Centre for Misfolding Diseases

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  • Currently displaying 301 - 320 of 2350 publications
Author(s)
Publication title
Journal Name
Publication year
Protein condensation diseases: therapeutic opportunities.
M Vendruscolo, M Fuxreiter
Nat Commun
(2022)
13
(doi: 10.1038/s41467-022-32940-7)
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
(doi: 10.1039/d2sc00066k)
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
(doi: 10.1038/s41467-022-33252-6)
Influence of denaturants on amyloid β42 aggregation kinetics.
T Weiffert, G Meisl, S Curk, R Cukalevski, A Šarić, TPJ Knowles, S Linse
Frontiers in Neuroscience
(2022)
16
(doi: 10.3389/fnins.2022.943355)
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
(doi: 10.1038/s41467-022-33252-6)
Effects of N-terminal acetylation on the aggregation of disease-related α-synuclein variants
R Bell, M Castellana-Cruz, A Nene, RJ Thrush, CK Xu, JR Kumita, M Vendruscolo
Journal of molecular biology
(2022)
435
(doi: 10.1016/j.jmb.2022.167825)
A chip-based supersonic microfluidic nebulizer for efficient sample introduction into inductively coupled plasma – Mass spectrometry
E Mavrakis, Z Toprakcioglu, N Lydakis-Simantiris, TPJ Knowles, SA Pergantis
Analytica chimica acta
(2022)
1229
(doi: 10.1016/j.aca.2022.340342)
Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species
G Fani, CE La Torre, R Cascella, C Cecchi, M Vendruscolo, F Chiti
Cellular and Molecular Life Sciences
(2022)
79
(doi: 10.1007/s00018-022-04513-w)
Analytical Solution to the Flory–Huggins Model
D Qian, TCT Michaels, TPJ Knowles
Journal of Physical Chemistry Letters
(2022)
13
(doi: 10.1021/acs.jpclett.2c01986)
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
Science advances
(2022)
8
(doi: 10.1126/sciadv.abn6831)
A conformational switch controlling the toxicity of the prion protein.
K Frontzek, M Bardelli, A Senatore, A Henzi, RR Reimann, S Bedir, M Marino, R Hussain, S Jurt, G Meisl, M Pedotti, F Mazzola, G Siligardi, O Zerbe, M Losa, T Knowles, A Lakkaraju, C Zhu, P Schwarz, S Hornemann, MG Holt, L Simonelli, L Varani, A Aguzzi
Nature Structural & Molecular Biology
(2022)
29
(doi: 10.1038/s41594-022-00814-7)
N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates.
R Bell, RJ Thrush, M Castellana-Cruz, M Oeller, R Staats, A Nene, P Flagmeier, CK Xu, S Satapathy, C Galvagnion, MR Wilson, CM Dobson, JR Kumita, M Vendruscolo
Biochemistry
(2022)
61
(doi: 10.1021/acs.biochem.2c00104)
Chemical and Enzymatic Methods for Post-Translational Protein-Protein Conjugation
RJ Taylor, MB Geeson, T Journeaux, GJL Bernardes
Journal of the American Chemical Society
(2022)
144
(doi: 10.1021/jacs.2c00129)
ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.
C Olivieri, GC Li, Y Wang, M V S, C Walker, J Kim, C Camilloni, A De Simone, M Vendruscolo, DA Bernlohr, SS Taylor, G Veglia
Sci Adv
(2022)
8
(doi: 10.1126/sciadv.abo0696)
Adsorption free energy predicts amyloid protein nucleation rates.
Z Toprakcioglu, A Kamada, TCT Michaels, M Xie, J Krausser, J Wei, A Saric, M Vendruscolo, TPJ Knowles
Proceedings of the National Academy of Sciences
(2022)
119
(doi: 10.1073/pnas.2109718119)
Are casein micelles extracellular condensates formed by liquid‐liquid phase separation?
A Horvath, M Fuxreiter, M Vendruscolo, C Holt, JA Carver
FEBS Lett
(2022)
596
(doi: 10.1002/1873-3468.14449)
DNA–Liposome Hybrid Carriers for Triggered Cargo Release
KN Baumann, T Schröder, PS Ciryam, D Morzy, P Tinnefeld, TPJ Knowles, S Hernández-Ainsa
ACS applied bio materials
(2022)
5
(doi: 10.1021/acsabm.2c002253713)
Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes
H Mikolajek, M Weckener, ZF Brotzakis, J Huo, EV Dalietou, A Le Bas, P Sormanni, PJ Harrison, PN Ward, S Truong, L Moynie, DK Clare, M Dumoux, J Dormon, C Norman, N Hussain, V Vogirala, RJ Owens, M Vendruscolo, JH Naismith
Proceedings of the National Academy of Sciences
(2022)
119
(doi: 10.1073/pnas.2205412119)
π‑Clamp-Mediated Homo- and Heterodimerization of Single-Domain Antibodies via Site-Specific Homobifunctional Conjugation
RJ Taylor, M Aguilar Rangel, MB Geeson, P Sormanni, M Vendruscolo, GJL Bernardes
J Am Chem Soc
(2022)
144
(doi: 10.1021/jacs.2c04747)
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
Nature Chemistry
(2022)
14
(doi: 10.1038/s41557-022-00976-3)
Yusuf Hamied Department of Chemistry
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