ReviewAnnual review of analytical chemistry (Palo Alto, Calif.)2017
The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein.
Review in Annual review of analytical chemistry (Palo Alto, Calif.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed.
- Article
- IR Action Spectroscopy of Mass- and Mobility-Selected α-Synuclein Segments: Structure Identification in Early-Stage Oligomers via the Amide A Region.The journal of physical chemistry. A · 2025Article
- Article
- Charge Detection Mass Spectrometry Reveals Conformational Heterogeneity in Megadalton-Sized Monoclonal Antibody Aggregates.Journal of the American Chemical Society · 2024Article
- Insights into conformational ensembles of compositionally identical disordered peptidomimetics.Polymer 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
- Gas-Phase Unfolding of Protein Complexes Distinguishes Conformational Isomers.Journal of the American Chemical Society · 2022Article
- Mechanistic insights into accelerated α-synuclein aggregation mediated by human microbiome-associated functional amyloids.The Journal of biological chemistry · 2022Article
- Tandem-trapped ion mobility spectrometry/mass spectrometry (The Analyst · 2022Review
- Reassembling protein complexes after controlled disassembly by top-down mass spectrometry in native mode.International journal of mass spectrometry · 2021Article
- Trapped Ion Mobility Spectrometry of Native Macromolecular Assemblies.Analytical chemistry · 2021Article
- Polyphenols as Potential Metal Chelation Compounds Against Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2021Review
- Evidence for Many Unique Solution Structures for Chymotrypsin Inhibitor 2: A Thermodynamic Perspective Derived from vT-ESI-IMS-MS Measurements.Journal of the American Chemical Society · 2020Article
- First-Principles Collision Cross Section Measurements of Large Proteins and Protein Complexes.Analytical chemistry · 2020Article
- Topological Characterization of Coordination-Driven Self-assembly Complexes: Applications of Ion Mobility-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- On the Preservation of Non-covalent Peptide Assemblies in a Tandem-Trapped Ion Mobility Spectrometer-Mass Spectrometer (TIMS-TIMS-MS).Journal of the American Society for Mass Spectrometry · 2019Article
- Fibril formation and therapeutic targeting of amyloid-like structures in a yeast model of adenine accumulation.Nature communications · 2019Article
- Conformational investigation of the structure-activity relationship of GdFFD and its analogues on an achatin-like neuropeptide receptor of Aplysia californica involved in the feeding circuit.Physical chemistry chemical physics : PCCP · 2018Article
- The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes.Current opinion in chemical biology · 2018Review
- Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations.Open biology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Ion mobility spectrometry-mass spectrometry (IMS-MS) methods are increasingly used to study noncovalent assemblies of peptides and proteins. This review focuses on the noncovalent self-assembly of amino acids and peptides, systems at the heart of the amyloid process that play a central role in a number of devastating diseases. Three different systems are discussed in detail: the 42-residue peptide amyloid-β42 implicated in the etiology of Alzheimer's disease, several amyloid-forming peptides with 6-11 residues, and the assembly of individual amino acids. We also discuss from a more fundamental perspective the processes that determine how quickly proteins and their assemblies denature when the analyte ion has been stripped of its solvent in an IMS-MS measurement and how to soften the measurement so that biologically meaningful data can be recorded.
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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.