ArticleMethods in molecular biology (Clifton, N.J.)2023
Affinity Purification-Mass Spectroscopy (AP-MS) and Co-Immunoprecipitation (Co-IP) Technique to Study Protein-Protein Interactions.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 13 citations in OpenAlex.
- A Brief Progress in Methods for Deciphering Protein-Protein Interaction Networks.International journal of molecular sciences · 2026Review
- Article
- Capturing protein-protein interactions in plants: recent advances, challenges, and opportunities.Frontiers in molecular biosciences · 2026Review
- Enhancing cross-organelle coordination to advance plant cytochrome P450 functionality in yeast.Science advances · 2025Article
- Ballistic Microscopy (BaM).bioRxiv : the preprint server for biology · 2025Article
- Progress and Prospects in FRET for the Investigation of Protein-Protein Interactions.Biosensors · 2025Review
- Complete end-to-end learning from protein feature representation to protein interactome inference.GigaScience · 2025Article
- Antibody-Mediated Protein A-APEX2 Labeling (AMAPEX) for Proximity Proteome Exploration.Methods in molecular biology (Clifton, N.J.) · 2025Article
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2 authors at 1 institution in 1 country.
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Abstract
Affinity purification-Mass spectroscopy (AP-MS) is a biochemical technique to identify the novel protein-protein interaction that occurs in the most relevant physiological conditions, whereas co-immunoprecipitation (Co-IP) is used to study the interaction between two known protein partners that are expressed in the native physiological conditions. Both AP-MS and Co-IP techniques are based on the ability of the interacting partners to pull-down with protein of interest. In this chapter, we have explained the AP-MS and Co-IP methods to study protein-protein interactions in the plant cells.
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