ArticleChemistry (Weinheim an der Bergstrasse, Germany)2026
Substrate-Selective Inhibition of the SARS-CoV-2 Papain-Like Protease: Inhibition of Hydrolysis of Human Over Viral Substrates.
Sakshi Sharma, Peter A C Wing, Wojtek Treyde, Shyam Basak, Simeon D Draganov, Taylah Andrews-Clark, Eidarus Salah, Petra Lukacik, Claire Strain-Damerell, Adán Pinto-Fernández and 4 more
Abstract read
In one paragraphArticle in Chemistry (Weinheim an der Bergstrasse, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
14 authors.
Simeon D DraganovCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Taylah Andrews-ClarkChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.
Eidarus SalahChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.
Petra LukacikHarwell Science and Innovation Campus, Diamond Light Source Ltd., Didcot, UK.
Claire Strain-DamerellHarwell Science and Innovation Campus, Diamond Light Source Ltd., Didcot, UK.
Adán Pinto-FernándezCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Fernanda DuarteChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.
Lennart BrewitzChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.
Funding
Biotechnology and Biological Sciences Research Council BB/J003018/1Biotechnology and Biological Sciences Research Council BB/R000344/1Cancer Research UK C8717/A18245Chinese Academy of Medical Sciences (CAMS) Innovation Fund for Medical Science (CIFMS), China 2024-I2M-2-001-1Engineering and Physical Sciences Research Council (EPSRC) EP/W524311/1Wellcome TrustWellcome Trust 106244/Z/14/Z
6 · The paper itselfAbstract
The SARS-CoV-2 papain-like protease (PL
Indexed as
Coronavirus 3C ProteasesCoronavirus Papain-Like ProteasesProtease InhibitorsSARS-CoV-2CytokinesHumansHydrolysisStructure-Activity RelationshipSubstrate SpecificityUbiquitinUbiquitinsCoronavirus 3C ProteasesCoronavirus Papain-Like ProteasesCytokinesISG15 protein, humanpapain-like protease, SARS-CoV-2Protease InhibitorsUbiquitinUbiquitinsdeubiquitinase / DUBinterferon‐stimulated gene 15 / ISG15mass spectrometryprotease inhibitionSARS‐CoV‐2 main protease / MproSARS‐CoV‐2 papain‐like protease / PLprosubstrate‐selective inhibitionubiquitinvirus‐host interactions
Identifiers
PMID42283263
PMCPMC13602897
What OpenQuestion holds
Textmetadata
Read underepoch 390