Evidence map›Paper›PMID 30927129›Full record

ReviewThe protein journal2019

Membrane Protein Integration and Topogenesis at the ER.

Martin Spiess, Tina Junne, Marco Janoschke

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. SecYEG-mediated translocation in a model synthetic cell.Synthetic biology (Oxford, England) · 2024
    Article
  8. Review
  9. Article
  10. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  11. Article
  12. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  13. Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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
  20. 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

3 authors at 1 institution in 1 country.

Martin SpiessBiozentrum, University of Basel, Klingelbergstrasse 70, 4056, Basel, Switzerland. martin.spiess@unibas.ch.ORCID 0000-0001-7139-0550
Tina JunneBiozentrum, University of Basel, Klingelbergstrasse 70, 4056, Basel, Switzerland.
Marco JanoschkeBiozentrum, University of Basel, Klingelbergstrasse 70, 4056, Basel, Switzerland.
University of Basel · CH

Funding

Swiss National Science Foundation 31003A-162643
6 · The paper itself

Abstract

Most membrane proteins are composed of hydrophobic α-helical transmembrane segments and are integrated into the lipid bilayer of the endoplasmic reticulum by the highly conserved Sec61 translocon. With respect to the integration mechanism, three types of transmembrane segments can be distinguished-the signal, the stop-transfer sequence, and the re-integration sequence-which in linear succession can account for all kinds of membrane protein topologies. The transmembrane orientation of the initial signal and to a weaker extent also of downstream transmembrane segments is affected by charged flanking residues according to the so-called positive-inside rule. The main driving force for transmembrane integration is hydrophobicity. Systematic analysis suggested thermodynamic equilibration of each peptide segment in the translocon with the membrane as the underlying mechanism. However, there is evidence that integration is not entirely sequence-autonomous, but depends also on the sequence context, from very closely spaced transmembrane segments to the folding state and properties of neighboring sequences. Topogenesis is even influenced by accessory proteins that appear to act as intramembrane chaperones.

Indexed as

Endoplasmic ReticulumEukaryotic CellsMembrane ProteinsMolecular ChaperonesProtein Conformation, alpha-HelicalProtein Sorting SignalsSEC Translocation ChannelsMembrane ProteinsMolecular ChaperonesProtein Sorting SignalsSEC Translocation ChannelsSec61Signal sequenceTransloconTransmembrane helix

Identifiers

PMID30927129
OpenAlexW2935400920

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.