ArticleCurrent protocols in chemical biology2013
Chemoenzymatic site-specific reversible immobilization and labeling of proteins from crude cellular extract without prior purification using oxime and hydrazine ligation.
Article in Current protocols in chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Engineering protein prenylation: an emerging tool for selective protein modification.Biochemical Society transactions · 2025Review
- Non-canonical amino acid labeling in proteomics and biotechnology.Journal of biological engineering · 2019Review
- Metabolic Labeling of Prenylated Proteins Using Alkyne-Modified Isoprenoid Analogues.Current protocols in chemical biology · 2018Article
- Application of meta- and para-Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release.Current protocols in protein science · 2015Article
- Protein prenylation: enzymes, therapeutics, and biotechnology applications.ACS chemical biology · 2015Review
- Enzymatic labeling of proteins: techniques and approaches.Bioconjugate chemistry · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
In a facile and potentially general method for protein modification at the C-terminus, aldehyde-modified proteins, obtained from enzymatic protein prenylation, react rapidly with hydrazide and aminooxy surfaces and fluorophores at neutral pH and in micromolar concentration ranges of reagents. This strategy was used for fluorescent labeling of eGFP-CVIA, as a model protein, with aminooxy and hydrazide fluorophores or PEGs, and immobilization onto and subsequent release of the protein from hydrazide-functionalized agarose beads using hydrazone-oxime exchange. This method is described in detail here and provides site-specifically PEGylated or fluorescently labeled proteins starting from crude cellular extract in three steps: prenylation, capture, and release.
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Registered trials
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