ReviewBioMed research international2014
Interaction analysis through proteomic phage display.
Review in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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
27 citing papers in PubMed.
- Using Biological Networks to Guide Biomedical Prediction.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Integrating endogenous TurboID and data-independent acquisition mass spectrometry for in vivo proximity labeling.The EMBO journal · 2026Article
- Selection of Nucleotide-Encoded Mass Libraries of Macrocyclic Peptides for Inaccessible Drug Targets.Chemical reviews · 2024Review
- HSP60 mimetic peptides from Mycobacterium leprae as new antigens for immunodiagnosis of Leprosy.AMB Express · 2023Article
- Identification of Protein Interaction Partners in Bacteria Using Affinity Purification and SILAC Quantitative Proteomics.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Heterologous expression of naturally evolved putative de novo proteins with chaperones.Protein science : a publication of the Protein Society · 2022Article
- Analyzing the Androgen Receptor Interactome in Prostate Cancer: Implications for Therapeutic Intervention.Cells · 2022Review
- Motifier: An IgOme Profiler Based on Peptide Motifs Using Machine Learning.Journal of molecular biology · 2021Article
- Mapping Protein-Protein Interaction Interface Peptides with Jun-Fos Assisted Phage Display and Deep Sequencing.ACS synthetic biology · 2020Article
- Identifying New Substrates and Functions for an Old Enzyme: Calcineurin.Cold Spring Harbor perspectives in biology · 2020Review
- Delayed Comparison and Apriori Algorithm (DCAA): A Tool for Discovering Protein-Protein Interactions From Time-Series Phosphoproteomic Data.Frontiers in molecular biosciences · 2020Article
- A Consensus Binding Motif for the PP4 Protein Phosphatase.Molecular cell · 2019Article
- Review
- Quantitative mapping of protein-peptide affinity landscapes using spectrally encoded beads.eLife · 2019Article
- The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 2019Review
- SAROTUP: a suite of tools for finding potential target-unrelated peptides from phage display data.International journal of biological sciences · 2019Article
- Split GFP technologies to structurally characterize and quantify functional biomolecular interactions of FTD-related proteins.Scientific reports · 2017Article
- Phage-displayed peptides that mimic epitopes of hepatitis E virus capsid.Medical microbiology and immunology · 2017Article
- cDNA phage display for the discovery of theranostic autoantibodies in rheumatoid arthritis.Immunologic research · 2017Review
- Intriguing Interaction of Bacteriophage-Host Association: An Understanding in the Era of Omics.Frontiers in microbiology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phage display is a powerful technique for profiling specificities of peptide binding domains. The method is suited for the identification of high-affinity ligands with inhibitor potential when using highly diverse combinatorial peptide phage libraries. Such experiments further provide consensus motifs for genome-wide scanning of ligands of potential biological relevance. A complementary but considerably less explored approach is to display expression products of genomic DNA, cDNA, open reading frames (ORFs), or oligonucleotide libraries designed to encode defined regions of a target proteome on phage particles. One of the main applications of such proteomic libraries has been the elucidation of antibody epitopes. This review is focused on the use of proteomic phage display to uncover protein-protein interactions of potential relevance for cellular function. The method is particularly suited for the discovery of interactions between peptide binding domains and their targets. We discuss the largely unexplored potential of this method in the discovery of domain-motif interactions of potential biological relevance.
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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.