Evidence map›Paper›PMID 36347042›Full record

ArticleAnalytical chemistry2022

High-Field Asymmetric Waveform Ion Mobility Spectrometry Interface Enhances Parallel Reaction Monitoring on an Orbitrap Mass Spectrometer.

Weixian Deng, Jihui Sha, Fanglei Xue, Yasaman Jami-Alahmadi, Kathrin Plath, James Wohlschlegel

Abstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Enhanced Sample Multiplexing-Based Targeted Proteomics with Intelligent Data Acquisition.Journal of the American Society for Mass Spectrometry · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Weixian DengDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095, United States.ORCID 0000-0003-2597-2255
Jihui ShaDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095, United States.
Fanglei XueUniversity of Technology Sydney, Ultimo, New South Wales 2007, Australia.
Yasaman Jami-AlahmadiDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095, United States.
Kathrin PlathDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095, United States.
James WohlschlegelDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095, United States.ORCID 0000-0003-3399-901X

Funding

Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
Biogenesis of Extramitochondrial Iron-Sulfur Proteins in EukaryotesR01GM112763 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2015 to 2018
$982k
NIGMS NIH HHS R01 GM089778NIGMS NIH HHS R01 GM112763
6 · The paper itself

Abstract

High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables gas-phase separations on a chromatographic time scale and has become a useful tool for proteomic applications. Despite its emerging utility, however, the molecular determinants underlying peptide separation by FAIMS have not been systematically investigated. Here, we characterize peptide transmission in a FAIMS device across a broad range of compensation voltages (CVs) and used machine learning to identify charge state and three-dimensional (3D) electrostatic peptide potential as major contributors to peptide intensity at a given CV. We also demonstrate that the machine learning model can be used to predict optimized CV values for peptides, which significantly improves parallel reaction monitoring workflows. Together, these data provide insight into peptide separation by FAIMS and highlight its utility in targeted proteomic applications.

Indexed as

Ion Mobility SpectrometryProteomicsMass SpectrometryPeptidesPeptides

Identifiers

PMID36347042
PMCPMC9685594

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.