Professor Christopher Dobson

Christopher Dobson

University position

Professor

Professor Christopher Dobson is pleased to consider applications from prospective PhD students.

Departments

Department of Chemistry

Email

cmd44@cam.ac.uk

Home page

http://www-dobson.ch.cam.ac.uk/

Research Themes

Cellular and Molecular Neuroscience

Clinical and Veterinary Neuroscience

Interests

Our group is investigating the molecular origins of neurodegenerative disorders, such as Alzheimer’s and Parkinson’s Disease, that are characterised neuropathologically by the presence of amyloid fibrils. The aim of our research is to understand the fundamental molecular origins of protein aggregation into amyloid and the relationship between this process and the pathogenesis of neurodegenerative diseases. We have used a combination of in vitro biophysics and computational modelling to describe very accurately the intrinsic physicochemical properties of proteins that determine their propensity to form amyloid fibrils in test tubes. More recently we have begun to study the determinants of amyloid aggregation in a Drosophila model of Alzheimer’s Disease (in collaboration with Prof. D. Lomas and Dr. D. Crowther here in Cambridge) and are using this model to understand in more detail the relationship between protein misfolding and pathogenesis.

Research Focus

Keywords

amyloid

neurodegeneration

aggregation

protein misfolding

protein folding

Clinical conditions

Alzheimer's disease

Dementia

Huntington's disease

Parkinson's disease

Prion diseases

Equipment

Atomic Force Microscopy

Behavioural analysis

CD Spectroscopy

Cell culture

Computational modelling

Computer Simulations

Drosophila Transgenesis and Analysis

FTIR Spectroscopy

Immunohistochemistry

Microscopy

NMR Spectrsocopy

Protein purification

Recombinant protein expression

Transmission EM

Collaborators

Cambridge

Carol Brayne

Damian Crowther

David Lomas

Carol Robinson

Michele Vendruscolo

Mark Welland

International

Fabrizio Chiti Web: http://www.fabriziochiti.it

Robert Griffin Web: http://web.mit.edu/chemist...

Massimo Stefani Web: http://www4.unifi.it/scibio/...

Mark Wilson Web: http://www.uow.edu.au/science...

Associated News Items


Key publications

Baglioni S, Casamenti F, Bucciantini M, Luheshi LM, Taddei N, Chiti F, Dobson CM, Stefani M (2006), “Prefibrillar amyloid aggregates could be generic toxins in higher organisms” J Neurosci 26(31):8160-7 Details

Dobson CM (2003), “Protein folding and misfolding” Nature 426(6968):884-90

Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM, Stefani M (2002), “Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases” Nature 416(6880):507-11

Publications

2014

Abeln S, Vendruscolo M, Dobson CM, Frenkel D (2014), “A simple lattice model that captures protein folding, aggregation and amyloid formation.” PLoS One 9(1):e85185 Details

Arosio P, Vendruscolo M, Dobson CM, Knowles TP (2014), “Chemical kinetics for drug discovery to combat protein aggregation diseases.” Trends Pharmacol Sci 35(3):127-135 Details

Bolognesi B, Cohen SI, Aran Terol P, Esbjörner EK, Giorgetti S, Mossuto MF, Natalello A, Brorsson AC, Knowles TP, Dobson CM, Luheshi LM (2014), “Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated aβ42 Peptide.” ACS Chem Biol 9(2):378-82 Details

Buell AK, Galvagnion C, Gaspar R, Sparr E, Vendruscolo M, Knowles TP, Linse S, Dobson CM (2014), “Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.” Proc Natl Acad Sci U S A Details

Cohen SI, Rajah L, Yoon CH, Buell AK, White DA, Sperling RA, Vendruscolo M, Terentjev EM, Dobson CM, Weitz DA, Knowles TP (2014), “Spatial propagation of protein polymerization.” Phys Rev Lett 112(9):098101 Details

Dobson CM (2014), “Dynamics and Timekeeping in Biological Systems.” Annu Rev Biochem Details

Esbjörner EK, Chan F, Rees E, Erdelyi M, Luheshi LM, Bertoncini CW, Kaminski CF, Dobson CM, Kaminski Schierle GS (2014), “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.” Chem Biol 21(6):732-42 Details

Fusco G, De Simone A, Gopinath T, Vostrikov V, Vendruscolo M, Dobson CM, Veglia G (2014), “Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.” Nat Commun 5:3827 Details

Garcia GA, Cohen SI, Dobson CM, Knowles TP (2014), “Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters.” Phys Rev E Stat Nonlin Soft Matter Phys 89(3-1):032712 Details

Knowles TP, Vendruscolo M, Dobson CM (2014), “The amyloid state and its association with protein misfolding diseases.” Nat Rev Mol Cell Biol 15(6):384-96 Details

Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, Vad BS, Paslawski W, Christiansen G, Valnickova-Hansen Z, Andreasen M, Enghild JJ, Pedersen JS, Dobson CM, Knowles TP, Otzen DE (2014), “The Role of Stable α-Synuclein Oligomers in the Molecular Events Underlying Amyloid Formation.” J Am Chem Soc Details

Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, Cohen SI, Dobson CM, Linse S, Knowles TP (2014), “Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.” Proc Natl Acad Sci U S A Details

Narayan P, Holmström KM, Kim DH, Whitcomb DJ, Wilson MR, St George-Hyslop P, Wood NW, Dobson CM, Cho K, Abramov AY, Klenerman D (2014), “Rare Individual Amyloid-β Oligomers Act on Astrocytes to Initiate Neuronal Damage.” Biochemistry 53(15):2442-53 Details

O'Brien EP, Ciryam P, Vendruscolo M, Dobson CM (2014), “Understanding the Influence of Codon Translation Rates on Cotranslational Protein Folding.” Acc Chem Res Details

O'Brien EP, Vendruscolo M, Dobson CM (2014), “Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.” Nat Commun 5:2988 Details

Pinotsi D, Buell AK, Galvagnion C, Dobson CM, Kaminski Schierle GS, Kaminski CF (2014), “Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.” Nano Lett 14(1):339-45 Details

Tóth G, Gardai SJ, Zago W, Bertoncini CW, Cremades N, Roy SL, Tambe MA, Rochet JC, Galvagnion C, Skibinski G, Finkbeiner S, Bova M, Regnstrom K, Chiou SS, Johnston J, Callaway K, Anderson JP, Jobling MF, Buell AK, Yednock TA, Knowles TP, Vendruscolo M, Christodoulou J, Dobson CM, Schenk D, McConlogue L (2014), “Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson's Disease.” PLoS One 9(2):e87133 Details

Wacker J, Rönicke R, Westermann M, Wulff M, Reymann KG, Dobson CM, Horn U, Crowther DC, Luheshi LM, Fändrich M (2014), “Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies.” Acta Neuropathol Commun 2(1):43 Details

Wyatt AR, Kumita JR, Mifsud RW, Gooden CA, Wilson MR, Dobson CM (2014), “Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.” Proc Natl Acad Sci U S A Details

2013

Aprile FA, Dhulesia A, Stengel F, Roodveldt C, Benesch JL, Tortora P, Robinson CV, Salvatella X, Dobson CM, Cremades N (2013), “Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.” PLoS One 8(6):e67961 Details

Buell AK, Hung P, Salvatella X, Welland ME, Dobson CM, Knowles TP (2013), “Electrostatic effects in filamentous protein aggregation.” Biophys J 104(5):1116-26 Details

Chan FT, Kaminski Schierle GS, Kumita JR, Bertoncini CW, Dobson CM, Kaminski CF (2013), “Protein amyloids develop an intrinsic fluorescence signature during aggregation.” Analyst 138(7):2156-62 Details

Ciryam P, Morimoto RI, Vendruscolo M, Dobson CM, O'Brien EP (2013), “In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome.” Proc Natl Acad Sci U S A 110(2):E132-40 Details

Ciryam P, Tartaglia GG, Morimoto RI, Dobson CM, Vendruscolo M (2013), “Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.” Cell Rep 5(3):781-90 Details

Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, Rajah L, Otzen DE, Vendruscolo M, Dobson CM, Knowles TP (2013), “Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.” Proc Natl Acad Sci U S A 110(24):9758-63 Details

De Genst E, Chan PH, Pardon E, Hsu ST, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M (2013), “A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.” J Phys Chem B 117(42):13245-58 Details

De Simone A, Montalvao RW, Dobson CM, Vendruscolo M (2013), “Characterization of the interdomain motions in hen lysozyme using residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations.” Biochemistry 52(37):6480-6 Details

Debelouchina GT, Bayro MJ, Fitzpatrick AW, Ladizhansky V, Colvin MT, Caporini MA, Jaroniec CP, Bajaj VS, Rosay M, Macphee CE, Vendruscolo M, Maas WE, Dobson CM, Griffin RG (2013), “Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.” J Am Chem Soc 135(51):19237-47 Details

Fitzpatrick AW, Debelouchina GT, Bayro MJ, Clare DK, Caporini MA, Bajaj VS, Jaroniec CP, Wang L, Ladizhansky V, Müller SA, MacPhee CE, Waudby CA, Mott HR, De Simone A, Knowles TP, Saibil HR, Vendruscolo M, Orlova EV, Griffin RG, Dobson CM (2013), “Atomic structure and hierarchical assembly of a cross-β amyloid fibril.” Proc Natl Acad Sci U S A 110(14):5468-73 Details

Guilliams T, El-Turk F, Buell AK, O'Day EM, Aprile FA, Esbjörner EK, Vendruscolo M, Cremades N, Pardon E, Wyns L, Welland ME, Steyaert J, Christodoulou J, Dobson CM, De Genst E (2013), “Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.” J Mol Biol 425(14):2397-411 Details

Narayan P, Ganzinger KA, McColl J, Weimann L, Meehan S, Qamar S, Carver JA, Wilson MR, St George-Hyslop P, Dobson CM, Klenerman D (2013), “Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.” J Am Chem Soc 135(4):1491-8 Details

Ouberai MM, Wang J, Swann MJ, Galvagnion C, Guilliams T, Dobson CM, Welland ME (2013), “α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.” J Biol Chem 288(29):20883-95 Details

Pinotsi D, Buell AK, Dobson CM, Kaminski Schierle GS, Kaminski CF (2013), “A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence.” Chembiochem 14(7):846-50 Details

Roodveldt C, Labrador-Garrido A, Gonzalez-Rey E, Lachaud CC, Guilliams T, Fernandez-Montesinos R, Benitez-Rondan A, Robledo G, Hmadcha A, Delgado M, Dobson CM, Pozo D (2013), “Preconditioning of microglia by α-synuclein strongly affects the response induced by toll-like receptor (TLR) stimulation.” PLoS One 8(11):e79160 Details

Vendruscolo M, Dobson CM (2013), “Structural biology: Protein self-assembly intermediates.” Nat Chem Biol 9(4):216-7 Details

Volpatti LR, Vendruscolo M, Dobson CM, Knowles TP (2013), “A clear view of polymorphism, twist, and chirality in amyloid fibril formation.” ACS Nano 7(12):10443-8 Details

Waudby CA, Camilloni C, Fitzpatrick AW, Cabrita LD, Dobson CM, Vendruscolo M, Christodoulou J (2013), “In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells.” PLoS One 8(8):e72286 Details

Wyatt AR, Constantinescu P, Ecroyd H, Dobson CM, Wilson MR, Kumita JR, Yerbury JJ (2013), “Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms.” FEBS Lett 587(5):398-403 Details

Xu LQ, Wu S, Buell AK, Cohen SI, Chen LJ, Hu WH, Cusack SA, Itzhaki LS, Zhang H, Knowles TP, Dobson CM, Welland ME, Jones GW, Perrett S (2013), “Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.” Philos Trans R Soc Lond B Biol Sci 368(1617):20110410 Details

Zhu M, De Simone A, Schenk D, Toth G, Dobson CM, Vendruscolo M (2013), “Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.” J Chem Phys 139(3):035101 Details

2012

Abelein A, Bolognesi B, Dobson CM, Gräslund A, Lendel C (2012), “Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly.” Biochemistry 51(1):126-37 Details

Ahn M, De Genst E, Kaminski Schierle GS, Erdelyi M, Kaminski CF, Dobson CM, Kumita JR (2012), “Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.” PLoS One 7(11):e50192 Details

Bemporad F, De Simone A, Chiti F, Dobson CM (2012), “Characterizing intermolecular interactions that initiate native-like protein aggregation.” Biophys J 102(11):2595-604 Details

Buell AK, Dhulesia A, White DA, Knowles TP, Dobson CM, Welland ME (2012), “Detailed analysis of the energy barriers for amyloid fibril growth.” Angew Chem Int Ed Engl 51(21):5247-51 Details

Buell AK, Dobson CM, Welland ME (2012), “Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances.” Methods Mol Biol 849:101-19 Details

