Evidence map›Paper›PMID 28485388›Full record

ArticleNature communications2017

Charting organellar importomes by quantitative mass spectrometry.

Christian D Peikert, Jan Mani, Marcel Morgenstern, Sandro Käser, Bettina Knapp, Christoph Wenger, Anke Harsman, Silke Oeljeklaus, André Schneider, Bettina Warscheid

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  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. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors.

Christian D PeikertFaculty of Biology, Department of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.ORCID 0000-0002-0187-3650
Jan ManiDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Marcel MorgensternFaculty of Biology, Department of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.
Sandro KäserDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Bettina KnappFaculty of Biology, Department of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.
Christoph WengerDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Anke HarsmanDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Silke OeljeklausFaculty of Biology, Department of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.
André SchneiderDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Bettina WarscheidFaculty of Biology, Department of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.

Funding

European Research Council 648235
6 · The paper itself

Abstract

Protein import into organelles is essential for all eukaryotes and facilitated by multi-protein translocation machineries. Analysing whether a protein is transported into an organelle is largely restricted to single constituents. This renders knowledge about imported proteins incomplete, limiting our understanding of organellar biogenesis and function. Here we introduce a method that enables charting an organelle's importome. The approach relies on inducible RNAi-mediated knockdown of an essential subunit of a translocase to impair import and quantitative mass spectrometry. To highlight its potential, we established the mitochondrial importome of Trypanosoma brucei, comprising 1,120 proteins including 331 new candidates. Furthermore, the method allows for the identification of proteins with dual or multiple locations and the substrates of distinct protein import pathways. We demonstrate the specificity and versatility of this ImportOmics method by targeting import factors in mitochondria and glycosomes, which demonstrates its potential for globally studying protein import and inventories of organelles.

Indexed as

Amino Acyl-tRNA SynthetasesGene Knockdown TechniquesMass SpectrometryMicrobodiesMitochondriaMitochondrial MembranesMitochondrial ProteinsProtein TransportProteomeProtozoan ProteinsSubstrate SpecificityTrypanosoma brucei bruceiAmino Acyl-tRNA SynthetasesMitochondrial ProteinsProteomeProtozoan Proteins

Identifiers

PMID28485388
PMCPMC5436138

What Socratic 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 Socratic graph.