Evidence map›Paper›PMID 26925049›Full record

ArticleFrontiers in microbiology2016

Bacterial Glycosyltransferases: Challenges and Opportunities of a Highly Diverse Enzyme Class Toward Tailoring Natural Products.

Jochen Schmid, Dominik Heider, Norma J Wendel, Nadine Sperl, Volker Sieber

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 111 citations in OpenAlex.

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  12. A genome-wide investigation ofFrontiers in microbiology · 2025
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  15. Exopolysaccharide Biosynthesis inInternational journal of molecular sciences · 2023
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  16. Review
  17. Pathological Features and Genomic Characterization of anPathogens (Basel, Switzerland) · 2023
    Article
  18. Article
  19. Proteome level analysis of drug-resistantFrontiers in microbiology · 2023
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Jochen SchmidChemistry of Biogenic Resources, Technische Universität München Straubing, Germany.
Dominik HeiderDepartment of Bioinformatics, Straubing Center of Science, University of Applied Sciences Weihenstephan-Triesdorf Straubing, Germany.
Norma J WendelDepartment of Bioinformatics, Straubing Center of Science, University of Applied Sciences Weihenstephan-Triesdorf Straubing, Germany.
Nadine SperlChemistry of Biogenic Resources, Technische Universität München Straubing, Germany.
Volker SieberChemistry of Biogenic Resources, Technische Universität München Straubing, Germany.
Biogen (Germany) · DEWeihenstephan-Triesdorf University of Applied Sciences · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme subclass of glycosyltransferases (GTs; EC 2.4) currently comprises 97 families as specified by CAZy classification. One of their important roles is in the biosynthesis of disaccharides, oligosaccharides, and polysaccharides by catalyzing the transfer of sugar moieties from activated donor molecules to other sugar molecules. In addition GTs also catalyze the transfer of sugar moieties onto aglycons, which is of great relevance for the synthesis of many high value natural products. Bacterial GTs show a higher sequence similarity in comparison to mammalian ones. Even when most GTs are poorly explored, state of the art technologies, such as protein engineering, domain swapping or computational analysis strongly enhance our understanding and utilization of these very promising classes of proteins. This perspective article will focus on bacterial GTs, especially on classification, screening and engineering strategies to alter substrate specificity. The future development in these fields as well as obstacles and challenges will be highlighted and discussed.

Indexed as

bacterial glycosyltransferasescategorization of glycosyltransferasesdocking experimentspolysaccharide glycosyltransferasesscreeningsubstrate specificity

Identifiers

PMID26925049
PMCPMC4757703
OpenAlexW2300549074

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.