Christopher Dobson, 1949–2019: Mentor, Friend, Scientist Extraordinaire

Literature Cited

1. 1. 

   Pritchard AM, Dobson CM. 1969. Mössbauer effect and iron corrosion kinetics. Nature 224:1295
   [Google Scholar]
2. 2. 

   Campbell ID, Dobson CM, Williams JP 1975. Studies of exchangeable hydrogens in lysozyme by means of Fourier transform proton magnetic resonance. Proc. R. Soc. B 189:485–502
   [Google Scholar]
3. 3. 

   Cave A, Dobson CM, Parello J, Williams RJ 1976. Conformation mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residues. FEBS Lett 65:190–94
   [Google Scholar]
4. 4. 

   Oswald RE, Bogusky MJ, Bamberger M, Smith RAG, Dobson CM 1989. Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR. Nature 337:579–82
   [Google Scholar]
5. 5. 

   Plaxco KW, Guijarro JI, Morton CJ, Pitkeathly M, Campbell ID, Dobson CM 1998. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry 37:2529–37
   [Google Scholar]
6. 6. 

   Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM 1998. Amyloid fibril formation by an SH3 domain. PNAS 95:4224–28
   [Google Scholar]
7. 7. 

   Wagman ME, Dobson CM, Karplus M 1980. Proton NMR studies of the association and folding of glucagon in solution. FEBS Lett 119:265–70
   [Google Scholar]
8. 8. 

   Poon S, Birkett NR, Fowler SB, Luisi BF, Dobson CM, Zurdo J 2009. Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1). Protein Pept. Lett. 16:1548–56
   [Google Scholar]
9. 9. 

   Levy RM, Dobson CM, Karplus M 1982. Dipolar NMR relaxation of nonprotonated aromatic carbons in proteins. Biophys. J. 39:107–13
   [Google Scholar]
10. 10. 

    Clayden NJ, Dobson CM, Hayes CJ, Rodger SA 1984. Hydration of tricalcium silicate followed by solid-state ²⁹Si n.m.r. spectroscopy. J. Chem. Soc. 21:1396–97
    [Google Scholar]
11. 11. 

    Redfield C, Dobson CM. 1988. Sequential ¹H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry 27:122–36
    [Google Scholar]
12. 12. 

    Redfield C, Dobson CM. 1990. ¹H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. Biochemistry 29:7201–14
    [Google Scholar]
13. 13. 

    Miranker A, Radford SE, Karplus M, Dobson CM 1991. Demonstration by NMR of folding domains in lysozyme. Nature 349:633–36
    [Google Scholar]
14. 14. 

    Miranker A, Robinson CV, Radford SE, Aplin RT, Dobson CM 1993. Detection of transient protein folding populations by mass spectrometry. Science 262:896–900
    [Google Scholar]
15. 15. 

    Kragelund BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM 1995. Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. Biochemistry 34:7217–24
    [Google Scholar]
16. 16. 

    Robinson CV, Chung EW, Kragelund BB, Knudsen J, Aplin RT et al. 1996. Probing the nature of noncovalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly. J. Am. Chem. Soc. 118:8646–53
    [Google Scholar]
17. 17. 

    Hernández H, Robinson CV. 2007. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat. Protoc. 2:715–26
    [Google Scholar]
18. 18. 

    Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM 1995. Following protein folding in real time using NMR spectroscopy. Nat. Struct. Biol. 2:865–70
    [Google Scholar]
19. 19. 

    Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM 1993. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: a two-dimensional NMR study. Biochemistry 32:1707–18
    [Google Scholar]
20. 20. 

    Robinson CV, Groß M, Eyles SJ, Ewbank JJ, Mayhew M et al. 1994. Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature 372:646–51
    [Google Scholar]
21. 21. 

    Benjamin DR, Robinson CV, Hendrick JP, Hartl FU, Dobson CM 1998. Mass spectrometry of ribosomes and ribosomal subunits. PNAS 95:7391–95
    [Google Scholar]
22. 22. 

    Rostom AA, Fucini P, Benjamin DR, Juenemann R, Nierhaus KH et al. 2000. Detection and selective dissociation of intact ribosomes in a mass spectrometer. PNAS 97:5185–90
    [Google Scholar]
23. 23. 

    Cabrita LD, Cassaignau AME, Launay HMM, Waudby CA, Wlodarski T et al. 2016. A structural ensemble of a ribosome–nascent chain complex during cotranslational protein folding. Nat. Struct. Mol. Biol. 23:278–85
    [Google Scholar]
24. 24. 

    Dobson CM, Šali A, Karplus M 1998. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. Engl. 37:868–93
    [Google Scholar]
25. 25. 

    Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL et al. 1997. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385:787–93
    [Google Scholar]
26. 26. 

    Canet D, Last AM, Tito P, Sunde M, Spencer A et al. 2002. Local cooperative in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9:308–15
    [Google Scholar]
27. 27. 

