Evidence map›Paper›PMID 37398176›Full record

ArticlebioRxiv : the preprint server for biology2023

Universal features of Nsp1-mediated translational shutdown by coronaviruses.

Katharina Schubert, Evangelos D Karousis, Ivo Ban, Christopher P Lapointe, Marc Leibundgut, Emilie Bäumlin, Eric Kummerant, Alain Scaiola, Tanja Schönhut, Jana Ziegelmüller and 3 more

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 5 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 2 countries.

Katharina SchubertDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Evangelos D KarousisDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Ivo BanDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Christopher P LapointeDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Marc LeibundgutDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Emilie BäumlinDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Eric KummerantDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Alain ScaiolaDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Tanja SchönhutDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Jana ZiegelmüllerDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Oliver MühlemannDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Nenad BanDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
ETH Zurich · CHUniversity of Bern · CHStanford University · US

Funding

Dynamics of TranslationR35GM145306 · NIGMS · STANFORD UNIVERSITY · PI JOSEPH D PUGLISI · 2022 to 2026
$3.8M
Defining modifiers and mechanisms of RAN translationRF1AG064690 · NIA · STANFORD UNIVERSITY · PI GITLER, AARON D., PUGLISI, JOSEPH D · 2019 to 2019
$2.8M
Defining modifiers and mechanisms of RAN translationR01AG064690 · NIA · STANFORD UNIVERSITY · PI Aaron D. Gitler, JOSEPH D PUGLISI · 2024 to 2026
$2.3M
From one end to the other: dynamics of human translation initiation and its controlK99GM144678 · NIGMS · STANFORD UNIVERSITY · PI LAPOINTE, CHRISTOPHER PAUL · 2022 to 2023
$164k
NIA NIH HHS R01 AG064690NIA NIH HHS RF1 AG064690NIGMS NIH HHS K99 GM144678NIGMS NIH HHS R35 GM145306
6 · The paper itself

Abstract

Nonstructural protein 1 (Nsp1) produced by coronaviruses shuts down host protein synthesis in infected cells. The C-terminal domain of SARS-CoV-2 Nsp1 was shown to bind to the small ribosomal subunit to inhibit translation, but it is not clear whether this mechanism is broadly used by coronaviruses, whether the N-terminal domain of Nsp1 binds the ribosome, or how Nsp1 specifically permits translation of viral mRNAs. Here, we investigated Nsp1 from three representative

Identifiers

PMID37398176
PMCPMC10312502
OpenAlexW4378982231

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.