ArticleJournal of the American Society for Mass Spectrometry2010
Mass spectrometry and the amyloid problem--how far can we go in the gas phase?
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed.
- Article
- Probing High-Order Transient Oligomers Using Ion Mobility Mass Spectrometry Coupled with Infrared Action Spectroscopy.Analytical chemistry · 2024Article
- Developments in Trapped Ion Mobility Mass Spectrometry to Probe the Early Stages of Peptide Aggregation.Journal of the American Society for Mass Spectrometry · 2023Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Structural Heterogeneity in the Preamyloid Oligomers of β-2-Microglobulin.Journal of molecular biology · 2020Article
- Ion mobility spectrometry combined with multivariate statistical analysis: revealing the effects of a drug candidate for Alzheimer's disease on Aβ1-40 peptide early assembly.Analytical and bioanalytical chemistry · 2019Article
- Formation of Neutral Peptide Aggregates as Studied by Mass-Selective IR Action Spectroscopy.Angewandte Chemie (International ed. in English) · 2019Article
- 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
- Addressing a Common Misconception: Ammonium Acetate as Neutral pH "Buffer" for Native Electrospray Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Probing the Time Scale of FPOP (Fast Photochemical Oxidation of Proteins): Radical Reactions Extend Over Tens of Milliseconds.Journal of the American Society for Mass Spectrometry · 2016Article
- Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.The Journal of biological chemistry · 2016Article
- Ion Mobility-Mass Spectrometry Differentiates Protein Quaternary Structures Formed in Solution and in Electrospray Droplets.Analytical chemistry · 2015Article
- Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion.Molecular & cellular proteomics : MCP · 2015Article
- 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
- The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics.Nature chemistry · 2014Review
- Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry.Molecular bioSystems · 2014Article
- Article
- Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Biochimica et biophysica acta · 2013Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
A number of proteins are capable of converting from their soluble, monomeric form into highly-ordered, insoluble aggregates known as amyloid fibrils. In vivo, these fibrils, which accumulate in organs and tissues, are associated with a wide range of amyloid diseases for which there are currently no therapeutic solutions. The molecular details of the pathway from native monomer through oligomeric intermediates to the final amyloid fibril remain a challenging enigma. Over the past few years, mass spectrometry has been applied to investigate the various stages of amyloid fibril formation, and this report summarizes the key steps achieved to date.
Indexed as
Identifiers
20363648What 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.