ArticleBiotechnology for biofuels2018
Deletion of a single glycosyltransferase in
Article in Biotechnology for biofuels, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Functional Comparison of Three Chitinases from Symbiotic Bacteria of Entomopathogenic Nematodes.Toxins · 2024Article
- Structural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase fromBiochemistry · 2021Article
- Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability ofApplied and environmental microbiology · 2020Article
- Insights into Thermophilic Plant Biomass Hydrolysis fromMicroorganisms · 2020Review
- The biology and biotechnology of the genus Caldicellulosiruptor: recent developments in 'Caldi World'.Extremophiles : life under extreme conditions · 2020Review
- Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme fromBiotechnology for biofuels · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein glycosylation pathways have been identified in a variety of bacteria and are best understood in pathogens and commensals in which the glycosylation targets are cell surface proteins, such as S layers, pili, and flagella. In contrast, very little is known about the glycosylation of bacterial enzymes, especially those secreted by cellulolytic bacteria.
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.