Evidence map›Paper›PMID 37831764›Full record

ArticleScience advances2023

Atomic structure of the open SARS-CoV-2 E viroporin.

João Medeiros-Silva, Aurelio J Dregni, Noah H Somberg, Pu Duan, Mei Hong

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. 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
4.9field-weighted citation impact, top 4% 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, 33 citations in OpenAlex.

  1. Article
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  12. Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025
    Article
  13. Article
  14. OPTO: Automated Optimization for Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
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  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

5 authors at 1 institution in 1 country.

João Medeiros-SilvaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0003-3532-4390
Aurelio J DregniDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0003-3422-4734
Noah H SombergDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0002-5222-0334
Pu DuanDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0002-7395-4353
Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0001-5255-5858
Massachusetts Institute of Technology · US

Funding

TRD3 NMRbox: Bayesian AnalyticsP41GM111135 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI HOCH, JEFFREY C · 2015 to 2024
$14.0M
Structures and Dynamics of Proton and Cation-Dependent Channels and TransportersR01GM088204 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2009 to 2024
$4.8M
TR&D 4 -- Advanced Magic Angle Spinning NMR methodsP41GM132079 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2021
$3.6M
NIGMS NIH HHS P41 GM111135NIGMS NIH HHS P41 GM132079NIGMS NIH HHS R01 GM088204
6 · The paper itself

Abstract

The envelope (E) protein of the SARS-CoV-2 virus forms cation-conducting channels in the endoplasmic reticulum Golgi intermediate compartment (ERGIC) of infected cells. The calcium channel activity of E is associated with the inflammatory responses of COVID-19. Using solid-state NMR (ssNMR) spectroscopy, we have determined the open-state structure of E's transmembrane domain (ETM) in lipid bilayers. Compared to the closed state, open ETM has an expansive water-filled amino-terminal chamber capped by key glutamate and threonine residues, a loose phenylalanine aromatic belt in the middle, and a constricted polar carboxyl-terminal pore filled with an arginine and a threonine residue. This structure gives insights into how protons and calcium ions are selected by ETM and how they permeate across the hydrophobic gate of this viroporin.

Indexed as

COVID-19Viroporin ProteinsCoronavirus Envelope ProteinsHumansIon TransportSARS-CoV-2ThreonineCoronavirus Envelope Proteinsenvelope protein, SARS-CoV-2ThreonineViroporin Proteins

Identifiers

PMID37831764
PMCPMC10575589
OpenAlexW4387611192

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.