ArticleBiophysical journal2012
Role of elongation and secondary pathways in S6 amyloid fibril growth.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Modulation of the Fibrillation Kinetics and Morphology of a Therapeutic Peptide by Cucurbit[7]uril.Molecular pharmaceutics · 2023Article
- Distinct growth regimes of α-synuclein amyloid elongation.Biophysical journal · 2023Article
- Macromolecular crowding modulates α-synuclein amyloid fiber growth.Biophysical journal · 2021Article
- Fast kinetics of environmentally induced α-synuclein aggregation mediated by structural alteration in NAC region and result in structure dependent cytotoxicity.Scientific reports · 2020Article
- An Easy Path for Correlative Electron and Super-Resolution Light Microscopy.Scientific reports · 2019Article
- Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.Physical chemistry chemical physics : PCCP · 2017Article
- Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Biophysical journal · 2017Article
- The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.Scientific reports · 2017Article
- Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.The Journal of biological chemistry · 2014Article
- Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Polymorphic fibrillation of the destabilized fourth fasciclin-1 domain mutant A546T of the Transforming growth factor-β-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
The concerted action of a large number of individual molecular level events in the formation and growth of fibrillar protein structures creates a significant challenge for differentiating between the relative contributions of different self-assembly steps to the overall kinetics of this process. The characterization of the individual steps is, however, an important requirement for achieving a quantitative understanding of this general phenomenon which underlies many crucial functional and pathological pathways in living systems. In this study, we have applied a kinetic modeling approach to interpret experimental data obtained for the aggregation of a selection of site-directed mutants of the protein S6 from Thermus thermophilus. By studying a range of concentrations of both the seed structures, used to initiate the reaction, and of the soluble monomer, which is consumed during the growth reaction, we are able to separate unambiguously secondary pathways from primary nucleation and fibril elongation. In particular, our results show that the characteristic autocatalytic nature of the growth process originates from secondary processes rather than primary nucleation events, and enables us to derive a scaling law which relates the initial seed concentration to the onset of the growth phase.
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