ArticleJournal of virological methods2016
Removal of nuclease contamination during purification of recombinant prototype foamy virus integrase.
Article in Journal of virological methods, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
The 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.
Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Evaluating the viral clearance ability of continuous monoclonal antibody purification steps, in order to inactivate and/or remove four model viruses.Iranian journal of microbiology · 2023Article
- Prototype Foamy Virus Integrase Displays Unique Biochemical Activities among Retroviral Integrases.Biomolecules · 2021Article
- Foamy Virus Integrase in Development of Viral Vector for Gene Therapy.Journal of microbiology and biotechnology · 2020Review
- Prototype foamy virus intasome aggregation is mediated by outer protein domains and prevented by protocatechuic acid.Scientific reports · 2019Article
- Nucleosome DNA unwrapping does not affect prototype foamy virus integration efficiency or site selection.PloS one · 2019Article
- Prototype foamy virus integrase is promiscuous for target choice.Biochemical and biophysical research communications · 2018Article
- Assembly and Purification of Prototype Foamy Virus Intasomes.Journal of visualized experiments : JoVE · 2018Article
- Detection and Removal of Nuclease Contamination During Purification of Recombinant Prototype Foamy Virus Integrase.Journal of visualized experiments : JoVE · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Retroviral infection requires integration of the viral genome into the host genome. Recombinant integrase proteins may be purified following bacterial expression. A bulk biochemical assay of integrase function relies on the conversion of supercoiled plasmids to linear or relaxed circles. Single molecule molecular tweezer assays of integrase also evaluate the conversion of supercoiled DNA to nicked and broken species. A bacterial nuclease that co-purifies with retroviral integrase may affect the quantitation of integration activity in bulk or single molecule assays. During purification of retroviral integrase from bacteria, fractions may be screened for contaminating nuclease activity. In order to efficiently separate the nuclease from integrase, the binding affinities of each protein must differ. We find that a co-purifying nuclease may be efficiently separated from integrase based on heparin affinity, but not ionic affinity.
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Identifiers
What OpenQuestion holds
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.