ArticleNature communications2020
Split Intein-Mediated Protein Ligation for detecting protein-protein interactions and their inhibition.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 58 citations in OpenAlex.
- Article
- A one-pot purification-free strategy for biotinylated antibody preparation enables sensitive ELISA detection of cardiac troponin I-C complex.Analytical and bioanalytical chemistry · 2025Article
- Photoswitchable intein for light control of covalent protein binding and cleavage.Nature communications · 2025Article
- Smartphone-based "monitoring workstation" for contamination-free and on-site colorimetric detection of living cells.Mikrochimica acta · 2025Article
- Decoding the functional impact of the cancer genome through protein-protein interactions.Nature reviews. Cancer · 2025Review
- The BCL11A transcription factor stimulates the enzymatic activities of the OGG1 DNA glycosylase.Biological chemistry · 2024Article
- Engineering conditional protein-protein interactions for dynamic cellular control.Biotechnology advances · 2024Review
- Cell-Int: a cell-cell interaction assay to identify native membrane protein interactions.Life science alliance · 2024Article
- SiMPl-GS: Advancing Cell Line Development via Synthetic Selection Marker for Next-Generation Biopharmaceutical Production.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Distinct phases of cellular signaling revealed by time-resolved protein synthesis.Nature chemical biology · 2024Article
- Int&in: A machine learning-based web server for active split site identification in inteins.Protein science : a publication of the Protein Society · 2024Article
- Cell surface β-lactamase recruitment: A facile selection to identify protein-protein interactions.Protein science : a publication of the Protein Society · 2024Article
- AI-guided pipeline for protein-protein interaction drug discovery identifies a SARS-CoV-2 inhibitor.Molecular systems biology · 2024Article
- The function of BCL11B in base excision repair contributes to its dual role as an oncogene and a haplo-insufficient tumor suppressor gene.Nucleic acids research · 2024Article
- Near-Infrared Optogenetic Module for Conditional Protein Splicing.Journal of molecular biology · 2023Article
- The DNA repair function of BCL11A suppresses senescence and promotes continued proliferation of triple-negative breast cancer cells.NAR cancer · 2022Article
- B cell linker protein (BLNK) is a regulator of Met receptor signaling and trafficking in non-small cell lung cancer.iScience · 2022Article
- A Conserved Histidine Residue Drives Extein Dependence in an Enhanced Atypically Split Intein.Journal of the American Chemical Society · 2022Article
- Met-HER3 crosstalk supports proliferation via MPZL3 in MET-amplified cancer cells.Cellular and molecular life sciences : CMLS · 2022Article
- IID 2021: towards context-specific protein interaction analyses by increased coverage, enhanced annotation and enrichment analysis.Nucleic acids research · 2022Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 4 countries.
Funding
Abstract
Here, to overcome many limitations accompanying current available methods to detect protein-protein interactions (PPIs), we develop a live cell method called Split Intein-Mediated Protein Ligation (SIMPL). In this approach, bait and prey proteins are respectively fused to an intein N-terminal fragment (IN) and C-terminal fragment (IC) derived from a re-engineered split intein GP41-1. The bait/prey binding reconstitutes the intein, which splices the bait and prey peptides into a single intact protein that can be detected by regular protein detection methods such as Western blot analysis and ELISA, serving as readouts of PPIs. The method is robust and can be applied not only in mammalian cell lines but in animal models such as C. elegans. SIMPL demonstrates high sensitivity and specificity, and enables exploration of PPIs in different cellular compartments and tracking of kinetic interactions. Additionally, we establish a SIMPL ELISA platform that enables high-throughput screening of PPIs and their inhibitors.
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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.