Cohen SI, Vendruscolo M, Dobson CM, Knowles TP (2012), “From macroscopic measurements to microscopic mechanisms of protein aggregation.” J Mol Biol 421(2-3):160-71 Details

Cremades N, Cohen SI, Deas E, Abramov AY, Chen AY, Orte A, Sandal M, Clarke RW, Dunne P, Aprile FA, Bertoncini CW, Wood NW, Knowles TP, Dobson CM, Klenerman D (2012), “Direct observation of the interconversion of normal and toxic forms of α-synuclein.” Cell 149(5):1048-59 Details

De Genst E, Dobson CM (2012), “Nanobodies as structural probes of protein misfolding and fibril formation.” Methods Mol Biol 911:533-58 Details

De Simone A, Kitchen C, Kwan AH, Sunde M, Dobson CM, Frenkel D (2012), “Intrinsic disorder modulates protein self-assembly and aggregation.” Proc Natl Acad Sci U S A 109(18):6951-6 Details

Evangelisti E, Cecchi C, Cascella R, Sgromo C, Becatti M, Dobson CM, Chiti F, Stefani M (2012), “Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers.” J Cell Sci 125(Pt 10):2416-27 Details

Fusco G, De Simone A, Hsu ST, Bemporad F, Vendruscolo M, Chiti F, Dobson CM (2012), “¹H, ¹³C and ¹⁵N resonance assignments of human muscle acylphosphatase.” Biomol NMR Assign 6(1):27-9 Details

Gregory JM, Barros TP, Meehan S, Dobson CM, Luheshi LM (2012), “The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila.” PLoS One 7(2):e31899 Details

Knowles TP, De Simone A, Fitzpatrick AW, Baldwin A, Meehan S, Rajah L, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM (2012), “Twisting transition between crystalline and fibrillar phases of aggregated peptides.” Phys Rev Lett 109(15):158101 Details

Kumita JR, Helmfors L, Williams J, Luheshi LM, Menzer L, Dumoulin M, Lomas DA, Crowther DC, Dobson CM, Brorsson AC (2012), “Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster.” FASEB J 26(1):192-202 Details

Lorenzen N, Cohen SI, Nielsen SB, Herling TW, Christiansen G, Dobson CM, Knowles TP, Otzen D (2012), “Role of elongation and secondary pathways in S6 amyloid fibril growth.” Biophys J 102(9):2167-75 Details

Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F (2012), “Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.” Proc Natl Acad Sci U S A 109(31):12479-84 Details

McGuire EK, Motskin M, Bolognesi B, Bergin SD, Knowles TP, Skepper J, Luheshi LM, McComb DW, Dobson CM, Porter AE (2012), “Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid β peptide in cells.” ACS Nano 6(6):4740-7 Details

Narayan P, Meehan S, Carver JA, Wilson MR, Dobson CM, Klenerman D (2012), “Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones.” Biochemistry 51(46):9270-6 Details

O'Brien EP, Christodoulou J, Vendruscolo M, Dobson CM (2012), “Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions.” J Am Chem Soc 134(26):10920-32 Details

O'Brien EP, Vendruscolo M, Dobson CM (2012), “Prediction of variable translation rate effects on cotranslational protein folding.” Nat Commun 3:868 Details

Roodveldt C, Andersson A, De Genst EJ, Labrador-Garrido A, Buell AK, Dobson CM, Tartaglia GG, Vendruscolo M (2012), “A rationally designed six-residue swap generates comparability in the aggregation behavior of α-synuclein and β-synuclein.” Biochemistry 51(44):8771-8 Details

Speretta E, Jahn TR, Tartaglia GG, Favrin G, Barros TP, Imarisio S, Lomas DA, Luheshi LM, Crowther DC, Dobson CM (2012), “Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity.” J Biol Chem 287(24):20748-54 Details

Waudby CA, Mantle MD, Cabrita LD, Gladden LF, Dobson CM, Christodoulou J (2012), “Rapid distinction of intracellular and extracellular proteins using NMR diffusion measurements.” J Am Chem Soc 134(28):11312-5 Details

2011

Baldwin AJ, Knowles TP, Tartaglia GG, Fitzpatrick AW, Devlin GL, Shammas SL, Waudby CA, Mossuto MF, Meehan S, Gras SL, Christodoulou J, Anthony-Cahill SJ, Barker PD, Vendruscolo M, Dobson CM (2011), “Metastability of native proteins and the phenomenon of amyloid formation.” J Am Chem Soc 133(36):14160-3 Details

Bayro MJ, Debelouchina GT, Eddy MT, Birkett NR, MacPhee CE, Rosay M, Maas WE, Dobson CM, Griffin RG (2011), “Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.” J Am Chem Soc 133(35):13967-74 Details

Buell AK, Dhulesia A, Mossuto MF, Cremades N, Kumita JR, Dumoulin M, Welland ME, Knowles TP, Salvatella X, Dobson CM (2011), “Population of nonnative states of lysozyme variants drives amyloid fibril formation.” J Am Chem Soc 133(20):7737-43 Details

Buell AK, Esbjörner EK, Riss PJ, White DA, Aigbirhio FI, Toth G, Welland ME, Dobson CM, Knowles TP (2011), “Probing small molecule binding to amyloid fibrils.” Phys Chem Chem Phys 13(45):20044-52 Details

Cabrita LD, Waudby CA, Dobson CM, Christodoulou J (2011), “Solution-state nuclear magnetic resonance spectroscopy and protein folding.” Methods Mol Biol 752:97-120 Details

Cohen SI, Vendruscolo M, Dobson CM, Knowles TP (2011), “Nucleated polymerisation in the presence of pre-formed seed filaments.” Int J Mol Sci 12(9):5844-52 Details

Cohen SI, Vendruscolo M, Dobson CM, Knowles TP (2011), “Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations.” J Chem Phys 135(6):065107 Details

Cohen SI, Vendruscolo M, Dobson CM, Knowles TP (2011), “Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.” J Chem Phys 135(6):065106 Details

Cohen SI, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM, Knowles TP (2011), “Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.” J Chem Phys 135(6):065105 Details

De Simone A, Dhulesia A, Soldi G, Vendruscolo M, Hsu ST, Chiti F, Dobson CM (2011), “Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility.” Proc Natl Acad Sci U S A 108(52):21057-62 Details

Fitzpatrick AW, Knowles TP, Waudby CA, Vendruscolo M, Dobson CM (2011), “Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation.” PLoS Comput Biol 7(10):e1002169 Details

Jahn TR, Kohlhoff KJ, Scott M, Tartaglia GG, Lomas DA, Dobson CM, Vendruscolo M, Crowther DC (2011), “Detection of early locomotor abnormalities in a Drosophila model of Alzheimer's disease.” J Neurosci Methods 197(1):186-9 Details

Kaminski Schierle GS, Bertoncini CW, Chan FT, van der Goot AT, Schwedler S, Skepper J, Schlachter S, van Ham T, Esposito A, Kumita JR, Nollen EA, Dobson CM, Kaminski CF (2011), “A FRET sensor for non-invasive imaging of amyloid formation in vivo.” Chemphyschem 12(3):673-80 Details

Kaminski Schierle GS, van de Linde S, Erdelyi M, Esbjörner EK, Klein T, Rees E, Bertoncini CW, Dobson CM, Sauer M, Kaminski CF (2011), “In situ measurements of the formation and morphology of intracellular β-amyloid fibrils by super-resolution fluorescence imaging.” J Am Chem Soc 133(33):12902-5 Details

Knowles TP, Devlin GL, Dobson CM, Welland ME (2011), “Probing protein aggregation with quartz crystal microbalances.” Methods Mol Biol 752:137-45 Details

Knowles TP, White DA, Abate AR, Agresti JJ, Cohen SI, Sperling RA, De Genst EJ, Dobson CM, Weitz DA (2011), “Observation of spatial propagation of amyloid assembly from single nuclei.” Proc Natl Acad Sci U S A 108(36):14746-51 Details

Kohlhoff KJ, Jahn TR, Lomas DA, Dobson CM, Crowther DC, Vendruscolo M (2011), “The iFly tracking system for an automated locomotor and behavioural analysis of Drosophila melanogaster.” Integr Biol (Camb) 3(7):755-60 Details

Levitan K, Chereau D, Cohen SI, Knowles TP, Dobson CM, Fink AL, Anderson JP, Goldstein JM, Millhauser GL (2011), “Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein.” J Mol Biol 411(2):329-33 Details

Mossuto MF, Bolognesi B, Guixer B, Dhulesia A, Agostini F, Kumita JR, Tartaglia GG, Dumoulin M, Dobson CM, Salvatella X (2011), “Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.” Angew Chem Int Ed Engl 50(31):7048-51 Details

Narayan P, Orte A, Clarke RW, Bolognesi B, Hook S, Ganzinger KA, Meehan S, Wilson MR, Dobson CM, Klenerman D (2011), “The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.” Nat Struct Mol Biol 19(1):79-83 Details

O'Brien EP, Christodoulou J, Vendruscolo M, Dobson CM (2011), “New scenarios of protein folding can occur on the ribosome.” J Am Chem Soc 133(3):513-26 Details

Raimondi S, Guglielmi F, Giorgetti S, Di Gaetano S, Arciello A, Monti DM, Relini A, Nichino D, Doglia SM, Natalello A, Pucci P, Mangione P, Obici L, Merlini G, Stoppini M, Robustelli P, Tartaglia GG, Vendruscolo M, Dobson CM, Piccoli R, Bellotti V (2011), “Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I.” J Mol Biol 407(3):465-76 Details

Shammas SL, Knowles TP, Baldwin AJ, Macphee CE, Welland ME, Dobson CM, Devlin GL (2011), “Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions.” Biophys J 100(11):2783-91 Details

Shammas SL, Waudby CA, Wang S, Buell AK, Knowles TP, Ecroyd H, Welland ME, Carver JA, Dobson CM, Meehan S (2011), “Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.” Biophys J 101(7):1681-9 Details

Vendruscolo M, Dobson CM (2011), “Protein dynamics: Moore's law in molecular biology.” Curr Biol 21(2):R68-70 Details

Vendruscolo M, Knowles TP, Dobson CM (2011), “Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.” Cold Spring Harb Perspect Biol 3(12) Details

Wang YQ, Buell AK, Wang XY, Welland ME, Dobson CM, Knowles TP, Perrett S (2011), “Relationship between prion propensity and the rates of individual molecular steps of fibril assembly.” J Biol Chem 286(14):12101-7 Details

Whyteside G, Alcocer MJ, Kumita JR, Dobson CM, Lazarou M, Pleass RJ, Archer DB (2011), “Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris.” PLoS One 6(7):e22692 Details

Wyatt AR, Yerbury JJ, Berghofer P, Greguric I, Katsifis A, Dobson CM, Wilson MR (2011), “Clusterin facilitates in vivo clearance of extracellular misfolded proteins.” Cell Mol Life Sci 68(23):3919-31 Details

2010

Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG (2010), “High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .” Biochemistry 49(35):7474-84 Details

Bodner CR, Maltsev AS, Dobson CM, Bax A (2010), “Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy.” Biochemistry 49(5):862-71 Details

Bolognesi B, Kumita JR, Barros TP, Esbjorner EK, Luheshi LM, Crowther DC, Wilson MR, Dobson CM, Favrin G, Yerbury JJ (2010), “ANS binding reveals common features of cytotoxic amyloid species.” ACS Chem Biol 5(8):735-40 Details

Brorsson AC, Bolognesi B, Tartaglia GG, Shammas SL, Favrin G, Watson I, Lomas DA, Chiti F, Vendruscolo M, Dobson CM, Crowther DC, Luheshi LM (2010), “Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.” Biophys J 98(8):1677-84 Details

Brorsson AC, Kumita JR, MacLeod I, Bolognesi B, Speretta E, Luheshi LM, Knowles TP, Dobson CM, Crowther DC (2010), “Methods and models in neurodegenerative and systemic protein aggregation diseases.” Front Biosci (Landmark Ed) 15:373-96 Details

Buell AK, Blundell JR, Dobson CM, Welland ME, Terentjev EM, Knowles TP (2010), “Frequency factors in a landscape model of filamentous protein aggregation.” Phys Rev Lett 104(22):228101 Details

Buell AK, Dobson CM, Knowles TP, Welland ME (2010), “Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors.” Biophys J 99(10):3492-7 Details

Buell AK, White DA, Meier C, Welland ME, Knowles TP, Dobson CM (2010), “Surface attachment of protein fibrils via covalent modification strategies.” J Phys Chem B 114(34):10925-38 Details

Cabrita LD, Dobson CM, Christodoulou J (2010), “Protein folding on the ribosome.” Curr Opin Struct Biol 20(1):33-45 Details

Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F (2010), “A causative link between the structure of aberrant protein oligomers and their toxicity.” Nat Chem Biol 6(2):140-7 Details

