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Yusuf Hamied Department of Chemistry

 
Author Correction: Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity (Nature Neuroscience, (2022), 25, 9, (1134-1148), 10.1038/s41593-022-01140-3)
ML Choi, A Chappard, BP Singh, C Maclachlan, M Rodrigues, EI Fedotova, AV Berezhnov, S De, CJ Peddie, D Athauda, GS Virdi, W Zhang, JR Evans, AI Wernick, ZS Zanjani, PR Angelova, N Esteras, AY Vinokurov, K Morris, K Jeacock, L Tosatto, D Little, P Gissen, DJ Clarke, T Kunath, L Collinson, D Klenerman, AY Abramov, MH Horrocks, S Gandhi
– Nat Neurosci
(2022)
25,
1582
Characterization of full-length p53 aggregates and their kinetics of formation
L Julian, JC Sang, Y Wu, G Meisl, JH Brelstaff, A Miller, MR Cheetham, M Vendruscolo, TPJ Knowles, FS Ruggeri, C Bryant, S Ros, KM Brindle, D Klenerman
– Biophysical journal
(2022)
121,
4280
An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients.
K Kulenkampff, D Emin, R Staats, YP Zhang, L Sakhnini, A Kouli, O Rimon, E Lobanova, CH Williams-Gray, FA Aprile, P Sormanni, D Klenerman, M Vendruscolo
– Chemical science
(2022)
13,
13815
Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease
D Emin, YP Zhang, E Lobanova, A Miller, X Li, Z Xia, H Dakin, DI Sideris, JYL Lam, RT Ranasinghe, A Kouli, Y Zhao, S De, TPJ Knowles, M Vendruscolo, FS Ruggeri, FI Aigbirhio, CH Williams-Gray, D Klenerman
– Nature Communications
(2022)
13,
5512
Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease
D Emin, YP Zhang, E Lobanova, A Miller, X Li, Z Xia, H Dakin, DI Sideris, JYL Lam, RT Ranasinghe, A Kouli, Y Zhao, S De, TPJ Knowles, M Vendruscolo, FS Ruggeri, FI Aigbirhio, CH Williams-Gray, D Klenerman
– Nature Communications
(2022)
13,
5512
Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity.
ML Choi, A Chappard, BP Singh, C Maclachlan, M Rodrigues, EI Fedotova, AV Berezhnov, S De, CJ Peddie, D Athauda, GS Virdi, W Zhang, JR Evans, AI Wernick, ZS Zanjani, PR Angelova, N Esteras, AY Vinokurov, K Morris, K Jeacock, L Tosatto, D Little, P Gissen, DJ Clarke, T Kunath, L Collinson, D Klenerman, AY Abramov, MH Horrocks, S Gandhi
– Nature Neuroscience
(2022)
25,
1134
Constructing a cost-efficient, high-throughput and high-quality single-molecule localization microscope for super-resolution imaging.
JSH Danial, JYL Lam, Y Wu, M Woolley, E Dimou, MR Cheetham, D Emin, D Klenerman
– Nat Protoc
(2022)
17,
2570
resPAINT: Accelerating Volumetric Super-Resolution Localisation Microscopy by Active Control of Probe Emission.
EW Sanders, AR Carr, E Bruggeman, M Körbel, SI Benaissa, RF Donat, AM Santos, J McColl, K O'Holleran, D Klenerman, SJ Davis, SF Lee, A Ponjavic
– Angewandte Chemie (Weinheim an der Bergstrasse, Germany)
(2022)
134,
e202206919
Uncovering the universality of self-replication in protein aggregation and its link to disease
G Meisl, CK Xu, JD Taylor, TCT Michaels, A Levin, D Otzen, D Klenerman, S Matthews, S Linse, M Andreasen, TPJ Knowles
– Sci Adv
(2022)
8,
eabn6831
Structure-specific amyloid precipitation in biofluids
M Rodrigues, P Bhattacharjee, A Brinkmalm, DT Do, CM Pearson, S De, A Ponjavic, JA Varela, K Kulenkampff, I Baudrexel, D Emin, FS Ruggeri, JE Lee, AR Carr, TPJ Knowles, H Zetterberg, TN Snaddon, S Gandhi, SF Lee, D Klenerman
– Nat Chem
(2022)
14,
1045
Mechanistic Models of Protein Aggregation Across Length-Scales and Time-Scales: From the Test Tube to Neurodegenerative Disease
G Meisl, TPJ Knowles, D Klenerman
– Frontiers in neuroscience
(2022)
16,
909861
Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses
JX Meng, Y Zhang, D Saman, AM Haider, S De, JC Sang, K Brown, K Jiang, J Humphrey, L Julian, E Hidari, SF Lee, G Balmus, RA Floto, CE Bryant, JLP Benesch, Y Ye, D Klenerman
– Nat Commun
(2022)
13,
2692
Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses
JX Meng, Y Zhang, D Saman, AM Haider, S De, JC Sang, K Brown, K Jiang, J Humphrey, L Julian, E Hidari, SF Lee, G Balmus, RA Floto, C Bryant, JLP Benesch, Y Ye, D Klenerman
– Nature Communications
(2022)
13,
An economic, square-shaped flat-field illumination module for TIRF-based super-resolution microscopy
JYL Lam, Y Wu, E Dimou, Z Zhang, MR Cheetham, M Körbel, Z Xia, D Klenerman, JSH Danial
– Biophysical reports
(2022)
2,
None
Rate‐limiting processes of tau aggregate accumulation in Alzheimer's disease
G Meisl, Y Zuo, K Allinson, T Rittman, SL DeVos, JS Sanchez, CK Xu, KE Duff, KA Johnson, JB Rowe, BT Hyman, T Knowles, D Klenerman
– Alzheimer's & Dementia
(2022)
17,
Simpler and faster quartz crystal microbalance for macromolecule detection using fixed frequency drive
A Guha, N Sandström, VP Ostanin, D Klenerman, SK Ghosh
– Sensors and Actuators B Chemical
(2022)
358,
131442
A Platform for Site-Specific DNA-Antibody Bioconjugation by Using Benzoylacrylic-Labelled Oligonucleotides
J Konč, L Brown, DR Whiten, Y Zuo, P Ravn, D Klenerman, GJL Bernardes
– Angewandte Chemie International Edition
(2021)
60,
25905
A Platform for Site‐Specific DNA‐Antibody Bioconjugation by Using Benzoylacrylic‐Labelled Oligonucleotides
J Konč, L Brown, DR Whiten, Y Zuo, P Ravn, D Klenerman, GJL Bernardes
– Angewandte Chemie
(2021)
133,
26109
In vivo rate-determining steps of tau seed accumulation in Alzheimer’s disease
G Meisl, E Hidari, K Allinson, T Rittman, SL DeVos, JS Sanchez, CK Xu, KE Duff, KA Johnson, JB Rowe, BT Hyman, TPJ Knowles, D Klenerman
– Science advances
(2021)
7,
eabh1448
Imaging protein aggregates in the serum and cerebrospinal fluid in Parkinson's disease (Aug, awab306, 2021)
– Brain
(2021)
144,
e90