ArticleBiophysical journal2018
Toward Single-Cell Single-Molecule Pull-Down.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Deciphering cellular complexity: advances and future directions in single-cell protein analysis.Frontiers in bioengineering and biotechnology · 2024Review
- Article
- Label-Free Single-Molecule Pulldown for the Detection of Released Cellular Protein Complexes.ACS central science · 2022Article
- An Optimized Single-Molecule Pull-Down Assay for Quantification of Protein Phosphorylation.Journal of visualized experiments : JoVE · 2022Article
- Next generation single-molecule techniques: Imaging, labeling, and manipulation in vitro and in cellulo.Molecular cell · 2022Review
- Facile single-molecule pull-down assay for analysis of endogenous proteins.Physical biology · 2019Article
- Utilizing functional cell-free extracts to dissect ribonucleoprotein complex biology at single-molecule resolution.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Single-molecule pull-down (SiMPull) can capture native protein complexes directly from cell lysates for analysis of complex composition and activities at the single-molecule level. Although SiMPull requires many fewer cells compared to conventional pull-down assays, all studies so far have been performed using lysates from many cells. In principle, extending SiMPull to the single-cell level will allow the investigation of cell-to-cell variations on the stoichiometry and activities of biomolecular complexes. We developed a protocol to lyse bacterial cells in situ and capture the released proteins on the imaging surface using antibodies. The use of lysozymes delayed the protein release until after the flow has ceased, and the use of a 10-μm spacer reduces the capture radius within which ∼70% of target proteins can be captured to below 30 μm. Proteins thus captured can be unambiguously assigned to the originating cell. The developed platform should be compatible with high-throughput protein analysis and protein-protein interaction analysis at the single-cell level through single-molecule imaging.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.