Caporini MA, Bajaj VS, Veshtort M, Fitzpatrick A, MacPhee CE, Vendruscolo M, Dobson CM, Griffin RG (2010), “Accurate determination of interstrand distances and alignment in amyloid fibrils by magic angle spinning NMR.” J Phys Chem B 114(42):13555-61 Details

Carulla N, Zhou M, Giralt E, Robinson CV, Dobson CM (2010), “Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange.” Acc Chem Res 43(8):1072-9 Details

De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, Meehan S, Dumoulin M, Hsu ST, Cremades N, Verschueren KH, Pardon E, Wyns L, Steyaert J, Christodoulou J, Dobson CM (2010), “Structure and properties of a complex of α-synuclein and a single-domain camelid antibody.” J Mol Biol 402(2):326-43 Details

Dhulesia A, Cremades N, Kumita JR, Hsu ST, Mossuto MF, Dumoulin M, Nietlispach D, Akke M, Salvatella X, Dobson CM (2010), “Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.” J Am Chem Soc 132(44):15580-8 Details

Hagan CL, Johnson RJ, Dhulesia A, Dumoulin M, Dumont J, De Genst E, Christodoulou J, Robinson CV, Dobson CM, Kumita JR (2010), “A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis.” Protein Eng Des Sel 23(7):499-506 Details

Hsu ST, Blaser G, Behrens C, Cabrita LD, Dobson CM, Jackson SE (2010), “Folding study of Venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions.” J Biol Chem 285(7):4859-69 Details

Lendel C, Bolognesi B, Wahlström A, Dobson CM, Gräslund A (2010), “Detergent-like interaction of Congo red with the amyloid beta peptide.” Biochemistry 49(7):1358-60 Details

Luheshi LM, Hoyer W, de Barros TP, van Dijk Härd I, Brorsson AC, Macao B, Persson C, Crowther DC, Lomas DA, Ståhl S, Dobson CM, Härd T (2010), “Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo.” PLoS Biol 8(3):e1000334 Details

Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, de Laureto PP, Dumoulin M, Fontana A, Dobson CM, Salvatella X (2010), “The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity.” J Mol Biol 402(5):783-96 Details

O'Brien EP, Hsu ST, Christodoulou J, Vendruscolo M, Dobson CM (2010), “Transient tertiary structure formation within the ribosome exit port.” J Am Chem Soc 132(47):16928-37 Details

Roodveldt C, Labrador-Garrido A, Gonzalez-Rey E, Fernandez-Montesinos R, Caro M, Lachaud CC, Waudby CA, Delgado M, Dobson CM, Pozo D (2010), “Glial innate immunity generated by non-aggregated alpha-synuclein in mouse: differences between wild-type and Parkinson's disease-linked mutants.” PLoS One 5(10):e13481 Details

Sandberg A, Luheshi LM, Söllvander S, Pereira de Barros T, Macao B, Knowles TP, Biverstål H, Lendel C, Ekholm-Petterson F, Dubnovitsky A, Lannfelt L, Dobson CM, Härd T (2010), “Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering.” Proc Natl Acad Sci U S A 107(35):15595-600 Details

Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M (2010), “Physicochemical determinants of chaperone requirements.” J Mol Biol 400(3):579-88 Details

van Ham TJ, Esposito A, Kumita JR, Hsu ST, Kaminski Schierle GS, Kaminski CF, Dobson CM, Nollen EA, Bertoncini CW (2010), “Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation.” J Mol Biol 395(3):627-42 Details

Waudby CA, Knowles TP, Devlin GL, Skepper JN, Ecroyd H, Carver JA, Welland ME, Christodoulou J, Dobson CM, Meehan S (2010), “The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.” Biophys J 98(5):843-51 Details

White DA, Buell AK, Knowles TP, Welland ME, Dobson CM (2010), “Protein aggregation in crowded environments.” J Am Chem Soc 132(14):5170-5 Details

2009

Allison JR, Varnai P, Dobson CM, Vendruscolo M (2009), “Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements.” J Am Chem Soc 131(51):18314-26 Details

Bayro MJ, Maly T, Birkett NR, Dobson CM, Griffin RG (2009), “Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy.” Angew Chem Int Ed Engl 48(31):5708-10 Details

Bodner CR, Dobson CM, Bax A (2009), “Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy.” J Mol Biol 390(4):775-90 Details

Buell AK, Tartaglia GG, Birkett NR, Waudby CA, Vendruscolo M, Salvatella X, Welland ME, Dobson CM, Knowles TP (2009), “Position-dependent electrostatic protection against protein aggregation.” Chembiochem 10(8):1309-12 Details

Bui JM, Gsponer J, Vendruscolo M, Dobson CM (2009), “Analysis of sub-tauc and supra-tauc motions in protein Gbeta1 using molecular dynamics simulations.” Biophys J 97(9):2513-20 Details

Cabrita LD, Hsu ST, Launay H, Dobson CM, Christodoulou J (2009), “Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.” Proc Natl Acad Sci U S A 106(52):22239-44 Details

Calamai M, Tartaglia GG, Vendruscolo M, Chiti F, Dobson CM (2009), “Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase.” J Mol Biol 387(4):965-74 Details

Carulla N, Zhou M, Arimon M, Gairí M, Giralt E, Robinson CV, Dobson CM (2009), “Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.” Proc Natl Acad Sci U S A 106(19):7828-33 Details

Chiti F, Dobson CM (2009), “Amyloid formation by globular proteins under native conditions.” Nat Chem Biol 5(1):15-22 Details

Frare E, Mossuto MF, de Laureto PP, Tolin S, Menzer L, Dumoulin M, Dobson CM, Fontana A (2009), “Characterization of oligomeric species on the aggregation pathway of human lysozyme.” J Mol Biol 387(1):17-27 Details

Hamada D, Tanaka T, Tartaglia GG, Pawar A, Vendruscolo M, Kawamura M, Tamura A, Tanaka N, Dobson CM (2009), “Competition between folding, native-state dimerisation and amyloid aggregation in beta-lactoglobulin.” J Mol Biol 386(3):878-90 Details

Hsu ST, Behrens C, Cabrita LD, Dobson CM (2009), “1H, 15N and 13C assignments of yellow fluorescent protein (YFP) Venus.” Biomol NMR Assign 3(1):67-72 Details

Hsu ST, Bertoncini CW, Dobson CM (2009), “Use of protonless NMR spectroscopy to alleviate the loss of information resulting from exchange-broadening.” J Am Chem Soc 131(21):7222-3 Details

Hsu ST, Cabrita LD, Christodoulou J, Dobson CM (2009), “1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states.” Biomol NMR Assign 3(1):29-31 Details

Hsu ST, Cabrita LD, Fucini P, Christodoulou J, Dobson CM (2009), “Probing side-chain dynamics of a ribosome-bound nascent chain using methyl NMR spectroscopy.” J Am Chem Soc 131(24):8366-7 Details

Hsu ST, Cabrita LD, Fucini P, Dobson CM, Christodoulou J (2009), “Structure, dynamics and folding of an immunoglobulin domain of the gelation factor (ABP-120) from Dictyostelium discoideum.” J Mol Biol 388(4):865-79 Details

Hsu ST, Dobson CM (2009), “1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli.” Biomol NMR Assign 3(1):17-20 Details

Knowles TP, Waudby CA, Devlin GL, Cohen SI, Aguzzi A, Vendruscolo M, Terentjev EM, Welland ME, Dobson CM (2009), “An analytical solution to the kinetics of breakable filament assembly.” Science 326(5959):1533-7 Details

Lendel C, Bertoncini CW, Cremades N, Waudby CA, Vendruscolo M, Dobson CM, Schenk D, Christodoulou J, Toth G (2009), “On the mechanism of nonspecific inhibitors of protein aggregation: dissecting the interactions of alpha-synuclein with Congo red and lacmoid.” Biochemistry 48(35):8322-34 Details

Luheshi LM, Dobson CM (2009), “Bridging the gap: from protein misfolding to protein misfolding diseases.” FEBS Lett 583(16):2581-6 Details

Poon S, Birkett NR, Fowler SB, Luisi BF, Dobson CM, Zurdo J (2009), “Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1).” Protein Pept Lett 16(12):1548-56 Details

Porter AE, Knowles TP, Muller K, Meehan S, McGuire E, Skepper J, Welland ME, Dobson CM (2009), “Imaging amyloid fibrils within cells using a Se-labelling strategy.” J Mol Biol 392(4):868-71 Details

Robustelli P, Cavalli A, Dobson CM, Vendruscolo M, Salvatella X (2009), “Folding of small proteins by Monte Carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology.” J Phys Chem B 113(22):7890-6 Details

Roodveldt C, Bertoncini CW, Andersson A, van der Goot AT, Hsu ST, Fernández-Montesinos R, de Jong J, van Ham TJ, Nollen EA, Pozo D, Christodoulou J, Dobson CM (2009), “Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.” EMBO J 28(23):3758-70 Details

Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M (2009), “A relationship between mRNA expression levels and protein solubility in E. coli.” J Mol Biol 388(2):381-9 Details

Vendruscolo M, Dobson CM (2009), “Quantitative approaches to defining normal and aberrant protein homeostasis.” Faraday Discuss 143:277-91; discussion 359-72 Details

Vuchelen A, O'Day E, De Genst E, Pardon E, Wyns L, Dumoulin M, Dobson CM, Christodoulou J, Hsu ST (2009), “(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.” Biomol NMR Assign 3(2):231-3 Details

White DA, Buell AK, Dobson CM, Welland ME, Knowles TP (2009), “Biosensor-based label-free assays of amyloid growth.” FEBS Lett 583(16):2587-92 Details

Yanamandra K, Alexeyev O, Zamotin V, Srivastava V, Shchukarev A, Brorsson AC, Tartaglia GG, Vogl T, Kayed R, Wingsle G, Olsson J, Dobson CM, Bergh A, Elgh F, Morozova-Roche LA (2009), “Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate.” PLoS One 4(5):e5562 Details

Yerbury JJ, Kumita JR, Meehan S, Dobson CM, Wilson MR (2009), “alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species.” J Biol Chem 284(7):4246-54 Details

2008

Auer S, Dobson CM, Vendruscolo M, Maritan A (2008), “Self-templated nucleation in peptide and protein aggregation.” Phys Rev Lett 101(25):258101 Details

Auer S, Meersman F, Dobson CM, Vendruscolo M (2008), “A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.” PLoS Comput Biol 4(11):e1000222 Details

Baldwin AJ, Anthony-Cahill SJ, Knowles TP, Lippens G, Christodoulou J, Barker PD, Dobson CM (2008), “Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements.” Angew Chem Int Ed Engl 47(18):3385-7 Details

Calloni G, Lendel C, Campioni S, Giannini S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X, Chiti F (2008), “Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.” J Am Chem Soc 130(39):13040-50 Details

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 (2008), “Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.” Biochemistry 47(42):11041-54 Details

Cheon M, Favrin G, Chang I, Dobson CM, Vendruscolo M (2008), “Calculation of the free energy barriers in the oligomerisation of Abeta peptide fragments.” Front Biosci 13:5614-22 Details

Gras SL, Tickler AK, Squires AM, Devlin GL, Horton MA, Dobson CM, MacPhee CE (2008), “Functionalised amyloid fibrils for roles in cell adhesion.” Biomaterials 29(11):1553-62 Details

Gsponer J, Christodoulou J, Cavalli A, Bui JM, Richter B, Dobson CM, Vendruscolo M (2008), “A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction.” Structure 16(5):736-46 Details

Knowles TP, Shu W, Huber F, Lang HP, Gerber C, Dobson CM, Welland ME (2008), “Label-free detection of amyloid growth with microcantilever sensors.” Nanotechnology 19(38):384007 Details

Luheshi LM, Crowther DC, Dobson CM (2008), “Protein misfolding and disease: from the test tube to the organism.” Curr Opin Chem Biol 12(1):25-31 Details

Macao B, Hoyer W, Sandberg A, Brorsson AC, Dobson CM, Härd T (2008), “Recombinant amyloid beta-peptide production by coexpression with an affibody ligand.” BMC Biotechnol 8:82 Details

Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, Klenerman D (2008), “Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.” Proc Natl Acad Sci U S A 105(38):14424-9 Details

Rivers RC, Kumita JR, Tartaglia GG, Dedmon MM, Pawar A, Vendruscolo M, Dobson CM, Christodoulou J (2008), “Molecular determinants of the aggregation behavior of alpha- and beta-synuclein.” Protein Sci 17(5):887-98 Details

Roodveldt C, Christodoulou J, Dobson CM (2008), “Immunological features of alpha-synuclein in Parkinson's disease.” J Cell Mol Med 12(5B):1820-9 Details

Strodel B, Fitzpatrick AW, Vendruscolo M, Dobson CM, Wales DJ (2008), “Characterizing the first steps of amyloid formation for the ccbeta peptide.” J Phys Chem B 112(32):9998-10004 Details

Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M (2008), “Prediction of aggregation-prone regions in structured proteins.” J Mol Biol 380(2):425-36 Details

Várnai P, Dobson CM, Vendruscolo M (2008), “Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analyses.” J Mol Biol 377(2):575-88 Details

2007

Auer S, Dobson CM, Vendruscolo M (2007), “Characterization of the nucleation barriers for protein aggregation and amyloid formation.” HFSP J 1(2):137-46 Details

Auer S, Miller MA, Krivov SV, Dobson CM, Karplus M, Vendruscolo M (2007), “Importance of metastable states in the free energy landscapes of polypeptide chains.” Phys Rev Lett 99(17):178104 Details

Baldwin AJ, Christodoulou J, Barker PD, Dobson CM, Lippens G (2007), “Contribution of rotational diffusion to pulsed field gradient diffusion measurements.” J Chem Phys 127(11):114505 Details

Cavalli A, Salvatella X, Dobson CM, Vendruscolo M (2007), “Protein structure determination from NMR chemical shifts.” Proc Natl Acad Sci U S A 104(23):9615-20 Details

Cheon M, Chang I, Mohanty S, Luheshi LM, Dobson CM, Vendruscolo M, Favrin G (2007), “Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.” PLoS Comput Biol 3(9):1727-38 Details

Hsu ST, Fucini P, Cabrita LD, Launay H, Dobson CM, Christodoulou J (2007), “Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy.” Proc Natl Acad Sci U S A 104(42):16516-21 Details

Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M, Dobson CM, Welland ME (2007), “Role of intermolecular forces in defining material properties of protein nanofibrils.” Science 318(5858):1900-3 Details

Knowles TP, Shu W, Devlin GL, Meehan S, Auer S, Dobson CM, Welland ME (2007), “Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass.” Proc Natl Acad Sci U S A 104(24):10016-21 Details

Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM (2007), “The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.” J Mol Biol 369(1):157-67 Details

Luheshi LM, Tartaglia GG, Brorsson AC, Pawar AP, Watson IE, Chiti F, Vendruscolo M, Lomas DA, Dobson CM, Crowther DC (2007), “Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity.” PLoS Biol 5(11):e290 Details

Meehan S, Knowles TP, Baldwin AJ, Smith JF, Squires AM, Clements P, Treweek TM, Ecroyd H, Tartaglia GG, Vendruscolo M, Macphee CE, Dobson CM, Carver JA (2007), “Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.” J Mol Biol 372(2):470-84 Details

Meinhardt J, Tartaglia GG, Pawar A, Christopeit T, Hortschansky P, Schroeckh V, Dobson CM, Vendruscolo M, Fändrich M (2007), “Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides.” Protein Sci 16(6):1214-22 Details

Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M (2007), “Life on the edge: a link between gene expression levels and aggregation rates of human proteins.” Trends Biochem Sci 32(5):204-6 Details

Vendruscolo M, Dobson CM (2007), “Chemical biology: More charges against aggregation.” Nature 449(7162):555 Details

Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR (2007), “The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.” FASEB J 21(10):2312-22 Details

2006

Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM (2006), “Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation.” J Mol Biol 356(1):189-208 Details

Bader R, Seeliger MA, Kelly SE, Ilag LL, Meersman F, Limones A, Luisi BF, Dobson CM, Itzhaki LS (2006), “Folding and fibril formation of the cell cycle protein Cks1.” J Biol Chem 281(27):18816-24 Details

Baldwin AJ, Bader R, Christodoulou J, MacPhee CE, Dobson CM, Barker PD (2006), “Cytochrome display on amyloid fibrils.” J Am Chem Soc 128(7):2162-3 Details

Calamai M, Kumita JR, Mifsud J, Parrini C, Ramazzotti M, Ramponi G, Taddei N, Chiti F, Dobson CM (2006), “Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes.” Biochemistry 45(42):12806-15 Details

Chandran V, Stollar EJ, Lindorff-Larsen K, Harper JF, Chazin WJ, Dobson CM, Luisi BF, Christodoulou J (2006), “Structure of the regulatory apparatus of a calcium-dependent protein kinase (CDPK): a novel mode of calmodulin-target recognition.” J Mol Biol 357(2):400-10 Details

Chiti F, Dobson CM (2006), “Protein misfolding, functional amyloid, and human disease.” Annu Rev Biochem 75:333-66 Details

Devlin GL, Knowles TP, Squires A, McCammon MG, Gras SL, Nilsson MR, Robinson CV, Dobson CM, MacPhee CE (2006), “The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner.” J Mol Biol 360(2):497-509 Details

Di Gaetano S, Guglielmi F, Arciello A, Mangione P, Monti M, Pagnozzi D, Raimondi S, Giorgetti S, Orrù S, Canale C, Pucci P, Dobson CM, Bellotti V, Piccoli R (2006), “Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential.” Biochem Biophys Res Commun 351(1):223-8 Details

Dobson CM (2006), “An accidental breach of a protein's natural defenses.” Nat Struct Mol Biol 13(4):295-7 Details

Dobson CM (2006), “Protein aggregation and its consequences for human disease.” Protein Pept Lett 13(3):219-27 Details

Dumoulin M, Kumita JR, Dobson CM (2006), “Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.” Acc Chem Res 39(9):603-10 Details

Fändrich M, Zandomeneghi G, Krebs MR, Kittler M, Buder K, Rossner A, Heinemann SH, Dobson CM, Diekmann S (2006), “Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation.” Acta Histochem 108(3):215-9 Details

Frare E, Mossuto MF, Polverino de Laureto P, Dumoulin M, Dobson CM, Fontana A (2006), “Identification of the core structure of lysozyme amyloid fibrils by proteolysis.” J Mol Biol 361(3):551-61 Details

Gsponer J, Hopearuoho H, Cavalli A, Dobson CM, Vendruscolo M (2006), “Geometry, energetics, and dynamics of hydrogen bonds in proteins: structural information derived from NMR scalar couplings.” J Am Chem Soc 128(47):15127-35 Details

Hall D, Dobson CM (2006), “Expanding to fill the gap: a possible role for inert biopolymers in regulating the extent of the 'macromolecular crowding' effect.” FEBS Lett 580(11):2584-90 Details

Knowles TP, Smith JF, Craig A, Dobson CM, Welland ME (2006), “Spatial persistence of angular correlations in amyloid fibrils.” Phys Rev Lett 96(23):238301 Details

Kumita JR, Johnson RJ, Alcocer MJ, Dumoulin M, Holmqvist F, McCammon MG, Robinson CV, Archer DB, Dobson CM (2006), “Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris.” FEBS J 273(4):711-20 Details

Meersman F, Dobson CM (2006), “Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties.” Biochim Biophys Acta 1764(3):452-60 Details

Meersman F, Dobson CM, Heremans K (2006), “Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions.” Chem Soc Rev 35(10):908-17 Details

Smith JF, Knowles TP, Dobson CM, Macphee CE, Welland ME (2006), “Characterization of the nanoscale properties of individual amyloid fibrils.” Proc Natl Acad Sci U S A 103(43):15806-11 Details

Squires AM, Devlin GL, Gras SL, Tickler AK, MacPhee CE, Dobson CM (2006), “X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils.” J Am Chem Soc 128(36):11738-9 Details

Vendruscolo M, Dobson CM (2006), “Structural biology. Dynamic visions of enzymatic reactions.” Science 313(5793):1586-7 Details

2005

Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM (2005), “Reversal of protein aggregation provides evidence for multiple aggregated States.” J Mol Biol 346(2):603-16 Details

Calamai M, Chiti F, Dobson CM (2005), “Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.” Biophys J 89(6):4201-10 Details

Calloni G, Zoffoli S, Stefani M, Dobson CM, Chiti F (2005), “Investigating the effects of mutations on protein aggregation in the cell.” J Biol Chem 280(11):10607-13 Details

Carulla N, Caddy GL, Hall DR, Zurdo J, Gairí M, Feliz M, Giralt E, Robinson CV, Dobson CM (2005), “Molecular recycling within amyloid fibrils.” Nature 436(7050):554-8 Details

Collins ES, Wirmer J, Hirai K, Tachibana H, Segawa S, Dobson CM, Schwalbe H (2005), “Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.” Chembiochem 6(9):1619-27 Details

Dedmon MM, Christodoulou J, Wilson MR, Dobson CM (2005), “Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species.” J Biol Chem 280(15):14733-40 Details

Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM (2005), “Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.” J Am Chem Soc 127(2):476-7 Details

Dirix C, Meersman F, MacPhee CE, Dobson CM, Heremans K (2005), “High hydrostatic pressure dissociates early aggregates of TTR105-115, but not the mature amyloid fibrils.” J Mol Biol 347(5):903-9 Details

Dobson CM (2005), “Structural biology: prying into prions.” Nature 435(7043):747-9 Details

Dumoulin M, Canet D, Last AM, Pardon E, Archer DB, Muyldermans S, Wyns L, Matagne A, Robinson CV, Redfield C, Dobson CM (2005), “Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.” J Mol Biol 346(3):773-88 Details

Fowler SB, Poon S, Muff R, Chiti F, Dobson CM, Zurdo J (2005), “Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.” Proc Natl Acad Sci U S A 102(29):10105-10 Details

Hall D, Hirota N, Dobson CM (2005), “A toy model for predicting the rate of amyloid formation from unfolded protein.” J Mol Biol 351(1):195-205 Details

Johnson RJ, Christodoulou J, Dumoulin M, Caddy GL, Alcocer MJ, Murtagh GJ, Kumita JR, Larsson G, Robinson CV, Archer DB, Luisi B, Dobson CM (2005), “Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.” J Mol Biol 352(4):823-36 Details

Kristjansdottir S, Lindorff-Larsen K, Fieber W, Dobson CM, Vendruscolo M, Poulsen FM (2005), “Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies.” J Mol Biol 347(5):1053-62 Details

Lindorff-Larsen K, Best RB, Depristo MA, Dobson CM, Vendruscolo M (2005), “Simultaneous determination of protein structure and dynamics.” Nature 433(7022):128-32 Details

Lindorff-Larsen K, Røgen P, Paci E, Vendruscolo M, Dobson CM (2005), “Protein folding and the organization of the protein topology universe.” Trends Biochem Sci 30(1):13-9 Details

Marcon G, Plakoutsi G, Canale C, Relini A, Taddei N, Dobson CM, Ramponi G, Chiti F (2005), “Amyloid formation from HypF-N under conditions in which the protein is initially in its native state.” J Mol Biol 347(2):323-35 Details

Paci E, Lindorff-Larsen K, Dobson CM, Karplus M, Vendruscolo M (2005), “Transition state contact orders correlate with protein folding rates.” J Mol Biol 352(3):495-500 Details

Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F (2005), “Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation.” Structure 13(8):1143-51 Details

Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM (2005), “Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases.” J Mol Biol 350(2):379-92 Details

Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, Chiti F (2005), “Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates.” J Mol Biol 351(4):910-22 Details

Salvatella X, Dobson CM, Fersht AR, Vendruscolo M (2005), “Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.” Proc Natl Acad Sci U S A 102(35):12389-94 Details

Vendruscolo M, Dobson CM (2005), “A glimpse at the organization of the protein universe.” Proc Natl Acad Sci U S A 102(16):5641-2 Details

Vendruscolo M, Dobson CM (2005), “Towards complete descriptions of the free-energy landscapes of proteins.” Philos Trans A Math Phys Eng Sci 363(1827):433-50; discussion 450-2 Details

Wain R, Smith LJ, Dobson CM (2005), “Oxidative refolding of amyloidogenic variants of human lysozyme.” J Mol Biol 351(3):662-71 Details

Wright CF, Teichmann SA, Clarke J, Dobson CM (2005), “The importance of sequence diversity in the aggregation and evolution of proteins.” Nature 438(7069):878-81 Details

2004

Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, Dobson CM, Stefani M (2004), “Prefibrillar amyloid protein aggregates share common features of cytotoxicity.” J Biol Chem 279(30):31374-82 Details

Christodoulou J, Larsson G, Fucini P, Connell SR, Pertinhez TA, Hanson CL, Redfield C, Nierhaus KH, Robinson CV, Schleucher J, Dobson CM (2004), “Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes.” Proc Natl Acad Sci U S A 101(30):10949-54 Details

De Felice FG, Vieira MN, Meirelles MN, Morozova-Roche LA, Dobson CM, Ferreira ST (2004), “Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure.” FASEB J 18(10):1099-101 Details

Dobson CM (2004), “Chemical space and biology.” Nature 432(7019):824-8 Details

Dobson CM (2004), “Experimental investigation of protein folding and misfolding.” Methods 34(1):4-14 Details

Dobson CM (2004), “Protein chemistry. In the footsteps of alchemists.” Science 304(5675):1259-62 Details

Dobson CM (2004), “Principles of protein folding, misfolding and aggregation.” Semin Cell Dev Biol 15(1):3-16 Details

DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM, Vendruscolo M (2004), “Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains.” J Mol Biol 341(5):1317-26 Details

Dumoulin M, Dobson CM (2004), “Probing the origins, diagnosis and treatment of amyloid diseases using antibodies.” Biochimie 86(9-10):589-600 Details

Frare E, Polverino De Laureto P, Zurdo J, Dobson CM, Fontana A (2004), “A highly amyloidogenic region of hen lysozyme.” J Mol Biol 340(5):1153-65 Details

Gilbert RJ, Fucini P, Connell S, Fuller SD, Nierhaus KH, Robinson CV, Dobson CM, Stuart DI (2004), “Three-dimensional structures of translating ribosomes by Cryo-EM.” Mol Cell 14(1):57-66 Details

Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG (2004), “High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.” Proc Natl Acad Sci U S A 101(3):711-6 Details

Kammerer RA, Kostrewa D, Zurdo J, Detken A, García-Echeverría C, Green JD, Müller SA, Meier BH, Winkler FK, Dobson CM, Steinmetz MO (2004), “Exploring amyloid formation by a de novo design.” Proc Natl Acad Sci U S A 101(13):4435-40 Details

Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE (2004), “Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.” Nature 430(6999):586-90 Details

Krebs MR, Macphee CE, Miller AF, Dunlop IE, Dobson CM, Donald AM (2004), “The formation of spherulites by amyloid fibrils of bovine insulin.” Proc Natl Acad Sci U S A 101(40):14420-4 Details

Krebs MR, Morozova-Roche LA, Daniel K, Robinson CV, Dobson CM (2004), “Observation of sequence specificity in the seeding of protein amyloid fibrils.” Protein Sci 13(7):1933-8 Details

Lindorff-Larsen K, Kristjansdottir S, Teilum K, Fieber W, Dobson CM, Poulsen FM, Vendruscolo M (2004), “Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein.” J Am Chem Soc 126(10):3291-9 Details

Lindorff-Larsen K, Vendruscolo M, Paci E, Dobson CM (2004), “Transition states for protein folding have native topologies despite high structural variability.” Nat Struct Mol Biol 11(5):443-9 Details

Meehan S, Berry Y, Luisi B, Dobson CM, Carver JA, MacPhee CE (2004), “Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation.” J Biol Chem 279(5):3413-9 Details

Quezada CM, Schulman BA, Froggatt JJ, Dobson CM, Redfield C (2004), “Local and global cooperativity in the human alpha-lactalbumin molten globule.” J Mol Biol 338(1):149-58 Details

Ventura S, Zurdo J, Narayanan S, Parreño M, Mangues R, Reif B, Chiti F, Giannoni E, Dobson CM, Aviles FX, Serrano L (2004), “Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.” Proc Natl Acad Sci U S A 101(19):7258-63 Details

Wright CF, Christodoulou J, Dobson CM, Clarke J (2004), “The importance of loop length in the folding of an immunoglobulin domain.” Protein Eng Des Sel 17(5):443-53 Details

2003

Azuaga AI, Canet D, Smeenk G, Berends R, Titgemeijer F, Duurkens R, Mateo PL, Scheek RM, Robillard GT, Dobson CM, van Nuland NA (2003), “Characterization of single-tryptophan mutants of histidine-containing phosphocarrier protein: evidence for local rearrangements during folding from high concentrations of denaturant.” Biochemistry 42(17):4883-95 Details

Bell HK, Dobson CM, Jackson SP, King CM (2003), “Localized morphoea preceded by a pigmented purpuric dermatosis.” Clin Exp Dermatol 28(4):369-71 Details

Canet D, Lyon CE, Scheek RM, Robillard GT, Dobson CM, Hore PJ, van Nuland NA (2003), “Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments.” J Mol Biol 330(2):397-407 Details

Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (2003), “Rationalization of the effects of mutations on peptide and protein aggregation rates.” Nature 424(6950):805-8 Details

Dobson CM (2003), “Protein folding and misfolding.” Nature 426(6968):884-90 Details

Dobson CM (2003), “Protein folding and disease: a view from the first Horizon Symposium.” Nat Rev Drug Discov 2(2):154-60 Details

Dumoulin M, Last AM, Desmyter A, Decanniere K, Canet D, Larsson G, Spencer A, Archer DB, Sasse J, Muyldermans S, Wyns L, Redfield C, Matagne A, Robinson CV, Dobson CM (2003), “A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.” Nature 424(6950):783-8 Details

Fändrich M, Forge V, Buder K, Kittler M, Dobson CM, Diekmann S (2003), “Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.” Proc Natl Acad Sci U S A 100(26):15463-8 Details

Hatters DM, MacRaild CA, Daniels R, Gosal WS, Thomson NH, Jones JA, Davis JJ, MacPhee CE, Dobson CM, Howlett GJ (2003), “The circularization of amyloid fibrils formed by apolipoprotein C-II.” Biophys J 85(6):3979-90 Details

Lindorff-Larsen K, Paci E, Serrano L, Dobson CM, Vendruscolo M (2003), “Calculation of mutational free energy changes in transition states for protein folding.” Biophys J 85(2):1207-14 Details

Mok KH, Nagashima T, Day IJ, Jones JA, Jones CJ, Dobson CM, Hore PJ (2003), “Rapid sample-mixing technique for transient NMR and photo-CIDNP spectroscopy: applications to real-time protein folding.” J Am Chem Soc 125(41):12484-92 Details

Nilsson MR, Dobson CM (2003), “Chemical modification of insulin in amyloid fibrils.” Protein Sci 12(11):2637-41 Details

Nilsson MR, Dobson CM (2003), “In vitro characterization of lactoferrin aggregation and amyloid formation.” Biochemistry 42(2):375-82 Details

Polverino de Laureto P, Taddei N, Frare E, Capanni C, Costantini S, Zurdo J, Chiti F, Dobson CM, Fontana A (2003), “Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.” J Mol Biol 334(1):129-41 Details

Stefani M, Dobson CM (2003), “Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution.” J Mol Med (Berl) 81(11):678-99 Details

Vendruscolo M, Paci E, Dobson CM, Karplus M (2003), “Rare fluctuations of native proteins sampled by equilibrium hydrogen exchange.” J Am Chem Soc 125(51):15686-7 Details

Vendruscolo M, Paci E, Karplus M, Dobson CM (2003), “Structures and relative free energies of partially folded states of proteins.” Proc Natl Acad Sci U S A 100(25):14817-21 Details

Vendruscolo M, Zurdo J, MacPhee CE, Dobson CM (2003), “Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems.” Philos Trans A Math Phys Eng Sci 361(1807):1205-22 Details

2002

Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM, Stefani M (2002), “Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.” Nature 416(6880):507-11 Details

Canet D, Last AM, Tito P, Sunde M, Spencer A, Archer DB, Redfield C, Robinson CV, Dobson CM (2002), “Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.” Nat Struct Biol 9(4):308-15 Details

Carver JA, Lindner RA, Lyon C, Canet D, Hernandez H, Dobson CM, Redfield C (2002), “The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study.” J Mol Biol 318(3):815-27 Details

Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, Dobson CM (2002), “Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.” Proc Natl Acad Sci U S A 99 Suppl 4:16419-26 Details

Chiti F, Taddei N, Baroni F, Capanni C, Stefani M, Ramponi G, Dobson CM (2002), “Kinetic partitioning of protein folding and aggregation.” Nat Struct Biol 9(2):137-43 Details

Dobson CM (2002), “Getting out of shape.” Nature 418(6899):729-30 Details

Fändrich M, Dobson CM (2002), “The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation.” EMBO J 21(21):5682-90 Details

Hamada D, Dobson CM (2002), “A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.” Protein Sci 11(10):2417-26 Details

Jaroniec CP, MacPhee CE, Astrof NS, Dobson CM, Griffin RG (2002), “Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.” Proc Natl Acad Sci U S A 99(26):16748-53 Details

Jiménez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR (2002), “The protofilament structure of insulin amyloid fibrils.” Proc Natl Acad Sci U S A 99(14):9196-201 Details

Klein-Seetharaman J, Oikawa M, Grimshaw SB, Wirmer J, Duchardt E, Ueda T, Imoto T, Smith LJ, Dobson CM, Schwalbe H (2002), “Long-range interactions within a nonnative protein.” Science 295(5560):1719-22 Details

López De La Paz M, Goldie K, Zurdo J, Lacroix E, Dobson CM, Hoenger A, Serrano L (2002), “De novo designed peptide-based amyloid fibrils.” Proc Natl Acad Sci U S A 99(25):16052-7 Details

Lyon CE, Suh ES, Dobson CM, Hore PJ (2002), “Probing the exposure of tyrosine and tryptophan residues in partially folded proteins and folding intermediates by CIDNP pulse-labeling.” J Am Chem Soc 124(44):13018-24 Details

Paci E, Vendruscolo M, Dobson CM, Karplus M (2002), “Determination of a transition state at atomic resolution from protein engineering data.” J Mol Biol 324(1):151-63 Details

Pertinhez TA, Bouchard M, Smith RA, Dobson CM, Smith LJ (2002), “Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS.” FEBS Lett 529(2-3):193-7 Details

Sandilands A, Hutcheson AM, Long HA, Prescott AR, Vrensen G, Löster J, Klopp N, Lutz RB, Graw J, Masaki S, Dobson CM, MacPhee CE, Quinlan RA (2002), “Altered aggregation properties of mutant gamma-crystallins cause inherited cataract.” EMBO J 21(22):6005-14 Details

2001

Canet D, Doering K, Dobson CM, Dupont Y (2001), “High-sensitivity fluorescence anisotropy detection of protein-folding events: application to alpha-lactalbumin.” Biophys J 80(4):1996-2003 Details

Chamberlain AK, Receveur V, Spencer A, Redfield C, Dobson CM (2001), “Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.” Protein Sci 10(12):2525-30 Details

Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M (2001), “Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.” Protein Sci 10(12):2541-7 Details

Chiti F, De Lorenzi E, Grossi S, Mangione P, Giorgetti S, Caccialanza G, Dobson CM, Merlini G, Ramponi G, Bellotti V (2001), “A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis.” J Biol Chem 276(50):46714-21 Details

Chiti F, Mangione P, Andreola A, Giorgetti S, Stefani M, Dobson CM, Bellotti V, Taddei N (2001), “Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin.” J Mol Biol 307(1):379-91 Details

Chiti F, Taddei N, Stefani M, Dobson CM, Ramponi G (2001), “Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.” Protein Sci 10(4):879-86 Details

Dobson CM (2001), “Protein folding and its links with human disease.” Biochem Soc Symp (68):1-26 Details

Dobson CM (2001), “The structural basis of protein folding and its links with human disease.” Philos Trans R Soc Lond B Biol Sci 356(1406):133-45 Details

Fändrich M, Fletcher MA, Dobson CM (2001), “Amyloid fibrils from muscle myoglobin.” Nature 410(6825):165-6 Details

Kamatari YO, Yamada H, Akasaka K, Jones JA, Dobson CM, Smith LJ (2001), “Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy.” Eur J Biochem 268(6):1782-93 Details

Paci E, Smith LJ, Dobson CM, Karplus M (2001), “Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation.” J Mol Biol 306(2):329-47 Details

Pertinhez TA, Bouchard M, Tomlinson EJ, Wain R, Ferguson SJ, Dobson CM, Smith LJ (2001), “Amyloid fibril formation by a helical cytochrome.” FEBS Lett 495(3):184-6 Details

Reader JS, Van Nuland NA, Thompson GS, Ferguson SJ, Dobson CM, Radford SE (2001), “A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding.” Protein Sci 10(6):1216-24 Details

Schwalbe H, Grimshaw SB, Spencer A, Buck M, Boyd J, Dobson CM, Redfield C, Smith LJ (2001), “A refined solution structure of hen lysozyme determined using residual dipolar coupling data.” Protein Sci 10(4):677-88 Details

Taddei N, Capanni C, Chiti F, Stefani M, Dobson CM, Ramponi G (2001), “Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.” J Biol Chem 276(40):37149-54 Details

Vendruscolo M, Paci E, Dobson CM, Karplus M (2001), “Three key residues form a critical contact network in a protein folding transition state.” Nature 409(6820):641-5 Details

Wain R, Pertinhez TA, Tomlinson EJ, Hong L, Dobson CM, Ferguson SJ, Smith LJ (2001), “The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.” J Biol Chem 276(49):45813-7 Details

Wijesinha-Bettoni R, Dobson CM, Redfield C (2001), “Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules.” J Mol Biol 312(1):261-73 Details

Wijesinha-Bettoni R, Dobson CM, Redfield C (2001), “Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.” J Mol Biol 307(3):885-98 Details

Zurdo J, Guijarro JI, Dobson CM (2001), “Preparation and characterization of purified amyloid fibrils.” J Am Chem Soc 123(33):8141-2 Details

