Evidence map›Paper›PMID 31302079›Full record

ReviewBiochimica et biophysica acta. Biomembranes2020

Structural insight into co-translational membrane protein folding.

Grant A Pellowe, Paula J Booth

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

2 authors at 1 institution in 1 country.

Grant A PelloweDepartment of Chemistry, King's College London, 7 Trinity Street, SE1 1DB, London, UK.
Paula J BoothDepartment of Chemistry, King's College London, 7 Trinity Street, SE1 1DB, London, UK. Electronic address: paula.booth@kcl.ac.uk.
King's College London · GB

Funding

European Research Council 294342Wellcome Trust 214259
6 · The paper itself

Abstract

Membrane protein folding studies lag behind those of water-soluble proteins due to immense difficulties of experimental study, resulting from the need to provide a hydrophobic lipid-bilayer environment when investigated in vitro. A sound understanding of folding mechanisms is important for membrane proteins as they contribute to a third of the proteome and are frequently associated with disease when mutated and/or misfolded. Membrane proteins largely consist of α-helical, hydrophobic transmembrane domains, which insert into the membrane, often using the SecYEG/Sec61 translocase system. This mini-review highlights recent advances in techniques that can further our understanding of co-translational folding and notably, the structure and insertion of nascent chains as they emerge from translating ribosomes. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.

Indexed as

Protein FoldingAnimalsHumansMembrane ProteinsProtein Translocation SystemsRibosomesSEC Translocation ChannelsMembrane ProteinsProtein Translocation SystemsSEC Translocation ChannelsAlpha-helicalCo-translationalFolding and insertionMembrane proteinsRibosome nascent chainsSEIRAS

Identifiers

PMID31302079
PMCPMC7618500
OpenAlexW2961998748

What OpenQuestion holds

Textmetadata
LicenceTDM
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.