An Analytical Solution to the Kinetics of Breakable Filament Assembly

By Tuomas P. J. Knowles, C. Waudby, Glyn L. Devlin, Samuel I. A. Cohen, A. Aguzzi, Michele Vendruscolo, Eugene M. Terentjev, M. Welland, Christopher M. Dobson. Science, 2009

1,109 citations recorded by the source corpus.

Subfields: Biomaterials, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/28713d928f1f9654917e819d737dd126cf32b50b

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Citations in the corpus

In vivo aspects of protein folding and quality control (2016, background): “Chaperones have been shown to interfere at various steps of the aggregation cascade (144), including primary nucleation, fibril elongation and fragmentation, and secondary nucleation by the fibril surface (145, 146).”
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (2012, methodology): “Recently, however, it has become evident that the kinetics of fibril growth can often be dominated by secondary nucleation events, such as fibril fragmentation (Cohen et al., 2011; Knowles et al., 2009), adding further elements of complexity to the kinetic process.”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “The ability to determine the rate constants of the various different microscopic steps in protein aggregation, therefore, enables the definition of the key kinetic and mechanistic features of the aggregation of proteins under a variety of conditions (135, 139) and makes it possible to investigate th”
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation (2014, methodology): “Having established the highly quantitative and reproducible nature of seeded aggregation of α-synuclein, we designed further experiments in PBS buffer at neutral pH to obtain insights into the relative significance of the other molecular processes that are generally important in filamentous growth, ”
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (2013, methodology): “Once a critical concentration of amyloid fibrils has formed, however, secondary nucleation will overtake primary nucleation as the major source of new oligomers and further proliferation becomes exponential in nature (14, 16, 22) due to positive feedback (Fig.”
Molecular mechanisms of protein aggregation from global fitting of kinetic models (2016, methodology): “Recent advances in reaction network theory have brought even the complicated pathways associated with amyloid formation within reach of chemical kinetics 11 .”