Evidence map›Paper›PMID 21326212›Full record

ArticleThe EMBO journal2011

TIM23-mediated insertion of transmembrane α-helices into the mitochondrial inner membrane.

Salomé Calado Botelho, Marie Osterberg, Andreas S Reichert, Koji Yamano, Patrik Björkholm, Toshiya Endo, Gunnar von Heijne, Hyun Kim

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Efficient integration of transmembrane domains depends on the folding properties of the upstream sequences.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Molecular insights into theThe Journal of biological chemistry · 2017
    Article
  9. Review
  10. Article
  11. Article
  12. Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

8 authors at 4 institutions in 4 countries.

Salomé Calado BotelhoDepartment of Biochemistry and Biophysics, Center for Biomembrane Research, Stockholm University, Stockholm, Sweden.
Marie Osterberg
Andreas S Reichert
Koji Yamano
Patrik Björkholm
Toshiya Endo
Gunnar von Heijne
Hyun Kim
Stockholm University · SENagoya University · JPFrankfurt Institute for Advanced Studies · DEScience for Life Laboratory · SE

Funding

European Research Council 232648
6 · The paper itself

Abstract

While overall hydrophobicity is generally recognized as the main characteristic of transmembrane (TM) α-helices, the only membrane system for which there are detailed quantitative data on how different amino acids contribute to the overall efficiency of membrane insertion is the endoplasmic reticulum (ER) of eukaryotic cells. Here, we provide comparable data for TIM23-mediated membrane protein insertion into the inner mitochondrial membrane of yeast cells. We find that hydrophobicity and the location of polar and aromatic residues are strong determinants of membrane insertion. These results parallel what has been found previously for the ER. However, we see striking differences between the effects elicited by charged residues flanking the TM segments when comparing the mitochondrial inner membrane and the ER, pointing to an unanticipated difference between the two insertion systems.

Indexed as

Amino Acid SequenceMembrane ProteinsMembrane Transport ProteinsMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsModels, BiologicalMolecular Sequence DataProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMembrane ProteinsMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsTIM23 protein, S cerevisiae

Identifiers

PMID21326212
PMCPMC3061034
OpenAlexW2155711873

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.