ArticleMethods in molecular biology (Clifton, N.J.)2020
Immunoprecipitation for the Analysis of Macromolecular Complexes in Trypanosoma cruzi.
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 1 paper.
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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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1 citing paper in PubMed, 1 citations in OpenAlex.
- Identification of novel compounds againstComputational and structural biotechnology journal · 2025Article
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3 authors at 1 institution in 1 country.
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Abstract
Immunoprecipitation is a helpful tool to assess interactions between proteins and proteins or nucleic acids (DNA or RNA). Its principle consists in capturing and enriching one or multiple target proteins from a complex sample with a specific antibody conjugated to a solid matrix and isolating the RNA and/or protein molecules associated to those target(s) group of proteins that can be further identified by advanced techniques such as RNA-seq and/or mass spectrometry. Since this technique allows for identifying, mapping, and checking new protein-protein and protein-RNA interactions, its use is very convenient in situations where many proteins remain with their functions uncharacterized, as is the case of the protozoan Trypanosoma cruzi. Here we describe a protocol that is based on the cryogrinding method for cell lysis and the use of antibodies conjugated to magnetic beads to capture and purify protein complexes in a robust and efficient way.
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