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Centre for Misfolding Diseases

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  • Currently displaying 1 - 20 of 2658 publications
Effects of system complexity on protein aggregation in neurodegeneration
M Sanguanini
(2021)
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
MM Schneider, S Gautam, TW Herling, E Andrzejewska, G Krainer, AM Miller, VA Trinkaus, QAE Peter, FS Ruggeri, M Vendruscolo, A Bracher, CM Dobson, FU Hartl, TPJ Knowles
– Nature Communications
(2021)
12,
1
Intermolecular reorganisation of single-component condensates during ageing promotes multiphase architectures
A Garaizar, J Espinosa, J Joseph, G Krainer, Y Shen, TPJ Knowles, R Collepardo-Guevara
(2021)
The cellular modifier MOAG‐4/SERF drives amyloid formation through charge complementation
A Pras, B Houben, FA Aprile, R Seinstra, R Gallardo, L Janssen, W Hogewerf, C Gallrein, M De Vleeschouwer, A Mata-Cabana, M Koopman, E Stroo, M de Vries, S Louise Edwards, J Kirstein, M Vendruscolo, SF Falsone, F Rousseau, J Schymkowitz, EAA Nollen
– EMBO Journal
(2021)
e107568
Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary Systems.
TA Hakala, EV Yates, PK Challa, Z Toprakcioglu, K Nadendla, D Matak-Vinkovic, CM Dobson, R Martínez, F Corzana, TPJ Knowles, GJL Bernardes
– J Am Chem Soc
(2021)
143,
16401
Interaction of Amyloid-β-(1-42) Peptide and Its Aggregates with Lipid/Water Interfaces Probed by Vibrational Sum-Frequency Generation Spectroscopy.
S Strazdaite, SJ Roeters, A Sakalauskas, T Sneideris, J Kirschner, KB Pedersen, B Schiøtt, F Jensen, T Weidner, V Smirnovas, G Niaura
– J Phys Chem B
(2021)
125,
11208
The signal peptide of the amyloid precursor protein forms amyloid-like aggregates and enhances Aβ42 aggregation
K Gadhave, T Bhardwaj, VN Uversky, M Vendruscolo, R Giri
– Cell Reports Physical Science
(2021)
2,
100599
New Frontiers for Machine Learning in Protein Science.
AS Morgunov, KL Saar, M Vendruscolo, TPJ Knowles
– Journal of Molecular Biology
(2021)
433,
167232
Dichloro Butenediamides as Irreversible Site‐Selective Protein Conjugation Reagent
V Laserna, D Abegg, CF Afonso, EM Martin, A Adibekian, P Ravn, F Corzana, GJL Bernardes
– Angewandte Chemie
(2021)
133,
23943
Dichloro Butenediamides as Irreversible Site‐Selective Protein Conjugation Reagent
V Laserna, D Abegg, CF Afonso, EM Martin, A Adibekian, P Ravn, F Corzana, GJL Bernardes
– Angew Chem Int Ed Engl
(2021)
60,
23750
Sequential storage and release of microdroplets.
Z Toprakcioglu, TPJ Knowles
– Microsystems and Nanoengineering
(2021)
7,
76
Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation.
MR Zimmermann, SC Bera, G Meisl, S Dasadhikari, S Ghosh, S Linse, K Garai, TPJ Knowles
– J Am Chem Soc
(2021)
143,
16621
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)
A maximum caliber approach for continuum path ensembles
PG Bolhuis, ZF Brotzakis, M Vendruscolo
– The European Physical Journal B
(2021)
94,
188
Nonhuman IAPP Variants Inhibit Human IAPP Aggregation
A Oakes, K Menefee, A Lamba, LM Palato, DJ Rinauro, A Tun, B Jauregui, K Chang, LA Nogaj, DA Moffet
– Protein and Peptide Letters
(2021)
28,
963
Liquid-liquid phase separation underpins the formation of replication factories in rotaviruses
F Geiger, J Acker, G Papa, X Wang, WE Arter, KL Saar, NA Erkamp, R Qi, JP Bravo, S Strauss, G Krainer, OR Burrone, R Jungmann, TP Knowles, H Engelke, A Borodavka
– EMBO Journal
(2021)
e107711
Combating small-molecule aggregation with machine learning
K Lee, A Yang, Y-C Lin, D Reker, GJL Bernardes, T Rodrigues
– Cell Reports Physical Science
(2021)
2,
100573
Deformable and Robust Core-Shell Protein Microcapsules Templated by Liquid-Liquid Phase-Separated Microdroplets
Y Xu, Y Shen, TCT Michaels, KN Baumann, D Vigolo, Q Peter, Y Lu, KL Saar, D Vella, H Zhu, B Li, H Yang, APM Guttenplan, M Rodriguez-Garcia, D Klenerman, TPJ Knowles
– Advanced Materials Interfaces
(2021)
8,
2101071
The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces
T Scheidt, JA Carozza, CC Kolbe, FA Aprile, O Tkachenko, MMJ Bellaiche, G Meisl, QAE Peter, TW Herling, S Ness, M Castellana-Cruz, JLP Benesch, M Vendruscolo, CM Dobson, P Arosio, TPJ Knowles
– Proceedings of the National Academy of Sciences of the United States of America
(2021)
118,
e2108790118
Aggregation condition–structure relationship of mouse prion protein fibrils
J Fridmanis, Z Toleikis, T Sneideris, M Ziaunys, R Bobrovs, V Smirnovas, K Jaudzems
– Int J Mol Sci
(2021)
22,
9635