Zurdo J, Guijarro JI, Jiménez JL, Saibil HR, Dobson CM (2001), “Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.” J Mol Biol 311(2):325-40 Details

2000

Bouchard M, Benjamin DR, Tito P, Robinson CV, Dobson CM (2000), “Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry.” Biophys J 78(2):1010-7 Details

Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV (2000), “Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy.” Protein Sci 9(10):1960-7 Details

Chamberlain AK, MacPhee CE, Zurdo J, Morozova-Roche LA, Hill HA, Dobson CM, Davis JJ (2000), “Ultrastructural organization of amyloid fibrils by atomic force microscopy.” Biophys J 79(6):3282-93 Details

Chiti F, Taddei N, Bucciantini M, White P, Ramponi G, Dobson CM (2000), “Mutational analysis of the propensity for amyloid formation by a globular protein.” EMBO J 19(7):1441-9 Details

Dinner AR, Sali A, Smith LJ, Dobson CM, Karplus M (2000), “Understanding protein folding via free-energy surfaces from theory and experiment.” Trends Biochem Sci 25(7):331-9 Details

Fändrich M, Tito MA, Leroux MR, Rostom AA, Hartl FU, Dobson CM, Robinson CV (2000), “Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry.” Proc Natl Acad Sci U S A 97(26):14151-5 Details

Hamada D, Chiti F, Guijarro JI, Kataoka M, Taddei N, Dobson CM (2000), “Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol.” Nat Struct Biol 7(1):58-61 Details

Konno T, Kamatari YO, Tanaka N, Kamikubo H, Dobson CM, Nagayama K (2000), “A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein.” Biochemistry 39(14):4182-90 Details

Krebs MR, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, Zurdo J, Robinson CV, Dobson CM (2000), “Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain.” J Mol Biol 300(3):541-9 Details

MacPhee CE, Dobson CM (2000), “Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin.” J Mol Biol 297(5):1203-15 Details

Maeda K, Lyon CE, Lopez JJ, Cemazar M, Dobson CM, Hore PJ (2000), “Improved photo-CIDNP methods for studying protein structure and folding.” J Biomol NMR 16(3):235-44 Details

Matagne A, Jamin M, Chung EW, Robinson CV, Radford SE, Dobson CM (2000), “Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.” J Mol Biol 297(1):193-210 Details

Morgan CJ, Wilkins DK, Smith LJ, Kawata Y, Dobson CM (2000), “A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase.” J Mol Biol 300(1):11-6 Details

Morozova-Roche LA, Zurdo J, Spencer A, Noppe W, Receveur V, Archer DB, Joniau M, Dobson CM (2000), “Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.” J Struct Biol 130(2-3):339-51 Details

Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, Robinson CV (2000), “Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry.” Biophys J 79(2):1053-65 Details

Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR (2000), “Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.” Biochemistry 39(11):2887-93 Details

Pertinhez TA, Hamada D, Smith LJ, Chiti F, Taddei N, Stefani M, Dobson CM (2000), “Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization.” Protein Sci 9(8):1466-73 Details

Rostom AA, Fucini P, Benjamin DR, Juenemann R, Nierhaus KH, Hartl FU, Dobson CM, Robinson CV (2000), “Detection and selective dissociation of intact ribosomes in a mass spectrometer.” Proc Natl Acad Sci U S A 97(10):5185-90 Details

Taddei N, Chiti F, Fiaschi T, Bucciantini M, Capanni C, Stefani M, Serrano L, Dobson CM, Ramponi G (2000), “Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.” J Mol Biol 300(3):633-47 Details

van den Berg B, Wain R, Dobson CM, Ellis RJ (2000), “Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell.” EMBO J 19(15):3870-5 Details

Villegas V, Zurdo J, Filimonov VV, Avilés FX, Dobson CM, Serrano L (2000), “Protein engineering as a strategy to avoid formation of amyloid fibrils.” Protein Sci 9(9):1700-8 Details

Wilkins DK, Dobson CM, Gross M (2000), “Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B.” Eur J Biochem 267(9):2609-16 Details

1999

Canet D, Sunde M, Last AM, Miranker A, Spencer A, Robinson CV, Dobson CM (1999), “Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.” Biochemistry 38(20):6419-27 Details

Chiti F, Taddei N, Giannoni E, van Nuland NA, Ramponi G, Dobson CM (1999), “Development of enzymatic activity during protein folding. Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase.” J Biol Chem 274(29):20151-8 Details

Chiti F, Taddei N, Webster P, Hamada D, Fiaschi T, Ramponi G, Dobson CM (1999), “Acceleration of the folding of acylphosphatase by stabilization of local secondary structure.” Nat Struct Biol 6(4):380-7 Details

Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM (1999), “Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.” Nat Struct Biol 6(11):1005-9 Details

Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G, Dobson CM (1999), “Designing conditions for in vitro formation of amyloid protofilaments and fibrils.” Proc Natl Acad Sci U S A 96(7):3590-4 Details

Dobson CM (1999), “Protein misfolding, evolution and disease.” Trends Biochem Sci 24(9):329-32 Details

Dobson CM, Karplus M (1999), “The fundamentals of protein folding: bringing together theory and experiment.” Curr Opin Struct Biol 9(1):92-101 Details

Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, Redfield C, Dobson CM (1999), “Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin.” J Mol Biol 288(4):673-88 Details

Gross M, Wilkins DK, Pitkeathly MC, Chung EW, Higham C, Clark A, Dobson CM (1999), “Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB.” Protein Sci 8(6):1350-7 Details

Hennig M, Bermel W, Spencer A, Dobson CM, Smith LJ, Schwalbe H (1999), “Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy.” J Mol Biol 288(4):705-23 Details

Jiménez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM, Sunde M, Saibil HR (1999), “Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.” EMBO J 18(4):815-21 Details

Leroux MR, Fändrich M, Klunker D, Siegers K, Lupas AN, Brown JR, Schiebel E, Dobson CM, Hartl FU (1999), “MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin.” EMBO J 18(23):6730-43 Details

Ptitsyn OB, Finkel'shteĭn AV, Dobson CM (1999), “[Self-organization of protein structures--a bridge between physics and biology].” Mol Biol (Mosk) 33(6):1012-5 Details

Radford SE, Dobson CM (1999), “From computer simulations to human disease: emerging themes in protein folding.” Cell 97(3):291-8 Details

Redfield C, Schulman BA, Milhollen MA, Kim PS, Dobson CM (1999), “Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds.” Nat Struct Biol 6(10):948-52 Details

Smith LJ, Dobson CM, van Gunsteren WF (1999), “Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH.” Proteins 36(1):77-86 Details

Smith LJ, Dobson CM, van Gunsteren WF (1999), “Side-chain conformational disorder in a molten globule: molecular dynamics simulations of the A-state of human alpha-lactalbumin.” J Mol Biol 286(5):1567-80 Details

Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G (1999), “Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme.” Biochemistry 38(7):2135-42 Details

van den Berg B, Chung EW, Robinson CV, Dobson CM (1999), “Characterisation of the dominant oxidative folding intermediate of hen lysozyme.” J Mol Biol 290(3):781-96 Details

van den Berg B, Chung EW, Robinson CV, Mateo PL, Dobson CM (1999), “The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.” EMBO J 18(17):4794-803 Details

van den Berg B, Ellis RJ, Dobson CM (1999), “Effects of macromolecular crowding on protein folding and aggregation.” EMBO J 18(24):6927-33 Details

Vis H, Dobson CM, Robinson CV (1999), “Selective association of protein molecules followed by mass spectrometry.” Protein Sci 8(6):1368-70 Details

Wilkins DK, Grimshaw SB, Receveur V, Dobson CM, Jones JA, Smith LJ (1999), “Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.” Biochemistry 38(50):16424-31 Details

1998

Benjamin DR, Robinson CV, Hendrick JP, Hartl FU, Dobson CM (1998), “Mass spectrometry of ribosomes and ribosomal subunits.” Proc Natl Acad Sci U S A 95(13):7391-5 Details

Chiti F, Magherini F, Taddei N, Ilardi C, Stefani M, Bucciantini M, Dobson CM, Ramponi G (1998), “Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues.” Protein Eng 11(7):557-61 Details

Chiti F, Taddei N, van Nuland NA, Magherini F, Stefani M, Ramponi G, Dobson CM (1998), “Structural characterization of the transition state for folding of muscle acylphosphatase.” J Mol Biol 283(4):893-903 Details

Chiti F, van Nuland NA, Taddei N, Magherini F, Stefani M, Ramponi G, Dobson CM (1998), “Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH.” Biochemistry 37(5):1447-55 Details

Conejero-Lara F, Parrado J, Azuaga AI, Dobson CM, Ponting CP (1998), “Analysis of the interactions between streptokinase domains and human plasminogen.” Protein Sci 7(10):2190-9 Details

de Jongh HH, Rospert S, Dobson CM (1998), “Comparison of the conformational state and in vitro refolding of yeast chaperonin protein cpn10 with bacterial GroES.” Biochem Biophys Res Commun 244(3):884-8 Details

Dobson CM, Ellis RJ (1998), “Protein folding and misfolding inside and outside the cell.” EMBO J 17(18):5251-4 Details

Dobson CM, Hore PJ (1998), “Kinetic studies of protein folding using NMR spectroscopy.” Nat Struct Biol 5 Suppl:504-7 Details

Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM (1998), “Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.” J Mol Biol 276(3):657-67 Details

Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM (1998), “Amyloid fibril formation by an SH3 domain.” Proc Natl Acad Sci U S A 95(8):4224-8 Details

Matagne A, Chung EW, Ball LJ, Radford SE, Robinson CV, Dobson CM (1998), “The origin of the alpha-domain intermediate in the folding of hen lysozyme.” J Mol Biol 277(5):997-1005 Details

Matagne A, Dobson CM (1998), “The folding process of hen lysozyme: a perspective from the 'new view'.” Cell Mol Life Sci 54(4):363-71 Details

Morgan CJ, Miranker A, Dobson CM (1998), “Characterization of collapsed states in the early stages of the refolding of hen lysozyme.” Biochemistry 37(23):8473-80 Details

Nettleton EJ, Sunde M, Lai Z, Kelly JW, Dobson CM, Robinson CV (1998), “Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.” J Mol Biol 281(3):553-64 Details

Penkett CJ, Redfield C, Jones JA, Dodd I, Hubbard J, Smith RA, Smith LJ, Dobson CM (1998), “Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus.” Biochemistry 37(48):17054-67 Details

Rostom AA, Sunde M, Richardson SJ, Schreiber G, Jarvis S, Bateman R, Dobson CM, Robinson CV (1998), “Dissection of multi-protein complexes using mass spectrometry: subunit interactions in transthyretin and retinol-binding protein complexes.” Proteins Suppl 2:3-11 Details

Smith LJ, Mark AE, Dobson CM, van Gunsteren WF (1998), “Molecular dynamics simulations of peptide fragments from hen lysozyme: insight into non-native protein conformations.” J Mol Biol 280(4):703-19 Details

van Nuland NA, Chiti F, Taddei N, Raugei G, Ramponi G, Dobson CM (1998), “Slow folding of muscle acylphosphatase in the absence of intermediates.” J Mol Biol 283(4):883-91 Details

1997

Balbach J, Forge V, Lau WS, Jones JA, van Nuland NA, Dobson CM (1997), “Detection of residue contacts in a protein folding intermediate.” Proc Natl Acad Sci U S A 94(14):7182-5 Details

Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CC, Pepys MB (1997), “Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.” Nature 385(6619):787-93 Details

Chung EW, Nettleton EJ, Morgan CJ, Gross M, Miranker A, Radford SE, Dobson CM, Robinson CV (1997), “Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.” Protein Sci 6(6):1316-24 Details

Lu H, Buck M, Radford SE, Dobson CM (1997), “Acceleration of the folding of hen lysozyme by trifluoroethanol.” J Mol Biol 265(2):112-7 Details

Matagne A, Radford SE, Dobson CM (1997), “Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process.” J Mol Biol 267(5):1068-74 Details

Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ (1997), “NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein.” J Mol Biol 274(2):152-9 Details

Schwalbe H, Fiebig KM, Buck M, Jones JA, Grimshaw SB, Spencer A, Glaser SJ, Smith LJ, Dobson CM (1997), “Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.” Biochemistry 36(29):8977-91 Details

1996

Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM (1996), “Protein folding monitored at individual residues during a two-dimensional NMR experiment.” Science 274(5290):1161-3 Details

Bolin KA, Pitkeathly M, Miranker A, Smith LJ, Dobson CM (1996), “Insight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozyme.” J Mol Biol 261(3):443-53 Details

Buck M, Schwalbe H, Dobson CM (1996), “Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol.” J Mol Biol 257(3):669-83 Details

Conejero-Lara F, Parrado J, Azuaga AI, Smith RA, Ponting CP, Dobson CM (1996), “Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance.” Protein Sci 5(12):2583-91 Details

