Evidence map›Paper›PMID 33774672›Full record

ArticleJournal of biochemistry2021

SARS-CoV-2 spike protein binding selectively accelerates substrate-specific catalytic activity of ACE2.

Anna A Kiseleva, Elizabeth M Troisi, Scott E Hensley, Rahul M Kohli, Jonathan A Epstein

Open access · bronzeAbstract read
In one paragraph

Article in Journal of biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  6. Monoclonal neutralizing antibodies against SARS-COV-2 S protein.American journal of translational research · 2024
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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.

Anna A KiselevaDepartment of Medicine, University of Pennsylvania, Perelman Center for Advanced Medicine, 3400 Civic Center Boulevard,Philadelphia, PA 19104, USA.ORCID 0000-0002-8720-5062
Elizabeth M TroisiDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania; 3610 Hamilton Walk, Philadelphia, PA 19104, USA.
Scott E HensleyDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania; 3610 Hamilton Walk, Philadelphia, PA 19104, USA.
Rahul M KohliDepartment of Medicine, University of Pennsylvania, Perelman Center for Advanced Medicine, 3400 Civic Center Boulevard,Philadelphia, PA 19104, USA.
Jonathan A EpsteinDepartment of Medicine, University of Pennsylvania, Perelman Center for Advanced Medicine, 3400 Civic Center Boulevard,Philadelphia, PA 19104, USA.
University of Pennsylvania · US

Funding

Cardiac lineage determination and nuclear architectureR35HL140018 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI EPSTEIN, JONATHAN A. · 2018 to 2024
$6.8M
Cotswold FoundationNHLBI NIH HHS R35 HL140018NIH HHS R35 HL140018WW Smith endowed chair
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel coronavirus that has given rise to the devastating global pandemic. In most cases, SARS-CoV-2 infection results in the development of viral pneumonia and acute respiratory distress syndrome, known as 'coronavirus disease 2019' or COVID-19. Intriguingly, besides the respiratory tract, COVID-19 affects other organs and systems of the human body. COVID-19 patients with pre-existing cardiovascular disease have a higher risk of death, and SARS-CoV-2 infection itself may cause myocardial inflammation and injury. One possible explanation of such phenomena is the fact that SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as the receptor required for viral entry. ACE2 is expressed in the cells of many organs, including the heart. ACE2 functions as a carboxypeptidase that can cleave several endogenous substrates, including angiotensin II, thus regulating blood pressure and vascular tone. It remains largely unknown if the SARS-CoV-2 infection alters the enzymatic properties of ACE2, thereby contributing to cardiovascular complications in patients with COVID-19. Here, we demonstrate that ACE2 cleavage of des-Arg9-bradykinin substrate analogue is markedly accelerated, while cleavage of angiotensin II analogue is minimally affected by the binding of spike protein. These findings may have implications for a better understanding of COVID-19 pathogenesis.

Indexed as

Angiotensin-Converting Enzyme 2CatalysisHumansProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusSubstrate SpecificityACE2 protein, humanAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2COVID-19SARS-CoV-2spike protein

Identifiers

PMID33774672
PMCPMC8083718
OpenAlexW3151740940

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.