C M Dobson

Summary

Affiliation: University of Cambridge
Country: UK

Publications

  1. ncbi request reprint Protein folding and misfolding
    Christopher M Dobson
    University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 426:884-90. 2003
  2. ncbi request reprint Dynamics and timekeeping in biological systems
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom email
    Annu Rev Biochem 83:159-64. 2014
  3. pmc Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo
    Leila M Luheshi
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Biol 8:e1000334. 2010
  4. pmc Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells
    Priyanka Narayan
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, United Kingdom CB2 1EW
    J Am Chem Soc 135:1491-8. 2013
  5. pmc Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation
    Anthony W Fitzpatrick
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Comput Biol 7:e1002169. 2011
  6. pmc Direct observation of the interconversion of normal and toxic forms of α-synuclein
    Nunilo Cremades
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Cell 149:1048-59. 2012
  7. pmc The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity
    Maria F Mossuto
    Institute for Research in Biomedicine, Barcelona, Spain
    J Mol Biol 402:783-96. 2010
  8. pmc Recombinant amyloid beta-peptide production by coexpression with an affibody ligand
    Bertil Macao
    Department of Medical Biochemistry, University of Gothenburg, Göeborg, Sweden
    BMC Biotechnol 8:82. 2008
  9. ncbi request reprint Protein chemistry. In the footsteps of alchemists
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK
    Science 304:1259-62. 2004
  10. ncbi request reprint Principles of protein folding, misfolding and aggregation
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Semin Cell Dev Biol 15:3-16. 2004

Detail Information

Publications100

  1. ncbi request reprint Protein folding and misfolding
    Christopher M Dobson
    University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 426:884-90. 2003
    ..Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases...
  2. ncbi request reprint Dynamics and timekeeping in biological systems
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom email
    Annu Rev Biochem 83:159-64. 2014
    ..This article introduces three reviews on the theme of circadian rhythms. ..
  3. pmc Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo
    Leila M Luheshi
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Biol 8:e1000334. 2010
    ....
  4. pmc Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells
    Priyanka Narayan
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, United Kingdom CB2 1EW
    J Am Chem Soc 135:1491-8. 2013
    ....
  5. pmc Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation
    Anthony W Fitzpatrick
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Comput Biol 7:e1002169. 2011
    ....
  6. pmc Direct observation of the interconversion of normal and toxic forms of α-synuclein
    Nunilo Cremades
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Cell 149:1048-59. 2012
    ..In the absence of added soluble protein, the assembly process is reversed and fibrils disaggregate to form stable oligomers, hence acting as a source of cytotoxic species...
  7. pmc The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity
    Maria F Mossuto
    Institute for Research in Biomedicine, Barcelona, Spain
    J Mol Biol 402:783-96. 2010
    ..These findings indicate that protein aggregation can give rise to species with different degree of cytotoxicity due to intrinsic differences in their physicochemical properties...
  8. pmc Recombinant amyloid beta-peptide production by coexpression with an affibody ligand
    Bertil Macao
    Department of Medical Biochemistry, University of Gothenburg, Göeborg, Sweden
    BMC Biotechnol 8:82. 2008
    ..ZAbeta3 binds to the amyloidogenic central and C-terminal part of Abeta with nanomolar affinity and consequently inhibits aggregation...
  9. ncbi request reprint Protein chemistry. In the footsteps of alchemists
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK
    Science 304:1259-62. 2004
  10. ncbi request reprint Principles of protein folding, misfolding and aggregation
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Semin Cell Dev Biol 15:3-16. 2004
    ..It focuses in particular on the emerging links between protein aggregation and the increasingly prevalent forms of debilitating disease with which it is now known to be associated...
  11. ncbi request reprint Experimental investigation of protein folding and misfolding
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EX, UK
    Methods 34:4-14. 2004
    ....
  12. ncbi request reprint Chemical space and biology
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 432:824-8. 2004
    ....
  13. ncbi request reprint Protein aggregation and its consequences for human disease
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Protein Pept Lett 13:219-27. 2006
    ....
  14. ncbi request reprint Rationalization of the effects of mutations on peptide and protein aggregation rates
    Fabrizio Chiti
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 424:805-8. 2003
    ....
