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Centre for Misfolding Diseases

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  • Currently displaying 21 - 40 of 2874 publications
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,
943355
(DOI: 10.3389/fnins.2022.943355)
Effects of N-terminal Acetylation on the Aggregation of Disease-related α-synuclein Variants: N-terminal acetylation of α-synuclein variants
R Bell, M Castellana-Cruz, A Nene, RJ Thrush, CK Xu, JR Kumita, M Vendruscolo
– Journal of molecular biology
(2022)
167825
(DOI: 10.1016/j.jmb.2022.167825)
Cytosolic sequestration of spatacsin by Protein Kinase A and 14-3-3 proteins
S Cogo, JE Tomkins, N Vavouraki, V Giusti, F Forcellato, C Franchin, I Tessari, G Arrigoni, L Cendron, C Manzoni, L Civiero, PA Lewis, E Greggio
– Neurobiology of Disease
(2022)
174,
105858
(DOI: 10.1016/j.nbd.2022.105858)
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,
340342
(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,
500
(DOI: 10.1007/s00018-022-04513-w)
Analytical Solution to the Flory-Huggins Model.
D Qian, TCT Michaels, TPJ Knowles
– J Phys Chem Lett
(2022)
13,
7853
(DOI: 10.1021/acs.jpclett.2c01986)
Development of potent inhibitors by fragment-linking strategies
EV Bedwell, WJ McCarthy, AG Coyne, C Abell
– Chemical Biology & Drug Design
(2022)
100,
469
(DOI: 10.1111/cbdd.14120)
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
(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 and Molecular Biology
(2022)
29,
831
(DOI: 10.1038/s41594-022-00814-7)
The 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,
1743
(DOI: 10.1021/acs.biochem.2c00104)
Photochemical Alkene Hydrophosphination with Bis(trichlorosilyl)phosphine.
MB Geeson, K Tanaka, R Taakili, R Benhida, CC Cummins
– Journal of the American Chemical Society
(2022)
144,
14452
(DOI: 10.1021/jacs.2c05248)
Chemical and Enzymatic Methods for Post-Translational Protein–Protein Conjugation
RJ Taylor, MB Geeson, T Journeaux, GJL Bernardes
– J Am Chem Soc
(2022)
144,
14404
(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,
eabo0696
(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 of the United States of America
(2022)
119,
e2109718119
(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 Letters
(2022)
596,
2072
(DOI: 10.1002/1873-3468.14449)
Both COVID-19 infection and vaccination induce high-affinity cross-clade responses to SARS-CoV-2 variants.
M Emmenegger, S Fiedler, SD Brugger, SRA Devenish, AS Morgunov, A Ilsley, F Ricci, AY Malik, T Scheier, L Batkitar, L Madrigal, M Rossi, G Meisl, AK Lynn, L Saleh, A von Eckardstein, TPJ Knowles, A Aguzzi
– iScience
(2022)
25,
104766
(DOI: 10.1016/j.isci.2022.104766)
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,
e2205412119
(DOI: 10.1073/pnas.2205412119)
DNA-Liposome Hybrid Carriers for Triggered Cargo Release
KN Baumann, T Schröder, PS Ciryam, D Morzy, P Tinnefeld, TPJ Knowles, S Hernández-Ainsa
– ACS Appl Bio Mater
(2022)
5,
3713
(DOI: 10.1021/acsabm.2c00225)
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
– Journal of the American Chemical Society
(2022)
144,
13026
(DOI: 10.1021/jacs.2c04747)
Injectable Granular Hydrogels as Colloidal Assembly Microreactors for Customized Structural Colored Objects
J Zhang, Y Qin, Y Ou, Y Shen, B Tang, X Zhang, Z Yu
– Angewandte Chemie
(2022)
134,
(DOI: 10.1002/ange.202206339)

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