ArticleMethods in molecular biology (Clifton, N.J.)2022
Single-Cell Single-Molecule Pull-Down (sc-SiMPull) for Detection of Protein Complexes from Embryonic Lysates.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Exploring Biophysics at the Membrane with Single-Molecule TIRF Microscopy.Advances in experimental medicine and biology · 2026Review
- ASPPs multimerize protein phosphatase 1.PLoS genetics · 2025Article
- Membrane extraction in native lipid nanodiscs reveals dynamic regulation of Cdc42 complexes during cell polarization.Biophysical journal · 2025Article
- Dimerization activates the Inversin complex inMolecular biology of the cell · 2024Article
- Deciphering cellular complexity: advances and future directions in single-cell protein analysis.Frontiers in bioengineering and biotechnology · 2024Review
- A particle size threshold governs diffusion and segregation of PAR-3 during cell polarization.Cell reports · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mapping how proteins form complexes and change binding partners is central to understanding cell signaling. Bulk biochemistry can provide a summary of what complexes are present in a cell, but information about the diversity of individual protein complexes is lost. Here, we describe single-cell , single-molecule pull-down (sc-SiMPull), a TIRF microscopy-based coimmunoprecipitation method, to visualize thousands of individual proteins, their binding partners, and protein complex stoichiometry directly from single-cell lysate. By iterating sc-SiMPull over time, temporal dynamics of protein complexes in response to signaling can be constructed.
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Registered trials
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