Evidence map›Paper›PMID 39957060›Full record

ArticleAnalytical chemistry2025

Adapting a Trapped Ion Mobility Spectrometry-Q-TOF for High

Yu-Fu Lin, Benjamin J Jones, Mark E Ridgeway, Erin M Panczyk, Arpad Somogyi, Desmond A Kaplan, Ila Marathe, Sangho Yun, Karen A Kirby, Stefan G Sarafianos and 3 more

Abstract read
In one paragraph

Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Collision-Induced Unfolding of High-Journal of the American Society for Mass Spectrometry · 2025
    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

13 authors.

Yu-Fu LinDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0003-0476-5193
Benjamin J JonesBruker Daltonics Inc., Billerica, Massachusetts 01821, United States.
Mark E RidgewayBruker Daltonics Inc., Billerica, Massachusetts 01821, United States.
Erin M PanczykBruker Daltonics Inc., Billerica, Massachusetts 01821, United States.ORCID 0000-0003-3779-6738
Arpad SomogyiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
Desmond A KaplanKapScience LLC, Tewksbury, Massachusetts 01876, United States.ORCID 0000-0003-3597-1547
Ila MaratheDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
Sangho YunDepartment of Chemistry, Texas A&M University, College Station, Texas 77840, United States.
Karen A KirbyCenter for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine and Children's Healthcare of Atlanta, Atlanta, Georgia 30307 United States.ORCID 0000-0003-2468-4796
Stefan G SarafianosCenter for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine and Children's Healthcare of Atlanta, Atlanta, Georgia 30307 United States.
Arthur D LaganowskyDepartment of Chemistry, Texas A&M University, College Station, Texas 77840, United States.ORCID 0000-0001-5012-5547
Melvin A ParkBruker Daltonics Inc., Billerica, Massachusetts 01821, United States.ORCID 0009-0004-1448-2896
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0003-0495-2538

Funding

Structural Biology CoreU54AI170855 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI Bruce Edward Torbett · 2022 to 2026
$36.7M
HBV Capsid EffectorsR01AI132833 · NIAID · EMORY UNIVERSITY · PI Raymond Felix Schinazi · 2017 to 2026
$5.3M
Native Mass Spectrometry Guided Structural Biology CenterRM1GM149374 · NIGMS · OHIO STATE UNIVERSITY · PI Vicki H. Wysocki · 2023 to 2026
$5.0M
NIAID NIH HHS R01 AI132833NIAID NIH HHS U54 AI170855NIGMS NIH HHS RM1 GM149374
6 · The paper itself

Abstract

Native mass spectrometry (nMS) is an increasingly popular technique for studying intact protein quaternary structure. When coupled with ion mobility, which separates ions based on their size, charge, and shape, it provides additional structural information on the protein complex of interest. We present here data from a novel prototype TIMS (trapped ion mobility spectrometry)-quadrupole-SID (surface-induced dissociation)-time of flight, TIMS-Q-SID-TOF, instrument for nMS. The modifications include changing the TIMS cartridge from concave to convex electrode geometry with a dual TIMS tunnel design and operating TIMS at 425 kHz radio frequency (RF) to improve the trapping efficiency for high mass-to-charge (

Indexed as

Ion Mobility SpectrometryMass SpectrometryChaperonin 60Hepatitis B virusSurface PropertiesChaperonin 60

Identifiers

PMID39957060
PMCPMC13054468

What OpenQuestion holds

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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.