Samuel I. A. Cohen

发表

From macroscopic measurements to microscopic mechanisms of protein aggregation.

Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles, 2012, Journal of molecular biology.

Nucleated Polymerisation in the Presence of Pre-Formed Seed Filaments

Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, 2011, International journal of molecular sciences.

The Kinetics and Mechanisms of Amyloid Formation

Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, 2013 .

An Analytical Solution to the Kinetics of Breakable Filament Assembly

Tuomas P. J. Knowles, Christopher A. Waudby, Michele Vendruscolo, 2009, Science.

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

Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, 2016, Proceedings of the National Academy of Sciences.

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

C. Dobson, A. Fink, G. Millhauser, 2011, Journal of molecular biology.

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

Alexander K. Buell, C. Dobson, Gary W. Jones, 2013, Philosophical Transactions of the Royal Society B: Biological Sciences.

Influence of specific HSP 70 domains on fibril formation of the yeast prion protein Ure 2

C. Dobson, Gary W. Jones, L. Itzhaki, 2013 .

SAR by kinetics for drug discovery in protein misfolding diseases

C. Dobson, M. Vendruscolo, S. Linse, 2018, Proceedings of the National Academy of Sciences.

Scaling analysis reveals the mechanism and rates of prion replication in vivo

C. Dobson, S. Hornemann, A. Aguzzi, 2021, Nature Structural & Molecular Biology.

Kinetic fingerprint of antibody therapies predicts outcomes of Alzheimer clinical trials

C. Dobson, M. Vendruscolo, P. Weinreb, 2019, bioRxiv.

Scaling analysis reveals molecular mechanism of prion self-replication in vivo .

C. Dobson, A. Aguzzi, C. Sigurdson, 2021 .

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

Michele Vendruscolo, Sara Linse, Christopher M Dobson, 2013, Proceedings of the National Academy of Sciences.

Secondary nucleation in amyloid formation.

S. Linse, T. Knowles, Xiaoting Yang, 2018, Chemical communications.

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

Sara Linse, Georg Meisl, Julius B Kirkegaard, 2014, Proceedings of the National Academy of Sciences.

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

Alexander K. Buell, A. Šarić, C. Dobson, 2018, Nature Chemistry.

Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease

Romain F. Laine, J. B. Kirkegaard, C. Dobson, 2021, Frontiers in Cell and Developmental Biology.

Multistep Inhibition of a-synuclein aggregation and toxicity in vitro 1 and in vivo by trodusquemine 2 3

J. B. Kirkegaard, C. Dobson, M. Vendruscolo, 2019 .

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

J. B. Kirkegaard, C. Dobson, M. Vendruscolo, 2018, ACS chemical biology.

Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates

C. Dobson, D. Klenerman, M. Vendruscolo, 2019, Science Advances.

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

C. Dobson, M. Vendruscolo, S. Linse, 2016, ACS nano.

Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

C. Dobson, M. Vendruscolo, P. Weinreb, 2020, Nature Structural & Molecular Biology.

Kinetic fingerprints differentiate anti-Aβ therapies

C. Dobson, M. Vendruscolo, P. Weinreb, 2019 .

The molecular chaperone Brichos breaks the catalytic cycle that generates toxic Aβ oligomers

Michele Vendruscolo, Sara Linse, Christopher M Dobson, 2015, Nature Structural &Molecular Biology.

Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

Christopher M. Dobson, Nicholas W. Wood, Carlos W. Bertoncini, 2012, Cell.

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

Michele Vendruscolo, Gabriella T Heller, Pietro Sormanni, 2017, Proceedings of the National Academy of Sciences.

Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide

A. Šarić, C. Dobson, M. Vendruscolo, 2020, bioRxiv.

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

C. Dobson, A. Natalello, T. Knowles, 2014, ACS chemical biology.

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

Michele Vendruscolo, Eugene M Terentjev, Christopher M Dobson, 2011, The Journal of chemical physics.

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

C. Dobson, T. Knowles, Samuel I. A. Cohen, 2014, Physical review. E, Statistical, nonlinear, and soft matter physics.

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

Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles, 2011, The Journal of chemical physics.

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

Michele Vendruscolo, Sara Linse, Michele Perni, 2016, Science Advances.

Observation of spatial propagation of amyloid assembly from single nuclei

A. Abate, C. Dobson, D. Weitz, 2011, Proceedings of the National Academy of Sciences.

Particle-Based Monte-Carlo Simulations of Steady-State Mass Transport at Intermediate Péclet Numbers

C. Dobson, M. Vendruscolo, T. Knowles, 2016 .

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

C. Dobson, M. Vendruscolo, F. Chiti, 2019, Nature Communications.

Hamiltonian Dynamics of Protein Filament Formation.

Michele Vendruscolo, Thomas C T Michaels, Christopher M Dobson, 2016, Physical review letters.

Kinetic profiling of therapeutic strategies for inhibiting the formation of amyloid oligomers.

M. Vendruscolo, T. Knowles, T. Michaels, 2022, The Journal of chemical physics.

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

C. Dobson, D. Otzen, T. Knowles, 2012, Biophysical journal.

Tau AD fragment aggregates proliferate through autocatalytic secondary nucleation

M. Vendruscolo, S. Linse, J. Habchi, 2021 .

Proliferation of Tau 304–380 Fragment Aggregates through Autocatalytic Secondary Nucleation

M. Vendruscolo, S. Linse, J. Habchi, 2021, ACS chemical neuroscience.

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

Alexander K. Buell, A. Šarić, C. Dobson, 2017, Chemical science.

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

Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles, 2011, The Journal of chemical physics.

Spatial propagation of protein polymerization.

Alexander K. Buell, D A Weitz, M Vendruscolo, 2014, Physical review letters.

Secondary nucleation in amyloid formation.

S. Linse, T. Knowles, Xiaoting Yang, 2018, Chemical communications.

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

C. Dobson, M. Vendruscolo, O. Hansson, 2016, Proceedings of the National Academy of Sciences.