研究领域

Biological

Our research interests are primarily focused on the investigation of the structures and properties of biological molecules, especially proteins, and their relationship to biological evolution and disease. We have particular interest in the fundamental science underlying disorders such as Alzheimer's and Parkinson's disease. In addition, however, we have recently become involved in the novel utilisation of biological molecules in materials science and nanotechnology. The methods we use are largely experimental, but do include theoretical and computational approaches. Much of the work is highly interdisciplinary, and people joining the group come from a wide variety of scientific backgrounds ranging from experimental biochemistry to theoretical physics. The research group is based in the Chemistry Department in a newly constructed laboratory located in the Unilever Building. The range of experimental techniques used by the group is very large, including NMR, EM, AFM and X-ray diffraction, as well as a variety of methods based on optical spectroscopy, including fluorescence and circular dichroism. Many, but not all, members of the group also use the techniques of protein chemistry and molecular biology. The group has close links with scientists in other laboratories in Cambridge, including the Clinical School, the Genetics Department and the Nanoscience Centre and, indeed, some members of the group have been largely based in these departments. New members of the group usually develop a project by discussion with me, along with other members of the research team. Group members are often involved in joint projects with other laboratories and may spend periods of time working with our collaborators in other parts of the world.

近期论文

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A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers SI Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstål, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TP Knowles, S Linse – Nature Structural & Molecular Biology (2015) 22, 207 (DOI: 10.1038/nsmb.2971) Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. C Galvagnion, AK Buell, G Meisl, TC Michaels, M Vendruscolo, TP Knowles, CM Dobson – Nature Chemical Biology (2015) 11, 229 (DOI: 10.1038/nchembio.1750) Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases. P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo – Trends Pharmacol Sci (2015) 36, 72 (DOI: 10.1016/j.tips.2014.12.004) Structure of a low-population intermediate state in the release of an enzyme product. A De Simone, FA Aprile, A Dhulesia, CM Dobson, M Vendruscolo – eLife (2015) 4 (DOI: 10.7554/eLife.02777) Protein Microgels from Amyloid Fibril Networks U Shimanovich, I Efimov, TO Mason, P Flagmeier, AK Buell, A Gedanken, S Linse, KS Åkerfeldt, CM Dobson, DA Weitz, TP Knowles – ACS Nano (2015) 9, 43 (DOI: 10.1021/nn504869d) A Relationship between the Transient Structure in the Monomeric State and the Aggregation Propensities of α-Synuclein and β-Synuclein JR Allison, RC Rivers, JC Christodoulou, M Vendruscolo, CM Dobson – Biochemistry (2014) 53, 7170 (DOI: 10.1021/bi5009326) Single-Molecule Imaging Reveals that Small Amyloid-β 1-42 Oligomers Interact with the Cellular Prion Protein (PrP C ) KA Ganzinger, P Narayan, SS Qamar, L Weimann, RT Ranasinghe, A Aguzzi, CM Dobson, J McColl, P St George-Hyslop, D Klenerman – Chembiochem (2014) 15, 2515 (DOI: 10.1002/cbic.201402377) Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation. C Månsson, P Arosio, R Hussein, HH Kampinga, RM Hashem, WC Boelens, CM Dobson, TP Knowles, S Linse, C Emanuelsson – J Biol Chem (2014) 289, 31066 (DOI: 10.1074/jbc.m114.595124) Antibodies and protein misfolding: From structural research tools to therapeutic strategies E De Genst, A Messer, CM Dobson – Biochimica et Biophysica Acta - Proteins and Proteomics (2014) 1844, 1907 (DOI: 10.1016/j.bbapap.2014.08.016) The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation. AK Buell, CM Dobson, TP Knowles – Essays Biochem (2014) 56, 11 (DOI: 10.1042/bse0560011)Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity B Mannini, E Mulvihill, C Sgromo, R Cascella, R Khodarahmi, M Ramazzotti, CM Dobson, C Cecchi, F Chiti – ACS Chem Biol (2014) 9, 2309 (DOI: 10.1021/cb500505m) Differences in nucleation behavior underlie the contrasting aggregation kinetics of the A beta 40 and A beta 42 peptides G Meisl, X Yang, E Hellstrand, B Frohm, JB Kirkegaard, SI Cohen, CM Dobson, S Linse, TP Knowles – Proceedings of the National Academy of Sciences of the United States of America (2014) 111, 9384 (DOI: 10.1073/pnas.1401564111) The amyloid state and its association with protein misfolding diseases. TP Knowles, M Vendruscolo, CM Dobson – Nature Reviews Molecular Cell Biology (2014) 15, 384 (DOI: 10.1038/nrm3810) 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 EK Esbjörner, F Chan, E Rees, M Erdelyi, LM Luheshi, CW Bertoncini, CF Kaminski, CM Dobson, GS Kaminski Schierle – Chemistry & Biology (2014) 21, 732 (DOI: 10.1016/j.chembiol.2014.03.014) Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation AK Buell, C Galvagnion, R Gaspar, E Sparr, M Vendruscolo, TP Knowles, S Linse, CM Dobson – Proceedings of the National Academy of Sciences of the United States of America (2014) 111, 7671 (DOI: 10.1073/pnas.1315346111) Hypochlorite-induced structural modifications enhance the chaperone activity of human alpha(2)-macroglobulin AR Wyatt, JR Kumita, RW Mifsud, CA Gooden, MR Wilson, CM Dobson – Proceedings of the National Academy of Sciences of the United States of America (2014) 111, E2081 (DOI: 10.1073/pnas.1403379111) Understanding the influence of codon translation rates on cotranslational protein folding EP O'Brien, P Ciryam, M Vendruscolo, CM Dobson – Accounts of Chemical Research (2014) 47, 1536 (DOI: 10.1021/ar5000117) Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies J Wacker, R Rönicke, M Westermann, M Wulff, KG Reymann, CM Dobson, U Horn, DC Crowther, LM Luheshi, M Fändrich – Acta Neuropathologica Communications (2014) 2, 43 (DOI: 10.1186/2051-5960-2-43) Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage. P Narayan, KM Holmström, DH Kim, DJ Whitcomb, MR Wilson, P St George-Hyslop, NW Wood, CM Dobson, K Cho, AY Abramov, D Klenerman – Biochemistry (2014) 53, 2442 (DOI: 10.1021/bi401606f) Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters GA Garcia, SIA Cohen, CM Dobson, TPJ Knowles – Physical Review E - Statistical, Nonlinear, and Soft Matter Physics (2014) 89, ARTN 032712 (DOI: 10.1103/PhysRevE.89.032712)