ArticlePloS one2012
Peptide array X-linking (PAX): a new peptide-protein identification approach.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- ArpC5 isoforms regulate Arp2/3 complex-dependent protrusion through differential Ena/VASP positioning.Science advances · 2023Article
- Peptide-based Interaction Proteomics.Molecular & cellular proteomics : MCP · 2020Review
- Mapping low-affinity/high-specificity peptide-protein interactions using ligand-footprinting mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- High-throughput methods for identification of protein-protein interactions involving short linear motifs.Cell communication and signaling : CCS · 2015Article
- WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.Molecular biology of the cell · 2015Article
- Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton.Developmental cell · 2014Article
- Learning from nature - novel synthetic biology approaches for biomaterial design.Acta biomaterialia · 2014Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Many protein interaction domains bind short peptides based on canonical sequence consensus motifs. Here we report the development of a peptide array-based proteomics tool to identify proteins directly interacting with ligand peptides from cell lysates. Array-formatted bait peptides containing an amino acid-derived cross-linker are photo-induced to crosslink with interacting proteins from lysates of interest. Indirect associations are removed by high stringency washes under denaturing conditions. Covalently trapped proteins are subsequently identified by LC-MS/MS and screened by cluster analysis and domain scanning. We apply this methodology to peptides with different proline-containing consensus sequences and show successful identifications from brain lysates of known and novel proteins containing polyproline motif-binding domains such as EH, EVH1, SH3, WW domains. These results suggest the capacity of arrayed peptide ligands to capture and subsequently identify proteins by mass spectrometry is relatively broad and robust. Additionally, the approach is rapid and applicable to cell or tissue fractions from any source, making the approach a flexible tool for initial protein-protein interaction discovery.
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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.