Department of Chemistry

Christopher M Dobson FRS Publications (2008)


Self-templated nucleation in peptide and protein aggregation.
Auer S, Dobson CM, Vendruscolo M, Maritan A
Computer Simulation, Hydrogen Bonding, Models, Molecular, Monte Carlo Method, Peptides, Protein Structure, Secondary, Proteins, Thermodynamics 2008, 25, 258101 -.


A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.
Auer S, Meersman F, Dobson CM, Vendruscolo M
Amyloid, Computer Simulation, Models, Molecular, Peptides, Protein Structure, Quaternary, Protein Structure, Secondary 2008, 27, e1000222 -. DOI: 10.1371/journal.pcbi.1000222


Recombinant amyloid beta-peptide production by coexpression with an affibody ligand
Macao B, Hoyer W, Sandberg A, Brorsson AC, Dobson CM, Hard T
BMC BIOTECHNOL 2008, 7, -. DOI: 10.1186/1472-6750-8-82


Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.
Chan PH, Pardon E, Menzer L, De Genst E, Kumita JR, Christodoulou J, Saerens D, Brans A, Bouillenne F, Archer DB, Robinson CV, Muyldermans S, Matagne A, Redfield C, Wyns L, Dobson CM, Dumoulin M
Amino Acid Sequence, Amyloid, Animals, Antibody Affinity, Camels, Catalytic Domain, Humans, Immunoglobulin Fragments, Molecular Sequence Data, Muramidase, Nuclear Magnetic Resonance, Biomolecular, Protein Engineering, Recombinant Proteins, Sequence Homology, Amino Acid 2008, 15, 11041-11054. DOI: 10.1021/bi8005797


Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.
Calloni G, Lendel C, Campioni S, Giannini S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X, Chiti F
Amino Acid Sequence, Amyloid, Carboxyl and Carbamoyl Transferases, Circular Dichroism, Cloning, Molecular, Escherichia coli Proteins, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Microscopy, Atomic Force, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Osmolar Concentration, Protein Engineering, Protein Folding, Protein Structure, Secondary, Spectrometry, Fluorescence, Structure-Activity Relationship, Urea 2008, 20, 13040-13050. DOI: 10.1021/ja8029224


Immunological features of alpha-synuclein in Parkinson's disease.
Roodveldt C, Christodoulou J, Dobson CM
Animals, Apoptosis, Humans, Immunity, Innate, Inflammation, Neuroglia, Parkinson Disease, alpha-Synuclein 2008, 22, 1820-1829. DOI: 10.1111/j.1582-4934.2008.00450.x


Label-free detection of amyloid growth with microcantilever sensors
Knowles TPJ, Shu W, Huber F, Lang HP, Gerber C, Dobson CM, Welland ME
NANOTECHNOLOGY 2008, 14, -. DOI: 10.1088/0957-4484/19/38/384007


Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.
Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, Klenerman D
Amyloid, Animals, Cattle, Fluorescence, Kinetics, Phosphatidylinositol 3-Kinases, Protein Folding, Spectrometry, Fluorescence, src Homology Domains 2008, 39, 14424-14429. DOI: 10.1073/pnas.0803086105


PHYS 90-Life on the edge: The origins and proliferation of protein misfolding diseases
Dobson CM
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY 2008, 0, -.


BIOT 243-Biophysical study of the aggregation of human lysozyme into amyloid fibrils
Dhulesia A, Baldwin AJ, Mossuto MF, Salvatella X, Dobson CM
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY 2008, 0, -.


BIOT 336-Exploring the energy landscape of human lysozyme toward an elucidation of the molecular mechanism of systemic amyloidosis
Dhulesia A, Kumita JR, Nietlispach D, Salvatella X, Dobson CM
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY 2008, 0, -.


Characterizing the first steps of amyloid formation for the ccbeta peptide.
Strodel B, Fitzpatrick AW, Vendruscolo M, Dobson CM, Wales DJ
Amyloid, Biopolymers, Molecular Structure, Peptides 2008, 6, 9998-10004. DOI: 10.1021/jp801222x


Life on the edge: The nature and origins of protein misfolding diseases
Dobson CM
J PEPT SCI 2008, 0, 26-26.


