Evidence map›Paper›PMID 31395906›Full record

ArticleScientific reports2019

Protein Complex Identification and quantitative complexome by CN-PAGE.

Michal Gorka, Corné Swart, Beata Siemiatkowska, Silvia Martínez-Jaime, Aleksandra Skirycz, Sebastian Streb, Alexander Graf

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Pooled it
  2. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Complexome Profiling: Assembly and Remodeling of Protein Complexes.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. 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

7 authors at 2 institutions in 2 countries.

Michal GorkaMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany. gorka@mpimp-golm.mpg.de.
Corné SwartMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany.
Beata SiemiatkowskaMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany.
Silvia Martínez-JaimeMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany.
Aleksandra SkiryczMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany.
Sebastian StrebFunctional Genomics Center Zurich, ETH Zurich, Winterthurerstr. 190, 8057, Zürich, Switzerland.
Alexander GrafMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany.
Max Planck Institute of Molecular Plant Physiology · DEETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The majority of cellular processes are carried out by protein complexes. Various size fractionation methods have previously been combined with mass spectrometry to identify protein complexes. However, most of these approaches lack the quantitative information which is required to understand how changes of protein complex abundance and composition affect metabolic fluxes. In this paper we present a proof of concept approach to quantitatively study the complexome in the model plant Arabidopsis thaliana at the end of the day (ED) and the end of the night (EN). We show that size-fractionation of native protein complexes by Clear-Native-PAGE (CN-PAGE), coupled with mass spectrometry can be used to establish abundance profiles along the molecular weight gradient. Furthermore, by deconvoluting complex protein abundance profiles, we were able to drastically improve the clustering of protein profiles. To identify putative interaction partners, and ultimately protein complexes, our approach calculates the Euclidian distance between protein profile pairs. Acceptable threshold values are based on a cut-off that is optimized by a receiver-operator characteristic (ROC) curve analysis. Our approach shows low technical variation and can easily be adapted to study in the complexome in any biological system.

Indexed as

ProteomicsArabidopsisArabidopsis ProteinsElectrophoresis, Polyacrylamide GelGene Expression Regulation, PlantMass SpectrometryMitochondriaMultiprotein ComplexesNative Polyacrylamide Gel ElectrophoresisArabidopsis ProteinsMultiprotein Complexes

Identifiers

PMID31395906
PMCPMC6687828
OpenAlexW2964649769

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.