2025
Urbanek A, Garland EF, Prescott EE, King MC, Olerinyova A, Wareing HE, Georgieva N, Bradshaw EL, Tzokov SB, Knight A, Tartakovskii AI, Malm T, Highley JR, De S. Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level. Adv. Sci. 12, 24102 (2025). https://doi.org/10.1002/advs.202410229
2024
Xia Z, Prescott EE, Urbanek A et al. Co-aggregation with Apolipoprotein E modulates the function of Amyloid-β in Alzheimer’s disease. Nat Commun 15, 4695 (2024). https://doi.org/10.1038/s41467-024-49028-z
Bell S.M, Wareing H, Capriglia F et al. Increasing hexokinase 1 expression improves mitochondrial and glycolytic functional deficits seen in sporadic Alzheimer’s disease astrocytes. Mol Psychiatry 30, 1369–1382 (2025). https://doi.org/10.1038/s41380-024-02746-8
2022
Emin D, Zhang YP, Lobanova E, Miller A, Li X, Xia Z, Dakin H, Sideris DI, Lam JYL, Ranasinghe RT, Kouli A, Zhao Y, De S, Knowles TPJ, Vendruscolo M, Ruggeri FS, Aigbirhio F, and Williams-Gray C, Klenerman D. Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease. Nat Commun 13, 5512 (2022). https://doi.org/10.1038/s41467-022-33252-6
Choi ML, Chappard A, Singh BP, Maclachlan C, Rodrigues M, Fedotova E, Berezhnov A, De S, Peddie C, Athauda D, Virdi GS, Zhang W, Evans JR, Wernick AI, Zanjani ZS, Angelova P, Esteras N, Vinokurov AY, Morris K, Jeacock K, Tosatto L, Little D, Gissen P, Clarke D, Kunath T, Klenerman D, Abramov AY, Horrocks MH, Gandhi S. Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity. Nat Neurosci 25, 1134–1148 (2022). https://doi.org/10.1038/s41593-022-01140-3
Rodrigues M, Bhattacharjee P, Brinkmalm A, Do D, Pearson C, De S, Ponjavic A, Klurenkampf K, Knowles TPJ., Zetterberg H, Snaddon T, Gandhi S, Lee SF, Klenerman D. Structure-specific amyloid precipitation in biofluids. Nat Chem. 14, 1045–1053 (2022). https://doi.org/10.1038/s41557-022-00976-3
Meng J, Zhang Y, Saman D, De S, Sang JC, Brown K, Jiang K, Humphrey J, Julian L, Hidari E, Lee SF, Balmus G, Floto RA, Bryant CE, Benesch JLP, Ye Y, Klenerman D. Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses. Nat Commun. 13, 2692 (2022). https://doi.org/10.1038/s41467-022-30461-x
Jannasch A., Szilagyi SA, Burmeister M, Davis QT, Hermsdorf GL, De S, Schäffer E. Fast 3D imaging of giant unilamellar vesicles using reflected light-sheet microscopy with single molecule sensitivity. J. Microsc. 2022; 285: 40–51. https://doi.org/10.1111/jmi.13070
2021
Sideris DI, Danial JSH, Emin D, Ruggeri FS, Xia Z Zhang YP, Lobanova E, Dakin H, De S, Miller A, Sang JC, Knowles TPJ, Vendruscolo M, Fraser G, Crowther DC, Klenerman D. Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer’s disease. Brain Communications. 3, 3 (2021) fcab147. https://doi.org/10.1093/braincomms/fcab147
Vilalta A, Zhou Y, Sevalle J, Griffin JK, Satoh K, Allendorf DH, De S, Puigdellívol M, Bruzas A, Burguillos MA, Dodd RB, Chen FY, Flagmeier P, Needham L-M, Enomoto M, Qamar S, Henderson J, Walter J, Fraser PE, Klenerman D, Lee SF, St George-Hyslop P, Brown GC. Wild-type sTREM2 blocks Aβ aggregation and neurotoxicity, but the Alzheimer's R47H mutant increases Aβ aggregation. J Biological Chem. 296, 100631 (2021). https://doi.org/10.1016/j.jbc.2021.100631
2020
Flagmeier P, De S, Michaels TCT, Emanuelsson C, Vendruscolo M, Linse S, Klenerman D, Knowles TPJ, Dobson CM. Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation. Nat Struct Mol Biol 27, 886–891 (2020). https://doi.org/10.1038/s41594-020-0471-z
