ArticleSaudi journal of biological sciences2023
Bioinformatic analysis of WxL domain proteins.
Article in Saudi journal of biological sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Phage P100 resistance in clinical and foodborneCurrent research in microbial sciences · 2026Article
- Integrated Genomic and Phenotypic Analysis ofMicroorganisms · 2025Article
- DUF916 and DUF3324 in the WxL protein cluster bind to WxL and link bacterial and host surfaces.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The WxL domain is found on the cell surface of many bacteria, most of which are commensal gut bacteria. Its functions are generally identified as being related to virulence and/or peptidoglycan attachment, but there is so far no clear function or structure for this domain. Here, a range of bioinformatics tools were used to clarify the structure and function. These indicate that WxL domains occur in cell surface-associated gene clusters that always contain a small WxL, large WxL and DUF916 domain; and that the small and large WxL proteins have distinct structure despite sharing two conserved WxL motifs. The two WxL motifs form a hydrophobic surface buried inside the protein. The likely function of the WxL domain is to attach to bacterial peptidoglycan, forming a platform to allow associated domains in the cluster to interact with host proteins.
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Registered trials
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