ArticleJournal of the American Chemical Society2008
Lipid modification of proteins through sortase-catalyzed transpeptidation.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 154 citations in OpenAlex.
- Sortase A-Mediated Farnesylation of Cdc42ACS synthetic biology · 2026Article
- Homogeneous antibody-drug conjugates with dual payloads: potential, methods and considerations.mAbs · 2025Review
- Site-Specific Functionalization of Recombinant Spider Silk Using Enzymatic Sortase Coupling.ACS omega · 2025Article
- Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025Article
- Site-Specific and Fluorescently Enhanced Installation of Post-Translational Protein Modifications via Bifunctional Biarsenical Linker.ACS omega · 2024Article
- The Transpeptidase Sortase A Binds Nucleic Acids and Mediates Mammalian Cell Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- SpSrtA-Catalyzed Isopeptide Ligation on Lysine Residues.Microorganisms · 2024Article
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy.Bioconjugate chemistry · 2023Article
- Structure Activity Relationship of the Stem Peptide in Sortase A Mediated Ligation from Staphylococcus aureus.Chembiochem : a European journal of chemical biology · 2022Article
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Enzymatic C-to-C Protein Ligation.Angewandte Chemie (International ed. in English) · 2022Article
- Review
- Engineering Ligand and Receptor Pairs with LIPSTIC to Track Cell-Cell Interactions.Current protocols · 2021Article
- Exploiting Protein N-Terminus for Site-Specific Bioconjugation.Molecules (Basel, Switzerland) · 2021Review
- Optimization of sortase A ligation for flexible engineering of complex protein systems.The Journal of biological chemistry · 2020Article
- Site-Specific Sequential Protein Labeling Catalyzed by a Single Recombinant Ligase.Journal of the American Chemical Society · 2019Article
- Broadening the scope of sortagging.RSC advances · 2019Review
- Recent progress in enzymatic protein labelling techniques and their applications.Chemical Society reviews · 2018Review
- One-Pot Dual Labeling of IgG 1 and Preparation of C-to-C Fusion Proteins Through a Combination of Sortase A and Butelase 1.Bioconjugate chemistry · 2018Article
- Protein Labeling via a Specific Lysine-Isopeptide Bond Using the Pilin Polymerizing Sortase from Corynebacterium diphtheriae.Journal of the American Chemical Society · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A general chemoenzymatic method for the site-specific attachment of lipids to protein substrates is described. Sortase A is used to append short lipid-modified oligoglycine peptides to the C terminus of protein substrates bearing a five amino acid sortase A recognition sequence (LPETG). We demonstrate the attachment of a range of hydrophobic modifications in excellent yield (60-90%), including a simple step for removing the sortase enzyme postreaction. Lipoproteins prepared using these procedures were subsequently shown to associate with mammalian cells in a lipid tail-dependent fashion and localized to the plasma membrane and endosomes.
Indexed as
Identifiers
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.