ArticleThe Journal of biological chemistry1999
A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold .
Article in The Journal of biological chemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 45 papers.
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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.
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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.
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Who cites it
45 citing papers in PubMed, 65 citations in OpenAlex.
- Chasing allosteric inhibition of the SARS-CoV-2 PLpro via molecular dynamics simulations with flooding fragments (MDFFr).Journal of computer-aided molecular design · 2025Article
- Analysis of Structures of SARS-CoV-2 Papain-like Protease Bound with Ligands Unveils Structural Features for Inhibiting the Enzyme.Molecules (Basel, Switzerland) · 2025Review
- Antiviral activity of natural phenolic compounds in complex at an allosteric site of SARS-CoV-2 papain-like protease.Communications biology · 2022Article
- Structure of the multiple functional domains from coronavirus nonstructural protein 3.Emerging microbes & infections · 2021Article
- Ancient gene duplications in RNA viruses revealed by protein tertiary structure comparisons.Virus evolution · 2021Article
- Targeting SARS-CoV-2 Proteases for COVID-19 Antiviral Development.Frontiers in chemistry · 2021Review
- Druggable targets from coronaviruses for designing new antiviral drugs.Bioorganic & medicinal chemistry · 2020Review
- Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated byFrontiers in cellular and infection microbiology · 2019Article
- Dissection of amino-terminal functional domains of murine coronavirus nonstructural protein 3.Journal of virology · 2015Article
- Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities.Virus research · 2014Review
- Hepatitis E virus inhibits type I interferon induction by ORF1 products.Journal of virology · 2014Article
- The footprint of genome architecture in the largest genome expansion in RNA viruses.PLoS pathogens · 2013Article
- Comparison of SARS and NL63 papain-like protease binding sites and binding site dynamics: inhibitor design implications.Journal of molecular biology · 2011Article
- Discovery of the first insect nidovirus, a missing evolutionary link in the emergence of the largest RNA virus genomes.PLoS pathogens · 2011Article
- Papain-like protease 1 from transmissible gastroenteritis virus: crystal structure and enzymatic activity toward viral and cellular substrates.Journal of virology · 2010Article
- RNA transcription analysis and completion of the genome sequence of yellow head nidovirus.Virus research · 2008Article
- Deubiquitination in virus infection.Virology · 2007Review
- Human coronavirus 229E papain-like proteases have overlapping specificities but distinct functions in viral replication.Journal of virology · 2007Article
- A contemporary view of coronavirus transcription.Journal of virology · 2007Review
- Replication of murine hepatitis virus is regulated by papain-like proteinase 1 processing of nonstructural proteins 1, 2, and 3.Journal of virology · 2006Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 2 institutions in 4 countries.
Funding
Abstract
A cysteine proteinase, papain-like proteinase (PL1pro), of the human coronavirus 229E (HCoV) regulates the expression of the replicase polyproteins, pp1a and ppa1ab, by cleavage between Gly111 and Asn112, far upstream of its own catalytic residue Cys1054. In this report, using bioinformatics tools, we predict that, unlike its distant cellular homologues, HCoV PL1pro and its coronaviral relatives have a poorly conserved Zn2+ finger connecting the left and right hand domains of a papain-like fold. Optical emission spectrometry has been used to confirm the presence of Zn2+ in a purified and proteolytically active form of the HCoV PL1pro fused with the Escherichia coli maltose-binding protein. In denaturation/renaturation experiments using the recombinant protein, its activity was shown to be strongly dependent upon Zn2+, which could be partly substituted by Co2+ during renaturation. The reconstituted, Zn2+-containing PL1pro was not sensitive to 1,10-phenanthroline, and the Zn2+-depleted protein was not reactivated by adding Zn2+ after renaturation. Consistent with the proposed essential structural role of Zn2+, PL1pro was selectively inactivated by mutations in the Zn2+ finger, including replacements of any of four conserved Cys residues predicted to co-ordinate Zn2+. The unique domain organization of HCoV PL1pro provides a potential framework for regulatory processes and may be indicative of a nonproteolytic activity of this enzyme.
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Registered trials
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.