Evidence map›Paper›PMID 35408866›Full record

ReviewInternational journal of molecular sciences2022

Potential Resistance of SARS-CoV-2 Main Protease (Mpro) against Protease Inhibitors: Lessons Learned from HIV-1 Protease.

János András Mótyán, Mohamed Mahdi, Gyula Hoffka, József Tőzsér

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Proteases: Role in Various Human Diseases.Current pharmaceutical biotechnology · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Biochemistry and biophysics reports · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Crystal structures of main protease (MMolecular biomedicine · 2023
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

János András MótyánDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0002-6079-5621
Mohamed MahdiDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0002-7959-5996
Gyula HoffkaDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
József TőzsérDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0001-5076-8729
University of Debrecen · HU

Funding

National Research, Development and Innovation Office TKP2021-EGA-20
6 · The paper itself

Abstract

Coronavirus disease 2019 (COVID-19), caused by the severe acute respiratory syndrome 2 (SARS-CoV-2), has been one of the most devastating pandemics of recent times. The lack of potent novel antivirals had led to global health crises; however, emergence and approval of potent inhibitors of the viral main protease (Mpro), such as Pfizer's newly approved nirmatrelvir, offers hope not only in the therapeutic front but also in the context of prophylaxis against the infection. By their nature, RNA viruses including human immunodeficiency virus (HIV) have inherently high mutation rates, and lessons learnt from previous and currently ongoing pandemics have taught us that these viruses can easily escape selection pressure through mutation of vital target amino acid residues in monotherapeutic settings. In this paper, we review nirmatrelvir and its binding to SARS-CoV-2 Mpro and draw a comparison to inhibitors of HIV protease that were rendered obsolete by emergence of resistance mutations, emphasizing potential pitfalls in the design of inhibitors that may be of important relevance to the long-term use of novel inhibitors against SARS-CoV-2.

Indexed as

COVID-19 Drug TreatmentProtease InhibitorsAntiviral AgentsCoronavirus 3C ProteasesHIV ProteaseHumansMolecular Docking SimulationPeptide HydrolasesSARS-CoV-23C-like proteinase, SARS-CoV-2Antiviral AgentsCoronavirus 3C ProteasesHIV Proteasep16 protease, Human immunodeficiency virus 1Peptide HydrolasesProtease Inhibitorsdrug resistanceHIV-1main protease (Mrpo)nirmatrelvirPAXLOVIDPF-07321332protease inhibitorresistanceSARS-CoV-2

Identifiers

PMID35408866
PMCPMC8998604
OpenAlexW4220742842

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.