ArticleJournal of the American Society for Mass Spectrometry2016
Examining the Influence of Phosphorylation on Peptide Ion Structure by Ion Mobility Spectrometry-Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed.
- Mass spectrometry structural analysis of intrinsically disordered phosphoproteins.International journal of mass spectrometry · 2025Article
- Peptide collision cross sections of 22 post-translational modifications.Analytical and bioanalytical chemistry · 2023Article
- Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond.Chemical communications (Cambridge, England) · 2023Review
- Influence of N Terminus Amino Acid on Peptide Cleavage in Solution through Diketopiperazine Formation.Journal of the American Society for Mass Spectrometry · 2022Article
- Diketopiperazine Formation from FPGThe journal of physical chemistry. B · 2021Article
- Deep learning the collisional cross sections of the peptide universe from a million experimental values.Nature communications · 2021Article
- Effect of Phosphorylation on the Collision Cross Sections of Peptide Ions in Ion Mobility Spectrometry.Mass spectrometry (Tokyo, Japan) · 2021Article
- Trapped Ion Mobility Spectrometry and Parallel Accumulation-Serial Fragmentation in Proteomics.Molecular & cellular proteomics : MCP · 2021Review
- Global Phosphoproteome Analysis Using High-Field Asymmetric Waveform Ion Mobility Spectrometry on a Hybrid Orbitrap Mass Spectrometer.Analytical chemistry · 2020Article
- diaPASEF: parallel accumulation-serial fragmentation combined with data-independent acquisition.Nature methods · 2020Article
- Native Top-Down Mass Spectrometry and Ion Mobility Spectrometry of the Interaction of Tau Protein with a Molecular Tweezer Assembly Modulator.Journal of the American Society for Mass Spectrometry · 2019Article
- Linear and Differential Ion Mobility Separations of Middle-Down Proteoforms.Analytical chemistry · 2018Article
- Benchmark Comparison for a Multi-Processing Ion Mobility Calculator in the Free Molecular Regime.Journal of the American Society for Mass Spectrometry · 2017Article
- A Priori Intrinsic PTM Size Parameters for Predicting the Ion Mobilities of Modified Peptides.Journal of the American Society for Mass Spectrometry · 2017Article
- Localization of Post-Translational Modifications in Peptide Mixtures via High-Resolution Differential Ion Mobility Separations Followed by Electron Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Ion mobility spectrometry-mass spectrometry (IMS-MS) techniques are used to study the general effects of phosphorylation on peptide structure. Cross sections for a library of 66 singly phosphorylated peptide ions from 33 pairs of positional isomers, and unmodified analogues were measured. Intrinsic size parameters (ISPs) derived from these measurements yield calculated collision cross sections for 85% of these phosphopeptide sequences that are within ±2.5% of experimental values. The average ISP for the phosphoryl group (0.64 ± 0.05) suggests that in general this moiety forms intramolecular interactions with the neighboring residues and peptide backbone, resulting in relatively compact structures. We assess the capability of ion mobility to separate positional isomers (i.e., peptide sequences that differ only in the location of the modification) and find that more than half of the isomeric pairs have >1% difference in collision cross section. Phosphorylation is also found to influence populations of structures that differ in the cis/trans orientation of Xaa-Pro peptide bonds. Several sequences with phosphorylated Ser or Thr residues located N-terminally adjacent to Pro residues show fewer conformations compared to the unmodified sequences.
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.