  15. pmc Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass
    Tuomas P J Knowles
    Nanoscience Centre, University of Cambridge, JJ Thomson Avenue, Cambridge, United Kingdom
    Proc Natl Acad Sci U S A 104:10016-21. 2007
    ....
  16. ncbi request reprint Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Philos Transact A Math Phys Eng Sci 361:1205-22. 2003
    ..More fundamentally, we believe that this research will result in a more coherent understanding of the origin, evolution and functional properties of living systems...
  17. ncbi request reprint The importance of sequence diversity in the aggregation and evolution of proteins
    Caroline F Wright
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 438:878-81. 2005
    ..We propose that such low sequence identities could have a crucial and general role in safeguarding proteins against misfolding and aggregation...
  18. pmc Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy
    Lisa D Cabrita
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 106:22239-44. 2009
    ....
  19. ncbi request reprint Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations
    Mireille Dumoulin
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 346:773-88. 2005
    ....
  20. ncbi request reprint Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein
    Kresten Lindorff-Larsen
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom
    J Am Chem Soc 126:3291-9. 2004
    ..The preferential formation of these contacts suggests that the sequence-dependent patterns of helical propensity and hydrophobicity are important determinants of the structure in the denatured state of ACBP...
  21. pmc Structures and relative free energies of partially folded states of proteins
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 100:14817-21. 2003
    ..The form of the landscape, together with the existence of distinct cores, supports the concept that robustness and modularity are the properties that make possible the folding of complex proteins...
  22. ncbi request reprint Getting out of shape
    Christopher M Dobson
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 418:729-30. 2002
  23. doi request reprint Prediction of aggregation-prone regions in structured proteins
    Gian Gaetano Tartaglia
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 380:425-36. 2008
    ....
  24. ncbi request reprint Long-range interactions within a nonnative protein
    Judith Klein-Seetharaman
    Massachusetts Institute of Technology, Department of Chemistry, Francis Bitter Magnet Laboratory, 170 Albany Street, Cambridge, MA 02139, USA
    Science 295:1719-22. 2002
    ..Thus, nativelike structure in the denatured protein is stabilized by the involvement of Trp62 in nonnative and long-range interactions...
  25. ncbi request reprint Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    Amol P Pawar
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 350:379-92. 2005
    ....
  26. ncbi request reprint Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species
    Matthew M Dedmon
    Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, United Kingdom
    J Biol Chem 280:14733-40. 2005
    ..This work therefore elucidates a specific role of Hsp70 in the pathogenesis of PD and supports the general concept that chaperone action is a crucial aspect in protecting against the otherwise damaging consequences of protein misfolding...
  27. ncbi request reprint Towards complete descriptions of the free-energy landscapes of proteins
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Philos Transact A Math Phys Eng Sci 363:433-50; discussion 450-2. 2005
    ....
  28. ncbi request reprint Reversal of protein aggregation provides evidence for multiple aggregated States
    Martino Calamai
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
    J Mol Biol 346:603-16. 2005
    ....
  29. doi request reprint Detergent-like interaction of Congo red with the amyloid beta peptide
    Christofer Lendel
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Biochemistry 49:1358-60. 2010
    ..Although CR promotes beta sheet formation and peptide aggregation, it may also solubilize toxic protein species, making them less harmful to critical cellular components and thereby reducing amyloid toxicity...
  30. pmc Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    Martino Calamai
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom
    Biophys J 89:4201-10. 2005
    ..In addition, the structures of the resulting aggregates are largely independent of the conformational properties of their soluble precursors...
  31. doi request reprint Structure and properties of a complex of α-synuclein and a single-domain camelid antibody
    Erwin J De Genst
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 402:326-43. 2010
    ....
  32. pmc Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip
    Cintia Roodveldt
    Department of Chemistry, University of Cambridge, Cambridge, UK
    EMBO J 28:3758-70. 2009
    ..Our findings indicate that a decreased expression of Hip could facilitate depletion of Hsp70 by amyloidogenic polypeptides, impairing chaperone proteostasis and stimulating neurodegeneration...
  33. pmc Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 104:16516-21. 2007
    ..These findings represent a step toward a detailed structural understanding of the cellular processes of cotranslational folding...
