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

Mutational and inhibitive analysis of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer-based assays.

Biochemical and biophysical research communications - 17 Jun 2005

Kuang Wan-Fen, Chow Lu-Ping, Wu Mei-Hua, Hwang Lih-Hwa

Abstract excerpt

The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays key roles in viral replication and is an attractive target for anti-SARS drug discovery. In this report, a fluorescence resonance energy transfer (FRET)-based method was developed to assess the proteolytic activity of SARS-CoV 3CL(pro). Two internally quenched fluorogenic peptides, 1NC and 2NC, corresponding to the...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Monoclonal
Share to Coronavirus 3C Proteases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine Endopeptidases

Share to Endopeptidases

Share to Fluorescence Resonance Energy Transfer

Share to Hydrolysis

Share to Protease Inhibitors

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 15883050
DOI: 10.1016/j.bbrc.2005.04.072
PMCID: PMC7092943

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

Mutational and inhibitive analysis of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer-based assays.PMID 15883050Read ↗

A novel auto-cleavage assay for studying mutational effects on the active site of severe acute respiratory syndrome coronavirus 3C-like protease.Semantic proximity Read ↗

Identification of novel proteolytically inactive mutations in coronavirus 3C-like protease using a combined approach.Semantic proximity Read ↗

Establishment of a green fluorescent protein (GFP)-based reporter for picornaviral 3C proteasesSemantic proximity Read ↗

Characterization and Inhibition of the Main Protease of Severe Acute Respiratory Syndrome CoronavirusSemantic proximity Read ↗

BRET-based self-cleaving biosensors for SARS-CoV-2 3CLpro Inhibitor DiscoverySemantic proximity Read ↗

Enhanced Expression and Solubility of Main Protease (Mpro) of SARS-CoV-2 from E. ColiSemantic proximity Read ↗

Orthogonal dual reporter-based gain-of-signal assay for probing SARS-CoV-2 3CL protease activity in living cells: inhibitor identification and mutation investigation.Semantic proximity Read ↗

Engineering a novel endopeptidase based on SARS 3CL(pro).Semantic proximity Read ↗

Production of a genetically encoded biosensor for evaluating enterovirus 71 3C protease inhibitorsSemantic proximity Read ↗

A Combinatorial Strategy for HRV 3C Protease Engineering to Achieve the N-terminal Free CleavageSemantic proximity Read ↗

In vivo dynamics of enterovirus protease revealed by fluorescence resonance emission transfer (FRET) based on a novel FRET pair.Semantic proximity Read ↗

Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.Semantic proximity Read ↗

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