Evidence map›Paper›PMID 42637721›Full record

ArticleNature communications2026

Direct lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly.

Mandira Dutta, Kimberly A Dolan, Souad Amiar, Elijah J Bass, Rokaia Sultana, Sean M Braet, Karen J Cárdenas-Martínez, Devika Sirohi, Ian K Hicklin, Richard J Kuhn and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Mandira Dutta *Department of Chemistry, The University of Chicago, Chicago, IL, USA.
Kimberly A Dolan *Department of Molecular & Cell Biology, Department of Neuroscience, California Institute for Quantitative Biology (QB3), Biophysics Graduate Program, University of California Berkeley, Berkeley, CA, USA.
Souad Amiar *Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN, USA.
Elijah J Bass *Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0009-0005-1875-6134
Rokaia SultanaBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0009-0009-5468-646X
Sean M BraetDepartment of Chemistry, Pennsylvania State University, University Park, PA, USA.ORCID http://orcid.org/0000-0003-3782-2262
Karen J Cárdenas-MartínezBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0002-7266-8769
Devika SirohiPurdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN, USA.
Ian K HicklinDepartment of Molecular & Cell Biology, Department of Neuroscience, California Institute for Quantitative Biology (QB3), Biophysics Graduate Program, University of California Berkeley, Berkeley, CA, USA.
Richard J KuhnPurdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0003-4148-1026
Ganesh S AnandDepartment of Chemistry, Pennsylvania State University, University Park, PA, USA.ORCID http://orcid.org/0000-0001-8995-3067
Gregory A VothDepartment of Chemistry, The University of Chicago, Chicago, IL, USA. gavoth@uchicago.edu.ORCID http://orcid.org/0000-0002-3267-6748
Stephen G BrohawnDepartment of Molecular & Cell Biology, Department of Neuroscience, California Institute for Quantitative Biology (QB3), Biophysics Graduate Program, University of California Berkeley, Berkeley, CA, USA. brohawn@berkeley.edu.ORCID http://orcid.org/0000-0001-6768-3406
Robert V StahelinBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN, USA. rstaheli@purdue.edu.ORCID http://orcid.org/0000-0001-5443-7863

Funding

Elucidation of Assembly and Budding Mechanisms of SARS-CoV-2R01AI169896 · NIAID · PURDUE UNIVERSITY · PI Robert Virgil Stahelin · 2022 to 2026
$3.8M
NIAID NIH HHS R01 AI169896U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) AI169896
6 · The paper itself

Abstract

M is the most abundant structural membrane protein in coronaviruses and is essential for the formation of infectious virus particles. SARS-CoV-2 M adopts two conformations, M

Indexed as

SARS-CoV-2Viral Matrix ProteinsVirus AssemblyAnimalsCoronavirus M ProteinsCryoelectron MicroscopyGolgi ApparatusHumansMolecular Dynamics SimulationProtein BindingProtein ConformationSphingolipidsCoronavirus M Proteinsmembrane protein, SARS-CoV-2SphingolipidsViral Matrix Proteins

Identifiers

PMID42637721
PMCPMC13503762

What Socratic holds

Textmetadata
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 Socratic graph.