ArticleCurrent protocols in chemical biology2014
Probing small-molecule microarrays with tagged proteins in cell lysates.
Article in Current protocols in chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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Who cites it
3 citing papers in PubMed.
- A NanoCurvS platform for quantitative and multiplex analysis of curvature-sensing proteins.Biomaterials science · 2023Article
- Advances in discovering small molecules to probe protein function in a systems context.Current opinion in chemical biology · 2016Review
- Screening of Small Molecule Microarrays for Ligands Targeted to the Extracellular Epitopes of Living Cells.Microarrays (Basel, Switzerland) · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The technique of small-molecule microarray (SMM) screening is based on the ability of small molecules to bind to various soluble proteins. This type of interaction is easily detected by the presence of a fluorescence signal produced by labeled antibodies that specifically recognize a unique sequence (tag) present on the target protein. The fluorescent signal intensity values are determined based on signal-to-noise ratios (SNRs). SMM screening is a high-throughput, unbiased method that can rapidly identify novel direct ligands for various protein targets. This binding-based assay format is generally applicable to most proteins, but it is especially useful for protein targets that do not possess an enzymatic activity. SMMs enable screening a protein in a purified form or in the context of a cellular lysate, likely providing a more physiologically relevant screening environment.
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