Evidence map›Paper›PMID 39514670›Full record

ArticleScience advances2024

A coronaviral pore-replicase complex links RNA synthesis and export from double-membrane vesicles.

Anan Chen, Ana-Mihaela Lupan, Rui Tong Quek, Stefan G Stanciu, Mihaela Asaftei, George A Stanciu, Kierra S Hardy, Taciani de Almeida Magalhães, Pamela A Silver, Timothy J Mitchison and 1 more

Abstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structural insights into SARS-CoV-2 nonstructural protein 4 (nsp4) biogenesis.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
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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

11 authors.

Anan ChenDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0009-0001-7433-4631
Ana-Mihaela LupanDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0003-3414-0098
Rui Tong QuekDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-0192-8279
Stefan G StanciuCenter for Microscopy-Microanalysis and Information Processing, National University of Science and Technology Politehnica Bucharest, 313 Splaiul Independenței, 060042 Bucharest, Romania.ORCID 0000-0002-1676-3040
Mihaela AsafteiCenter for Microscopy-Microanalysis and Information Processing, National University of Science and Technology Politehnica Bucharest, 313 Splaiul Independenței, 060042 Bucharest, Romania.ORCID 0000-0002-2532-4285
George A StanciuCenter for Microscopy-Microanalysis and Information Processing, National University of Science and Technology Politehnica Bucharest, 313 Splaiul Independenței, 060042 Bucharest, Romania.
Kierra S HardyDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Taciani de Almeida MagalhãesDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Pamela A SilverDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-7856-4071
Timothy J MitchisonDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0001-7781-1897
Adrian SalicDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-0748-9545

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronavirus-infected cells contain double-membrane vesicles (DMVs) that are key for viral RNA replication and transcription, perforated by hexameric pores connecting the vesicular lumen to the cytoplasm. How pores form and traverse two membranes, and how DMVs organize RNA synthesis, is unknown. Using structure prediction and functional assays, we show that the nonstructural viral membrane protein nsp4 is the key pore organizer, spanning the double membrane and forming most of the pore lining. Nsp4 interacts with nsp3 on the cytoplasmic side and with the viral replicase inside the DMV. Newly synthesized mRNAs exit the DMV into the cytoplasm, passing through a narrow ring of conserved nsp4 residues. Steric constraints imposed by the ring predict that modified nucleobases block mRNA transit, resulting in broad-spectrum anticoronaviral activity.

Indexed as

RNA, ViralViral Nonstructural ProteinsCoronavirusHumansModels, MolecularRNA-Dependent RNA PolymeraseRNA, MessengerViral Replicase Complex ProteinsVirus ReplicationRNA-Dependent RNA PolymeraseRNA, MessengerRNA, ViralViral Nonstructural ProteinsViral Replicase Complex Proteins

Identifiers

PMID39514670
PMCPMC11546809

What OpenQuestion 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 OpenQuestion graph.