ArticleAnalytical chemistry2024
High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.
Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Accurate Sizing and Resolution of Nominal 200 nm Diameter Polystyrene Nanospheres With Charge Detection Mass Spectrometry.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Understanding the Aggregation Mechanism of and Developing Stabilization Strategies for Recombinant Fibroblast Growth Factor 2.Biomolecules · 2026Article
- Adeno-associated virus serotype 9 structural heterogeneity and stability characterized by charge detection mass spectrometry.Molecular therapy. Methods & clinical development · 2025Article
- Effects of Hydration on Transthyretin Conformational Dynamics and Oligomerization.Biochemistry · 2025Article
- Self-Assembly, Rearrangement, and Disassembly of {CrAngewandte Chemie (International ed. in English) · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Dissecting Hidden Liraglutide Oligomerization Pathways via Direct Mass Technology, Electron-Capture Dissociation, and Molecular Dynamics.Analytical chemistry · 2025Article
- Characterizing Monoclonal Antibody Aggregation Using Charge Detection Mass Spectrometry and Industry Standard Methods.Journal of the American Society for Mass Spectrometry · 2025Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Protein aggregation is involved in many human diseases, but characterizing the sizes and shapes of intermediate oligomers (∼10-100 nm) that are important to the formation of macroscale aggregates like amyloid fibrils is a significant analytical challenge. Here, charge detection mass spectrometry (CDMS) is used to characterize individual conformational states of bovine serum albumin oligomers with up to ∼225 molecules (15 MDa). Elongated, partially folded, and globular conformational families for each oligomer can be readily distinguished based on the extent of charging. The abundances of individual conformers vary with changes in the monomer concentration or by adding aggregation inhibitors, such as SDS, heparin, or MgCl
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