ArticleJournal of molecular biology2006
Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
56 citing papers in PubMed, 147 citations in OpenAlex.
- Unambiguous assignment of kinked-β sheets leads to insights into molecular grammar of reversibility in biomolecular condensates.Protein science : a publication of the Protein Society · 2025Article
- Computational Study of AmyloidβInorganic chemistry · 2024Article
- Generating Ensembles of Dynamic Misfolding Proteins.Frontiers in neuroscience · 2022Review
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- A game-theoretic approach to deciphering the dynamics of amyloid-Royal Society open science · 2020Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- His6, His13, and His14 residues in Aβ 1-40 peptide significantly and specifically affect oligomeric equilibria.Scientific reports · 2019Article
- Detection of Amyloid Beta (Aβ) Oligomeric Composition Using Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI MS).Journal of the American Society for Mass Spectrometry · 2018Article
- Side-chain moieties from the N-terminal region of Aβ are Involved in an oligomer-stabilizing network of interactions.PloS one · 2018Article
- Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Pharmaceutical research · 2017Review
- Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways.Scientific reports · 2017Article
- Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation.Journal of molecular biology · 2016Article
- pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Boundaries of mass resolution in native mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.PLoS computational biology · 2014Article
- Cation-induced stabilization of protein complexes in the gas phase: mechanistic insights from hemoglobin dissociation studies.Journal of the American Society for Mass Spectrometry · 2014Article
- Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry.Molecular bioSystems · 2014Article
- Interpretation and deconvolution of nanodisc native mass spectra.Journal of the American Society for Mass Spectrometry · 2014Article
- Article
- β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH.PloS one · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Numerous debilitating human disorders result from protein misfolding and amyloid formation. Despite the grave nature of these maladies, our understanding of the structural mechanism of fibril assembly is limited. Of paramount importance is the need to identify and characterize oligomeric species formed early during fibril assembly, so that the nature of the initiating assembly mechanism can be revealed and species that may be toxic to cells identified. However, the transient nature of early oligomeric species, combined with their heterogeneity and instability, has precluded detailed analysis to date. Here, we have used electrospray ionisation mass spectrometry (ESI-MS), complemented by analytical ultracentrifugation (AUC) and measurements of thioflavin-T fluorescence, to monitor the early stages of assembly of amyloid-like fibrils formed from human beta-2-microglobulin (beta2m) in vitro. We show that worm-like fibrils that form with nucleation-independent kinetics assemble by a mechanism consistent with monomer addition, with species ranging from monomer to > or = 13-mer being identified directly and uniquely as transient assembly intermediates. By contrast, only monomers, dimers, trimers and tetramers are observed during nucleated growth, which leads to the formation of long straight fibrils. The results highlight the unique power of non-covalent ESI-MS to identify protein assembly intermediates in complex heterogeneous systems and demonstrate its great potential to identify and characterise individual species formed early during amyloid assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.