ArticleScientific reports2014
Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 19 citations in OpenAlex.
- Sited-Directed Fluorescence Spectroscopy for Studies on the Folding and Insertion of Proteins in Lipid Bilayers and Model Membranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Contributions of Yersinia pestis outer membrane protein Ail to plague pathogenesis.Current opinion in infectious diseases · 2022Review
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- 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
- Article
- Position-Specific contribution of interface tryptophans on membrane protein energetics.Biochimica et biophysica acta. Biomembranes · 2018Article
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific.Biochimica et biophysica acta · 2016Article
- Role of cysteines in mammalian VDAC isoforms' function.Biochimica et biophysica acta · 2016Review
- Implications of aromatic-aromatic interactions: From protein structures to peptide models.Protein science : a publication of the Protein Society · 2015Review
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
No grant is acknowledged in the PubMed record.
Abstract
Attachment invasion locus (Ail) protein of Yersinia pestis is a crucial outer membrane protein for host invasion and determines bacterial survival within the host. Despite its importance in pathogenicity, surprisingly little is known on Ail biophysical properties. We investigate the contribution of micelle concentrations and interface tryptophans on the Ail β-barrel refolding and unfolding processes. Our results reveal that barrel folding is surprisingly independent of micelle amounts, but proceeds through an on-pathway intermediate that requires the interface W42 for cooperative barrel refolding. On the contrary, the unfolding event is strongly controlled by absolute micelle concentrations. We find that upon Trp → Phe substitution, protein stabilities follow the order W149F>WT>W42F for the refolding, and W42F>WT>W149F for unfolding. W42 confers cooperativity in barrel folding, and W149 clamps the post-folded barrel structure to its micelle environment. Our analyses reveal, for the first time, that interface tryptophan mutation can indeed render greater β-barrel stability. Furthermore, hysteresis in Ail stems from differential barrel-detergent interaction strengths in a micelle concentration-dependent manner, largely mediated by W149. The kinetically stabilized Ail β-barrel has strategically positioned tryptophans to balance efficient refolding and subsequent β-barrel stability, and may be evolutionarily chosen for optimal functioning of Ail during Yersinia pathogenesis.
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.