Prediction of aggregation-prone regions in structured proteins.
Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M
Amino Acid Sequence, Amyloid, Amyloid beta-Peptides, Animals, Calcitonin, Computer Simulation, Glucagon, Humans, Insulin, Islet Amyloid Polypeptide, Models, Molecular, Molecular Sequence Data, Muramidase, Myoglobin, Peptide Fragments, Prealbumin, Protein Conformation, Protein Folding, Proteins, Software, Trans-Activators, Transcriptional Elongation Factors, alpha-Synuclein 2008, 100, 425-436. DOI: 10.1016/j.jmb.2008.05.013


Life on the edge: the origins and proliferation of protein misfolding diseases
Dobson CM
FEBS JOURNAL 2008, 0, 27-27.


A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction.
Gsponer J, Christodoulou J, Cavalli A, Bui JM, Richter B, Dobson CM, Vendruscolo M
Calcium, Calmodulin, Ligands, Models, Molecular, Motion, Myosin-Light-Chain Kinase, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Signal Transduction 2008, 35, 736-746. DOI: 10.1016/j.str.2008.02.017


Molecular determinants of the aggregation behavior of alpha- and beta-synuclein.
Rivers RC, Kumita JR, Tartaglia GG, Dedmon MM, Pawar A, Vendruscolo M, Dobson CM, Christodoulou J
Amino Acid Sequence, Amyloid beta-Peptides, Humans, Molecular Sequence Data, Mutagenesis, Insertional, Nuclear Magnetic Resonance, Biomolecular, Parkinson Disease, Protein Conformation, Protein Folding, Recombinant Fusion Proteins, Sequence Deletion, Sodium Dodecyl Sulfate, Solubility, alpha-Synuclein, beta-Synuclein 2008, 29, 887-898. DOI: 10.1110/ps.073181508


Functionalised amyloid fibrils for roles in cell adhesion
Gras SL, Tickler AK, Squires AM, Devlin GL, Horton MA, Dobson CM, MacPhee CE
BIOMATERIALS 2008, 34, 1553-1562. DOI: 10.1016/j.biomaterials.2007.11.028


Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analyses.
Várnai P, Dobson CM, Vendruscolo M
Computer Simulation, Models, Chemical, Models, Molecular, Mutation, Protein Folding, Protein Structure, Tertiary, Ubiquitin 2008, 6, 575-588. DOI: 10.1016/j.jmb.2008.01.012


Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins
Dalal S, Canet D, Kaiser SE, Dobson CM, Regan L
PROTEIN ENG DES SEL 2008, 2, 197-206. DOI: 10.1093/protein/gzm088


Characterization of folding the four-helix bundle protein Rop by real-time NMR
van Nuland NAJ, Dobson CM, Regan L
PROTEIN ENG DES SEL 2008, 4, 165-170. DOI: 10.1093/protein/gzm081


Protein misfolding and disease: from the test tube to the organism.
Luheshi LM, Crowther DC, Dobson CM
Animals, Disease, Disease Models, Animal, Humans, Protein Folding, Proteins 2008, 45, 25-31. DOI: 10.1016/j.cbpa.2008.02.011


Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements
Baldwin AJ, Anthony-Cahill SJ, Knowles TPJ, Lippens G, Christodoulou J, Barker PD, Dobson CM
ANGEW CHEM INT EDIT 2008, 11, 3385-3387. DOI: 10.1002/anie.200703915


“Protein Folding and Misfolding: From Atoms to Organisms' in Physical biology: From Atoms to Medicine
Dobson CM
2008, 289-335.


Calculation of the free energy barriers in the oligomerisation of Abeta peptide fragments.
Cheon M, Favrin G, Chang I, Dobson CM, Vendruscolo M
Amyloid beta-Peptides, Binding Sites, Oligopeptides, Peptide Fragments, Protein Conformation, Thermodynamics 2008, 9, 5614-5622.