Evidence map›Paper›PMID 33333742›Full record

ArticleInternational journal of molecular sciences2020

Identification of Host Cellular Protein Substrates of SARS-COV-2 Main Protease.

Márió Miczi, Mária Golda, Balázs Kunkli, Tibor Nagy, József Tőzsér, János András Mótyán

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.6field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. tRNA modifications in viral replication.The Journal of biological chemistry · 2026
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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

6 authors at 1 institution in 1 country.

Márió MicziDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Mária GoldaDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Balázs KunkliDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0003-1266-2792
Tibor NagyDepartment of Applied Chemistry, Faculty of Science and Technology, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0001-8568-914X
József TőzsérDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0001-5076-8729
János András MótyánDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0002-6079-5621
University of Debrecen · HU

Funding

GINOP 2.3.3-15-2016-00021NKFIH 1150-6/2019
6 · The paper itself

Abstract

The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease-19 (COVID-19) being associated with severe pneumonia. Like with other viruses, the interaction of SARS-CoV-2 with host cell proteins is necessary for successful replication, and cleavage of cellular targets by the viral protease also may contribute to the pathogenesis, but knowledge about the human proteins that are processed by the main protease (3CLpro) of SARS-CoV-2 is still limited. We tested the prediction potentials of two different in silico methods for the identification of SARS-CoV-2 3CLpro cleavage sites in human proteins. Short stretches of homologous host-pathogen protein sequences (SSHHPS) that are present in SARS-CoV-2 polyprotein and human proteins were identified using BLAST analysis, and the NetCorona 1.0 webserver was used to successfully predict cleavage sites, although this method was primarily developed for SARS-CoV. Human C-terminal-binding protein 1 (CTBP1) was found to be cleaved in vitro by SARS-CoV-2 3CLpro, the existence of the cleavage site was proved experimentally by using a His

Indexed as

Alcohol OxidoreductasesAmino Acid SequenceCoronavirus 3C ProteasesCOVID-19DNA-Binding ProteinsHost-Pathogen InteractionsHumansSARS-CoV-2Substrate SpecificityAlcohol OxidoreductasesCoronavirus 3C ProteasesC-terminal binding proteinDNA-Binding Proteins3CL proteasecleavage site identificationcleavage site predictioncoronavirusCOVID-19host protein cleavagemain proteaseNetCoronaSARSSARS-CoV-2SSHHPS

Identifiers

PMID33333742
PMCPMC7765187
OpenAlexW3110781773

What OpenQuestion holds

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LicenceCC BY
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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.