ArticleNature biotechnology2018
Encoding human serine phosphopeptides in bacteria for proteome-wide identification of phosphorylation-dependent interactions.
Article in Nature biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- De Novo Engineered Living Materials via Elastin-Like Polypeptide-Mediated Self-Assembly.ACS synthetic biology · 2026Article
- Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Full-Body AI Agent: A Perspective on Multi-Scale Collaborative AI for Systemic Biology and Precision Medicine.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- BeyondChemical reviews · 2025Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Reaching New Heights in Genetic Code Manipulation with High Throughput Screening.Chemical reviews · 2024Review
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Computational approaches to identify sites of phosphorylation.Proteomics · 2024Review
- A Multipathway Phosphopeptide Standard for Rapid Phosphoproteomics Assay Development.Molecular & cellular proteomics : MCP · 2023Article
- A central role for regulated protein stability in the control of TFE3 and MITF by nutrients.Molecular cell · 2023Article
- Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine.Nature communications · 2022Article
- A multi-purpose, regenerable, proteome-scale, human phosphoserine resource for phosphoproteomics.Nature methods · 2022Article
- Uncovering post-translational modification-associated protein-protein interactions.Current opinion in structural biology · 2022Review
- The metabolomic landscape plays a critical role in glioma oncogenesis.Cancer science · 2022Review
- Genetic Code Expansion: A Brief History and Perspective.Biochemistry · 2021Review
- Site-specific phosphorylation of PSD-95 dynamically regulates the postsynaptic density as observed by phase separation.iScience · 2021Article
- Multi-omic regulatory networks capture downstream effects of kinase inhibition in Mycobacterium tuberculosis.NPJ systems biology and applications · 2021Article
- Reporter system architecture affects measurements of noncanonical amino acid incorporation efficiency and fidelity.Molecular systems design & engineering · 2020Article
- Prolyl Isomerase Pin1 in Human Cancer: Function, Mechanism, and Significance.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Post-translational phosphorylation is essential to human cellular processes, but the transient, heterogeneous nature of this modification complicates its study in native systems. We developed an approach to interrogate phosphorylation and its role in protein-protein interactions on a proteome-wide scale. We genetically encoded phosphoserine in recoded E. coli and generated a peptide-based heterologous representation of the human serine phosphoproteome. We designed a single-plasmid library encoding >100,000 human phosphopeptides and confirmed the site-specific incorporation of phosphoserine in >36,000 of these peptides. We then integrated our phosphopeptide library into an approach known as Hi-P to enable proteome-level screens for serine-phosphorylation-dependent human protein interactions. Using Hi-P, we found hundreds of known and potentially new phosphoserine-dependent interactors with 14-3-3 proteins and WW domains. These phosphosites retained important binding characteristics of the native human phosphoproteome, as determined by motif analysis and pull-downs using full-length phosphoproteins. This technology can be used to interrogate user-defined phosphoproteomes in any organism, tissue, or disease of interest.
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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.