Evidence map›Paper›PMID 24055377›Full record

ArticleJournal of molecular biology2014

Transmembrane segments form tertiary hairpins in the folding vestibule of the ribosome.

Liwei Tu, Pooja Khanna, Carol Deutsch

Abstract read
In one paragraph

Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.7field-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

45 citing papers in PubMed, 63 citations in OpenAlex.

  1. Translation fidelity mechanisms and their changes in aging.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Folding and Insertion of Transmembrane Helices at the ER.International journal of molecular sciences · 2021
    Review
  14. Article
  15. 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
  16. Review
  17. Article
  18. Article
  19. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  20. Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021
    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.

Liwei TuDepartment of Physiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
Pooja KhannaDepartment of Physiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
Carol DeutschDepartment of Physiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA. Electronic address: cjd@mail.med.upenn.edu.
University of Pennsylvania · US

Funding

FUNCTION AND ASSEMBLY OF POTASSIUM CHANNELSR01GM052302 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEUTSCH, CAROL J · 1995 to 2024
$13.4M
NIGMS NIH HHS GM 52302NIGMS NIH HHS R01 GM052302
6 · The paper itself

Abstract

Folding of membrane proteins begins in the ribosome as the peptide is elongated. During this process, the nascent peptide navigates along 100Å of tunnel from the peptidyltransferase center to the exit port. Proximal to the exit port is a "folding vestibule" that permits the nascent peptide to compact and explore conformational space for potential tertiary folding partners. The latter occurs for cytosolic subdomains but has not yet been shown for transmembrane segments. We now demonstrate, using an accessibility assay and an improved intramolecular crosslinking assay, that the helical transmembrane S3b-S4 hairpin ("paddle") of a voltage-gated potassium (Kv) channel, a critical region of the Kv voltage sensor, forms in the vestibule. S3-S4 hairpin interactions are detected at an early stage of Kv biogenesis. Moreover, this vestibule hairpin is consistent with a closed-state conformation of the Kv channel in the plasma membrane.

Indexed as

Protein FoldingAmino Acid SequenceKv1.3 Potassium ChannelMolecular Sequence DataProtein ConformationRibosomesKv1.3 Potassium Channelbismaleimide hexaneBMHendoplasmic reticulumERfolding of nascent peptidesintramolecular crosslinkingLDSlithium dodecyl sulfatePBSPDMPEG-MALpeptidyl transferase centerphenyldimaleimidephosphate-buffered salinepolyethylene glycol maleimidepotassium channel voltage sensor biogenesisPTCtransmembrane helical hairpinvoltage sensor domainVSD

Identifiers

PMID24055377
PMCPMC3872176
OpenAlexW1965352738

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.