Standout Papers

Protein Misfolding, Functional Amyloid, and Human Disease 2002 2026 2010 2018 5.2k
  1. Protein Misfolding, Functional Amyloid, and Human Disease (2006)
    Fabrizio Chiti, Christopher M. Dobson Annual Review of Biochemistry
  2. Protein folding and misfolding (2003)
    Christopher M. Dobson Nature
  3. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002)
    Monica Bucciantini, Elisa Giannoni et al. Nature
  4. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade (2017)
    Fabrizio Chiti, Christopher M. Dobson Annual Review of Biochemistry
  5. The amyloid state and its association with protein misfolding diseases (2014)
    Tuomas P. J. Knowles, Michele Vendruscolo et al. Nature Reviews Molecular Cell Biology
  6. Protein misfolding, evolution and disease (1999)
    Christopher M. Dobson Trends in Biochemical Sciences
  7. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution (2003)
    Massimo Stefani, Christopher M. Dobson Journal of Molecular Medicine
  8. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (2013)
    Samuel I. A. Cohen, Sara Linse et al. Proceedings of the National Academy of Sciences
  9. An Analytical Solution to the Kinetics of Breakable Filament Assembly (2009)
    Tuomas P. J. Knowles, Christopher A. Waudby et al. Science
  10. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis (1997)
    David R. Booth, Margaret Sunde et al. Nature
  11. Designing conditions for in vitro formation of amyloid protofilaments and fibrils (1999)
    Fabrizio Chiti, Paul Webster et al. Proceedings of the National Academy of Sciences
  12. Rationalization of the effects of mutations on peptide andprotein aggregation rates (2003)
    Fabrizio Chiti, Massimo Stefani et al. Nature
  13. Hydrodynamic Radii of Native and Denatured Proteins Measured by Pulse Field Gradient NMR Techniques (1999)
    Shaun B. Grimshaw, Véronique Receveur‐Brechot et al. Biochemistry
  14. The structural basis of protein folding and its links with human disease (2001)
    Christopher M. Dobson Philosophical Transactions of the Royal Society B Biological Sciences
  15. Protein Folding: A Perspective from Theory and Experiment (1998)
    Christopher M. Dobson, Andrej Săli et al. Angewandte Chemie International Edition
  16. The protofilament structure of insulin amyloid fibrils (2002)
    José L. Jiménez, Ewan J. Nettleton et al. Proceedings of the National Academy of Sciences
  17. Principles of protein folding, misfolding and aggregation (2004)
    Christopher M. Dobson Seminars in Cell and Developmental Biology
  18. Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (2012)
    Nunilo Cremades, Samuel I. A. Cohen et al. Cell
  19. Chemical space and biology (2004)
    Christopher M. Dobson Nature
  20. Amyloid formation by globular proteins under native conditions (2008)
    Fabrizio Chiti, Christopher M. Dobson Nature Chemical Biology
  21. Amyloid fibrils from muscle myoglobin (2001)
    Marcus Fändrich, Christopher M. Dobson et al. Nature
  22. Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils (2007)
    Tuomas P. J. Knowles, Anthony W. P. Fitzpatrick et al. Science
  23. The folding of hen lysozyme involves partially structured intermediates and multiple pathways (1992)
    Sheena E. Radford, Christopher M. Dobson et al. Nature
  24. Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations (2004)
    Matthew M. Dedmon, Kresten Lindorff‐Larsen et al. Journal of the American Chemical Society
  25. Simultaneous determination of protein structure and dynamics (2005)
    Kresten Lindorff‐Larsen, Robert B. Best et al. Nature Cell Biology
  26. Amyloid fibril formation by an SH3 domain (1998)
    J. Iñaki Guijarro, Margaret Sunde et al. Proceedings of the National Academy of Sciences
  27. Molecular mechanisms of protein aggregation from global fitting of kinetic models (2016)
    Georg Meisl, Julius B. Kirkegaard et al. Nature Protocols
  28. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation (2014)
    Alexander K. Buell, Céline Galvagnion et al. Proceedings of the National Academy of Sciences
  29. Characterization of the nanoscale properties of individual amyloid fibrils (2006)
    J. F. Smith, Tuomas P. J. Knowles et al. Proceedings of the National Academy of Sciences
  30. Long-Range Interactions Within a Nonnative Protein (2002)
    Judith Klein‐Seetharaman, Shaun B. Grimshaw et al. Science
  31. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers (2017)
    Giuliana Fusco, Serene W. Chen et al. Science
  32. Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation (2015)
    Céline Galvagnion, Alexander K. Buell et al. Nature Chemical Biology
  33. Prediction of “Aggregation-prone” and “Aggregation-susceptible” Regions in Proteins Associated with Neurodegenerative Diseases (2005)
    Amol Pawar, Jesús Zurdo et al. Journal of Molecular Biology
  34. Detection of Transient Protein Folding Populations by Mass Spectrometry (1993)
    Andrew D. Miranker, Carol V. Robinson et al. Science
  35. Half a century of amyloids: past, present and future (2020)
    Pu Chun Ke, Ruhong Zhou et al. Chemical Society Reviews
  36. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides (2014)
    Georg Meisl, Xiaoting Yang et al. Proceedings of the National Academy of Sciences
  37. Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms (2019)
    Suman De, David C. Wirthensohn et al. Nature Communications
  38. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation (2015)
    Serene W. Chen, Srdja Drakulić et al. Proceedings of the National Academy of Sciences
  39. The characterization of hardened alkali-activated blast-furnace slag pastes and the nature of the calcium silicate hydrate (C-S-H) phase (1994)
    I.G. Richardson, Adrian R. Brough et al. Cement and Concrete Research
  40. Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide (2020)
    Thomas C. T. Michaels, Anđela Šarić et al. Nature Chemistry
  41. The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells (2021)
    Roberta Cascella, Serene W. Chen et al. Nature Communications

Immediate Impact

24 by Nobel laureates 92 from Science/Nature 141 standout
Sub-graph 1 of 16

Citing Papers

Single-cell transcriptomic analysis of Alzheimer’s disease
2019 StandoutNature
Cryo-EM structures of tau filaments from Alzheimer’s disease
2017 StandoutNature
60 intermediate papers

Works of Christopher M. Dobson being referenced

Atomic structure and hierarchical assembly of a cross-β amyloid fibril
2013
Protein Misfolding, Functional Amyloid, and Human Disease
2006 Standout
and 49 more

Author Peers

Author Last Decade Papers Cites
Christopher M. Dobson 64994 35411 20067 834 93.7k
Vladimir N. Uversky 50938 10686 13737 1.1k 71.7k
David Eisenberg 45622 12033 9841 404 60.7k
Michele Vendruscolo 28961 13607 7947 562 40.5k
Guido Kroemer 125595 18148 4262 1.3k 229.0k
Matthias Mann 148683 11975 5738 837 211.4k
Tuomas P. J. Knowles 18790 14500 3917 461 31.8k
Klaus Schulten 62362 3756 22827 510 115.8k
Ad Bax 60959 3619 18408 459 88.3k
Herman J. C. Berendsen 59262 3379 23566 161 110.3k
Ruth Nussinov 42884 5885 10341 785 52.9k

All Works

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