Evidence map›Paper›PMID 39036877›Full record

ReviewBioscience reports2024

3-chymotrypsin-like protease in SARS-CoV-2.

Kenana Al Adem, Juliana C Ferreira, Adrian J Villanueva, Samar Fadl, Farah El-Sadaany, Imen Masmoudi, Yugmee Gidiya, Tariro Gurudza, Thyago H S Cardoso, Nitin K Saksena and 1 more

Abstract readReview
In one paragraph

Review in Bioscience reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. MarinePharmaceuticals (Basel, Switzerland) · 2026
    Article
  3. Review
  4. Review
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

11 authors.

Kenana Al AdemScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Juliana C FerreiraScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Adrian J VillanuevaScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Samar FadlScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Farah El-SadaanyScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Imen MasmoudiScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Yugmee GidiyaScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Tariro GurudzaScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Thyago H S CardosoOMICS Centre of Excellence, G42 Healthcare, Masdar City, Abu Dhabi, United Arab Emirates.
Nitin K SaksenaVictoria University, Footscray Campus, Melbourne, VIC. Australia.
Wael M RabehScience Division, New York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.ORCID 0000-0001-6071-8581

Funding

New York University Abu Dhabi (NYUAD) AD055
6 · The paper itself

Abstract

Coronaviruses constitute a significant threat to the human population. Severe acute respiratory syndrome coronavirus-2, SARS-CoV-2, is a highly pathogenic human coronavirus that has caused the coronavirus disease 2019 (COVID-19) pandemic. It has led to a global viral outbreak with an exceptional spread and a high death toll, highlighting the need for effective antiviral strategies. 3-Chymotrypsin-like protease (3CLpro), the main protease in SARS-CoV-2, plays an indispensable role in the SARS-CoV-2 viral life cycle by cleaving the viral polyprotein to produce 11 individual non-structural proteins necessary for viral replication. 3CLpro is one of two proteases that function to produce new viral particles. It is a highly conserved cysteine protease with identical structural folds in all known human coronaviruses. Inhibitors binding with high affinity to 3CLpro will prevent the cleavage of viral polyproteins, thus impeding viral replication. Multiple strategies have been implemented to screen for inhibitors against 3CLpro, including peptide-like and small molecule inhibitors that covalently and non-covalently bind the active site, respectively. In addition, allosteric sites of 3CLpro have been identified to screen for small molecules that could make non-competitive inhibitors of 3CLpro. In essence, this review serves as a comprehensive guide to understanding the structural intricacies and functional dynamics of 3CLpro, emphasizing key findings that elucidate its role as the main protease of SARS-CoV-2. Notably, the review is a critical resource in recognizing the advancements in identifying and developing 3CLpro inhibitors as effective antiviral strategies against COVID-19, some of which are already approved for clinical use in COVID-19 patients.

Indexed as

Antiviral AgentsCoronavirus 3C ProteasesCOVID-19SARS-CoV-2COVID-19 Drug TreatmentHumansProtease InhibitorsVirus Replication3C-like proteinase, SARS-CoV-2Antiviral AgentsCoronavirus 3C ProteasesProtease Inhibitors3-chymotrypsin-like protease (3CLpro)Covalent inhibitorsCOVID-19main proteaseNon-covalent inhibitorsSARS-CoV-2

Identifiers

PMID39036877
PMCPMC11300678

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.