Evidence map›Paper›PMID 26692813›Full record

ArticleInternational journal of mass spectrometry2015

Probing Asymmetric Charge Partitioning of Protein Oligomers during Tandem Mass Spectrometry.

Philip D Compton, Luca Fornelli, Neil L Kelleher, Owen S Skinner

Abstract read
In one paragraph

Article in International journal of mass spectrometry, 2015. 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. Review
  4. Article
  5. Article
  6. Unfolding and Folding of the Three-Helix Bundle Protein KIX in the Absence of Solvent.Journal of the American Society for Mass Spectrometry · 2016
    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

4 authors.

Philip D ComptonDepartments of Chemistry and Molecular Biosciences and the Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, USA.
Luca FornelliDepartments of Chemistry and Molecular Biosciences and the Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, USA.
Neil L KelleherDepartments of Chemistry and Molecular Biosciences and the Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, USA.
Owen S SkinnerDepartments of Chemistry and Molecular Biosciences and the Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, USA.

Funding

Eukaryotic Post-Translational ModificationsR01GM067193 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2015
$4.0M
NIGMS NIH HHS R01 GM067193
6 · The paper itself

Abstract

Dissociation of gaseous protein complexes produced by native electrospray often induces an asymmetric partitioning of charge between ejected subunits. We present a simple asymmetric charge partitioning factor (ACPF) to quantify the magnitude of asymmetry in this effect. When applied to monomer ejection from the cytochrome c dimer and β-amylase tetramer, we found that the ~60-70% of precursor charge ending up in the ejected monomers corresponds to ACPFs of 1.38 and 2.51, respectively. Further, we used site-specific fragmentation from electron transfer dissociation (ETD) to identify differences in fragmentation and characterize domains of secondary-structure present in the dimer, ejected monomers, and monomers obtained directly from electrospray ionization (ESI). We found evidence of structural changes between the dimer and ejected monomer, but also that the ejected monomer had a nearly identical set of fragment ions produced by ETD as the ESI monomer with the same charge state. Surprisingly, APCF values for ETD fragment ions generated directly from the dimer revealed that the fragments undergo asymmetric charge partitioning at over twice the magnitude of that observed for ejection of the monomer.

Indexed as

asymmetric charge partitioningelectron transfer dissociationprotein complexesproteomics

Identifiers

PMID26692813
PMCPMC4673687

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Registered trials

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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.