Christopher M. Dobson

Author

University of Cambridge ORCID

Also Known As

, C DOBSON, C Dobson, C M Dobson, C. Dobson, C. M. DOBSON, C. M. Dobson, C.M Dobson, C.M. DOBSON, C.M. Dobson

Publications

118K

Citations

161

H-Index

323

Concepts

All Affiliations

University of Cambridge University of Oxford University of Florence University College London Harvard University

About

Christopher M. Dobson is an author at University of Cambridge specializing in medicine, natural sciences, and protein folding.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	112	336	44.9K
2	Engineering	50	93	10.4K
3	Health Sciences	5	5	245
4	Language Studies	1	1	71
5	Law	1	1	45

Christopher M. Dobson

700

Publications

87.2K

Citations

151

H-Index

Page 1

	Year	Citations
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Monica Bucciantini, Elisa Giannoni, Fabrizio Chiti, Nature Aggregates ImpliesProtein FunctionBiochemistryProtein AssemblyProtein Folding	2002	2.4K
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism Samuel I. A. Cohen, Sara Linse, Leila M. Luheshi, Proceedings of the National Academy of Sciences Protein AssemblyHomogeneous Primary NucleationMolecular BiologyNeurochemical BiomarkersPeptide Science	2013	1.4K
An Analytical Solution to the Kinetics of Breakable Filament Assembly Tuomas P. J. Knowles, Christopher A. Waudby, Glyn L. Devlin, Science Biophysical ModelingEngineeringMechanical EngineeringMolecular BiologyCytoskeleton	2009	1.1K
Rationalization of the effects of mutations on peptide andprotein aggregation rates Fabrizio Chiti, Massimo Stefani, Niccolò Taddei, Nature EngineeringProtein FoldingNatural SciencesPeptide EngineeringComputational Biology	2003	1.1K
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis David R. Booth, Margaret Sunde, Vittorio Bellotti, Nature Human Lysozyme VariantsAlzheimer's DiseaseProtein AssemblyProtein FoldingNatural Sciences	1997	1K
Designing conditions for <i>in vitro</i> formation of amyloid protofilaments and fibrils Fabrizio Chiti, Paul Webster, Niccolò Taddei, Proceedings of the National Academy of Sciences Protein AssemblyBiofabricationCytoskeletonBiomedical EngineeringAnalytical Ultracentrifugation	1999	1K
Chemical space and biology Christopher M. Dobson Nature	2004	1K
Hydrodynamic Radii of Native and Denatured Proteins Measured by Pulse Field Gradient NMR Techniques Deborah K. Wilkins, Shaun B. Grimshaw, Véronique Receveur‐Brechot, Biochemistry	1999	993
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein Nunilo Cremades, Samuel I. A. Cohen, Emma Deas, Cell	2012	881
The protofilament structure of insulin amyloid fibrils José L. Jiménez, Ewan J. Nettleton, Mario Bouchard, Proceedings of the National Academy of Sciences	2002	832

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