ArticleJournal of molecular recognition : JMR
Efficient identification of tubby-binding proteins by an improved system of T7 phage display.
Article in Journal of molecular recognition : JMR. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 55 citations in OpenAlex.
- A method for rapid and reliable quantification of VEGF-cell binding activity.Biochemical and biophysical research communications · 2024Article
- Optimal Humanized Scg3-Neutralizing Antibodies for Anti-Angiogenic Therapy of Diabetic Retinopathy.International journal of molecular sciences · 2024Article
- Peptide discovery across the spectrum of neuroinflammation; microglia and astrocyte phenotypical targeting, mediation, and mechanistic understanding.Frontiers in molecular neuroscience · 2024Review
- Anti-Scg3 Gene Therapy to Treat Choroidal Neovascularization in Mice.Biomedicines · 2023Article
- Secretogranin III Selectively Promotes Vascular Leakage in the Deep Vascular Plexus of Diabetic Retinopathy.International journal of molecular sciences · 2023Article
- Review
- Advances in phage display based nano immunosensors for cholera toxin.Frontiers in immunology · 2023Review
- Comparative ligandomics implicates secretogranin III as a disease-restricted angiogenic factor in laser-induced choroidal neovascularization.The FEBS journal · 2022Article
- The Use of Bacteriophages in Biotechnology and Recent Insights into Proteomics.Antibiotics (Basel, Switzerland) · 2022Review
- T7 Phage as an Emerging Nanobiomaterial with Genetically Tunable Target Specificity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Secretogranin III stringently regulates pathological but not physiological angiogenesis in oxygen-induced retinopathy.Cellular and molecular life sciences : CMLS · 2022Article
- Protein Engineering: Advances in Phage Display for Basic Science and Medical Research.Biochemistry. Biokhimiia · 2022Review
- Selectively targeting disease-restricted secretogranin III to alleviate choroidal neovascularization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Comparative Ligandomic Analysis of Human Lung Epithelial Cells Exposed to PMBiomedical and environmental sciences : BES · 2020Article
- Anti-secretogranin III therapy of oxygen-induced retinopathy with optimal safety.Angiogenesis · 2019Article
- Plant/Bacterial Virus-Based Drug Discovery, Drug Delivery, and Therapeutics.Pharmaceutics · 2019Review
- Function-first ligandomics for ocular vascular research and drug target discovery.Experimental eye research · 2019Article
- Ligandomics: a paradigm shift in biological drug discovery.Drug discovery today · 2018Review
- Virus-Derived Peptides for Clinical Applications.Chemical reviews · 2017Review
- Secretogranin III as a disease-associated ligand for antiangiogenic therapy of diabetic retinopathy.The Journal of experimental medicine · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Mutation in the tubby gene causes adult-onset obesity, progressive retinal, and cochlear degeneration with unknown mechanism. In contrast, mutations in tubby-like protein 1 (Tulp1), whose C-terminus is highly homologous to tubby, only lead to retinal degeneration. We speculate that their diverse N-terminus may define their distinct disease profile. To elucidate the binding partners of tubby, we used tubby N-terminus (tubby-N) as bait to identify unknown binding proteins with open-reading-frame (ORF) phage display. T7 phage display was engineered with three improvements: high-quality ORF phage display cDNA library, specific phage elution by protease cleavage, and dual phage display for sensitive high throughput screening. The new system is capable of identifying unknown bait-binding proteins in as fast as approximately 4-7 days. While phage display with conventional cDNA libraries identifies high percentage of out-of-frame unnatural short peptides, all 28 tubby-N-binding clones identified by ORF phage display were ORFs. They encode 16 proteins, including 8 nuclear proteins. Fourteen proteins were analyzed by yeast two-hybrid assay and protein pull-down assay with ten of them independently verified. Comparative binding analyses revealed several proteins binding to both tubby and Tulp1 as well as one tubby-specific binding protein. These data suggest that tubby-N is capable of interacting with multiple nuclear and cytoplasmic protein binding partners. These results demonstrated that the newly-engineered ORF phage display is a powerful technology to identify unknown protein-protein interactions.
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