ArticleThe Journal of chemical physics2011
Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations.
Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Modeling Protein Aggregation Kinetics from NMR Data.Journal of molecular biology · 2025Review
- Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.Nature chemical biology · 2025Article
- Molecular mechanisms of amyloid inhibition: an NMR-driven framework with polyphenols as a case study.Frontiers in molecular biosciences · 2025Article
- Investigation on environmental factors contributing to bispecific antibody stability and the reversal of self-associated aggregates.Bioresources and bioprocessing · 2024Article
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Effects of Macromolecular Cosolutes on the Kinetics of Huntingtin Aggregation Monitored by NMR Spectroscopy.The journal of physical chemistry letters · 2024Article
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- Quantitative NMR analysis of the mechanism and kinetics of chaperone Hsp104 action on amyloid-β42 aggregation and fibril formation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Detecting Early Cognitive Decline in Alzheimer's Disease with Brain Synaptic Structural and Functional Evaluation.Biomedicines · 2023Review
- Quantitative NMR analysis of the kinetics of prenucleation oligomerization and aggregation of pathogenic huntingtin exon-1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease.Molecular aspects of medicine · 2022Review
- A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics.Chemical science · 2021Article
- Biomimetic peptide self-assembly for functional materials.Nature reviews. Chemistry · 2020Article
- Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Polymer-Peptide Conjugates Convert Amyloid into Protein Nanobundles through Fragmentation and Lateral Association.ACS applied nano materials · 2020Article
- Hemoglobin S polymerization and sickle cell disease: A retrospective on the occasion of the 70th anniversary of Pauling's Science paper.American journal of hematology · 2020Review
- The catalytic nature of protein aggregation.The Journal of chemical physics · 2020Article
- Active Modulation of States of Prestress in Self-Assembled Short Peptide Gels.Biomacromolecules · 2019Article
- The role of annealing and fragmentation in human tau aggregation dynamics.The Journal of biological chemistry · 2019Article
- Parallel chromatography and in situ scattering to interrogate competing protein aggregation pathways.Protein science : a publication of the Protein Society · 2018Article
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4 authors.
Funding
Abstract
We explore the long-time behavior and equilibrium properties of a system of linear filaments growing through nucleated polymerisation. We show that the length distribution for breakable filaments evolves through two well defined limiting cases: first, a steady state distribution determined by the balance of breakage and elongation is reached; upon monomer depletion at the end of the growth phase, an equilibrium length distribution biased towards smaller filament fragments emerges. We furthermore compute the time evolution of the concentration of small oligomeric filament fragments. For frangible filaments, oligomers are present both at early times and at equilibrium, whereas in the absence of fragmentation, oligomers are only present in significant quantities at the beginning of the polymerisation reaction. Finally, we discuss the significance of these results for the biological consequences of filamentous protein aggregation.
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