Evidence map›Paper›PMID 32608033›Full record

ReviewMass spectrometry reviews2021

THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY-MASS SPECTROMETRY.

Jacob W McCabe, Michael J Hebert, Mehdi Shirzadeh, Christopher S Mallis, Joanna K Denton, Thomas E Walker, David H Russell

Open access · greenAbstract readReview
In one paragraph

Review in Mass spectrometry reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  12. Modified Ion Source for the Improved Collisional Activation of Protein Complexes.Journal of the American Society for Mass Spectrometry · 2023
    Article
  13. Article
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  18. Review
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  20. Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022
    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

7 authors at 1 institution in 1 country.

Jacob W McCabeDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
Michael J HebertDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
Mehdi ShirzadehDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
Christopher S MallisDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
Joanna K DentonDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
Thomas E WalkerDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
David H RussellDepartment of Chemistry, Texas A&M University, College Station, TX, 77843.
Texas A&M University · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid bindingDP2GM123486 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI LAGANOWSKY, ARTHUR D · 2016 to 2016
$2.2M
Development of high resolution mobility measurements for structural biologyR01GM121751 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., LAGANOWSKY, ARTHUR D · 2017 to 2020
$1.7M
NIGMS NIH HHS DP2 GM123486NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM121751
6 · The paper itself

Abstract

Studies of large proteins, protein complexes, and membrane protein complexes pose new challenges, most notably the need for increased ion mobility (IM) and mass spectrometry (MS) resolution. This review covers evolutionary developments in IM-MS in the authors' and key collaborators' laboratories with specific focus on developments that enhance the utility of IM-MS for structural analysis. IM-MS measurements are performed on gas phase ions, thus "structural IM-MS" appears paradoxical-do gas phase ions retain their solution phase structure? There is growing evidence to support the notion that solution phase structure(s) can be retained by the gas phase ions. It should not go unnoticed that we use "structures" in this statement because an important feature of IM-MS is the ability to deal with conformationally heterogeneous systems, thus providing a direct measure of conformational entropy. The extension of this work to large proteins and protein complexes has motivated our development of Fourier-transform IM-MS instruments, a strategy first described by Hill and coworkers in 1985 (Anal Chem, 1985, 57, pp. 402-406) that has proved to be a game-changer in our quest to merge drift tube (DT) and ion mobility and the high mass resolution orbitrap MS instruments. DT-IMS is the only method that allows first-principles determinations of rotationally averaged collision cross sections (CSS), which is essential for studies of biomolecules where the conformational diversities of the molecule precludes the use of CCS calibration approaches. The Fourier transform-IM-orbitrap instrument described here also incorporates the full suite of native MS/IM-MS capabilities that are currently employed in the most advanced native MS/IM-MS instruments. © 2020 John Wiley & Sons Ltd. Mass Spec Rev.

Indexed as

Fourier AnalysisMass SpectrometryPeptidesProtein ConformationProtein FoldingProteinsProtein StabilitySolventsSpectrometry, Mass, Electrospray IonizationUbiquitinWaterPeptidesProteinsSolventsUbiquitinWater1st principles CCSconformational heterogeneitycryogenic ion-mobility MSdrift tube ion mobilitynative MS/IM-MSorbitrap MS

Identifiers

PMID32608033
PMCPMC7989064
OpenAlexW3039382236

What OpenQuestion holds

Textmetadata
LicenceTDM
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.