Evidence map›Paper›PMID 25970171›Full record

ArticleProtein science : a publication of the Protein Society2015

Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment.

Albert Konijnenberg, Ludovic Bannwarth, Duygu Yilmaz, Armağan Koçer, Catherine Venien-Bryan, Frank Sobott

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. 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
1.9field-weighted citation impact, top 16% 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, 46 citations in OpenAlex.

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  18. Standard Proteoforms and Their Complexes for Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019
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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 at 4 institutions in 3 countries.

Albert KonijnenbergDepartment of Chemistry, Biomolecular & Analytical Mass Spectrometry group, University of Antwerp, Antwerp, Belgium.
Ludovic BannwarthBioinformatique et BioPhysique, Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie (IMPMC), Université Pierre et Marie Curie, Paris, France.
Duygu YilmazDepartment of Neuroscience, University of Groningen, Groningen, The Netherlands.
Armağan KoçerDepartment of Neuroscience, University of Groningen, Groningen, The Netherlands.
Catherine Venien-BryanBioinformatique et BioPhysique, Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie (IMPMC), Université Pierre et Marie Curie, Paris, France.
Frank SobottDepartment of Chemistry, Biomolecular & Analytical Mass Spectrometry group, University of Antwerp, Antwerp, Belgium.
Sorbonne Université · FRUniversity of Groningen · NLAntwerp Management School · BEProvince of Antwerp · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here we study the intact stoichiometry and top-down fragmentation behavior of three integral membrane proteins which were natively reconstituted into detergent micelles: the mechano-sensitive ion channel of large conductance (MscL), the Kirbac potassium channel and the p7 viroporin from the hepatitis C virus. By releasing the proteins under nondenaturing conditions inside the mass spectrometer, we obtained their oligomeric sizes. Increasing the ion activation (collision energy) causes unfolding and subsequent ejection of a highly charged monomer from the membrane protein complexes. Further increase of the ion activation then causes collision-induced dissociation (CID) of the ejected monomers, with fragments observed which were predominantly found to stem from membrane-embedded regions. These experiments show how in a single experiment, we can probe the relation between higher-order structure and protein sequence, by combining the native MS data with fragmentation obtained from top-down MS.

Indexed as

Amino Acid SequenceHepacivirusHepatitis CHumansIon ChannelsModels, MolecularMolecular Sequence DataPotassium ChannelsProtein MultimerizationSpectrometry, Mass, Electrospray IonizationViral ProteinsIon ChannelsPotassium ChannelsViral Proteinscollision-induced dissociationintegral membrane proteinsion channelsmass spectrometrytop-down sequencing

Identifiers

PMID25970171
PMCPMC4534180
OpenAlexW2115690303

What OpenQuestion holds

Textmetadata
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.