Evidence map›Paper›PMID 34611326›Full record

ReviewNature reviews. Molecular cell biology2022

Mechanisms of SARS-CoV-2 entry into cells.

Cody B Jackson, Michael Farzan, Bing Chen, Hyeryun Choe

Open access · bronzeAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,860 papers.

0numbers the graph read from it
0cells of the map it votes in
1,860citing papers in PubMed
157.9field-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

1,860 citing papers in PubMed, 3,127 citations in OpenAlex.

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  17. Intelligent Programmable Membrane Nanosponge for Early Virus Blocking.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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1,800 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Cody B JacksonDepartment of Immunology and Microbiology, Scripps Research, Jupiter, FL, USA.ORCID http://orcid.org/0000-0002-0686-9423
Michael FarzanDepartment of Immunology and Microbiology, Scripps Research, Jupiter, FL, USA.ORCID http://orcid.org/0000-0002-2990-5319
Bing ChenDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA. bchen@crystal.harvard.edu.ORCID http://orcid.org/0000-0002-8625-1657
Hyeryun ChoeDepartment of Immunology and Microbiology, Scripps Research, Jupiter, FL, USA. hchoe@scripps.edu.ORCID http://orcid.org/0000-0003-4538-7176
Scripps Research Institute · USBoston Children's Hospital · US

Funding

Optimizing eCD4-Ig for eradication and a functional cureR01AI129868 · NIAID · UNIVERSITY OF FLORIDA · PI FARZAN, MICHAEL R. · 2017 to 2021
$5.2M
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
Structural Basis of Coreceptor Recognition by HIV-1 Envelope SpikeR01AI141002 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING · 2018 to 2022
$2.6M
NIAID NIH HHS R01 AI129868NIAID NIH HHS R01 AI141002NIAID NIH HHS R01 AI147884
6 · The paper itself

Abstract

The unprecedented public health and economic impact of the COVID-19 pandemic caused by infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been met with an equally unprecedented scientific response. Much of this response has focused, appropriately, on the mechanisms of SARS-CoV-2 entry into host cells, and in particular the binding of the spike (S) protein to its receptor, angiotensin-converting enzyme 2 (ACE2), and subsequent membrane fusion. This Review provides the structural and cellular foundations for understanding the multistep SARS-CoV-2 entry process, including S protein synthesis, S protein structure, conformational transitions necessary for association of the S protein with ACE2, engagement of the receptor-binding domain of the S protein with ACE2, proteolytic activation of the S protein, endocytosis and membrane fusion. We define the roles of furin-like proteases, transmembrane protease, serine 2 (TMPRSS2) and cathepsin L in these processes, and delineate the features of ACE2 orthologues in reservoir animal species and S protein adaptations that facilitate efficient human transmission. We also examine the utility of vaccines, antibodies and other potential therapeutics targeting SARS-CoV-2 entry mechanisms. Finally, we present key outstanding questions associated with this critical process.

Indexed as

Virus InternalizationAnimalsEvolution, MolecularHumansMembrane FusionPeptidyl-Dipeptidase ASARS-CoV-2Viral ProteinsPeptidyl-Dipeptidase AViral Proteins

Identifiers

PMID34611326
PMCPMC8491763
OpenAlexW3203433659

What OpenQuestion 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 OpenQuestion graph.