ArticleJournal of molecular biology2007
Determining the critical nucleus and mechanism of fibril elongation of the Alzheimer's Abeta(1-40) peptide.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Droplet growth, Ostwald's rule, and emergence of order in Fused in Sarcoma.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Alzheimer's Disease: A Review of Pathology, Current Treatments, and the Potential Therapeutic Effect of Decreasing Oxidative Stress by Combined Vitamin D and l-Cysteine Supplementation.Antioxidants & redox signaling · 2024Review
- Mechanistic Kinetic Model Reveals How Amyloidogenic Hydrophobic Patches Facilitate the Amyloid-β Fibril Elongation.ACS chemical neuroscience · 2022Article
- Multiscale Models for Fibril Formation: Rare Events Methods, Microkinetic Models, and Population Balances.Life (Basel, Switzerland) · 2021Article
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Overview on the Effects ofMolecules (Basel, Switzerland) · 2018Review
- Thermodynamics of Amyloid-β Fibril Elongation: Atomistic Details of the Transition State.ACS chemical neuroscience · 2018Article
- Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.Physical chemistry chemical physics : PCCP · 2017Article
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.Biochemical and biophysical research communications · 2017Article
- Elucidating Important Sites and the Mechanism for Amyloid Fibril Formation by Coarse-Grained Molecular Dynamics.ACS chemical neuroscience · 2017Article
- Weak self-association of cytochrome c peroxidase molecules observed by paramagnetic NMR.Journal of biomolecular NMR · 2016Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Alzheimer's disease: analysis of a mathematical model incorporating the role of prions.Journal of mathematical biology · 2014Article
- Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulations.Journal of the American Chemical Society · 2014Article
- The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Biochemistry · 2014Article
- Fiber diffraction data indicate a hollow core for the Alzheimer's aβ 3-fold symmetric fibril.Journal of molecular biology · 2012Article
- Elevation of glutathione as a therapeutic strategy in Alzheimer disease.Biochimica et biophysica acta · 2012Review
- Controlling the aggregation and rate of release in order to improve insulin formulation: molecular dynamics study of full-length insulin amyloid oligomer models.Journal of molecular modeling · 2012Article
- Role of water in protein aggregation and amyloid polymorphism.Accounts of chemical research · 2012Article
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4 authors.
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Abstract
We use a coarse-grained protein model to characterize the critical nucleus, structural stability, and fibril elongation propensity of Abeta(1-40) oligomers for the C(2x) and C(2z) quaternary forms proposed by solid-state NMR. By estimating equilibrium populations of structurally stable and unstable protofibrils, we determine the shift in the dominant population from free monomer to ordered fibril at a critical nucleus of ten chains for the C(2x) and C(2z) forms. We find that a minimum assembly of 16 monomer chains is necessary to mimic a mature fibril, and show that its structural stability correlates with a plateau in the hydrophobic residue density and a decrease in the likelihood of losing hydrophobic interactions by rotating the fibril subunits. While Abeta(1-40) protofibrils show similar structural stability for both C(2x) and C(2z) quaternary structures, we find that the fibril elongation propensity is greater for the C(2z) form relative to the C(2x) form. We attribute the increased propensity for elongation of the C(2z) form as being due to a stagger in the interdigitation of the N-terminal and C-terminal beta-strands, resulting in structural asymmetry in the presented fibril ends that decreases the amount of incorrect addition to the N terminus on one end. We show that because different combinations of stagger and quaternary structure affect the structural symmetry of the fibril end, we propose that differences in quaternary structures will affect directional growth patterns and possibly different morphologies in the mature fiber.
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