Christopher M. Dobson

发表

Inversion of the Balance between Hydrophobic and Hydrogen Bonding Interactions in Protein Folding and Aggregation

Anthony W. Fitzpatrick, Tuomas P. J. Knowles, Christopher A. Waudby, 2011, PLoS Comput. Biol..

From Computer Simulations Meeting Review to Human Disease: Emerging Themes in Protein Folding

Christopher M. Dobson, United Kingdom, Sheena E. Radford, 1999 .

Monitoring Protein Folding Using Time-Resolved Biophysical Techniques

Christopher M. Dobson, Kevin W. Plaxco, C. Dobson, 1998 .

A Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates

Michele Vendruscolo, Christopher M. Dobson, Stefan Auer, 2008, PLoS Comput. Biol..

Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils

Michele Vendruscolo, Christopher M. Dobson, Sandipan Mohanty, 2007, PLoS Comput. Biol..

Obituary: Nico van Nuland 1961–2017

Christopher M. Dobson, André Matagne, 2018, European Biophysics Journal.

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

Christopher M. Dobson, Mireille Dumoulin, Lode Wyns, 2003, Nature.

Resolution enhancement of protein PMR spectra using the difference between a broadened and a normal spectrum

Christopher M. Dobson, Iain D. Campbell, C. Dobson, 1973 .

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

Clemens F. Kaminski, Christopher M. Dobson, Carlos W. Bertoncini, 2014, Chemistry & biology.

The amyloid state and its association with protein misfolding diseases

Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, 2014, Nature Reviews Molecular Cell Biology.

A Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal Transduction

Michele Vendruscolo, Christopher M. Dobson, Jörg Gsponer, 2008, Structure.

Amyloid fibrils from muscle myoglobin

Christopher M. Dobson, C. Dobson, M. Fändrich, 2001, Nature.

Supplementary Information Quantitative Analysis of Co-oligomer Formation by Amyloid-beta Peptide S1. Additional Controls for Aβ Sample Preparation S1.1. Tem Imaging

Tuomas P. J. Knowles, Christopher M. Dobson, Daan Frenkel, 2022 .

Protein-misfolding diseases: Getting out of shape

Christopher M. Dobson, C. Dobson, 2002, Nature.

Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Christopher M. Dobson, Mireille Dumoulin, Xavier Salvatella, 2010, Journal of the American Chemical Society.

Nuclear Overhauser effects and the assignment of the proton NMR spectra of proteins

Christopher M. Dobson, C. Dobson, C. Redfield, 1984 .

Comparison of four independently determined structures of human recombinant interleukin–4

Christopher M. Dobson, G. Marius Clore, Alexander Wlodawer, 1994, Nature Structural Biology.

Clusterin facilitates in vivo clearance of extracellular misfolded proteins

Christopher M. Dobson, Andrew Katsifis, Paula Berghofer, 2011, Cellular and Molecular Life Sciences.

Structural basis of the stability of a lysozyme molten globule

Christopher M. Dobson, Donald T. Haynie, C. Dobson, 1995, Nature Structural Biology.

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Christopher M. Dobson, Sheena E. Radford, Carol V. Robinson, 1997, Nature.

Progressive Changes in the Structure of Hardened C3S Cement Pastes due to Carbonation

Christopher M. Dobson, C. Dobson, I. Richardson, 1991 .

A residue-specific NMR view of the non-cooperative unfolding of a molten globule

Christopher M. Dobson, P. S. Kim, C. Dobson, 1997, Nature Structural Biology.

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

Tuomas P. J. Knowles, Christopher M. Dobson, Nicholas W. Wood, 2016, Proceedings of the National Academy of Sciences.

Structural biology: Prying into prions

Christopher M. Dobson, C. Dobson, 2005, Nature.

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

Christopher M. Dobson, Ernest Giralt, Carol V. Robinson, 2009, Proceedings of the National Academy of Sciences.

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 .

Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy

Clemens F. Kaminski, Alexander K. Buell, Christopher M. Dobson, 2013, Nano letters.

