ArticleThe Journal of biological chemistry2018
Structural and thermodynamic insights into β-1,2-glucooligosaccharide capture by a solute-binding protein in
Article in The Journal of biological chemistry, 2018. 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, 23 citations in OpenAlex.
- Insights into the recognition of cyclic α-(1→6)-glucan by a solute-binding protein of an ABC transporter from Tepidibacillus decaturensis.The Journal of biological chemistry · 2026Article
- A β-1,2-glucan-associated glycoside hydrolase family 1 β-glucosidase from Streptomyces griseus.Protein science : a publication of the Protein Society · 2025Article
- New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025Article
- Cloning and Functional Analysis of Skin Host Defense Peptides from Yakushima Tago's Brown Frog (Antibiotics (Basel, Switzerland) · 2024Article
- Utilization of dietary mixed-linkage β-glucans by the Firmicute Blautia producta.The Journal of biological chemistry · 2023Article
- Novel functional insights into a modified sugar-binding protein from Synechococcus MITS9220.Scientific reports · 2022Article
- Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway.PloS one · 2020Article
- Substrate preference of an ABC importer corresponds to selective growth on β-(1,6)-galactosides inThe Journal of biological chemistry · 2019Article
- Evolutionary adaptation in fucosyllactose uptake systems supports bifidobacteria-infant symbiosis.Science advances · 2019Article
- Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family.The Journal of biological chemistry · 2019Article
- Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149, and GH161 glycoside hydrolase families.The Journal of biological chemistry · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-1,2-Glucans are bacterial carbohydrates that exist in cyclic or linear forms and play an important role in infections and symbioses involving Gram-negative bacteria. Although several β-1,2-glucan-associated enzymes have been characterized, little is known about how β-1,2-glucan and its shorter oligosaccharides (Sop
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.