ArticleScience advances2022
Direct observation of the molecular mechanism underlying protein polymerization.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Characterization of RNA using mass photometry: Method and technical perspectives.Molecular therapy. Nucleic acids · 2026Article
- Molecule by Molecule Characterization of a Polymer Molecular Mass Distribution via Mass Photometry.Angewandte Chemie (International ed. in English) · 2026Article
- R5 and R7 positions on fluoroquinolone scaffolds drive F-actin filament disruption.Scientific reports · 2026Article
- Characterizing Monoclonal Antibody Aggregation Using Charge Detection Mass Spectrometry and Industry Standard Methods.Journal of the American Society for Mass Spectrometry · 2025Article
- Cardiolipin membranes drive Myosin VI activation, oligomerization, and processive cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing.Nature communications · 2025Article
- Mass photometry as a fast, facile characterization tool for direct measurement of mRNA length.Biology methods & protocols · 2025Article
- High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.Analytical chemistry · 2024Article
- Charge Detection Mass Spectrometry Reveals Conformational Heterogeneity in Megadalton-Sized Monoclonal Antibody Aggregates.Journal of the American Chemical Society · 2024Article
- Cascaded momentum-space polarization filters enabled label-free black-field microscopy for single nanoparticles analysis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Label-Free Imaging of DNA Interactions with 2D Materials.ACS photonics · 2024Article
- Assessing nanobody interaction with SARS-CoV-2 Nsp9.PloS one · 2024Article
- Biophysical Analysis of Therapeutic Antibodies in the Early Development Pipeline.Biologics : targets & therapy · 2024Review
- Mass photometric detection and quantification of nanoscale α-synuclein phase separation.Nature chemistry · 2023Article
- Effect of temperature and nucleotide on the binding of BiP chaperone to a protein substrate.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein assembly is a main route to generating complexity in living systems. Revealing the relevant molecular details is challenging because of the intrinsic heterogeneity of species ranging from few to hundreds of molecules. Here, we use mass photometry to quantify and monitor the full range of actin oligomers during polymerization with single-molecule sensitivity. We find that traditional nucleation-based models cannot account for the observed distributions of actin oligomers. Instead, the key step of filament formation is a slow transition between distinct states of an actin filament mediated by cation exchange or ATP hydrolysis. The resulting model reproduces important aspects of actin polymerization, such as the critical concentration for filament formation and bulk growth behavior. Our results revise the mechanism of actin nucleation, shed light on the role and function of actin-associated proteins, and introduce a general and quantitative means to studying protein assembly at the molecular level.
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Registered trials
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