ArticleNature communications2018
Modular assembly of proteins on nanoparticles.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed.
- Nanosystems Containing Proteins: From Fundamentals to Applications.Chemistry, an Asian journal · 2026Review
- Measuring molecular forces inside living cells using magnetic tweezers.Biophysical reviews · 2025Review
- Design Principles for Engineering Ionic Liquid-Gold Nanoparticles for Therapeutic Delivery to the Brain.ACS nano · 2025Article
- Click biology highlights the opportunities from reliable biological reactions.Nature chemical biology · 2025Review
- Microglial Clearance of Alzheimer's Amyloid-Beta Obstructed by Nanoplastics.Environmental science. Nano · 2025Article
- Nanobody-Based Lateral Flow Assay for Rapid Zika Virus Detection.ACS synthetic biology · 2025Article
- Anticancer Nanoparticle Carriers of the Proapoptotic Protein CytochromePharmaceutics · 2025Review
- Bioluminescent detection of viral surface proteins using branched multivalent protein switches.RSC chemical biology · 2024Article
- Faraday cage-type self-powered immunosensor based on hybrid enzymatic biofuel cell.Analytical and bioanalytical chemistry · 2023Article
- Multivariate Analysis of Protein-Nanoparticle Binding Data Reveals a Selective Effect of Nanoparticle Material on the Formation of Soft Corona.Nanomaterials (Basel, Switzerland) · 2023Article
- Spontaneous and site-specific immobilization of PNGase FRSC advances · 2023Article
- Theranostic Applications of 2D Graphene-Based Materials for Solid Tumors Treatment.Nanomaterials (Basel, Switzerland) · 2023Review
- Gold Nanoparticle-Based Plasmonic Biosensors.Biosensors · 2023Review
- Protein Nanoparticle-Mediated Delivery of Recombinant Influenza Hemagglutinin Enhances Immunogenicity and Breadth of the Antibody Response.ACS infectious diseases · 2023Article
- Iron acquisition and mineral transformation by cyanobacteria living in extreme environments.Materials today. Bio · 2022Article
- From nanoparticles to crystals: one-pot programmable biosynthesis of photothermal gold structures and their use for biomedical applications.Journal of nanobiotechnology · 2022Article
- Atropine-functionalized gold nanoparticles binding to muscarinic receptors after passage across the intestinal epithelium.Royal Society open science · 2022Article
- Fluorescent Nanoparticles for Super-Resolution Imaging.Chemical reviews · 2022Review
- Valence-controlled protein conjugation on nanoparticlesChemical science · 2022Article
- Cloning & expression of SAK enzyme fromJournal of medicine and life · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Generally, the high diversity of protein properties necessitates the development of unique nanoparticle bio-conjugation methods, optimized for each different protein. Here we describe a universal bio-conjugation approach which makes use of a new recombinant fusion protein combining two distinct domains. The N-terminal part is Glutathione S-Transferase (GST) from Schistosoma japonicum, for which we identify and characterize the remarkable ability to bind gold nanoparticles (GNPs) by forming gold-sulfur bonds (Au-S). The C-terminal part of this multi-domain construct is the SpyCatcher from Streptococcus pyogenes, which provides the ability to capture recombinant proteins encoding a SpyTag. Here we show that SpyCatcher can be immobilized covalently on GNPs through GST without the loss of its full functionality. We then show that GST-SpyCatcher activated particles are able to covalently bind a SpyTag modified protein by simple mixing, through the spontaneous formation of an unusual isopeptide bond.
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.