  34. pmc Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    Mookyung Cheon
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Comput Biol 3:1727-38. 2007
    ..We discuss how the increase in solvent-exposed hydrophobic surface resulting from such a competition offers an explanation for recent observations concerning the cytotoxicity of oligomeric species formed prior to mature amyloid fibrils...
  35. ncbi request reprint Geometry, energetics, and dynamics of hydrogen bonds in proteins: structural information derived from NMR scalar couplings
    Joerg Gsponer
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Am Chem Soc 128:15127-35. 2006
    ....
  36. ncbi request reprint Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation
    Reto Bader
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 356:189-208. 2006
    ..Comparison with the behaviour of other amyloidogenic systems suggests that the general mechanistic features outlined here are likely to be common to at least a wide variety of peptides and proteins...
  37. ncbi request reprint Importance of metastable states in the free energy landscapes of polypeptide chains
    Stefan Auer
    University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Phys Rev Lett 99:178104. 2007
    ..These mestastable states are therefore likely to be of particular significance in determining the generic tendency of proteins to aggregate into potentially pathogenic agents...
  38. pmc Molecular determinants of the aggregation behavior of alpha- and beta-synuclein
    Robert C Rivers
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom
    Protein Sci 17:887-98. 2008
    ..This conclusion provides new insights into the role of alpha-synuclein in disease and into the factors that regulate the balance between solubility and aggregation of a natively unfolded protein...
  39. ncbi request reprint Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins
    Sarah Meehan
    Department of Chemistry, University of Cambridge, Cambridge, UK
    J Mol Biol 372:470-84. 2007
    ..Overall, this study suggests that there could be a fine balance in vivo between the native functional sHsp state and the formation of amyloid fibrils...
  40. pmc A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction
    Jörg Gsponer
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Structure 16:736-46. 2008
    ..Based on these results and the combination of modern free energy landscape theory with classical allostery models, we suggest that a coupled equilibrium shift mechanism controls the efficient binding of CaM to a wide range of ligands...
  41. doi request reprint Protein misfolding and disease: from the test tube to the organism
    Leila M Luheshi
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Curr Opin Chem Biol 12:25-31. 2008
    ....
  42. doi request reprint Immunological features of alpha-synuclein in Parkinson's disease
    Cintia Roodveldt
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    J Cell Mol Med 12:1820-9. 2008
    ....
  43. pmc Analysis of sub-tauc and supra-tauc motions in protein Gbeta1 using molecular dynamics simulations
    Jennifer M Bui
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    Biophys J 97:2513-20. 2009
    ..These results provide further characterization of the large structural fluctuations in the native states of proteins that occur on timescales longer than the rotational correlation time...
  44. doi request reprint 1H, 15N and 13C assignments of yellow fluorescent protein (YFP) Venus
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
    Biomol NMR Assign 3:67-72. 2009
    ....
  45. doi request reprint 1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom
    Biomol NMR Assign 3:29-31. 2009
    ..We have recently used the pair of domains 5 and 6 of ABP-120 as a model system for studying multi-domain nascent chain folding on the ribosome. Here we present the NMR assignments of domain 5 in its native and 8M urea-denatured states...
  46. doi request reprint 1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK
    Biomol NMR Assign 3:17-20. 2009
    ....
  47. doi request reprint Bridging the gap: from protein misfolding to protein misfolding diseases
    Leila M Luheshi
    Department of Chemistry, University of Cambridge, Cambridge, UK
    FEBS Lett 583:2581-6. 2009
    ....
  48. pmc Folding study of Venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    J Biol Chem 285:4859-69. 2010
    ....
  49. doi request reprint A relationship between mRNA expression levels and protein solubility in E. coli
    Gian Gaetano Tartaglia
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Mol Biol 388:381-9. 2009
    ..coli with an accuracy of 86%...
  50. doi request reprint Use of protonless NMR spectroscopy to alleviate the loss of information resulting from exchange-broadening
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    J Am Chem Soc 131:7222-3. 2009
    ..Human alpha-synuclein, which is associated with Parkinson's disease, is used as a model system to illustrate the usefulness of protonless NMR spectroscopy in recovering hitherto missing spectral information...
  51. doi request reprint Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements
    Jane R Allison
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK
    J Am Chem Soc 131:18314-26. 2009
    ..Our findings indicate that our procedure provides an accurate estimate of the relative statistical weights of the different conformations populated by alpha-synuclein in its natively unfolded state...
