ArticleJournal of the American Chemical Society2019
A Chemically Disrupted Proximity System for Controlling Dynamic Cellular Processes.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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Who cites it
21 citing papers in PubMed.
- High-resolution measurement of ERK activation state reveals determinants of BRAF regulation and drug sensitivity.bioRxiv : the preprint server for biology · 2026Article
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- MEK interactions tune RAF kinase sensitivity to conformation-selective inhibition.Nature chemical biology · 2026Article
- A Single-Chain Light-Activatable Transcriptional Reporter for Fluorescently Tagging Mammalian Cells In Vitro.Chembiochem : a European journal of chemical biology · 2026Article
- Identification of affinity-optimized peptide binders of a viral protease for chemical genetic applications.Bioorganic & medicinal chemistry letters · 2026Article
- Engineered Allosteric RNA Editors Enable Compact, Stimulus-Responsive Post-Transcriptional Circuits.bioRxiv : the preprint server for biology · 2026Article
- A Modular Platform for the Optogenetic Control of Small GTPase Activity in Living Cells Reveals Long-Range RhoA Signaling.bioRxiv : the preprint server for biology · 2025Article
- Programmable solid-state condensates for spatiotemporal control of mammalian gene expression.Nature chemical biology · 2025Article
- Methods for Controlling Small GTPase Activity.Chembiochem : a European journal of chemical biology · 2025Review
- Protease-Containing Nanobodies for Detecting and Manipulating Intracellular Antigens Using Antiviral Drugs.ACS chemical biology · 2025Article
- Late-Stage Reshaping of Phage-Displayed Libraries to Macrocyclic and Bicyclic Landscapes using a Multipurpose Linchpin.Journal of the American Chemical Society · 2025Article
- Turn-on protein switches for controlling actin binding in cells.Nature communications · 2024Article
- Engineered poly(A)-surrogates for translational regulation and therapeutic biocomputation in mammalian cells.Cell research · 2024Article
- Turn-On Protein Switches for Controlling Actin Binding in Cells.bioRxiv : the preprint server for biology · 2023Article
- Controlled Protein Activities with Viral Proteases, Antiviral Peptides, and Antiviral Drugs.ACS chemical biology · 2023Article
- Spatial Chemoproteomics for Mapping the Active Proteome.Israel journal of chemistry · 2023Article
- High-performance multiplex drug-gated CAR circuits.Cancer cell · 2022Article
- An Evolutionary Strategy for Identification of Higher Order, Green Fluorescent Host-Guest Pairs Compatible with Living Systems.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Cyclodextrin-Based Peptide Self-Assemblies (Spds) That Enhance Peptide-Based Fluorescence Imaging and Antimicrobial Efficacy.Journal of the American Chemical Society · 2020Article
- Phosphine-Activated Lysine Analogues for Fast Chemical Control of Protein Subcellular Localization and Protein SUMOylation.Chembiochem : a European journal of chemical biology · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Chemical methods that allow the spatial proximity of proteins to be temporally modulated are powerful tools for studying biology and engineering synthetic cellular behaviors. Here, we describe a new chemically controlled method for rapidly disrupting the interaction between two basally colocalized protein binding partners. Our chemically disrupted proximity (CDP) system is based on the interaction between the hepatitis C virus protease (HCVp) NS3a and a genetically encoded peptide inhibitor. Using clinically approved antiviral inhibitors as chemical disrupters of the NS3a/peptide interaction, we demonstrate that our CDP system can be used to confer temporal control over diverse intracellular processes. This NS3a-based CDP system represents a new modality for engineering chemical control over intracellular protein function that is complementary to currently available techniques.
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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.