Evidence map›Paper›PMID 30887461›Full record

ArticleJournal of the American Society for Mass Spectrometry2019

Generation of Charge-Reduced Ions of Membrane Protein Complexes for Native Ion Mobility Mass Spectrometry Studies.

John W Patrick, Arthur Laganowsky

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

26 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. To 200,000ACS central science · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Implementing Digital-Waveform Technology for ExtendedJournal of the American Society for Mass Spectrometry · 2021
    Article
  20. Review
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

2 authors at 1 institution in 1 country.

John W PatrickDepartment of Chemistry, Texas A&M University, College Station, TX, 77842, USA.
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, TX, 77842, USA. ALaganowsky@chem.tamu.edu.ORCID http://orcid.org/0000-0001-5012-5547
Texas A&M University · US

Funding

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
National Institute of General Medical Sciences DP2GM123486NIGMS NIH HHS DP2 GM123486
6 · The paper itself

Abstract

Recent advances in native mass spectrometry (MS) have enabled the elucidation of how small molecule binding to membrane proteins modulates their structure and function. The protein-stabilizing osmolyte, trimethylamine oxide (TMAO), exhibits attractive properties for native MS studies. Here, we report significant charge reduction, nearly threefold, for three membrane protein complexes in the presence of this osmolyte without compromising mass spectral resolution. TMAO improves the ability to resolve individual lipid-binding events to the ammonia channel (AmtB) by over 200% compared to typical native conditions. The generation of ions with compact structure and access to a larger number of lipid-binding events through the incorporation of TMAO increases the utility of IM-MS for structural biology studies. Graphical Abstract.

Indexed as

AquaporinsBacterial ProteinsCation Transport ProteinsEscherichia coliEscherichia coli ProteinsExcipientsIon ChannelsIon Mobility SpectrometryIonsMethylaminesMycobacterium tuberculosisProtein ConformationAmtB protein, E coliaqpZ protein, E coliAquaporinsBacterial ProteinsCation Transport ProteinsEscherichia coli ProteinsExcipientsIon ChannelsIonsMethylaminesTb-MscL protein, Mycobacterium tuberculosistrimethyloxamineIon mobilityLipidMembrane proteinNative mass spectrometry

Identifiers

PMID30887461
PMCPMC6504596
OpenAlexW2921184407

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.