Evidence map›Paper›PMID 32694201›Full record

ArticleScience (New York, N.Y.)2020

Distinct conformational states of SARS-CoV-2 spike protein.

Yongfei Cai, Jun Zhang, Tianshu Xiao, Hanqin Peng, Sarah M Sterling, Richard M Walsh, Shaun Rawson, Sophia Rits-Volloch, Bing Chen

Open access · hybridAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 805 papers.

0numbers the graph read from it
0cells of the map it votes in
805citing papers in PubMed
27.0field-weighted citation impact, top 1% 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

805 citing papers in PubMed, 1,347 citations in OpenAlex.

  1. Trial
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  10. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  11. Article
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  15. Nanobodies targeting SARS-CoV-2 variants.Acta pharmaceutica Sinica. B · 2026
    Review
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745 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Yongfei Cai *Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0000-0002-3628-3802
Jun Zhang *Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Tianshu XiaoDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0000-0003-1287-1228
Hanqin PengDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0000-0002-5357-8215
Sarah M SterlingThe Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0003-0017-0408
Richard M WalshThe Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-8939-8988
Shaun RawsonThe Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-2973-2630
Sophia Rits-VollochDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Bing ChenDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA. bchen@crystal.harvard.edu.ORCID 0000-0002-8625-1657
Boston Children's Hospital · USHarvard University · US

Funding

Structure of the full-length spike protein of SARS-CoV-2 in the context of membraneR01AI147884 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING · 2020 to 2024
$3.4M
NIAID NIH HHS R01 AI147884
6 · The paper itself

Abstract

Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.

Indexed as

Angiotensin-Converting Enzyme 2Cryoelectron MicroscopyHEK293 CellsHost-Pathogen InteractionsHumansPeptidyl-Dipeptidase AProtein DomainsProtein MultimerizationProtein Structure, SecondaryReceptors, VirusSpike Glycoprotein, CoronavirusVirus InternalizationACE2 protein, humanAngiotensin-Converting Enzyme 2Peptidyl-Dipeptidase AReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID32694201
PMCPMC7464562
OpenAlexW3042332408

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.