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Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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K. A. Connors: Chemical Kinetics: The Study of Reaction Rates in Solution, VCH Verlagsgesellschaft Weinheim, New York, ISBN 3‐527‐28037‐5, 480 Seiten, Preis: DM 168,–.

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Kinetics of sickle hemoglobin polymerization

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Kinetics of sickle hemoglobin polymerization

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Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease

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[20] Analysis of circular dichroism spectra

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Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?

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The Recombinant Amyloid-β Peptide Aβ1–42 Aggregates Faster and Is More Neurotoxic than Synthetic Aβ1–42

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From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation

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Chemical kinetics: The study of reaction rates in solution

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A theory of linear and helical aggregations of macromolecules

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[17] Analysis of protein aggregation kinetics

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Alzheimer's Disease Amyloid Propagation by a Template-Dependent Dock-Lock Mechanism

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Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process

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Aβ40 and Aβ42 Amyloid Fibrils Exhibit Distinct Molecular Recycling Properties

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Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

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Protein folding and misfolding

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Atomic structures of amyloid cross-β spines reveal varied steric zippers

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Protein aggregation diseases: pathogenicity and therapeutic perspectives

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Thermodynamics of the Polymerization of Protein

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Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments

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Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations

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Fiber-dependent amyloid formation as catalysis of an existing reaction pathway

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Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide

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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

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Thermodynamics of the Earth

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A facile method for expression and purification of the Alzheimer’s disease‐associated amyloid β‐peptide

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The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics

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Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease

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Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer Addition

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inferred← citeshttps://doi.org/10.1016/j.sbi.2024.102951openalex-snapshot

Characterizing heterogeneity in amyloid formation processes

inferred← citeshttps://doi.org/10.1016/j.semcdb.2017.08.046openalex-snapshot

Amyloid and membrane complexity: The toxic interplay revealed by AFM

inferred← citeshttps://doi.org/10.1016/j.snb.2019.127086openalex-snapshot

Two instantaneous fluorogenic steps for detection of nanomolar amyloid beta monomer and its interaction with stoichiometric copper(II) ion

inferred← citeshttps://doi.org/10.1016/j.talanta.2026.130348openalex-snapshot

Simultaneous and ultrasensitive detection of Alzheimer's disease blood biomarkers using magnetic SERS-encoded tags-based LFIA assay

inferred← citeshttps://doi.org/10.1016/j.xcrp.2022.101028openalex-snapshot

Identifying the role of co-aggregation of Alzheimer’s amyloid-β with amorphous protein aggregates of non-amyloid proteins

inferred← citeshttps://doi.org/10.1016/j.xcrp.2025.102930openalex-snapshot

Nucleation dynamics in amyloid-beta dimerization revealed by single-molecule fingerprinting

inferred← citeshttps://doi.org/10.1016/j.xcrp.2025.103031openalex-snapshot

A global thermodynamic-kinetic model capturing the hallmarks of liquid-liquid phase separation and amyloid aggregation

inferred← citeshttps://doi.org/10.1017/s0033583516000172openalex-snapshot

Secondary nucleation of monomers on fibril surface dominatesα-synuclein aggregation and provides autocatalytic amyloid amplification

inferred← citeshttps://doi.org/10.1017/s0033583520000025openalex-snapshot

Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases

inferred← citeshttps://doi.org/10.1017/s0033583520000104openalex-snapshot

Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases – ERRATUM

inferred← citeshttps://doi.org/10.1021/acs.accounts.3c00370openalex-snapshot

Metal Binding of Alzheimer’s Amyloid-β and Its Effect on Peptide Self-Assembly

inferred← citeshttps://doi.org/10.1021/acs.analchem.2c03009openalex-snapshot

Droplet-Based Microfluidic Temperature-Jump Platform for the Rapid Assessment of Biomolecular Kinetics

inferred← citeshttps://doi.org/10.1021/acs.analchem.9b03566openalex-snapshot

Real-Time Monitoring of Self-Aggregation of β-Amyloid by a Fluorescent Probe Based on Ruthenium Complex

inferred← citeshttps://doi.org/10.1021/acs.biochem.2c00371openalex-snapshot

Development of a Systematic Strategy toward Promotion of α-Synuclein Aggregation Using 2-Hydroxyisophthalamide-Based Systems