Miranker A, Robinson CV, Radford SE, Dobson CM (1996), “Investigation of protein folding by mass spectrometry.” FASEB J 10(1):93-101 Details

Miranker AD, Dobson CM (1996), “Collapse and cooperativity in protein folding.” Curr Opin Struct Biol 6(1):31-42 Details

Parrado J, Conejero-Lara F, Smith RA, Marshall JM, Ponting CP, Dobson CM (1996), “The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments.” Protein Sci 5(4):693-704 Details

Parrado J, Escuredo PR, Conejero-Lara F, Kotik M, Ponting CP, Asenjo JA, Dobson CM (1996), “Molecular characterisation of a thermoactive beta-1,3-glucanase from Oerskovia xanthineolytica.” Biochim Biophys Acta 1296(2):145-51 Details

Plaxco KW, Dobson CM (1996), “Time-resolved biophysical methods in the study of protein folding.” Curr Opin Struct Biol 6(5):630-6 Details

Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM (1996), “Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.” Proc Natl Acad Sci U S A 93(20):10703-6 Details

Smith LJ, Bolin KA, Schwalbe H, MacArthur MW, Thornton JM, Dobson CM (1996), “Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations.” J Mol Biol 255(3):494-506 Details

Smith LJ, Fiebig KM, Schwalbe H, Dobson CM (1996), “The concept of a random coil. Residual structure in peptides and denatured proteins.” Fold Des 1(5):R95-106 Details

Yang JJ, van den Berg B, Pitkeathly M, Smith LJ, Bolin KA, Keiderling TA, Redfield C, Dobson CM, Radford SE (1996), “Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme.” Fold Des 1(6):473-84 Details

1995

Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM (1995), “Following protein folding in real time using NMR spectroscopy.” Nat Struct Biol 2(10):865-70 Details

Buck M, Boyd J, Redfield C, MacKenzie DA, Jeenes DJ, Archer DB, Dobson CM (1995), “Structural determinants of protein dynamics: analysis of 15N NMR relaxation measurements for main-chain and side-chain nuclei of hen egg white lysozyme.” Biochemistry 34(12):4041-55 Details

Buck M, Schwalbe H, Dobson CM (1995), “Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.” Biochemistry 34(40):13219-32 Details

Dobson CM (1995), “Finding the right fold.” Nat Struct Biol 2(7):513-7 Details

Haezebrouck P, Joniau M, Van Dael H, Hooke SD, Woodruff ND, Dobson CM (1995), “An equilibrium partially folded state of human lysozyme at low pH.” J Mol Biol 246(3):382-7 Details

Kotik M, Radford SE, Dobson CM (1995), “Comparison of the refolding of hen lysozyme from dimethyl sulfoxide and guanidinium chloride.” Biochemistry 34(5):1714-24 Details

Kragelund BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM (1995), “Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein.” Biochemistry 34(21):7217-24 Details

Morozova LA, Haynie DT, Arico-Muendel C, Van Dael H, Dobson CM (1995), “Structural basis of the stability of a lysozyme molten globule.” Nat Struct Biol 2(10):871-5 Details

Radford SE, Dobson CM (1995), “Insights into protein folding using physical techniques: studies of lysozyme and alpha-lactalbumin.” Philos Trans R Soc Lond B Biol Sci 348(1323):17-25 Details

Schulman BA, Redfield C, Peng ZY, Dobson CM, Kim PS (1995), “Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.” J Mol Biol 253(5):651-7 Details

Smith LJ, Mark AE, Dobson CM, van Gunsteren WF (1995), “Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes.” Biochemistry 34(34):10918-31 Details

Yang JJ, Buck M, Pitkeathly M, Kotik M, Haynie DT, Dobson CM, Radford SE (1995), “Conformational properties of four peptides spanning the sequence of hen lysozyme.” J Mol Biol 252(4):483-91 Details

1994

Alexandrescu AT, Ng YL, Dobson CM (1994), “Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin.” J Mol Biol 235(2):587-99 Details

Bartik K, Redfield C, Dobson CM (1994), “Measurement of the individual pKa values of acidic residues of hen and turkey lysozymes by two-dimensional 1H NMR.” Biophys J 66(4):1180-4 Details

Buck M, Radford SE, Dobson CM (1994), “Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea.” J Mol Biol 237(3):247-54 Details

Dobson CM (1994), “Protein folding. Solid evidence for molten globules.” Curr Biol 4(7):636-40 Details

Dobson CM, Evans PA, Radford SE (1994), “Understanding how proteins fold: the lysozyme story so far.” Trends Biochem Sci 19(1):31-7 Details

Eyles SJ, Radford SE, Robinson CV, Dobson CM (1994), “Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.” Biochemistry 33(44):13038-48 Details

Hadfield AT, Harvey DJ, Archer DB, MacKenzie DA, Jeenes DJ, Radford SE, Lowe G, Dobson CM, Johnson LN (1994), “Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product.” J Mol Biol 243(5):856-72 Details

Hooke SD, Radford SE, Dobson CM (1994), “The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme.” Biochemistry 33(19):5867-76 Details

Itzhaki LS, Evans PA, Dobson CM, Radford SE (1994), “Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes.” Biochemistry 33(17):5212-20 Details

Nowak UK, Cooper A, Saunders D, Smith RA, Dobson CM (1994), “Unfolding studies of the protease domain of urokinase-type plasminogen activator: the existence of partly folded states and stable subdomains.” Biochemistry 33(10):2951-60 Details

Redfield C, Smith LJ, Boyd J, Lawrence GM, Edwards RG, Gershater CJ, Smith RA, Dobson CM (1994), “Analysis of the solution structure of human interleukin-4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques.” J Mol Biol 238(1):23-41 Details

Redfield C, Smith RA, Dobson CM (1994), “Structural characterization of a highly-ordered 'molten globule' at low pH.” Nat Struct Biol 1(1):23-9 Details

Robinson CV, Gross M, Eyles SJ, Ewbank JJ, Mayhew M, Hartl FU, Dobson CM, Radford SE (1994), “Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.” Nature 372(6507):646-51 Details

Smith LJ, Alexandrescu AT, Pitkeathly M, Dobson CM (1994), “Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule.” Structure 2(8):703-12 Details

Smith LJ, Redfield C, Smith RA, Dobson CM, Clore GM, Gronenborn AM, Walter MR, Naganbushan TL, Wlodawer A (1994), “Comparison of four independently determined structures of human recombinant interleukin-4.” Nat Struct Biol 1(5):301-10 Details

Taddei N, Buck M, Broadhurst RW, Stefani M, Ramponi G, Dobson CM (1994), “Equilibrium unfolding studies of horse muscle acylphosphatase.” Eur J Biochem 225(3):811-7 Details

1993

Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM (1993), “Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.” Biochemistry 32(7):1707-18 Details

Bartik K, Dobson CM, Redfield C (1993), “1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme.” Eur J Biochem 215(2):255-66 Details

Buck M, Radford SE, Dobson CM (1993), “A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding.” Biochemistry 32(2):669-78 Details

Chyan CL, Wormald C, Dobson CM, Evans PA, Baum J (1993), “Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study.” Biochemistry 32(21):5681-91 Details

Dobson CM (1993), “Flexible friends.” Curr Biol 3(8):530-2 Details

Miranker A, Robinson CV, Radford SE, Aplin RT, Dobson CM (1993), “Detection of transient protein folding populations by mass spectrometry.” Science 262(5135):896-900 Details

Nowak UK, Li X, Teuten AJ, Smith RA, Dobson CM (1993), “NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen activator.” Biochemistry 32(1):298-309 Details

O'Connell JP, Kelly SM, Raleigh DP, Hubbard JA, Price NC, Dobson CM, Smith BJ (1993), “On the role of the C-terminus of alpha-calcitonin-gene-related peptide (alpha CGRP). The structure of des-phenylalaninamide37-alpha CGRP and its interaction with the CGRP receptor.” Biochem J 291 ( Pt 1):205-10 Details

Smith LJ, Sutcliffe MJ, Redfield C, Dobson CM (1993), “Structure of hen lysozyme in solution.” J Mol Biol 229(4):930-44 Details

Taguchi JE, Heyes SJ, Barford D, Johnson LN, Dobson CM (1993), “Solid state 31P cross-polarization/magic angle sample spinning nuclear magnetic resonance of crystalline glycogen phosphorylase b.” Biophys J 64(2):492-501 Details

Teuten AJ, Broadhurst RW, Smith RA, Dobson CM (1993), “Characterization of structural and folding properties of streptokinase by n.m.r. spectroscopy.” Biochem J 290 ( Pt 2):313-9 Details

Teuten AJ, Cooper A, Smith RA, Dobson CM (1993), “Binding of a substrate analogue can induce co-operative structure in the plasmin serine-proteinase domain.” Biochem J 293 ( Pt 2):567-72 Details

Van Dael H, Haezebrouck P, Morozova L, Arico-Muendel C, Dobson CM (1993), “Partially folded states of equine lysozyme. Structural characterization and significance for protein folding.” Biochemistry 32(44):11886-94 Details

1992

Alexandrescu AT, Broadhurst RW, Wormald C, Chyan CL, Baum J, Dobson CM (1992), “1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin.” Eur J Biochem 210(3):699-709 Details

Cooper A, Eyles SJ, Radford SE, Dobson CM (1992), “Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme.” J Mol Biol 225(4):939-43 Details

Dobson CM (1992), “Resting places on folding pathways.” Curr Biol 2(7):343-5 Details

Heyes SJ, Clayden NJ, Dobson CM (1992), “13C-CP/MAS NMR studies of the cyclomalto-oligosaccharide (cyclodextrin) hydrates.” Carbohydr Res 233:1-14 Details

Li X, Smith RA, Dobson CM (1992), “Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase.” Biochemistry 31(40):9562-71 Details

Li XA, Sutcliffe MJ, Schwartz TW, Dobson CM (1992), “Sequence-specific 1H NMR assignments and solution structure of bovine pancreatic polypeptide.” Biochemistry 31(4):1245-53 Details

Lumb KJ, Aplin RT, Radford SE, Archer DB, Jeenes DJ, Lambert N, MacKenzie DA, Dobson CM, Lowe G (1992), “A study of D52S hen lysozyme-GlcNAc oligosaccharide complexes by NMR spectroscopy and electrospray mass spectrometry.” FEBS Lett 296(2):153-7 Details

Lumb KJ, Dobson CM (1992), “1H nuclear magnetic resonance studies of the interaction of urea with hen lysozyme. Origins of the conformational change induced in hen lysozyme by N-acetylglucosamine oligosaccharides.” J Mol Biol 227(1):9-14 Details

Radford SE, Buck M, Topping KD, Dobson CM, Evans PA (1992), “Hydrogen exchange in native and denatured states of hen egg-white lysozyme.” Proteins 14(2):237-48 Details

Radford SE, Dobson CM, Evans PA (1992), “The folding of hen lysozyme involves partially structured intermediates and multiple pathways.” Nature 358(6384):302-7 Details

Raleigh DP, Evans PA, Pitkeathly M, Dobson CM (1992), “A peptide model for proline isomerism in the unfolded state of staphylococcal nuclease.” J Mol Biol 228(2):338-42 Details

Redfield C, Boyd J, Smith LJ, Smith RA, Dobson CM (1992), “Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.” Biochemistry 31(43):10431-7 Details

Smith LJ, Redfield C, Boyd J, Lawrence GM, Edwards RG, Smith RA, Dobson CM (1992), “Human interleukin 4. The solution structure of a four-helix bundle protein.” J Mol Biol 224(4):899-904 Details

Sutcliffe MJ, Dobson CM, Oswald RE (1992), “Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics.” Biochemistry 31(11):2962-70 Details

1991

Broadhurst RW, Dobson CM, Hore PJ, Radford SE, Rees ML (1991), “A photochemically induced dynamic nuclear polarization study of denatured states of lysozyme.” Biochemistry 30(2):405-12 Details

Cheetham JC, Raleigh DP, Griest RE, Redfield C, Dobson CM, Rees AR (1991), “Antigen mobility in the combining site of an anti-peptide antibody.” Proc Natl Acad Sci U S A 88(18):7968-72 Details

Cheetham JC, Redfield C, Griest RE, Raleigh DP, Dobson CM, Rees AR (1991), “Use of two-dimensional 1H nuclear magnetic resonance to study high-affinity antibody-peptide interactions.” Methods Enzymol 203:202-28 Details

Dobson CM (1991), “NMR spectroscopy and protein folding: studies of lysozyme and alpha-lactalbumin.” Ciba Found Symp 161:167-81; discussion 181-9 Details

Evans PA, Topping KD, Woolfson DN, Dobson CM (1991), “Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme.” Proteins 9(4):248-66 Details

Miranker A, Radford SE, Karplus M, Dobson CM (1991), “Demonstration by NMR of folding domains in lysozyme.” Nature 349(6310):633-6 Details

