activity
20112025
most citedCrucial role of non-specific interactions in amyloid nucleation

197 citations · 492 across the 14 of their papers we have counts for

collaborators

14 papers

physics.chem-ph2025★ 4 cited

Kinetics of seeded protein aggregation: theory and application

Alexander J. Dear, Georg Meisl, Jing Hu +2

``Seeding'' is the addition of preformed fibrils to a solution of monomeric protein to accelerate its aggregation into new fibrils. It is a versatile and widely-used tool for scien…

cond-mat.soft2024

Competing addition processes give distinct growth regimes in the assembly of 1D filaments

Sk Ashif Akram, Tyler Brown, Stephen Whitelam +3

We present a model to describe the concentration-dependent growth of protein filaments. Our model contains two states, a low entropy/high affinity ordered state and a high entropy/…

q-bio.QM2020

Hamiltonian Dynamics of Saturated Elongation in Amyloid Fiber Formation

Liu Hong, Xizhou Liu, Thomas C. T. Michaels +1

Elongation is a fundament process in amyloid fiber growth, which is normally characterized by a linear relationship between the fiber elongation rate and the monomer concentration.…

q-bio.BM2020★ 30 cited

The role of clearance mechanisms in the kinetics of toxic protein aggregates involved in neurodegenerative diseases

Travis B. Thompson, Georg Meisl, Tuomas Knowles +1

Protein aggregates in the brain play a central role in cognitive decline and structural damage associated with neurodegenerative diseases. For instance, in Alzheimer's disease the…

cond-mat.soft2020

Deformable and robust core-shell protein microcapsules templated by liquid-liquid phase separated microdroplets

Yufan Xu, Yi Shen, Thomas C. T. Michaels +13

Microcapsules are a key class of microscale materials with applications in areas ranging from personal care to biomedicine, and with increasing potential to act as extracellular ma…

physics.bio-ph2020★ 3 cited

Mechanism, scaling and rates of protein aggregation from in vivo measurements

Georg Meisl, Alexander J Dear, Thomas CT Michaels +1

The formation and proliferation of protein aggregates play a central role in a number of devastating neuro-degenerative diseases. Many experimental studies indicate that the abilit…

physics.bio-ph2018★ 27 cited

Reaction rate theory for supramolecular kinetics: application to protein aggregation

Thomas C. T. Michaels, Lucie X. Liu, Samo Curk +3

Probing the reaction mechanisms of supramolecular processes in soft- and biological matter, such as protein aggregation, is inherently challenging. These processes emerge from the…

cond-mat.soft2016★ 95 cited

Kinetics of spontaneous filament nucleation via oligomers: insights from theory and simulation

Anđela Šarić, Thomas C. T. Michaels, Alessio Zaccone +2

Nucleation processes are at the heart of a large number of phenomena, from cloud formation to protein crystallization. A recently emerging area where nucleation is highly relevant…

physics.bio-ph2016★ 3 cited

Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers

Patrick Varilly, Adam P. Willard, Julius B. Kirkegaard +2

Aggregation of amphiphiles through the action of hydrophobic interactions is a common feature in soft condensed matter systems and is of particular importance in the context of bio…

q-bio.MN2016★ 82 cited

A general reaction network unifies the aggregation behaviour of the A42 peptide and its variants

Georg Meisl, Xiaoting Yang, Christopher M. Dobson +2

The amyloid peptide (A42), whose aggregation is associated with Alzheimer's disease, is an amphiphatic peptide with a high propensity to self-assemble. A42 has a net nega…

cond-mat.soft2015★ 41 cited

Consistent treatment of hydrophobicity in protein lattice models accounts for cold denaturation

Erik van Dijk, Patrick Varilly, Tuomas Knowles +2

The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavourable interactions between hydrophobic residues and water through the formation of a hyd…

physics.bio-ph2015★ 10 cited

Oligomers of heat-shock proteins: Structures that don't imply function

William M. Jacobs, Tuomas P. J. Knowles, Daan Frenkel

Most proteins must remain soluble in the cytosol in order to perform their biological functions. To protect against undesired protein aggregation, living cells maintain a populatio…

q-bio.BM2014★ 197 cited

Crucial role of non-specific interactions in amyloid nucleation

Anđela Šarić, Yassmine C. Chebaro, Tuomas P. J. Knowles +1

Protein oligomers have been implicated as toxic agents in a wide range of amyloid-related diseases. Yet it has remained unsolved whether the oligomers are a necessary step in the f…

physics.bio-ph2011

Nucleated polymerisation in the presence of pre-formed seed filaments

Samuel I. A. Cohen, Michele Vendruscolo, Christopher M. Dobson +1

We revisit the classical problem of nucleated polymerisation and derive a range of exact results describing polymerisation in systems intermediate between the well-known limiting c…