inferred← citeshttps://doi.org/10.1021/acs.biochem.3c00095openalex-snapshot

PAP(248–286) Conformational Changes during the Lag Phase of Amyloid Fibril Formation

inferred← citeshttps://doi.org/10.1021/acs.biochem.3c00349openalex-snapshot

Phase Separation and Fibrillization of Human Annexin A7 Are Mediated by Its Proline-Rich Domain

inferred← citeshttps://doi.org/10.1021/acs.biochem.4c00478openalex-snapshot

Aβ40 Fibril Assembly on Human Cerebral Smooth Muscle Cells Impairs Cell Viability

inferred← citeshttps://doi.org/10.1021/acs.biochem.5b00976openalex-snapshot

Heterogeneity and Turnover of Intermediates during Amyloid-β (Aβ) Peptide Aggregation Studied by Fluorescence Correlation Spectroscopy

inferred← citeshttps://doi.org/10.1021/acs.biochem.5b01259openalex-snapshot

Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00729openalex-snapshot

Aggregation and Fibril Structure of AβM01–42 and Aβ1–42

inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00353openalex-snapshot

Conserved S/T Residues of the Human Chaperone DNAJB6 Are Required for Effective Inhibition of Aβ42 Amyloid Fibril Formation

inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00393openalex-snapshot

An Efficient Method for the Expression and Purification of Aβ(M1–42)

inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00800openalex-snapshot

Targeting the Amyloid-β Fibril Surface with a Constrained Helical Peptide Inhibitor

inferred← citeshttps://doi.org/10.1021/acs.biomac.0c00989openalex-snapshot

On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide

inferred← citeshttps://doi.org/10.1021/acs.biomac.9b01475openalex-snapshot

Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers

inferred← citeshttps://doi.org/10.1021/acs.chemmater.4c01125openalex-snapshot

Off–On Pathway Complexity in Self-Assembly of Cadmium Cholate Hydrogel with Topological Evolution Triggered by Secondary Nucleation

inferred← citeshttps://doi.org/10.1021/acs.chemmater.6c01047openalex-snapshot

Solvent Microheterogeneity-Regulated Supramolecular Morphological Anisotropy in an Aggregation-Induced Emission-Active Phenylalanine Derivative

inferred← citeshttps://doi.org/10.1021/acs.chemmater.8b05335openalex-snapshot

Nucleation Kinetics and Molecular Mechanism in Transition-Metal Nanoparticle Formation: The Intriguing, Informative Case of a Bimetallic Precursor, {[(1,5-COD)Ir I ·HPO 4 ] 2 } 2–

inferred← citeshttps://doi.org/10.1021/acs.iecr.6c02494openalex-snapshot

Exploring the Step-Growth Polymerization Reaction Kinetics and Polydispersity of Amyloid Beta Aggregation

inferred← citeshttps://doi.org/10.1021/acs.inorgchem.5c04609openalex-snapshot

Screening π-Extended Ruthenium(II) Complexes for the Photoinduced Oxidative Modulation of Amyloid-β Peptide Aggregation

inferred← citeshttps://doi.org/10.1021/acs.jcim.3c00370openalex-snapshot

Prion-like Aggregation of the Heptapeptide GNNQQNY into Amyloid Nanofiber Is Governed by Configuration Entropy

inferred← citeshttps://doi.org/10.1021/acs.jcim.3c00898openalex-snapshot

Direct Observation of Seeded Conformational Conversion of hIAPP In Silico Reveals the Mechanisms for Morphological Dependence and Asymmetry of Fibril Growth

inferred← citeshttps://doi.org/10.1021/acs.jcim.5c01967openalex-snapshot

Molecular Mechanism of Beta-Amyloid Aggregation Inhibition by KLVFF

inferred← citeshttps://doi.org/10.1021/acs.jcim.6c01001openalex-snapshot

N-Terminal Chirality and Sequence Variations Modulate the Conformational Landscape of Amyloid-Beta 42

inferred← citeshttps://doi.org/10.1021/acs.jctc.7b00803openalex-snapshot

Self-Assembly Pathways of β-Sheet-Rich Amyloid-β(1–40) Dimers: Markov State Model Analysis on Millisecond Hybrid-Resolution Simulations

inferred← citeshttps://doi.org/10.1021/acs.jmedchem.9b01970openalex-snapshot

Calorimetric Studies of Binary and Ternary Molecular Interactions between Transthyretin, Aβ Peptides, and Small-Molecule Chaperones toward an Alternative Strategy for Alzheimer’s Disease Drug Discovery

inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c07129openalex-snapshot

Experimentally Consistent Simulation of Aβ21–30 Peptides with a Minimal NMR Bias

inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c07175openalex-snapshot

Investigating the Effects of Molecular Crowding on the Kinetics of Protein Aggregation

inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c11250openalex-snapshot

Modeling Amyloid Aggregation Kinetics: A Case Study with Sup35NM

inferred← citeshttps://doi.org/10.1021/acs.jpcb.1c00959openalex-snapshot

Stochastic Kinetic Treatment of Protein Aggregation and the Effects of Macromolecular Crowding

inferred← citeshttps://doi.org/10.1021/acs.jpcb.2c06375openalex-snapshot

Self-Assembly of Amyloid-Beta (Aβ) Peptides from Solution to Near In Vivo Conditions

inferred← citeshttps://doi.org/10.1021/acs.jpcb.4c07144openalex-snapshot

Inhibition and Degradation of Amyloid Beta Fibrils by Peptide Inhibitors

inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b04488openalex-snapshot

Comparison of Human and Bovine Insulin Amyloidogenesis under Uniform Shear

inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b09663openalex-snapshot

An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation

inferred← citeshttps://doi.org/10.1021/acs.jpcb.5c07335openalex-snapshot

Aβ 42 Adopts a Stronger Binding Affinity to the Gold Surface than Aβ 40

inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b10189openalex-snapshot

From Aβ Filament to Fibril: Molecular Mechanism of Surface-Activated Secondary Nucleation from All-Atom MD Simulations

inferred← citeshttps://doi.org/10.1021/acs.jpcb.6c01000openalex-snapshot

The Monomeric Conformational Ensembles of Aβ40 and Aβ42 Encode Their Differential Amyloid Aggregation Propensity

inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b07805openalex-snapshot

Statistical Mechanics of Globular Oligomer Formation by Protein Molecules

inferred← citeshttps://doi.org/10.1021/acs.jpclett.2c01065openalex-snapshot

Kinetic Mechanism of Amyloid-β-(16–22) Peptide Fibrillation

inferred← citeshttps://doi.org/10.1021/acs.jpclett.6c01930openalex-snapshot

Multipathway Aggregation Drives Concentration-Dependent Amyloid Polymorphism and Time-Dependent Morphological Evolution

inferred← citeshttps://doi.org/10.1021/acs.jpclett.7b03442openalex-snapshot

What is Responsible for Atypical Dependence of the Rate of Amyloid Formation on Protein Concentration: Fibril-Catalyzed Initiation of New Fibrils or Competition with Oligomers?

inferred← citeshttps://doi.org/10.1021/acs.jpclett.8b00815openalex-snapshot

A Natively Monomeric Deubiquitinase UCH-L1 Forms Highly Dynamic but Defined Metastable Oligomeric Folding Intermediates

inferred← citeshttps://doi.org/10.1021/acs.jpclett.8b02375openalex-snapshot

Molecular Determinants of Aβ 42 Adsorption to Amyloid Fibril Surfaces

inferred← citeshttps://doi.org/10.1021/acs.jpclett.9b00423openalex-snapshot

Multiscale Aggregation of the Amyloid Aβ16–22 Peptide: From Disordered Coagulation and Lateral Branching to Amorphous Prefibrils

inferred← citeshttps://doi.org/10.1021/acs.jpclett.9b01050openalex-snapshot

Reorientational Dynamics of Amyloid-β from NMR Spin Relaxation and Molecular Simulation

inferred← citeshttps://doi.org/10.1021/acs.langmuir.3c02923openalex-snapshot

Protein Corona Formation and Aggregation of Amyloid β 1–40-Coated Gold Nanocolloids

inferred← citeshttps://doi.org/10.1021/acs.langmuir.6b00704openalex-snapshot

Supramolecular Nanostructure Formation of Coassembled Amyloid Inspired Peptides

inferred← citeshttps://doi.org/10.1021/acs.langmuir.7b02744openalex-snapshot

Kinetics of Surface-Mediated Fibrillization of Amyloid-β (12–28) Peptides

inferred← citeshttps://doi.org/10.1021/acs.langmuir.8b00254openalex-snapshot

Bifunctionality of Iminodiacetic Acid-Modified Lysozyme on Inhibiting Zn 2+ -Mediated Amyloid β-Protein Aggregation

