ArticleMethods in molecular biology (Clifton, N.J.)2020
Proximity Labeling for the Identification of Coronavirus-Host Protein Interactions.
Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Nairobi sheep disease virus: an emerging threat with unresolved pathogenesis and zoonotic potential.Journal of virology · 2026Review
- The development of proximity labeling technology and its applications in mammals, plants, and microorganisms.Cell communication and signaling : CCS · 2023Review
- Potential application of TurboID-based proximity labeling in studying the protein interaction network in plant response to abiotic stress.Frontiers in plant science · 2022Review
- Proximity-dependent biotinylation detects associations between SARS coronavirus nonstructural protein 1 and stress granule-associated proteins.The Journal of biological chemistry · 2021Article
- Mass spectrometry analytical responses to the SARS-CoV2 coronavirus in review.Trends in analytical chemistry : TRAC · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biotin-based proximity labeling circumvents major pitfalls of classical biochemical approaches to identify protein-protein interactions. It consists of enzyme-catalyzed biotin tags ubiquitously apposed on proteins located in close proximity of the labeling enzyme, followed by affinity purification and identification of biotinylated proteins by mass spectrometry. Here we outline the methods by which the molecular microenvironment of the coronavirus replicase/transcriptase complex (RTC), i.e., proteins located within a close perimeter of the RTC, can be determined by different proximity labeling approaches using BirA
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Registered trials
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