Reflections on professor Sir Christopher M. Dobson (1949-2019)

[en] I have been invited to summarize my career with an emphasis on the time I spent in the laboratory of Prof Christopher M. Dobson, who sadly passed away on September 8th 2019, and to describe his role as a mentor. I accepted this slightly unusual request as it constitutes a unique way for me to express my deep gratitude and admiration for Chris.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Dumoulin, Mireille ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Département des sciences biomédicales et précliniques

Language :

English

Title :

Reflections on professor Sir Christopher M. Dobson (1949-2019)

Publication date :

12 February 2020

Journal title :

Biophysical Reviews

ISSN :

1867-2450

eISSN :

1867-2469

Publisher :

Springer, Germany

Volume :

Issue :

Pages :

13-18

Peer reviewed :

Peer reviewed

Available on ORBi :

since 15 May 2020

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62 (10 by ULiège)

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Bibliography

Ahn M, Hagan CL, Bernardo-Gancedo A, De Genst E, Newby FN, Christodoulou J, Dhulesia A, Dumoulin M, Robinson CV, Dobson CM, Kumita JR (2016) The significance of the location of mutations for the native-state dynamics of human lysozyme. Biophys J 111(11):2358–2367. 10.1016/j.bpj.2016.10.028
Buell AK, Dhulesia A, Mossuto MF, Cremades N, Kumita JR, Dumoulin M, Welland ME, Knowles TPJ, Salvatella X, Dobson CM (2011) Population of nonnative states of lysozyme variants drives amyloid fibril formation. J Am Chem Soc 133(20):7737–7743. 10.1021/ja109620d
Canet, D., Last, A.M., Tito, P., Sunde, M., Spencer, A., Archer, D.B., Redfield, C., Robinson, C.V., Dobson, C.M. 2002. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nature and Structural Biology, 9(4):308-15.
Cawez F, Duray E, Hu Y, Vandenameele J, Romão E, Vincke C, Dumoulin M, Galleni M, Muyldermans S, Vandevenne M (2018) Combinatorial design of a nanobody that specifically targets structured RNAs. J Mol Biol 430(11):1652–1670. 10.1016/j.jmb.2018.03.032
De Genst E, Chan PH, Pardon E, Hsu STD, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M (2013) A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation. J Phys Chem B 117(42):13245–13258
Dobson CM (2017) The amyloid phenomenon and its links with human disease. Cold Spring Harb Perspect Biol 9(6):a023648. 10.1101/cshperspect.a023648
Dobson CM, Knowles TPJ, Vendruscolo M (2019) The Amyloid Phenomenon and Its Significance in Biology and Medicine, Cold Spring Harb Perspect Biol a033878. 10.1101/cshperspect.a033878
Dumoulin M, Hayashi R (1998) High pressure, a unique tool for food texturization. Food Sci Technol Int Tokyo 4(2):99–113
Dumoulin M, Ozawa S, Hayashi R (1998) Textural properties of pressure-induced gels of food proteins obtained under different temperatures including subzero. J Food Sci 63(1):92–95
Dumoulin M, Conrath K, Van Meirhaeghe A, Meersman F, Heremans K, Frenken LG, Muyldermans S, Wyns L, Matagne A (2002) Single-domain antibody fragments with high conformational stability. Protein Sci 11(3):500–515
Dumoulin M, Last AM, Desmyter A, Decanniere K, Canet D, Larsson G, Spencer A, Archer DB, Sasse J, Muyldermans S, Wyns L, Redfield C, Matagne A, Robinson CV, Dobson CM (2003) A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature 424(6950):783–788
Dumoulin M, Kumita JR, Dobson CM (2007) Normal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants. Acc Chem Res 39(9):603–610
Frare E, Mossuto MF, Polverino de Laureto P, Dumoulin M, Dobson CM, Fontana A (2006) Identification of the core structure of lysozyme amyloid fibrils by proteolysis. J Mol Biol 361(3):551–561
Gustot A, Raussens V, Dehousse M, Dumoulin M, Bryant CE, Ruysschaert JM, Lonez C (2013) Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure. Cell Mol Life Science 70(16):2999–3012. 10.1007/s00018-012-1245-5
Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N, Hamers R (1993) Naturally occurring antibodies devoid of light chains. Nature 363(6428):446–448
Huynen C, Willet N, Buell AK, Duwez AS, Jerôme C, Dumoulin M (2015) Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils. Biochim Biophys Acta 1854(3):239–248. 10.1016/j.bbapap.2014.12.002
Kumita JR, Helmfors L, Williams J, Luheshi LM, Menzer L, Dumoulin M, Lomas DA, Crowther DC, Dobson CM, Brorsson AC (2012) Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster. FASEB J 26(1):192–202. 10.1096/fj.11-185983
Mossuto MF, Bolognesi B, Guixer B, Dhulesia A, Agostini F, Kumita JR, Tartaglia GG, Dumoulin M, Dobson CM, Salvatella X (2011) Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein. Angew Chem Int Ed 50(31):7048–7051. 10.1002/anie.201100986
Pansieri J, Plissonneau M, Stransky-Heilkron N, Dumoulin M, Heinrich-Balard L, Rivory P, Morfin J-F, Toth E, Saraiva MJ, Allémann E, Tillement O, Forge V, Lux F, Marquette C (2017) Multimodal imaging Gd-nanoparticles functionalized with Pittsburgh compound B or a nanobody for amyloid plaques targeting. Nanomedicine (Lond) 12(14):1675–1687. 10.2217/nnm-2017-0079
Scarafone N, Pain C, Fratamico A, Gaspard G, Yilmaz N, Filée P, Galleni M, Matagne A, Dumoulin M (2012) Amyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein. PLoS One 7(3):e31253. 10.1371/journal.pone.0031253
Vandevenne, M., Filee, P., Scarafone, N., Cloes, B., Gaspard, G., Yilmaz, N., Dumoulin, M., François, J.M., Frère, J.M., Galleni, M. (2007) The BlaP β-lactamase as a model protein scaffold to study the insertion of protein fragments. Protein Science 16 (10):2260-2271