ArticleBio-protocol2022
DSP-crosslinking and Immunoprecipitation to Isolate Weak Protein Complex.
Article in Bio-protocol, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Protocol for analyzing protein interactomes under starvation in fission yeast using in vivo cross-linking.STAR protocols · 2026Article
- A pore-forming toxin initiates ABI1 complex switching to promote bacterial cell-to-cell spread.Nature communications · 2026Article
- An atypical F-type ATPase is necessary for the function of the antibody cleavage system MIB-MIP in mycoplasmas.PLoS pathogens · 2026Article
- HCR-Proxy resolves site-specific proximal RNA microenvironments at subcompartmental resolution.Nucleic acids research · 2026Article
- Article
- UBQLN2 is necessary for UBE3A-mediated proteasomal degradation of the domesticated retroelement PEG10.Journal of cell science · 2025Article
- Mitochondria-localized MBD2c facilitates mtDNA transcription and drug resistance.Nature chemical biology · 2025Article
- FixNCut: A Practical Guide to Sample Preservation by Reversible Fixation for Single Cell Assays.Bio-protocol · 2024Article
- Muskelin acts as a substrate receptor of the highly regulatedbioRxiv : the preprint server for biology · 2024Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Detecting protein-protein interactions (PPIs) is one of the most used approaches to reveal the molecular regulation of protein of interests (POIs). Immunoprecipitation of POIs followed by mass spectrometry or western blot analysis enables us to detect co-precipitated POI-binding proteins. However, some binding proteins are lost during cell lysis or immunoprecipitation if the protein binding affinity is weak. Crosslinking POI and its binding proteins stabilizes the PPI and increases the chance of detecting the interacting proteins. Here, we introduce the method of DSP (dithiobis(succinimidyl propionate))-mediated crosslinking, followed by tandem immunoprecipitation (FLAG and HA tags). The eluted proteins interacting with POI can be analyzed by mass spectrometry or western blotting. This method has the potential to be applied to various cytoplasmic proteins. Graphical abstract.
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