ReviewNature protocols2024
A nanobody-based strategy for rapid and scalable purification of human protein complexes.
Review in Nature protocols, 2024. 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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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.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Structures of the lipid II flippase from the monoderm pathogen Staphylococcus aureus.The Journal of biological chemistry · 2026Article
- Structural basis of cotranslational protein N-terminal acetylation by NatB in human cells.Nature communications · 2026Article
- No evidence for direct physical interaction of 5-HTbioRxiv : the preprint server for biology · 2026Article
- Structural evolution of the MTCH family of mitochondrial insertases.Science advances · 2026Article
- Activating adaptor-like sequences in pericentrin mediate its transport by dynein.bioRxiv : the preprint server for biology · 2026Article
- Pollen-inspired multifunctional nanocarrier for porcine circovirus 2 vaccine delivery.Journal of nanobiotechnology · 2026Article
- Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM Structures of Brain-Derived G Protein-Coupled Receptors: The First Direct Visualization from Mammalian Brain Tissue.bioRxiv : the preprint server for biology · 2026Article
- NAC promotes co-translational protein folding at the ribosomal tunnel exit.Molecular cell · 2026Article
- A novel CLDN6 nanobody-based bispecific T-cell engager delivered by self-amplifying RNA platform exhibits potent antitumor efficacy.Journal of nanobiotechnology · 2026Article
- The ER membrane protein complex acts as a chaperone to promote the biogenesis of multi-bundle membrane proteins.bioRxiv : the preprint server for biology · 2026Article
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD.Science advances · 2025Article
- Structural and functional analysis of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fibroblast Growth Factor-Derived Peptides: Sources, Functions, and Applications.Bioengineering (Basel, Switzerland) · 2025Review
- Integrative biophysical characterization of molecular interactions: A case study with the sfGFP-nanobody complex.Analytical biochemistry · 2025Article
- USP37 prevents unscheduled replisome unloading through MCM complex deubiquitination.Nature communications · 2025Article
- Utilizing small molecules to probe and harness the proteome by pooled protein tagging with ligandable domains.Frontiers in pharmacology · 2025Review
- Nanobodies: From High-Throughput Identification to Therapeutic Development.Molecular & cellular proteomics : MCP · 2024Review
- A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER.The Journal of cell biology · 2023Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The isolation of proteins in high yield and purity is a major bottleneck for the analysis of their three-dimensional structure, function and interactome. Here, we present a streamlined workflow for the rapid production of proteins or protein complexes using lentiviral transduction of human suspension cells, combined with highly specific nanobody-mediated purification and proteolytic elution. Application of the method requires prior generation of a plasmid coding for a protein of interest (POI) fused to an N- or C-terminal GFP or ALFA peptide tag using a lentiviral plasmid toolkit we have designed. The plasmid is then used to generate human suspension cell lines stably expressing the tagged fusion protein by lentiviral transduction. By leveraging the picomolar affinity of the GFP and ALFA nanobodies for their respective tags, the POI can be specifically captured from the resulting cell lysate even when expressed at low levels and under a variety of conditions, including detergents and mild denaturants. Finally, rapid and specific elution of the POI (in its tagged or untagged form) under native conditions is achieved within minutes at 4 °C, using the engineered SUMO protease SENP
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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.