ArticleAnalytical chemistry2019
Topological Analysis of Transthyretin Disassembly Mechanism: Surface-Induced Dissociation Reveals Hidden Reaction Pathways.
Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed.
- Solution Phase Protein Dynamics: Influences of ESI Buffers on Hydration.Analytical chemistry · 2026Article
- On the Utility of Infrared Photoactivation for Native Top-Down and Complex-Down Orbitrap Mass Spectrometry of Soluble Proteoform Complexes.Journal of the American Society for Mass Spectrometry · 2026Article
- Time-Resolved Study of In Situ Generated Protein Subcomplexes by Tandem-Trapped Ion Mobility Spectrometry.Journal of mass spectrometry : JMS · 2026Article
- Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology.Analytical chemistry · 2025Article
- Hydration (HJournal of the American Chemical Society · 2025Article
- Structure and Stabilities of Solution and Gas Phase Protein Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- Water Plays Key Roles in Stabilities of Wild Type and Mutant Transthyretin Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Probing the Dissociation Pathway of a Kinetically Labile Transthyretin Mutant.Journal of the American Chemical Society · 2024Article
- Elucidating Structures of Protein Complexes by Collision-Induced Dissociation at Elevated Gas Pressures.Journal of the American Society for Mass Spectrometry · 2023Article
- Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions.Annual review of biophysics · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Implementing Digital-Waveform Technology for ExtendedJournal of the American Society for Mass Spectrometry · 2021Article
- Surface-induced dissociation of protein complexes on a cyclic ion mobility spectrometer.The Analyst · 2021Article
- THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY-MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021Review
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
- First-Principles Collision Cross Section Measurements of Large Proteins and Protein Complexes.Analytical chemistry · 2020Article
- Structural Analysis of the Effect of a Dual-FLAG Tag on Transthyretin.Biochemistry · 2020Article
- Native IM-Orbitrap MS: Resolving What Was Hidden.Trends in analytical chemistry : TRAC · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The proposed mechanism of fibril formation of transthyretin (TTR) involves self-assembly of partially unfolded monomers. However, the mechanism(s) of disassembly to monomer and potential intermediates involved in this process are not fully understood. In this study, native mass spectrometry and surface-induced dissociation (SID) are used to investigate the TTR disassembly mechanism(s) and the effects of temperature and ionic strength on the kinetics of TTR complex formation. Results from the SID of hybrid tetramers formed during subunit exchange provide strong evidence for a two-step mechanism whereby the tetramer dissociates to dimers that then dissociate to monomers. Also, the SID results uncovered a hidden pathway in which a specific topology of the hybrid tetramer is directly produced by assembly of dimers in the early steps of TTR disassembly. Implementation of SID to dissect protein topology during subunit exchange provides unique opportunities to gain unparalleled insight into disassembly pathways.
Indexed as
Identifiers
What OpenQuestion holds
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.