Evidence map›Paper›PMID 30225732›Full record

ArticleJournal of the American Society for Mass Spectrometry2019

LILBID and nESI: Different Native Mass Spectrometry Techniques as Tools in Structural Biology.

Oliver Peetz, Nils Hellwig, Erik Henrich, Julija Mezhyrova, Volker Dötsch, Frank Bernhard, Nina Morgner

Erratum issuedOpen access · bronzeAbstract 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. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Two conformations of the Tom20 preprotein receptor in the TOM holo complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
    Review
  9. Review
  10. Microbiome research reports · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Deconvolving Native and Intact Protein Mass Spectra with UniDec.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Assembly and regulation of the chlorhexidine-specific efflux pump AceI.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Oliver PeetzInstitute of Physical and Theoretical Chemistry, J.W. Goethe-University, Frankfurt am Main, Germany.
Nils HellwigInstitute of Physical and Theoretical Chemistry, J.W. Goethe-University, Frankfurt am Main, Germany.
Erik HenrichInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J.W. Goethe-University, Frankfurt am Main, Germany.
Julija MezhyrovaInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J.W. Goethe-University, Frankfurt am Main, Germany.
Volker DötschInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J.W. Goethe-University, Frankfurt am Main, Germany.
Frank BernhardInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J.W. Goethe-University, Frankfurt am Main, Germany.
Nina MorgnerInstitute of Physical and Theoretical Chemistry, J.W. Goethe-University, Frankfurt am Main, Germany. morgner@chemie.uni-frankfurt.de.ORCID http://orcid.org/0000-0002-1872-490X
Goethe University Frankfurt · DE

Funding

Cluster of Excellence Frankfurt Macromolecular ComplexesDeutsche Forschungsgemeinschaft SFB807European Research Council 337567
6 · The paper itself

Abstract

Native mass spectrometry is applied for the investigation of proteins and protein complexes worldwide. The challenge in native mass spectrometry is maintaining the features of the proteins of interest, such as oligomeric state, bound ligands, or the conformation of the protein complex, during transfer from solution to gas phase. This is an essential prerequisite to allow conclusions about the solution state protein complex, based on the gas phase measurements. Therefore, soft ionization techniques are required. Widely used for the analysis of protein complexes are nanoelectro spray ionization (nESI) mass spectrometers. A newer ionization method is laser induced liquid bead ion desorption (LILBID), which is based on the release of protein complexes from solution phase via infrared (IR) laser desorption. We use both methods in our lab, depending on the requirements of the biological system we are interested in. Here we benchmark the performance of our LILBID mass spectrometer in comparison to a nESI instrument, regarding sample conditions, buffer and additive tolerances, dissociation mechanism and applicability towards soluble and membrane protein complexes. Graphical Abstract ᅟ.

Indexed as

AntiportersAvidinBacterial ProteinsBuffersDetergentsEscherichia coli ProteinsGlycerolLasersMass SpectrometryMembrane ProteinsPotassium ChannelsSpectrometry, Mass, Electrospray IonizationAntiportersAvidinBacterial ProteinsBuffersDetergentsEmrE protein, E coliEscherichia coli ProteinsGlycerolMembrane ProteinsPotassium Channelsprokaryotic potassium channelIon sourceLILBIDMembrane proteinsNative mass spectrometrynESISoluble proteins

Identifiers

PMID30225732
PMCPMC6318263
OpenAlexW2890868428

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.