  52. doi request reprint Folding of small proteins by Monte Carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology
    Paul Robustelli
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Phys Chem B 113:7890-6. 2009
    ..We provide an initial demonstration of this procedure by determining the structure of two small proteins, with alpha and beta folds, respectively...
  53. doi request reprint Probing side-chain dynamics of a ribosome-bound nascent chain using methyl NMR spectroscopy
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Am Chem Soc 131:8366-7. 2009
    ....
  54. doi request reprint Structure, dynamics and folding of an immunoglobulin domain of the gelation factor (ABP-120) from Dictyostelium discoideum
    Shang Te Danny Hsu
    Department of Chemistry, University of Cambridge, Cambridge, UK
    J Mol Biol 388:865-79. 2009
    ....
  55. ncbi request reprint Quantitative approaches to defining normal and aberrant protein homeostasis
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW
    Faraday Discuss 143:277-91; discussion 359-72. 2009
    ....
  56. ncbi request reprint Role of intermolecular forces in defining material properties of protein nanofibrils
    Tuomas P Knowles
    Nanoscience Centre, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0FF, UK
    Science 318:1900-3. 2007
    ..We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions...
  57. pmc Calculation of mutational free energy changes in transition states for protein folding
    Kresten Lindorff-Larsen
    University of Cambridge, University Chemical Laboratory, Cambridge, United Kingdom
    Biophys J 85:1207-14. 2003
    ..Taken together, these results show that the procedure developed here is a tool of general validity for analyzing, assessing, and improving the quality of the structures of transition states for protein folding...
  58. pmc Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values
    Xavier Salvatella
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 102:12389-94. 2005
    ....
  59. ncbi request reprint Rare fluctuations of native proteins sampled by equilibrium hydrogen exchange
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    J Am Chem Soc 125:15686-7. 2003
    ..The measured protection factors are used to bias Monte Carlo simulations to sample the structures of the exchange competent species. The approach is illustrated by its application to the case of alpha-lactalbumin...
  60. ncbi request reprint Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties
    Filip Meersman
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Biochim Biophys Acta 1764:452-60. 2006
    ..Some implications regarding the nature of toxic species, associated with at least many of the amyloid disorders, and recently proposed structural models are discussed...
  61. ncbi request reprint A toy model for predicting the rate of amyloid formation from unfolded protein
    Damien Hall
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, UK
    J Mol Biol 351:195-205. 2005
    ....
  62. pmc A glimpse at the organization of the protein universe
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 102:5641-2. 2005
  63. ncbi request reprint Expanding to fill the gap: a possible role for inert biopolymers in regulating the extent of the 'macromolecular crowding' effect
    Damien Hall
    Chemistry Department, University of Cambridge, Lensfield Road, Cambridge CB21EW, United Kingdom
    FEBS Lett 580:2584-90. 2006
    ..This ability would confer on the non-reactive polymer a novel role in influencing other processes in solution affected by macromolecular crowding...
  64. ncbi request reprint Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
    Mireille Dumoulin
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Biochimie 86:589-600. 2004
    ....
  65. ncbi request reprint The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner
    Glyn L Devlin
    Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge CB3 0HE, UK
    J Mol Biol 360:497-509. 2006
    ....
  66. pmc The formation of spherulites by amyloid fibrils of bovine insulin
    Mark R H Krebs
    Department of Physics, Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE, United Kingdom
    Proc Natl Acad Sci U S A 101:14420-4. 2004
    ..The ability of amyloid fibrils to form such higher-order assemblies supports the hypothesis that they represent a generic form of polypeptide structure with properties that are analogous to those of classical synthetic polymers...
  67. pmc Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes
    John Christodoulou
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 101:10949-54. 2004
    ....
  68. ncbi request reprint A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme
    Mireille Dumoulin
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 424:783-8. 2003
    ....
  69. ncbi request reprint Molecular recycling within amyloid fibrils
    Natàlia Carulla
    University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK
    Nature 436:554-8. 2005
    ..This insight into the dynamic nature of amyloid fibrils, and the ability to determine the parameters that define this behaviour, have important implications for the design of therapeutic strategies directed against amyloid disease...