Angelova, PR, Choi, ML, Berezhnov, AV et al. Alpha synuclein aggregation drives ferroptosis: an interplay of iron, calcium and lipid peroxidation. Cell Death Differ 27, 2781–2796 (2020). https://doi.org/10.1038/s41418-020-0542-z
Whiten DR, Brownjohn PW, Moore S, De S, Strano A, Zuo Y, Haneklaus M, Klenerman D, Livesey Fj. Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer’s disease neurons. Brain Communications. 2, 2 (2020) fcaa146. https://doi.org/10.1093/braincomms/fcaa146
Sanderson JB, De S, Jiang H, Rover M, Jin M, Lagomarsino VN, Young-Pearse TL, Pochapsky T, Hyman B, Klenerman D, Selkoe DJ, Bartels T. Analysis of α-synuclein species enriched from cerebral cortex of humans with sporadic dementia with Lewy bodies. Brain Communications. 2, 1 (2020) fcaa010. https://doi.org/10.1093/braincomms/fcaa010
2019
De S and Klenerman D. Imaging individual protein aggregates to follow aggregation and determine the role of aggregates in neurodegenerative disease. Biochimica et Biophysica Acta Proteins and Proteomics. 1867, 870 (2019). https://doi.org/10.1016/j.bbapap.2018.12.010
De S, Whiten DR, Ruggeri FS, Hughes C, Rodrigues M, Sideris DI, Taylor DG, Muyldermans S, Knowles TPJ, Vendruscolo M, Bryant CE, Blennow K, Skoog I, Kern S, Zetterberg H, Klenerman D. Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression. acta neuropathol commun. 7, 120 (2019). https://doi.org/10.1186/s40478-019-0777-4
De S, Wirthensohn DC, Flagmeier P, Hughes C, Aprile FA, Whiten DR, Emin D, Xia Z, Varela JA, Sormanni P, Kundel F, Knowles TPJ, Dobson CM, C. Bryant, M. Vendruscolo M, Klenerman D. Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms. Nat Commun. 10, 1541 (2019). https://doi.org/10.1038/s41467-019-09477-3
Weiffert T, Meisl G, Flagmeier P, De S, Dunning CJR, Frohm B, Zetterberg H, Blennow K, Portelius E, Klenerman D, Dobson CM, Knowles TPJ, Linse S. Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5–42. ACS Chemical Neuroscience 10, 5 (2019) 2374-2384. https://doi.org/10.1021/acschemneuro.8b00676
Sang JC, Lee J-E, Dear AJ, De S, Meisl G, Thackray AM, Bujdoso R, Knowles TPJ, Klenerman D. Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species. Chem. Sci. 10, 4588-4597 (2019). https://doi.org/10.1039/C8SC05627G
2018
Whiten DR, Cox D, Horrocks MH, Taylor CG, De S, Flagmeier P, Tosatto L, Kumita JR, Ecroyd H, Dobson CM, Klenerman D, Wilson MR. Single-Molecule Characterisation of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers. Cell Reports. 23, 3492 (2018). https://doi.org/10.1016/j.celrep.2018.05.074
Varela JA, Rodrigues M, De S, Flagmeier P, Gandhi S, Dobson CM, Klenerman D, Lee SF. Optical structural analysis of individual α-synuclein oligomers. Angewandte Chemie - Int. Ed. 57, 4886 (2018). https://doi.org/10.1002/anie.201710779
Kundel F, De S, Flagmeier P, Horrocks M, Kjaergaard M, Shammas S, Jackson S, Dobson CM, D. Klenerman D. Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity. ACS Chemical Biology. 13, 636 (2018). https://doi.org/10.1021/acschembio.7b01039
2017
Drews A, De S, Flagmeier P, Wirthensohn DC, Chen WH, Whiten DR, Rodrigues M, Vincke C, Muyldermans S, Paterson RW, Slattery CF, Fox NC, Schott JM, Zetterberg H, Dobson CM, Klenerman D. Inhibiting the Ca2+ influx induced by human CSF. Cell Reports. 21, 3310 (2017). https://doi.org/10.1016/j.celrep.2017.11.057
Flagmeier F, De S, Wirthensohn DC, Lee SF, Vincke C, Muyldermans S, Knowles TPJ, Gandhi S, Dobson CM, Klenerman D. Ultrasensitive measurement of Ca2+ influx into lipid vesicles induced by protein aggregates. Angewandte Chemie - Int. Ed. 26, 7750 (2017). https://doi.org/10.1002/anie.201700966