ArticleStructure (London, England : 1993)2015
Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed, 79 citations in OpenAlex.
- On the Feasibility of Clinical Studies with Cross-Linking Mass Spectrometry.Journal of proteome research · 2026Article
- Cellular and molecular outcomes of Pseudomonas putida KT2440 exposure to aluminium.Folia microbiologica · 2025Article
- Cappable-Seq reveals the transcriptional landscape of stress responses in the bacterial endosymbiontMicrobial genomics · 2025Article
- Multiple Chaperone DnaK-FliC Flagellin Interactions are Required for Pseudomonas aeruginosa Flagellum Assembly and Indicate a New Function for DnaK.Microbial biotechnology · 2025Article
- Cross-linking mass spectrometry for mapping protein complex topologies in situ.Essays in biochemistry · 2023Article
- Recombinant Actifensin and Defensin-d2 Induce Critical Changes in the Proteomes of Multidrug-Resistant Pseudomonas aeruginosa and Candida albicans.Microbiology spectrum · 2022Article
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- Applications and advancements of FT-ICR-MS for interactome studies.Mass spectrometry reviews · 2022Review
- Targeted Cross-Linking Mass Spectrometry on Single-Step Affinity Purified Molecular Complexes in the Yeast Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Targeted in situ cross-linking mass spectrometry and integrative modeling reveal the architectures of three proteins from SARS-CoV-2.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Isobaric Quantitative Protein Interaction Reporter Technology for Comparative Interactome Studies.Analytical chemistry · 2020Article
- Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- In Vivo Cross-Linking MS Reveals Conservation in OmpA Linkage to Different Classes of β-Lactamase Enzymes.Journal of the American Society for Mass Spectrometry · 2020Article
- In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria.Journal of proteome research · 2020Article
- Pushing beyond the Envelope: the Potential Roles of OprF inJournal of bacteriology · 2019Review
- Prediction of an Upper Limit for the Fraction of Interprotein Cross-Links in Large-Scale In Vivo Cross-Linking Studies.Journal of proteome research · 2019Article
- Evaluation of Different Stationary Phases in the Separation of Inter-Cross-Linked Peptides.Journal of proteome research · 2019Article
- Increased sensitivity with automated validation of XL-MS cleavable peptide crosslinks.Bioinformatics (Oxford, England) · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
In pathogenic Gram-negative bacteria, interactions among membrane proteins are key mediators of host cell attachment, invasion, pathogenesis, and antibiotic resistance. Membrane protein interactions are highly dependent upon local properties and environment, warranting direct measurements on native protein complex structures as they exist in cells. Here we apply in vivo chemical cross-linking mass spectrometry, to reveal the first large-scale protein interaction network in Pseudomonas aeruginosa, an opportunistic human pathogen, by covalently linking interacting protein partners, thereby fixing protein complexes in vivo. A total of 626 cross-linked peptide pairs, including previously unknown interactions of many membrane proteins, are reported. These pairs not only define the existence of these interactions in cells but also provide linkage constraints for complex structure predictions. Structures of three membrane proteins, namely, SecD-SecF, OprF, and OprI are predicted using in vivo cross-linked sites. These findings improve understanding of membrane protein interactions and structures in cells.
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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.