The structural basis of protein folding and its links with human disease von Dobson, C. M., Ellis, R. J., Fersht, A. R., Dobson, Christopher M.

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Real-time PCR detection of bacteria belonging to the Firmicutes Phylum von Haakensen, M., Dobson, C.M., Deneer, H., Ziola, B.

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Protein folding and misfolding von Dobson, Christopher M.

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A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme von DUMOULIN, Mireille, LAST, Alexander M, WYNS, Lode, REDFIELD, Christina, MATAGNE, André, ROBINSON, Carol V, DOHSON, Christopher M, DESMYTER, Aline, DECANNIERE, Klaas, CANET, Denis, LARSSON, Göran, SPENCER, Andrew, ARCHER, David B, SASSE, Jurgen, MUYLDERMANS, Serge

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Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy von BOUCHARD, MARIO, ZURDO, JESÚS, NETTLETON, EWAN J., DOBSON, CHRISTOPHER M., ROBINSON, CAROL V.

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Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain von Krebs, Mark R.H, Wilkins, Deborah K, Chung, Evonne W, Pitkeathly, Maureen C, Chamberlain, Aaron K, Zurdo, Jesus, Robinson, Carol V, Dobson, Christopher M

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Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain von Zurdo, Jesús, Guijarro, J.I, Jiménez, Jose L, Saibil, Helen R, Dobson, Christopher M

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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis von Booth, David R., Sunde, Margaret, Bellotti, Vittorio, Robinson, Carol V., Hutchinson, Winston L., Fraser, Paul E., Hawkins, Philip N., Dobson, Christopher M., Radford, Sheena E., Blake, Colin C. F., Pepys, Mark B.

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Protein misfolding, evolution and disease von Dobson, Christopher M.

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Preparation and Characterization of Purified Amyloid Fibrils von Zurdo, Jesús, Guijarro, J. Iñaki, Dobson, Christopher M

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Dielectric properties of soils in the 0.3-1.3-GHz range von Peplinski, N.R., Ulaby, F.T., Dobson, M.C.

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Rationalization of the effects of mutations on peptide and protein aggregation rates von CHITI, Fabrizo, STEFANI, Massimo, TADDEL, Niccoli, RAMPONI, Glampietro, DOBSON, Christopher M

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Protein solubility and protein homeostasis: a generic view of protein misfolding disorders von Vendruscolo, Michele, Knowles, Tuomas P J, Dobson, Christopher M

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The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation von Fändrich, Marcus, Dobson, Christopher M.

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Prediction of “Aggregation-prone” and “Aggregation-susceptible” Regions in Proteins Associated with Neurodegenerative Diseases von Pawar, Amol P., DuBay, Kateri F., Zurdo, Jesús, Chiti, Fabrizio, Vendruscolo, Michele, Dobson, Christopher M.

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The characterization of hardened alkali-activated blast-furnace slag pastes and the nature of the calcium silicate hydrate (C-S-H) phase von Richardson, I.G., Brough, A.R., Groves, G.W., Dobson, C.M.

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Sensitivity to soil moisture by active and passive microwave sensors von Du, Y., Ulaby, F.T., Dobson, M.C.

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Detection of Transient Protein Folding Populations by Mass Spectrometry von Miranker, Andrew, Robinson, Carol V., Radford, Sheena E., Aplin, Robin T., Dobson, Christopher M.

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The folding process of hen lysozyme: a perspective from the 'new view' von Matagne, A, Dobson, C.M

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases von Bucciantini, Monica, Giannoni, Elisa, Chiti, Fabrizio, Baroni, Fabiana, Formigli, Lucia, Zurdo, Jesús, Taddei, Niccolò, Ramponi, Giampietro, Dobson, Christopher M., Stefani, Massimo

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