ArticleThe Journal of biological chemistry2017
Mechanical forces regulate the reactivity of a thioester bond in a bacterial adhesin.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 36 citations in OpenAlex.
- Review
- Single-molecule magnetic tweezers to probe the equilibrium dynamics of individual proteins at physiologically relevant forces and timescales.Nature protocols · 2024Review
- Dynamic Covalent Hydrogels: Strong yet Dynamic.Gels (Basel, Switzerland) · 2022Review
- An ester bond underlies the mechanical strength of a pathogen surface protein.Nature communications · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Protein folding modulates the chemical reactivity of a Gram-positive adhesin.Nature chemistry · 2021Article
- Binding Strength of Gram-Positive Bacterial Adhesins.Frontiers in microbiology · 2020Review
- The molecular mechanisms underlying mussel adhesion.Nanoscale advances · 2019Review
- Calcium stabilizes the strongest protein fold.Nature communications · 2018Article
- A new structural class of bacterial thioester domains reveals a slipknot topology.Protein science : a publication of the Protein Society · 2018Article
- Disruption of staphylococcal aggregation protects against lethal lung injury.The Journal of clinical investigation · 2018Article
- Smart superglue in streptococci? The proof is in the pulling.The Journal of biological chemistry · 2017Article
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
Bacteria must withstand large mechanical shear forces when adhering to and colonizing hosts. Recent structural studies on a class of Gram-positive bacterial adhesins have revealed an intramolecular Cys-Gln thioester bond that can react with surface-associated ligands to covalently anchor to host surfaces. Two other examples of such internal thioester bonds occur in certain anti-proteases and in the immune complement system, both of which react with the ligand only after the thioester bond is exposed by a proteolytic cleavage. We hypothesized that mechanical forces in bacterial adhesion could regulate thioester reactivity to ligand analogously to such proteolytic gating. Studying the pilus tip adhesin Spy0125 of
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.