inferred← citeshttps://doi.org/10.1021/acs.nanolett.6c02842openalex-snapshot

Real-Time Single Molecule Imaging Reveals Pathway-Selective Action of Aducanumab on Amyloid-β Aggregation

inferred← citeshttps://doi.org/10.1021/acsami.4c11542openalex-snapshot

Formation of Nanofibrillar Self-Healing Hydrogels Using Antimicrobial Peptides

inferred← citeshttps://doi.org/10.1021/acsami.5c20362openalex-snapshot

Chemical Strategies to Modulate Amyloidogenesis Associated with Neurodegenerative Diseases

inferred← citeshttps://doi.org/10.1021/acsami.8b01917openalex-snapshot

Lipid-Modified Graphene-Transistor Biosensor for Monitoring Amyloid-β Aggregation

inferred← citeshttps://doi.org/10.1021/acsbiomedchemau.6c00061openalex-snapshot

Fine-Tuning hIAPP Amyloidogenesis: Probing Molecular Mechanisms via Fluorinated Core Substitutions

inferred← citeshttps://doi.org/10.1021/acscentsci.5c00614openalex-snapshot

Recruitment of Aβ into α-Synuclein Condensates Catalyzes Primary Nucleation of α-Synuclein Aggregation

inferred← citeshttps://doi.org/10.1021/acschembio.2c00344openalex-snapshot

Amyloid Fibril Formation of Arctic Amyloid‑β 1–42 Peptide is Efficiently Inhibited by the BRICHOS Domain

inferred← citeshttps://doi.org/10.1021/acschembio.9b00324openalex-snapshot

The Toxicity of Misfolded Protein Oligomers Is Independent of Their Secondary Structure

inferred← citeshttps://doi.org/10.1021/acschemneuro.0c00110openalex-snapshot

Dissecting the Structural Organization of Multiprotein Amyloid Aggregates Using a Bottom-Up Approach

inferred← citeshttps://doi.org/10.1021/acschemneuro.0c00163openalex-snapshot

Structural Characteristics of Monomeric Aβ42 on Fibril in the Early Stage of Secondary Nucleation Process

inferred← citeshttps://doi.org/10.1021/acschemneuro.0c00300openalex-snapshot

Fast Purification of Recombinant Monomeric Amyloid-β from E. coli and Amyloid-β-mCherry Aggregates from Mammalian Cells

inferred← citeshttps://doi.org/10.1021/acschemneuro.0c00478openalex-snapshot

An α-Cyanostilbene Derivative for the Enhanced Detection and Imaging of Amyloid Fibril Aggregates

inferred← citeshttps://doi.org/10.1021/acschemneuro.1c00072openalex-snapshot

Pulsed Hydrogen–Deuterium Exchange Reveals Altered Structures and Mechanisms in the Aggregation of Familial Alzheimer’s Disease Mutants

inferred← citeshttps://doi.org/10.1021/acschemneuro.1c00454openalex-snapshot

Proliferation of Tau 304–380 Fragment Aggregates through Autocatalytic Secondary Nucleation

inferred← citeshttps://doi.org/10.1021/acschemneuro.1c00784openalex-snapshot

Taylor Dispersion Analysis and Atomic Force Microscopy Provide a Quantitative Insight into the Aggregation Kinetics of Aβ (1–40)/Aβ (1–42) Amyloid Peptide Mixtures

inferred← citeshttps://doi.org/10.1021/acschemneuro.2c00411openalex-snapshot

Simple, Reliable Protocol for High-Yield Solubilization of Seedless Amyloid-β Monomer

inferred← citeshttps://doi.org/10.1021/acschemneuro.2c00504openalex-snapshot

Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation

inferred← citeshttps://doi.org/10.1021/acschemneuro.3c00044openalex-snapshot

Molecular Mechanisms of Amyloid-β Self-Assembly Seeded by In Vivo-Derived Fibrils and Inhibitory Effects of the BRICHOS Chaperone

inferred← citeshttps://doi.org/10.1021/acschemneuro.3c00655openalex-snapshot

Extracellular Vesicles Slow Down Aβ(1–42) Aggregation by Interfering with the Amyloid Fibril Elongation Step

inferred← citeshttps://doi.org/10.1021/acschemneuro.4c00127openalex-snapshot

Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces

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