Evidence map›Paper›PMID 32663362›Full record

ReviewChemMedChem2020

ACE2, the Receptor that Enables Infection by SARS-CoV-2: Biochemistry, Structure, Allostery and Evaluation of the Potential Development of ACE2 Modulators.

Lissy Z F Gross, Mariana Sacerdoti, Albrecht Piiper, Stefan Zeuzem, Alejandro E Leroux, Ricardo M Biondi

Open access · bronzeAbstract readReview
In one paragraph

Review in ChemMedChem, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.9field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. ACE2: Friend or Foe in Post-COVID-19 Neurodegeneration?International journal of molecular sciences · 2025
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Allosteric Binders of ACE2 Are Promising Anti-SARS-CoV-2 Agents.ACS pharmacology & translational science · 2022
    Article
  11. Article
  12. Article
  13. Allosteric binders of ACE2 are promising anti-SARS-CoV-2 agents.bioRxiv : the preprint server for biology · 2022
    Article
  14. Inhibition of ACE2-Spike Interaction by an ACE2 Binder Suppresses SARS-CoV-2 Entry.Angewandte Chemie (International ed. in English) · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17.Biochemical and biophysical research communications · 2021
    Article
  20. Article
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

6 authors at 2 institutions in 2 countries.

Lissy Z F GrossChemical Biology of Regulatory Mechanisms, IBioBA-CONICET-Partner Institute of the Max Planck Society, Godoy Cruz 2390, Buenos Aires, Argentina.
Mariana SacerdotiChemical Biology of Regulatory Mechanisms, IBioBA-CONICET-Partner Institute of the Max Planck Society, Godoy Cruz 2390, Buenos Aires, Argentina.
Albrecht PiiperInternal Medicine I, Frankfurt University Hospital, Theodor-Stern-Kai 7, Frankfurt am Main, Germany.
Stefan ZeuzemInternal Medicine I, Frankfurt University Hospital, Theodor-Stern-Kai 7, Frankfurt am Main, Germany.
Alejandro E LerouxChemical Biology of Regulatory Mechanisms, IBioBA-CONICET-Partner Institute of the Max Planck Society, Godoy Cruz 2390, Buenos Aires, Argentina.
Ricardo M BiondiChemical Biology of Regulatory Mechanisms, IBioBA-CONICET-Partner Institute of the Max Planck Society, Godoy Cruz 2390, Buenos Aires, Argentina.ORCID 0000-0002-8873-7167
Biomedicine Research Institute of Buenos Aires - CONICET - Partner Institute of the Max Planck Society · ARGoethe University Frankfurt · DE

Funding

ANPCyT PICT 2016-3525ANPCyT PICT 2017-0388ANPCyT PICT PRH-2016-4835CONICETFOCEM-Mercosur COF 03/11
6 · The paper itself

Abstract

Angiotensin converting enzyme 2 (ACE2) is the human receptor that interacts with the spike protein of coronaviruses, including the one that produced the 2020 coronavirus pandemic (COVID-19). Thus, ACE2 is a potential target for drugs that disrupt the interaction of human cells with SARS-CoV-2 to abolish infection. There is also interest in drugs that inhibit or activate ACE2, that is, for cardiovascular disorders or colitis. Compounds binding at alternative sites could allosterically affect the interaction with the spike protein. Herein, we review biochemical, chemical biology, and structural information on ACE2, including the recent cryoEM structures of full-length ACE2. We conclude that ACE2 is very dynamic and that allosteric drugs could be developed to target ACE2. At the time of the 2020 pandemic, we suggest that available ACE2 inhibitors or activators in advanced development should be tested for their ability to allosterically displace the interaction between ACE2 and the spike protein.

Indexed as

Allosteric RegulationAngiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsBetacoronavirusCatalytic DomainHumansPeptidyl-Dipeptidase AProtein BindingProtein DomainsReceptors, VirusSARS-CoV-2Spike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsPeptidyl-Dipeptidase AReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2allosterycoronavirusdrug developmentprotein dynamics

Identifiers

PMID32663362
PMCPMC7405163
OpenAlexW3043649437

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.