    Jiménez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM et al. 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J 18:815–21
    [Google Scholar]
28. 28. 

    Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV 2000. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci 9:1960–67
    [Google Scholar]
29. 29. 

    Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, Robinson CV 2000. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79:1053–65
    [Google Scholar]
30. 30. 

    Jiménez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR 2002. The protofilament structure of insulin amyloid fibrils. PNAS 99:9196–201
    [Google Scholar]
31. 31. 

    Fändrich M, Fletcher MA, Dobson CM 2001. Amyloid fibrils from muscle myoglobin. Nature 410:165–66
    [Google Scholar]
32. 32. 

    Dobson CM. 2002. Protein-misfolding diseases: getting out of shape. Nature 418:729–30
    [Google Scholar]
33. 33. 

    Chiti F, Dobson CM. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333–66
    [Google Scholar]
34. 34. 

    Chiti F, Dobson CM. 2017. Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade. Annu. Rev. Biochem. 86:27–68
    [Google Scholar]
35. 35. 

    Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M et al. 2007. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318:1900–3
    [Google Scholar]
36. 36. 

    Herling TW, Garcia GA, Michaels TCT, Grentz W, Dean J et al. 2015. Force generation by the growth of amyloid aggregates. PNAS 112:9524–29
    [Google Scholar]
37. 37. 

    Knowles TPJ, Waudby CA, Devlin GL, Cohen SIA, Aguzzi A et al. 2009. An analytical solution to the kinetics of breakable filament assembly. Science 326:1533–37
    [Google Scholar]
38. 38. 

    Knowles TPJ, White DA, Abate AR, Agresti JJ, Cohen SIA et al. 2011. Observation of spatial propagation of amyloid assembly from single nuclei. PNAS 108:14746–51
    [Google Scholar]
39. 39. 

    Cohen SIA, Linse S, Luheshi LM, Hellstrand E, White DA et al. 2013. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. PNAS 110:9758–63
    [Google Scholar]
40. 40. 

    Frankel R, Törnquist M, Meisl G, Hansson O, Andreasson U et al. 2019. Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid. Commun. Biol. 2:365
    [Google Scholar]
41. 41. 

    Dobson CM. 2003. Protein folding and misfolding. Nature 426:884–90
    [Google Scholar]
42. 42. 

    Fusco G, Chen SW, Williamson PTF, Cascella R, Perni M et al. 2017. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science 358:1440–43
    [Google Scholar]
43. 43. 

    Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M 2007. Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Biochem. Sci. 32:204–6
    [Google Scholar]
44. 44. 

    Vecchi G, Sormanni P, Mannini B, Vandelli A, Tartaglia GG et al. 2020. Proteome-wide observation of the phenomenon of life on the edge of solubility. PNAS 117:1015–20
    [Google Scholar]
45. 45. 

    Habchi J, Arosio P, Perni M, Costa AR, Yagi-Utsumi M et al. 2016. An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease. Sci. Adv. 2:e1501244
    [Google Scholar]
46. 46. 

    Habchi J, Chia S, Limbocker R, Mannini B, Ahn M et al. 2017. Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease. PNAS 114:E200–8
    [Google Scholar]
47. 47. 

    Chia S, Habchi J, Michaels TCT, Cohen SIA, Linse S et al. 2018. SAR by kinetics for drug discovery in protein misfolding diseases. PNAS 115:10245–50
    [Google Scholar]
48. 48. 

    Habchi J, Chia S, Galvagnion C, Michaels TCT, Bellaiche MMJ et al. 2018. Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes. Nat. Chem. 10:673–83
    [Google Scholar]
49. 49. 

    Limbocker R, Chia S, Ruggeri FS, Perni M, Cascella R et al. 2019. Trodusquemine enhances Aβ₄₂ aggregation but suppresses its toxicity by displacing oligomers from cell membranes. Nat. Commun. 10:225
    [Google Scholar]
50. 50. 

    Munke A, Persson J, Weiffert T, De Genst E, Meisl G et al. 2017. Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication. PNAS 114:6444–49
    [Google Scholar]
51. 51. 

    Perni M, Galvagnion C, Maltsev A, Meisl G, Müller MBD et al. 2017. A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. PNAS 114:E1009–17
    [Google Scholar]
52. 52. 

    Lindstedt PR, Aprile FA, Matos MJ, Perni M, Bertoldo JB et al. 2019. Enhancement of the anti-aggregation activity of a molecular chaperone using a rationally designed post-translational modification. ACS Cent. Sci. 5:1417–24
    [Google Scholar]
53. 53. 

    van Ham TJ, Thijssen KL, Breitling R, Hofstra RMW, Plasterk RHA, Nollen EAA 2008. C. elegans model identifies genetic modifiers of α-synuclein inclusion formation during aging. PLOS Genet 4:e1000027
    [Google Scholar]