Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease.

Molecular cell - 19 May 2016

Békés Miklós, van der Heden van Noort Gerbrand J, Ekkebus Reggy, Ovaa Huib, Huang Tony T, Lima Christopher D

Abstract excerpt

Deubiquitinating enzymes (DUBs) recognize and cleave linkage-specific polyubiquitin (polyUb) chains, but mechanisms underlying specificity remain elusive in many cases. The severe acute respiratory syndrome (SARS) coronavirus papain-like protease (PLpro) is a DUB that cleaves ISG15, a two-domain Ub-like protein, and Lys48-linked polyUb chains, releasing diUb(Lys48) products. To elucidate this specificity, we...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Coronavirus 3C Proteases
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysine

Share to Polyubiquitin

Share to Protein Interaction Domains and Motifs

Share to Severe acute respiratory syndrome-related coronavirus

Share to Ubiquitination

Share to Ubiquitins

Source

Open in PubMed Open full text

Identifiers

PMID: 27203180
DOI: 10.1016/j.molcel.2016.04.016
PMCID: PMC4875570

Genes

ISG15

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease.PMID 27203180Read ↗

Structural basis for catalysis and ubiquitin recognition by the severe acute respiratory syndrome coronavirus papain-like protease.Semantic proximity Read ↗

Ubiquitin variants potently inhibit SARS-CoV-2 PLpro and viral replication via a novel site distal to the protease active siteSemantic proximity Read ↗

Structural and Biochemical Characterization of Porcine Epidemic Diarrhea Virus Papain-Like Protease 2.Semantic proximity Read ↗

Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression.Semantic proximity Read ↗

Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin.Semantic proximity Read ↗

The substrate selectivity of papain-like proteases from human-infecting coronaviruses correlates with innate immune suppressionSemantic proximity Read ↗

Deubiquitinating activity of SARS-CoV-2 papain-like protease does not influence virus replication or innate immune responses in vivoSemantic proximity Read ↗

SARS-CoV-2 papain-like protease inhibits ISGylation of the viral nucleocapsid protein to evade host anti-viral immunitySemantic proximity Read ↗

Structurally Guided Removal of DeISGylase Biochemical Activity from Papain-Like Protease Originating from Middle East Respiratory Syndrome Coronavirus.Semantic proximity Read ↗

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde.Semantic proximity Read ↗

Potent and Selective Covalent Inhibition of the Papain-like Protease from SARS-CoV-2Semantic proximity Read ↗

Potent and Selective Covalent Inhibition of the Papain-like Protease from SARS-CoV-2Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.