ArticleThe journal of physical chemistry. B2017
Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers.
Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
22 citing papers in PubMed, 36 citations in OpenAlex.
- Structure-activity of outer membrane proteins in native bacterial membrane vesicles by solid-state NMR.bioRxiv : the preprint server for biology · 2026Article
- Nuclear magnetic resonance of membrane proteins-Advances and opportunities.Current opinion in structural biology · 2026Review
- In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion.Journal of the American Chemical Society · 2025Article
- A pH-sensitive motif in an outer membrane protein activates bacterial membrane vesicle production.Nature communications · 2024Article
- Dynamic Nuclear Polarization Illuminates Key Protein-Lipid Interactions in the Native Bacterial Cell Envelope.Biochemistry · 2023Article
- Dynamic nuclear polarization illuminates key protein-lipid interactions in the native bacterial cell envelope.bioRxiv : the preprint server for biology · 2023Article
- Yersinia pestis ΔApplied and environmental microbiology · 2023Article
- Contributions of Yersinia pestis outer membrane protein Ail to plague pathogenesis.Current opinion in infectious diseases · 2022Review
- Deletion of Yersinia pestisJournal of bacteriology · 2021Article
- Article
- Comparative analysis ofJournal of biomolecular NMR · 2021Article
- Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents.Biochemistry · 2021Article
- Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope.Biophysical journal · 2021Article
- Mutually constructive roles of Ail and LPS in Yersinia pestis serum survival.Molecular microbiology · 2020Article
- Membrane proteins in magnetically aligned phospholipid polymer discs for solid-state NMR spectroscopy.Biochimica et biophysica acta. Biomembranes · 2020Article
- Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate.Biochimica et biophysica acta. Biomembranes · 2020Article
- Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation.The Journal of biological chemistry · 2020Article
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.Current opinion in structural biology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Yersinia pestis the causative agent of plague, is highly pathogenic and poses very high risk to public health. The outer membrane protein Ail (Adhesion invasion locus) is one of the most highly expressed proteins on the cell surface of Y. pestis, and a major target for the development of medical countermeasures. Ail is essential for microbial virulence and is critical for promoting the survival of Y. pestis in serum. Structures of Ail have been determined by X-ray diffraction and solution NMR spectroscopy, but the protein's activity is influenced by the detergents in these samples, underscoring the importance of the surrounding environment for structure-activity studies. Here we describe the backbone structure of Ail, determined in lipid bilayer nanodiscs, using solution NMR spectroscopy. We also present solid-state NMR data obtained for Ail in membranes containing lipopolysaccharide (LPS), a major component of the bacterial outer membranes. The protein in lipid bilayers, adopts the same eight-stranded β-barrel fold observed in the crystalline and micellar states. The membrane composition, however, appears to have a marked effect on protein dynamics, with LPS enhancing conformational order and slowing down the
Indexed as
Identifiers
What OpenQuestion holds
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.