ArticleMethods (San Diego, Calif.)2016
Single-molecule pull-down for investigating protein-nucleic acid interactions.
Article in Methods (San Diego, Calif.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- Select amino acids in DGCR8 are essential for the UGU-pri-miRNA interaction and processing.Communications biology · 2020Article
- Facile single-molecule pull-down assay for analysis of endogenous proteins.Physical biology · 2019Article
- Toward Single-Cell Single-Molecule Pull-Down.Biophysical journal · 2018Article
- SRSF3 recruits DROSHA to the basal junction of primary microRNAs.RNA (New York, N.Y.) · 2018Article
- Microprocessor depends on hemin to recognize the apical loop of primary microRNA.Nucleic acids research · 2018Article
- Viral suppressors of RNAi employ a rapid screening mode to discriminate viral RNA from cellular small RNA.Nucleic acids research · 2018Article
- Utilizing Biotinylated Proteins Expressed in Yeast to Visualize DNA-Protein Interactions at the Single-Molecule Level.Frontiers in microbiology · 2017Article
- TRBP ensures efficient Dicer processing of precursor microRNA in RNA-crowded environments.Nature communications · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The genome and transcriptome are constantly modified by proteins in the cell. Recent advances in single-molecule techniques allow for high spatial and temporal observations of these interactions between proteins and nucleic acids. However, due to the difficulty of obtaining functional protein complexes, it remains challenging to study the interactions between macromolecular protein complexes and nucleic acids. Here, we combined single-molecule fluorescence with various protein complex pull-down techniques to determine the function and stoichiometry of ribonucleoprotein complexes. Through the use of three examples of protein complexes from eukaryotic cells (Drosha, Dicer, and TUT4 protein complexes), we provide step-by-step guidance for using novel single-molecule techniques. Our single-molecule methods provide sub-second and nanometer resolution and can be applied to other nucleoprotein complexes that are essential for cellular processes.
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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.