  70. doi request reprint Protein dynamics: Moore's law in molecular biology
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Curr Biol 21:R68-70. 2011
    ..Such simulations are increasingly revealing the inner workings of biological systems by generating atomic-level descriptions of their behaviour that make testable predictions about key molecular processes...
  71. ncbi request reprint Spatial propagation of protein polymerization
    S I A Cohen
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom and School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, USA
    Phys Rev Lett 112:098101. 2014
    ....
  72. ncbi request reprint Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1)
    S Poon
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK
    Protein Pept Lett 16:1548-56. 2009
    ....
  73. pmc Direct characterization of amyloidogenic oligomers by single-molecule fluorescence
    Angel Orte
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
    Proc Natl Acad Sci U S A 105:14424-9. 2008
    ....
  74. ncbi request reprint Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
    Sarah Meehan
    Biological Physics Group, Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE, United Kingdom
    J Biol Chem 279:3413-9. 2004
    ..The ability of the crystallins to convert into fibrils under destabilizing conditions suggests that this process could contribute to the development of cataract with aging...
  75. ncbi request reprint Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis
    Patrizia Polverino De Laureto
    CRIBI Biotechnology Centre, University of Padua, Viale G Colombo 3, 35121, Padua, Italy
    J Mol Biol 334:129-41. 2003
    ..In addition, the disordered and non-native character of the polypeptide chains in the early aggregates could be important in determining the high cytotoxicity that has been revealed in previous studies of these species...
  76. ncbi request reprint Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
    Mireille Dumoulin
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Acc Chem Res 39:603-10. 2006
    ..It also discusses the significance of these studies for our general understanding of normal and aberrant protein folding in the context of human health and disease...
  77. pmc Characterization of the nanoscale properties of individual amyloid fibrils
    Jeffrey F Smith
    Nanoscience Centre, University of Cambridge, JJ Thomson Avenue, Cambridge CB3 0FF, United Kingdom
    Proc Natl Acad Sci U S A 103:15806-11. 2006
    ....
  78. ncbi request reprint Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions
    Filip Meersman
    Department of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200F, B 3001 Leuven, Belgium
    Chem Soc Rev 35:908-17. 2006
    ..We also discuss the effect of pressure on protein folding and free energy landscapes. From a molecular viewpoint, pressure effects can be rationalised in terms of packing and hydration of proteins...
  79. ncbi request reprint Characterization of single-tryptophan mutants of histidine-containing phosphocarrier protein: evidence for local rearrangements during folding from high concentrations of denaturant
    Ana I Azuaga
    Bijvoet Center for Biomolecular Research, University of Utrecht, Padualaan 8, 3584 CH, Utrecht, The Netherlands
    Biochemistry 42:4883-95. 2003
    ....
  80. pmc De novo designed peptide-based amyloid fibrils
    Manuela Lopez de la Paz
    European Molecular Biology Laboratory, Meyerhofstrasse 1, D 69117 Heidelberg, Germany Europe
    Proc Natl Acad Sci U S A 99:16052-7. 2002
    ..The present results, in conjunction with x-ray fiber diffraction, electron microscopy, and Fourier transform infrared measurements, have allowed us to propose a detailed structural model of the fibrils...
  81. ncbi request reprint Identification of the core structure of lysozyme amyloid fibrils by proteolysis
    Erica Frare
    CRIBI Biotechnology Centre, University of Padua, Viale G Colombo 3, 35121 Padua, Italy
    J Mol Biol 361:551-61. 2006
    ..The majority of amyloid fibrils formed from lysozyme under the conditions used here contain a core structure involving some 50% of the polypeptide chain that is flanked by proteolytically accessible N and C-terminal regions...
  82. pmc Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Florence, Italy
    Proc Natl Acad Sci U S A 99:16419-26. 2002
    ....
  83. ncbi request reprint Unfolding and aggregation during the thermal denaturation of streptokinase
    Ana I Azuaga
    Departamento de Quimica Fisica e Instituto de Biotecnologia, Facultad de Ciencias, Universidad de Granada, Granada, Spain
    Eur J Biochem 269:4121-33. 2002
    ..It is likely that this region is able to act as a nucleus for the aggregation of the full-length protein...