Oswald RE, Sutcliffe MJ, Bamberger M, Loring RH, Braswell E, Dobson CM (1991), “Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: sequence-specific assignments, secondary structure, and dimer formation.” Biochemistry 30(20):4901-9 Details

Pedersen TG, Sigurskjold BW, Andersen KV, Kjaer M, Poulsen FM, Dobson CM, Redfield C (1991), “A nuclear magnetic resonance study of the hydrogen-exchange behaviour of lysozyme in crystals and solution.” J Mol Biol 218(2):413-26 Details

Radford SE, Woolfson DN, Martin SR, Lowe G, Dobson CM (1991), “A three-disulphide derivative of hen lysozyme. Structure, dynamics and stability.” Biochem J 273(Pt 1):211-7 Details

Redfield C, Smith LJ, Boyd J, Lawrence GM, Edwards RG, Smith RA, Dobson CM (1991), “Secondary structure and topology of human interleukin 4 in solution.” Biochemistry 30(46):11029-35 Details

Smith LJ, Sutcliffe MJ, Redfield C, Dobson CM (1991), “Analysis of phi and chi 1 torsion angles for hen lysozyme in solution from 1H NMR spin-spin coupling constants.” Biochemistry 30(4):986-96 Details

Sutcliffe MJ, Dobson CM (1991), “Relaxation data in NMR structure determination: model calculations for the lysozyme-Gd3+ complex.” Proteins 10(2):117-29 Details

Teuten AJ, Smith RA, Dobson CM (1991), “Domain interactions in human plasminogen studied by proton NMR.” FEBS Lett 278(1):17-22 Details

1990

Archer DB, Jeenes DJ, MacKenzie DA, Brightwell G, Lambert N, Lowe G, Radford SE, Dobson CM (1990), “Hen egg white lysozyme expressed in, and secreted from, Aspergillus niger is correctly processed and folded.” Biotechnology (N Y) 8(8):741-5 Details

Dobson CM (1990), “Protein conformation. Hinge-bending and folding.” Nature 348(6298):198-9 Details

Redfield C, Dobson CM (1990), “1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme.” Biochemistry 29(31):7201-14 Details

1989

Baum J, Dobson CM, Evans PA, Hanley C (1989), “Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin.” Biochemistry 28(1):7-13 Details

Bogusky MJ, Dobson CM, Smith RA (1989), “Reversible independent unfolding of the domains of urokinase monitored by 1H NMR.” Biochemistry 28(16):6728-35 Details

Evans PA, Kautz RA, Fox RO, Dobson CM (1989), “A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease.” Biochemistry 28(1):362-70 Details

Oswald RE, Bogusky MJ, Bamberger M, Smith RA, Dobson CM (1989), “Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR.” Nature 337(6207):579-82 Details

Post CB, Dobson CM, Karplus M (1989), “A molecular dynamics analysis of protein structural elements.” Proteins 5(4):337-54 Details

1988

Dobson CM, Evans PA (1988), “Protein structure . Trapping folding intermediates.” Nature 335(6192):666-7 Details

Redfield C, Dobson CM (1988), “Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution.” Biochemistry 27(1):122-36 Details

1987

Delepierre M, Dobson CM, Karplus M, Poulsen FM, States DJ, Wedin RE (1987), “Electrostatic effects and hydrogen exchange behaviour in proteins. The pH dependence of exchange rates in lysozyme.” J Mol Biol 197(1):111-30 Details

Dobson CM, Lian LY (1987), “A 31P MAS NMR study of cytidine 2'-phosphate bound to ribonuclease A in the crystalline state.” FEBS Lett 225(1-2):183-7 Details

States DJ, Creighton TE, Dobson CM, Karplus M (1987), “Conformations of intermediates in the folding of the pancreatic trypsin inhibitor.” J Mol Biol 195(3):731-9 Details

1986

Dobson CM, Karplus M (1986), “Internal motion of proteins: nuclear magnetic resonance measurements and dynamic simulations.” Methods Enzymol 131:362-89 Details

Fox RO, Evans PA, Dobson CM (1986), “Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy.” Nature 320(6058):192-4 Details

Post CB, Brooks BR, Karplus M, Dobson CM, Artymiuk PJ, Cheetham JC, Phillips DC (1986), “Molecular dynamics simulations of native and substrate-bound lysozyme. A study of the average structures and atomic fluctuations.” J Mol Biol 190(3):455-79 Details

1985

Boyd J, Dobson CM, Redfield C (1985), “Assignment of resonances in the 1H NMR spectrum of human lysozyme.” Eur J Biochem 153(2):383-96 Details

Boyd J, Dobson CM, Redfield C (1985), “Identification of glycine spin systems in 1H NMR spectra of proteins using multiple quantum coherences.” FEBS Lett 186(1):35-40 Details

Campbell ID, Dobson CM, Williams RJ (1985), “The study of conformational states of proteins by nuclear magnetic resonance.” Biochem J 231(1):1-10 Details

Fett JW, Strydom DJ, Lobb RR, Alderman EM, Vallee BL, Artymiuk PJ, Collett S, Phillips DC, Dobson CM, Redfield C (1985), “Lysozyme: a major secretory product of a human colon carcinoma cell line.” Biochemistry 24(4):965-75 Details

Hoch JC, Dobson CM, Karplus M (1985), “Vicinal coupling constants and protein dynamics.” Biochemistry 24(15):3831-41 Details

Redfield C, Dobson CM, Scheek RM, Stob S, Kaptein R (1985), “Surface accessibility of aromatic residues in human lysozyme using photochemically induced dynamic nuclear polarization NMR spectroscopy.” FEBS Lett 185(2):248-52 Details

1984

Delepierre M, Dobson CM, Howarth MA, Poulsen FM (1984), “Identification using 1H NMR spectroscopy of slowly exchanging amide hydrogens of hen lysozyme in solution.” Eur J Biochem 145(2):389-95 Details

Dobson CM, Evans PA, Williamson KL (1984), “Proton NMR studies of denatured lysozyme.” FEBS Lett 168(2):331-4 Details

Huang TH, Bachovchin WW, Griffin RG, Dobson CM (1984), “High-resolution nitrogen-15 nuclear magnetic resonance studies of alpha-lytic protease in solid state. Direct comparison of enzyme structure in solution and in the solid state.” Biochemistry 23(25):5933-7 Details

States DJ, Dobson CM, Karplus M (1984), “A new two-disulphide intermediate in the refolding of reduced bovine pancreatic trypsin inhibitor.” J Mol Biol 174(2):411-8 Details

1983

Bentley GA, Delepierre M, Dobson CM, Wedin RE, Mason SA, Poulsen FM (1983), “Exchange of individual hydrogens for a protein in a crystal and in solution.” J Mol Biol 170(1):243-7 Details

Delepierre M, Dobson CM, Selvarajah S, Wedin RE, Poulsen FM (1983), “Correlation of hydrogen exchange behaviour and thermal stability of lysozyme.” J Mol Biol 168(3):687-92 Details

1982

Delepierre M, Dobson CM, Poulsen FM (1982), “Studies of beta-sheet structure in lysozyme by proton nuclear magnetic resonance. Assignments and analysis of spin-spin coupling constants.” Biochemistry 21(19):4756-61 Details

Hoch JC, Dobson CM, Karplus M (1982), “Fluctuations and averaging of proton chemical shifts in the bovine pancreatic trypsin inhibitor.” Biochemistry 21(6):1118-25 Details

Levy RM, Dobson CM, Karplus M (1982), “Dipolar NMR relaxation of nonprotonated aromatic carbons in proteins. Structural and dynamical effects.” Biophys J 39(1):107-13 Details

Redfield C, Poulsen FM, Dobson CM (1982), “Complete assignment of the 1H NMR spectrum of the aromatic residues of lysozyme.” Eur J Biochem 128(2-3):527-31 Details

Wedin RE, Delepierre M, Dobson CM, Poulsen FM (1982), “Mechanisms of hydrogen exchange in proteins from nuclear magnetic resonance studies of individual tryptophan indole NH hydrogens in lysozyme.” Biochemistry 21(5):1098-103 Details

1981

Blake CC, Cassels R, Dobson CM, Poulsen FM, Williams RJ, Wilson KS (1981), “Structure and binding properties of hen lysozyme modified at tryptophan 62.” J Mol Biol 147(1):73-95 Details

Brown-Mason A, Dobson CM, Woodworth RC (1981), “Efficient incorporation of deuterated amino acids into quail egg white proteins for nuclear magnetic resonance studies.” J Biol Chem 256(4):1506-9 Details

Costa JL, Dobson CM, Fay DD, Kirk KL, Poulsen FM, Valeri CR, Vecchione JJ (1981), “Nuclear magnetic resonance studies of amine storage in pig platelets.” FEBS Lett 136(2):325-8 Details

1980

Dobson CM, Hoch JC, Olejniczak ET, Poulsen FM (1980), “Conformations and conformational dynamics of proteins in solution studied by nuclear magnetic double resonance.” Biophys J 32(1):625-8 Details

Munowitz MG, Dobson CM, Griffin RG, Harrison SC (1980), “On the rigidity of RNA in tomato bushy stunt virus.” J Mol Biol 141(3):327-33 Details

Poulsen FM, Hoch JC, Dobson CM (1980), “A structural study of the hydrophobic box region of lysozyme in solution using nuclear Overhauser effects.” Biochemistry 19(12):2597-607 Details

States DJ, Dobson CM, Karplus M, Creighton TE (1980), “A conformational isomer of bovine pancreatic trypsin inhibitor protein produced by refolding.” Nature 286(5773):630-2 Details

Wagman ME, Dobson CM, Karplus M (1980), “Proton NMR studies of the association and folding of glucagon in solution.” FEBS Lett 119(2):265-70 Details

1979

Campbell ID, Dobson CM (1979), “The application of high resolution nuclear magnetic resonance to biological systems.” Methods Biochem Anal 25:1-133 Details

Woodworth RC, Dobson CM (1979), “Selective substitution of 2H and 3H into aromatic amino acids catalyzed by Raney nickel.” FEBS Lett 101(2):329-32 Details

1978

Cassels R, Dobson CM, Poulsen FM, Williams RJ (1978), “Study of the tryptophan residues of lysozyme using 1H nuclear magnetic resonance.” Eur J Biochem 92(1):81-97 Details

Dobson CM, Ferguson SJ, Poulsen FM, Williams RJ (1978), “Complete assignment of aromatic 1H nuclear magnetic resonances of the tyrosine residues of hen lysozyme.” Eur J Biochem 92(1):99-103 Details

Dobson CM, Geraldes CF, Ratcliffe G, Williams RJ (1978), “Nuclear-magnetic-resonance studies of 5'-ribonucleotide and 5'-deoxyribonucleotide conformations in solution using the lanthanide probe method.” Eur J Biochem 88(1):259-66 Details

1977

Blake CC, Grace DE, Johnson LN, Perkins SJ, Phillips DC, Cassels R, Dobson CM, Poulsen FM, Williams RJ (1977), “Physical and chemical properties of lysozyme.” Ciba Found Symp (60):137-85 Details

1976

Cave A, Dobson CM, Parello J, Williams RJ (1976), “Conformation mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residues.” FEBS Lett 65(2):190-4 Details

1975

Campbell ID, Dobson CM, Williams JP (1975), “Studies of exchangeable hydrogens in lysozyme by means of Fourier transform proton magnetic resonance.” Proc R Soc Lond B Biol Sci 189(1097):485-502 Details

Campbell ID, Dobson CM, Williams RJ (1975), “Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobility.” Proc R Soc Lond B Biol Sci 189(1097):503-9 Details

Campbell ID, Dobson CM, Williams RJ, Wright PE (1975), “Pulse methods for the simplification of protein NMR spectra.” FEBS Lett 57(1):96-9 Details

Dobson CM, Moore GR, Williams RJ (1975), “Assignment of aromatic amino acid PMR resonances of horse ferricytochrome c.” FEBS Lett 51(1):60-5 Details

Dobson CM, Williams RJ (1975), “An NMR study of the dynamics of inhibitor-induced conformational changes in lysozyme.” FEBS Lett 56(2):362-5 Details

1974

Campbell ID, Dobson CM, Jeminet G, Williams RJ (1974), “Pulsed NMR methods for the observation and assignment of exchangeable hydrogens: application to bacitracin.” FEBS Lett 49(1):115-9 Details

Dobson CM, Hoyle NJ, Geraldes CF, Bruschi M, LeGall J, Wright PE, Williams RJ (1974), “Outline structure of cytochrome c3 and consideration of its properties.” Nature 249(456):425-9 Details

1973

Campbell ID, Dobson CM, Williams RJ, Xavier AV (1973), “The determination of the structure of proteins in solution: lysozyme.” Ann N Y Acad Sci 222:163-74 Details