Kinetic partitioning of protein folding and aggregation

Christopher M. Dobson, Niccolò Taddei, Fabrizio Chiti, 2002, Nature Structural Biology.

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

Carlo Camilloni, Christopher A. Waudby, Michele Vendruscolo, 2016, Proceedings of the National Academy of Sciences.

Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding

Christopher M. Dobson, Niccolò Taddei, Fabrizio Chiti, 1999, Nature Structural Biology.

Use of protonless NMR spectroscopy to alleviate the loss of information resulting from exchange-broadening.

Christopher M. Dobson, Carlos W. Bertoncini, Shang-Te Danny Hsu, 2009, Journal of the American Chemical Society.

Molecular recycling within amyloid fibrils

Christopher M. Dobson, Ernest Giralt, Carol V. Robinson, 2005, Nature.

Alzheimer’s disease: addressing a twenty-first century plague

Christopher M. Dobson, C. Dobson, 2015, Rendiconti Lincei.

Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease

Alexander K. Buell, Tuomas P. J. Knowles, Michele Vendruscolo, 2014, PloS one.

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

Christopher M. Dobson, Nicholas W. Wood, Henrik Zetterberg, 2016, ACS chemical neuroscience.

Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.

Alexander K. Buell, Christopher M. Dobson, Ehud Gazit, 2016, Journal of the American Chemical Society.

Demonstration by NMR of folding domains in lysozyme

Christopher M. Dobson, Sheena E. Radford, Martin Karplus, 1991, Nature.

A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation

Sanne Abeln, Michele Vendruscolo, Christopher M. Dobson, 2014, PloS one.

Physical determinants of the self-replication of protein fibrils

Alexander K. Buell, Tuomas P. J. Knowles, Christopher M. Dobson, 2016, Nature Physics.

Direct Observation of the Three Regions in α-Synuclein that Determine its Membrane-Bound Behaviour

Michele Vendruscolo, Christopher M. Dobson, Gianluigi Veglia, 2014, Nature Communications.

Following protein folding in real time using NMR spectroscopy

Christopher M. Dobson, Nico A. J. van Nuland, C. Dobson, 1995, Nature Structural Biology.

An Analytical Solution to the Kinetics of Breakable Filament Assembly

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

The effects of guanidine hydrochloride on the ’random coil‘ conformations and NMR chemical shifts of the peptide series GGXGG

Christopher M. Dobson, Kevin W. Plaxco, Jonathan A. Jones, 1997, Journal of biomolecular NMR.

Protein Folding: Solid evidence for molten globules

Christopher M. Dobson, C. Dobson, 1994, Current Biology.

Hydration of Portland cement followed by29Si solid-state NMR spectroscopy

Christopher M. Dobson, Julian Richard Barnes, C. M. Dobson, 1985 .

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

Christopher M. Dobson, C. Dobson, Mark R. Wilson, 2015, PloS one.

The protofilament structure of insulin amyloid fibrils

Christopher M. Dobson, Carol V. Robinson, Helen R. Saibil, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The physical basis of protein misfolding disorders

Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, 2015 .

Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms

Christopher M. Dobson, Fabrizio Chiti, Leila M. Luheshi, 2006, The Journal of Neuroscience.

Structural characterization of a highly–ordered ‘molten globule’ at low pH

Christopher M. Dobson, C. Dobson, R. Smith, 1994, Nature Structural Biology.

Dynamic Visions of Enzymatic Reactions

Michele Vendruscolo, Christopher M. Dobson, C. Dobson, 2006, Science.

The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

Christopher M. Dobson, Mireille Dumoulin, Xavier Salvatella, 2010, Journal of molecular biology.

Unfolded proteins, compact states and molten globules

Christopher M. Dobson, 1992, Current 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.

Chemical shifts of aromatic protons in protein NMR spectra

Jeffrey C. Hoch, Christopher M. Dobson, J. Hoch, 1983 .

Exploration of partially unfolded states of human α-lactalbumin by molecular dynamics simulation

Christopher M. Dobson, Emanuele Paci, Martin Karplus, 2001 .

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.

Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways

Michele Vendruscolo, Christopher M. Dobson, C. Dobson, 2002 .