  84. pmc The protofilament structure of insulin amyloid fibrils
    Jose L Jimenez
    Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, United Kingdom
    Proc Natl Acad Sci U S A 99:9196-201. 2002
    ..Comparison of the various fibril structures suggests that very small, local changes in beta-sheet twist are important in establishing the long-range coiling of the protofilaments into fibrils of diverse morphology...
  85. ncbi request reprint The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study
    John A Carver
    Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    J Mol Biol 318:815-27. 2002
    ..Thus, alpha-crystallin is not a chaperone that is involved in protein folding per se. Rather, its role is to stabilise compromised, partly folded, molten globule states of proteins that are destined for precipitation...
  86. pmc Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides
    Jessica Meinhardt
    Leibniz Institut für Altersforschung, Fritz Lipmann Institut, D 07745 Jena, Germany
    Protein Sci 16:1214-22. 2007
    ....
  87. pmc The circularization of amyloid fibrils formed by apolipoprotein C-II
    Danny M Hatters
    Department of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Australia
    Biophys J 85:3979-90. 2003
    ....
  88. ncbi request reprint Transition state contact orders correlate with protein folding rates
    Emanuele Paci
    Institute of Molecular Biophysics and Physics and Astronomy, University of Leeds, Leeds LS2 9JT, UK
    J Mol Biol 352:495-500. 2005
    ....
  89. ncbi request reprint Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein
    David C Thorn
    School of Chemistry and Physics, The University of Adelaide, Adelaide, South Australia 5005, Australia
    Biochemistry 44:17027-36. 2005
    ..Casein proteins may therefore play a preventative role in the development of corpora amylacea, a disorder associated with the accumulation of amyloid deposits in mammary tissue...
  90. pmc Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4
    Daniela C Vaz
    Centro de Neurociências de Coimbra, Universidade de Coimbra, Coimbra, Portugal
    Protein Sci 15:33-44. 2006
    ..Moreover, a smaller change in heat capacity of unfolding was also observed for the mutants. Thus, disulfide bridges in IL4 play a critical role in maintaining the thermodynamic stability and core packing of the helix bundle...
  91. ncbi request reprint Investigating the effects of mutations on protein aggregation in the cell
    Giulia Calloni
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    J Biol Chem 280:10607-13. 2005
    ..These results suggest that the principles being established to rationalize aggregation behavior in vitro have general validity for situations in vivo where aggregation has both biotechnological and medical relevance...
  92. ncbi request reprint An accidental breach of a protein's natural defenses
    Christopher M Dobson
    Nat Struct Mol Biol 13:295-7. 2006
  93. ncbi request reprint Chemical biology: More charges against aggregation
    Michele Vendruscolo
    Nature 449:555. 2007
  94. ncbi request reprint Structural biology. Dynamic visions of enzymatic reactions
    Michele Vendruscolo
    Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
    Science 313:1586-7. 2006
  95. ncbi request reprint A highly amyloidogenic region of hen lysozyme
    Erica Frare
    CRIBI Biotechnology Centre, University of Padua, Viale G Colombo 3, 35121 Padua, Italy
    J Mol Biol 340:1153-65. 2004
    ....
  96. ncbi request reprint Kinetic partitioning of protein folding and aggregation
    Fabrizio Chiti
    Dipartimento di Scienze Biochimiche, Universita degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    Nat Struct Biol 9:137-43. 2002
    ....
  97. ncbi request reprint Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    Fernanda G De Felice
    Departamento de Bioquimica Medica, Instituto de Ciencias Biomedicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21944 590, Brazil
    FASEB J 18:1099-101. 2004
    ....
  98. ncbi request reprint Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    Georgia Plakoutsi
    Dipartimento di Scienze Biochimiche, Universita di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
    J Mol Biol 351:910-22. 2005
    ....
  99. pmc Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
    Marcus Fändrich
    Institut fur Molekulare Biotechnologie, Beutenbergstrasse 11, D 07745 Jena, Germany
    Proc Natl Acad Sci U S A 100:15463-8. 2003
    ..However, it is inevitable that such conditions often stabilize protein folding intermediates...
  100. ncbi request reprint Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    Massimo Stefani
    Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy
    J Mol Med (Berl) 81:678-99. 2003
    ..It also suggests some intriguing new factors that could be of great significance in the evolution of biological molecules and the mechanisms that regulate their behaviour...