Biologically Inspired Design and Development of a Variable Stiffness Powered Ankle-foot Prosthesis von Dobson, Alexander A, Wei, Guowu, Ren, Lei

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Public parks and the pandemic: How park usage has been affected by COVID-19 policies von Volenec, Zoe M, Abraham, Joel O, Becker, Alexander D, Dobson, Andy P

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Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation von Buell, Alexander K., Galvagnion, Céline, Gaspar, Ricardo, Sparr, Emma, Vendruscolo, Michele, Knowles, Tuomas P. J., Linse, Sara, Dobson, Christopher M.

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Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death von Hildebrand, Joanne M., Tanzer, Maria C., Lucet, Isabelle S., Young, Samuel N., Spall, Sukhdeep K., Sharma, Pooja, Pierotti, Catia, Garnier, Jean-Marc, Dobson, Renwick C.J., Webb, Andrew I., Tripaydonis, Anne, Babon, Jeffrey J., Mulcair, Mark D., Scanlon, Martin J., Alexander, Warren S., Wilks, Andrew F., Czabotar, Peter E., Lessene, Guillaume, Murphy, James M., Silke, John

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Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide von Michaels, Thomas C. T., Šarić, Andela, Curk, Samo, Bernfur, Katja, Arosio, Paolo, Meisl, Georg, Dear, Alexander J., Cohen, Samuel I. A., Dobson, Christopher M., Vendruscolo, Michele, Linse, Sara, Knowles, Tuomas P. J.

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Kinetic diversity of amyloid oligomers von Dear, Alexander J., Michaels, Thomas C. T., Meisl, Georg, Klenerman, David, Wu, Si, Perrett, Sarah, Linse, Sara, Dobson, Christopher M., Knowles, Tuomas P. J.

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Electrostatic Effects in Filamentous Protein Aggregation von Buell, Alexander K, Hung, Peter, Salvatella, Xavier, Welland, Mark E, Dobson, Christopher M, Knowles, Tuomas P.J

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The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism von Murphy, James M., Czabotar, Peter E., Hildebrand, Joanne M., Lucet, Isabelle S., Zhang, Jian-Guo, Alvarez-Diaz, Silvia, Lewis, Rowena, Lalaoui, Najoua, Metcalf, Donald, Webb, Andrew I., Young, Samuel N., Varghese, Leila N., Tannahill, Gillian M., Hatchell, Esme C., Majewski, Ian J., Okamoto, Toru, Dobson, Renwick C.J., Hilton, Douglas J., Babon, Jeffrey J., Nicola, Nicos A., Strasser, Andreas, Silke, John, Alexander, Warren S.

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How Many Parameters Does It Take to Describe Disease Tolerance? von Louie, Alexander, Song, Kyung Han, Hotson, Alejandra, Thomas Tate, Ann, Schneider, David S

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Ostwald’s rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers von Levin, Aviad, Mason, Thomas O., Adler-Abramovich, Lihi, Buell, Alexander K., Meisl, George, Galvagnion, Celine, Bram, Yaron, Stratford, Samuel A., Dobson, Christopher M., Knowles, Tuomas P. J., Gazit, Ehud

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Multi-dimensional super-resolution imaging enables surface hydrophobicity mapping von Bongiovanni, Marie N., Godet, Julien, Horrocks, Mathew H., Tosatto, Laura, Carr, Alexander R., Wirthensohn, David C., Ranasinghe, Rohan T., Lee, Ji-Eun, Ponjavic, Aleks, Fritz, Joelle V., Dobson, Christopher M., Klenerman, David, Lee, Steven F.

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Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation von Flagmeier, Patrick, Meisl, Georg, Vendruscolo, Michele, Knowles, Tuomas P. J., Dobson, Christopher M., Buell, Alexander K., Galvagnion, Céline

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Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein von Galvagnion, Céline, Brown, James W. P., Ouberai, Myriam M., Flagmeier, Patrick, Vendruscolo, Michele, Buell, Alexander K., Sparr, Emma, Dobson, Christopher M.

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Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy von Pinotsi, Dorothea, Buell, Alexander K, Galvagnion, Celine, Dobson, Christopher M, Kaminski Schierle, Gabriele S, Kaminski, Clemens F

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Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease von Tóth, Gergely, Gardai, Shyra J, Zago, Wagner, Bertoncini, Carlos W, Cremades, Nunilo, Roy, Susan L, Tambe, Mitali A, Rochet, Jean-Christophe, Galvagnion, Celine, Skibinski, Gaia, Finkbeiner, Steven, Bova, Michael, Regnstrom, Karin, Chiou, San-San, Johnston, Jennifer, Callaway, Kari, Anderson, John P, Jobling, Michael F, Buell, Alexander K, Yednock, Ted A, Knowles, Tuomas P J, Vendruscolo, Michele, Christodoulou, John, Dobson, Christopher M, Schenk, Dale, McConlogue, Lisa

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Binding of the Molecular Chaperone αB-Crystallin to Aβ Amyloid Fibrils Inhibits Fibril Elongation von Shammas, Sarah L., Waudby, Christopher A., Wang, Shuyu, Buell, Alexander K., Knowles, Tuomas P.J., Ecroyd, Heath, Welland, Mark E., Carver, John A., Dobson, Christopher M., Meehan, Sarah

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Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation von Galvagnion, Céline, Buell, Alexander K, Meisl, Georg, Michaels, Thomas C T, Vendruscolo, Michele, Knowles, Tuomas P J, Dobson, Christopher M

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Aortic Biomechanics: Reply von Gregory, Alexander J., Dobson, Gary M.

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A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence von Pinotsi, Dorothea, Buell, Alexander K., Dobson, Christopher M., Kaminski Schierle, Gabriele S., Kaminski, Clemens F.

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Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants von Tosatto, Laura, Horrocks, Mathew H., Dear, Alexander J., Knowles, Tuomas P. J., Dalla Serra, Mauro, Cremades, Nunilo, Dobson, Christopher M., Klenerman, David

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