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Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
12 papers
Recent·Most cited
D. Qian, H. Ausserwoger, W. E. Arter, R. Scrutton, T. J. Welsh, T. Kartanas, N. Ermann, S. Qamar, C. Fischer, T. Sneideris, P. St George-Hyslop, R. V. Pappu, T. Knowles
This paper introduces a dominance analysis framework to determine the molecular mechanism of condensate modulation, demonstrating its application to G3BP1/RNA condensates disrupted by suramin.
bioRxiv · Nov 2, 2023 · PreprintBiophysics
G. Krainer, R. P. B. Jacquat, M. M. Schneider, T. J. Welsh, J. Fan, Q. A. E. Peter, E. A. Andrzejewska, G. Sneideriene, M. A. Czekalska, H. Ausserwoeger, L. Chai, W. E. Arter, K. L. Saar, T. W. Herling, T. M. Franzmann, , T. P. J. Knowles
This paper introduces smMDS, a method for digital sizing of proteins in solution, enabling sensitive and accurate measurement of protein sizes and interactions.
bioRxiv · Jul 12, 2023Biophysics
C. K. Xu, G. Meisl, E. Andrzejewska, G. Krainer, A. J. Dear, M. C. Cruz, S. Turi, R. Jacquat, W. E. Arter, M. Vendruscolo, S. Linse, T. P. Knowles
This study shows α-synuclein oligomers form via secondary nucleation on fibril surfaces, not from monomers, and this process is enhanced by agitation under physiological conditions.
bioRxiv · May 28, 2023Biophysics
G. Sneideriene, M. A. Czekalska, C. K. Xu, A. Jayaram, G. Krainer, W. E. Arter, Q. Peter, M. Castellana-Cruz, K. L. Saar, A. Levin, T. Mueller, S. Fiedler, S. R. A. Devenish, H. Fiegler, J. R. Kumita, T. Knowles
This study shows that alpha-synuclein oligomers bind more strongly to curved lipid membranes and displace monomeric alpha-synuclein, suggesting a new mechanism for Parkinson's disease toxicity.
bioRxiv · Mar 21, 2023Biophysics
H. Zhu, M. Narita, J. A. Joseph, G. Krainer, W. E. Arter, I. Olan, K. L. Saar, N. Ermann, J. R. Espinosa, Y. Shen, M. A. Kuri, R. Qi, T. J. Welsh, Y. Xu, R. Collepardo-Guevara, , T. Knowles
This study shows HMGA1a undergoes phase separation in the nucleus, driven by protein-DNA interactions and its disordered C-terminal tail.
bioRxiv · Oct 14, 2021Biophysics
G. Krainer, T. J. Welsh, J. A. Joseph, J. R. Espinosa, S. Wittmann, E. de Csillery, A. Sridhar, Z. Toprakcioglu, G. Gudiskyte, M. A. Czekalska, W. E. Arter, P. St George-Hyslop, A. A. Hyman, R. Collepardo-Guevara, S. Alberti, T. P. Knowles
The paper shows that proteins forming liquid condensates can reenter a phase-separated state at high salt concentrations due to hydrophobic and non-ionic interactions, distinct from low-salt electrostatic-driven phase separation.
Nature Communications · Feb 17, 2021Peer-reviewedBiophysics
F. Geiger, G. Papa, W. E. Arter, J. Acker, K. L. Saar, N. Erkamp, R. Qi, J. P. K. Bravo, S. Strauss, G. Krainer, O. R. Burrone, R. Jungmann, T. Knowles, H. Engelke, A. Borodavka
This study shows rotavirus replication factories are RNA-protein condensates formed by phase separation, with unique features that could be targeted for antiviral therapies.
bioRxiv · Dec 18, 2020Biophysics
K. L. Saar, A. S. Morgunov, R. Qi, W. E. Arter, G. Krainer, A. A. Lee, T. Knowles
This paper develops machine learning models to predict protein condensate formation using sequence determinants and embeddings, achieving high accuracy and sensitivity.
bioRxiv · Oct 26, 2020 · PreprintBiophysics
W. E. Arter, R. Qi, N. A. Erkamp, G. Krainer, K. Didi, T. J. Welsh, J. Acker, J. Nixon-Abell, S. Qamar, J. Guillen-Boixet, T. M. Franzmann, D. Kuster, A. A. Hyman, A. Borodavka, P. St George-Hyslop, , T. P. Knowles
This paper introduces a microdroplet platform to rapidly generate high-resolution phase diagrams of biomolecular condensates and demonstrates its application in studying phase transitions.
bioRxiv · Jun 4, 2020 · PreprintBiophysics
G. Krainer, K. L. Saar, W. E. Arter, T. J. Welsh, M. A. Czekalska, R. P. B. Jacquat, Q. Peter, W. Traberg-Christensen, A. Pujari, A. K. Jayaram, P. Challa, C. G. Taylor, L.-M. van der Linden, T. Franzmann, R. M. Owens, , T. P. J. Knowles
This paper introduces a single-molecule microfluidic platform for digital protein biomarker detection, demonstrating its ability to quantify protein concentrations and provide insights beyond traditional immunoassays.
bioRxiv · May 24, 2020 · PreprintBiophysics
T. J. Welsh, G. Krainer, J. R. Espinosa, J. A. Joseph, A. Sridhar, M. Jahnel, W. E. Arter, K. L. Saar, S. Alberti, R. Collepardo-Guevara, T. P. J. Knowles
The paper investigates how surface electrostatics influence the stability of biomolecular condensates by comparing their fusion propensity using zeta potential measurements and molecular modeling.
bioRxiv · Apr 20, 2020Biophysics
W. E. Arter, C. K. Xu, M. Castellana-Cruz, T. W. Herling, G. Krainer, K. L. Saar, J. R. Kumita, C. M. Dobson, T. P. Knowles
This study demonstrates microfluidic free-flow electrophoresis for rapidly separating and characterizing alpha-synuclein oligomers in solution.
bioRxiv · Mar 10, 2020 · PreprintBiophysics