ArticleSTAR protocols2021
Mapping of domain-mediated protein-protein interaction by SPOT peptide assay.
Article in STAR protocols, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- PepLess: A computational tool developed to optimize SPOT synthesis and analyze related immunoassay data.Biochemistry and biophysics reports · 2025Article
- Low-cost synthesis of peptide libraries and their use for binding studies via temperature-related intensity change.STAR protocols · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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Abstract
Identification of peptides mediating protein-protein interaction (PPI) is crucial for understanding the function of interlinked proteins in cellular processes and amino acid-associated diseases. Traditional PPI assays are laborious, involving the generation of many truncated proteins. SPOT peptide assay allows high-throughput detection of domains essential for PPI by synthesizing several hundred peptides on a cellulose membrane. Here, we present a rapid SPOT peptide protocol for identifying the binding motifs, which mediate interaction between the chromatin remodeling factors BAF155/BAF170 and the epigenetic factor Kdm6b. For complete details on the use and execution of this protocol, please refer to Narayanan et al. (2015).
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