Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 27298346

2016
2016
Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.

Journal of the American Chemical Society| PubMed ID: 27387359

2016
2016
2016
2016
Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.

Chembiochem : a European journal of chemical biology| PubMed ID: 27472818

2016
2016
Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 27573854

2016
2016
2016
2016
2016
2016
2016
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 28011763

2017
The Amyloid Phenomenon and Its Links with Human Disease.

Cold Spring Harbor perspectives in biology| PubMed ID: 28062560

2017
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 28096355

2017
2017
Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 28396410

2017
Ultrasensitive Measurement of Ca Influx into Lipid Vesicles Induced by Protein Aggregates.

Angewandte Chemie (International ed. in English)| PubMed ID: 28474754

2017
2017
2017
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 28584111

2017
Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 28652376

2017
2017
2017
Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 28698377

2017
2018
The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis.

Biochimica et biophysica acta. Molecular basis of disease| PubMed ID: 28711596

2017
2017
2017
Gradient-free determination of isoelectric points of proteins on chip.

Physical chemistry chemical physics : PCCP| PubMed ID: 28817152

2017
2017
2017
Thermodynamics of Polypeptide Supramolecular Assembly in the Short-Chain Limit.

Journal of the American Chemical Society| PubMed ID: 28994295

2017
2018
2017
Clusterin protects neurons against intracellular proteotoxicity.

Acta neuropathologica communications| PubMed ID: 29115989

2017
2017
2017
Inhibiting the Ca Influx Induced by Human CSF.

Cell reports| PubMed ID: 29241555

2017
2017
2018
2018
Optical Structural Analysis of Individual α-Synuclein Oligomers.

Angewandte Chemie (International ed. in English)| PubMed ID: 29342318

2018
2018
Biophotonics of Native Silk Fibrils.

Macromolecular bioscience| PubMed ID: 29377575

2018
2018
2018
2018
2018
2018
2018
2018
2018
2018
Cooperative Assembly of Hsp70 Subdomain Clusters.

Biochemistry| PubMed ID: 29763298

2018
2018
2018
Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils.

Chemical communications (Cambridge, England)| PubMed ID: 29951679

2018
2018
2018
Structural differences between toxic and nontoxic HypF-N oligomers.

Chemical communications (Cambridge, England)| PubMed ID: 30020284

2018
2018
Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.

Chembiochem : a European journal of chemical biology| PubMed ID: 30051958

2018
2018
Obituary: Nico van Nuland 1961-2017.

European biophysics journal : EBJ| PubMed ID: 30116857

2018
2018
2018
SAR by kinetics for drug discovery in protein misfolding diseases.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 30257937

2018
Statistical Mechanics of Globular Oligomer Formation by Protein Molecules.

The journal of physical chemistry. B| PubMed ID: 30336667

2018
2018
2018